|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-588 |
1.60e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 274 EKREETQKKLSNlVEEKM---NLIVEEIE-QLcgacskqespnKSL---------YREMSE----LRSQKQAMEVRYFDA 336
Cdd:COG1196 172 ERKEEAERKLEA-TEENLerlEDILGELErQL-----------EPLerqaekaerYRELKEelkeLEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 337 QKE-HTEQMNQLRIELdAKLKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVK 415
Cdd:COG1196 240 ELEeLEAELEELEAEL-EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 416 EQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEQHKKVM 495
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 496 NKQVANTIKQHADFEELggnYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMREQMVIDQKLLNARSELIATL 575
Cdd:COG1196 399 AAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330
....*....|...
gi 28573859 576 QKNEEDSRTKLDQ 588
Cdd:COG1196 476 EAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-586 |
5.44e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.38 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 274 EKREETQKKlsnLVEEKMNLI-VEEIeqlcgacskqespnkslyreMSELRSQKQAMEvryfdAQKEHTEQMNQLRIELD 352
Cdd:TIGR02168 172 ERRKETERK---LERTRENLDrLEDI--------------------LNELERQLKSLE-----RQAEKAERYKELKAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 353 AKLKQELASRdqiIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERa 432
Cdd:TIGR02168 224 ELELALLVLR---LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 433 rnsVDKNLKHID----YLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEQHKKVMNKQVANT----IK 504
Cdd:TIGR02168 300 ---LEQQKQILRerlaNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELesrlEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 505 QHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMREQMVIDQKL-----LNARSELIATLQKNE 579
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKelqaeLEELEEELEELQEEL 456
|
....*..
gi 28573859 580 EDSRTKL 586
Cdd:TIGR02168 457 ERLEEAL 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-528 |
1.17e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRYFDAQKEHT 341
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 342 EqmnqLRIELdAKLKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKR 421
Cdd:TIGR02168 814 L----LNEEA-ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 422 LEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKE-KDLIIADLKLQLQSLEQHKKVMNKQVA 500
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEE 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 28573859 501 NT---IKQH---------------ADFEELGGNYKEALQQISDLRE 528
Cdd:TIGR02168 969 EArrrLKRLenkikelgpvnlaaiEEYEELKERYDFLTAQKEDLTE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
336-588 |
1.58e-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: 54.69 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 336 AQKEHTEQMNQ----LRIELDAkLKQELASRDQIIVELRKSLRRSEDMLSEQSIRlaennsklltedstIEVLRSEVAKL 411
Cdd:TIGR02169 671 SEPAELQRLRErlegLKRELSS-LQSELRRIENRLDELSQELSDASRKIGEIEKE--------------IEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 412 KTVKEQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRP------------DAMDAGVKEKDLIIA 479
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsripeiqaelSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 480 DLKLQLQSLEQHKKVMNKQVANTIKQHADFEElggNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMREQmv 559
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-- 890
|
250 260
....*....|....*....|....*....
gi 28573859 560 idqkLLNARSELIAtLQKNEEDSRTKLDQ 588
Cdd:TIGR02169 891 ----RDELEAQLRE-LERKIEELEAQIEK 914
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-544 |
3.06e-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: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLcgacskqESPNKSLYREMSELRSQKQAMEVRYfdaqKEHT 341
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-------EEDLSSLEQEIENVKSELKELEARI----EELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 342 EQMNQLRIELdAKLKQELAsrDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKR 421
Cdd:TIGR02169 772 EDLHKLEEAL-NDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 422 LEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEQHKKVMNKQVAN 501
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 28573859 502 TIKQHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLE 544
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
317-589 |
1.77e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 317 REMSELRSQKQAMEvryfdaqkehtEQMNQLRIELDAkLKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLT 396
Cdd:TIGR02168 677 REIEELEEKIEELE-----------EKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 397 EDSTIEVLRSEVAKLKTVKEQMVKRLEEAdkglerarnsvdknlkhidylEGELKEARELIVHLEQRPDAMDAGVKEKDL 476
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEA---------------------EEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 477 IIADLKLQLQSLEQHKKVMNKQVANTIKQHADFEELggnYKEALQQISDLRETLSVTNAKLEmqsklevQLRKEVSKMRE 556
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERR---LEDLEEQIEELSEDIESLAAEIE-------ELEELIEELES 873
|
250 260 270
....*....|....*....|....*....|...
gi 28573859 557 QMVIDQKLLNARSELIATLQKNEEDSRTKLDQM 589
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELREL 906
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-544 |
2.67e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRyfDAQKEHT 341
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER--LANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 342 EQMNQLRIELDAK----LKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQ 417
Cdd:TIGR02168 318 LEELEAQLEELESkldeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 418 MVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEA------------RELIVHLEQRPDAMDAGVKEKDLIIADLKLQL 485
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 28573859 486 QSLEQHKKVMNKQVANTIKQHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLE 544
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
420-589 |
5.32e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 420 KRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEQHKKVMNKQV 499
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 500 ANTIKQH------------------ADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMREQMVID 561
Cdd:COG4942 107 AELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190
....*....|....*....|....*....|..
gi 28573859 562 QKLL----NARSELIATLQKNEEDSRTKLDQM 589
Cdd:COG4942 187 RAALealkAERQKLLARLEKELAELAAELAEL 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
373-581 |
1.41e-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: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 373 LRRSEDMLSeqsiRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQmvKRLEEADKGLERARNSVDKNLKHIDYLEGELKE 452
Cdd:COG4913 247 AREQIELLE----PIRELAERYAAARERLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 453 ARELIVHLEQRpdAMDAGVKEkdliIADLKLQLQSLEQHKKVMN---KQVANTIKQ--------HADFEELGGNYKEALQ 521
Cdd:COG4913 321 LREELDELEAQ--IRGNGGDR----LEQLEREIERLERELEERErrrARLEALLAAlglplpasAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28573859 522 QISDLRETLSVTNAKLEMQsklEVQLRKEVSKMRE--------QMVIDQKLLNARSELIATLQKNEED 581
Cdd:COG4913 395 ALEEELEALEEALAEAEAA---LRDLRRELRELEAeiaslerrKSNIPARLLALRDALAEALGLDEAE 459
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
301-528 |
2.86e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 301 LCGACSKQESPNKSLYREMSELRSQKQAMEVRYFDAQKEHteqmnqlrieldAKLKQELASRDQIIVELRKSLRRSEDML 380
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE------------KALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 381 SEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKR-----------LEEADKGLERARNSVDKNLKHIDYLEGE 449
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 450 LKEARELIVHLEQRPDAMDAGVKEKdliiADLKLQLQSLEQHKKVMNKQVANTIKQHADF-EELGGNYKEALQQISDLRE 528
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAEL----EEERAALEALKAERQKLLARLEKELAELAAElAELQQEAEELEALIARLEA 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-557 |
3.21e-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: 46.97 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRYFDAQKEHT 341
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 342 EQMNQLRIELD--AKLKQELASRDQIIVELRKSLRRSED-------MLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLK 412
Cdd:TIGR02168 758 ELEAEIEELEErlEEAEEELAEAEAEIEELEAQIEQLKEelkalreALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 413 TVKEQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQrpdAMDAGVKEKDliiaDLKLQLQSLEQHK 492
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE---ALALLRSELE----ELSEELRELESKR 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28573859 493 KVMNKQVANTIKQHADFEElggNYKEALQQISDLRETLSVT-NAKLEMQSKLEVQLRKEVSKMREQ 557
Cdd:TIGR02168 911 SELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRR 973
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
264-439 |
4.03e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 264 QRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLcgacskqESPNKSLYREMSElrsqkqamEVRYFDAQKEHTEQ 343
Cdd:PRK01156 576 VISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD-------KSYIDKSIREIEN--------EANNLNNKYNEIQE 640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 344 MNQLRIELDAK---LKQELASRDQII---VELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQ 417
Cdd:PRK01156 641 NKILIEKLRGKidnYKKQIAEIDSIIpdlKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
170 180
....*....|....*....|....*...
gi 28573859 418 MVKRLEEADK------GLERARNSVDKN 439
Cdd:PRK01156 721 INETLESMKKikkaigDLKRLREAFDKS 748
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
313-538 |
4.12e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 313 KSLYREMSELRSQKQAM--EVRYFDAQKEH---TEQMNQLRIELDAKLKQELASRDQIIVELRKSLRRSEDM-------- 379
Cdd:PRK02224 202 KDLHERLNGLESELAELdeEIERYEEQREQareTRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREreelaeev 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 380 --LSEQSIRLAENNSKLLTE----DSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEA 453
Cdd:PRK02224 282 rdLRERLEELEEERDDLLAEagldDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 454 RELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEqhkkvmnKQVANTikqHADFEELGGNYKEALQQISDLRETLSVT 533
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELR-------ERFGDA---PVDLGNAEDFLEELREERDELREREAEL 431
|
....*
gi 28573859 534 NAKLE 538
Cdd:PRK02224 432 EATLR 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-571 |
4.41e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 263 IQRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLcgacskqESPNKSLYREMSELRSQKQAMEvryfdaqkEHTE 342
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI-------SSELPELREELEKLEKEVKELE--------ELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 343 QMNQLRIELdAKLKQELASRDQIIVELRKSLRRSEDMLSEqsirlAENNSKLLTEdstIEVLRSEVAKLKTVKEQMVKRL 422
Cdd:PRK03918 239 EIEELEKEL-ESLEGSKRKLEEKIRELEERIEELKKEIEE-----LEEKVKELKE---LKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 423 EEADKGLERAR---NSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKE------------------KDLIIADL 481
Cdd:PRK03918 310 REIEKRLSRLEeeiNGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkkrlTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 482 KLQLQSLEQHKKVMNKQVANTIKQHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEV--QLRKEVSKMREQMV 559
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELK 469
|
330
....*....|...
gi 28573859 560 -IDQKLLNARSEL 571
Cdd:PRK03918 470 eIEEKERKLRKEL 482
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
398-589 |
4.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 398 DSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEkdlI 477
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE---R 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 478 IADLKLQLQSLEQHKKVMN-KQVANTIKQHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMRE 556
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|...
gi 28573859 557 QMvidQKLLNARSELIATLQKNEEDSRTKLDQM 589
Cdd:COG3883 172 EL---EAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
398-565 |
4.75e-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: 44.92 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 398 DSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRpdaMDAGVKEKDLi 477
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNVRNNKEY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 478 iADLKLQLQSLEQHKKVMNKQVANTIKQHadfEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMREQ 557
Cdd:COG1579 92 -EALQKEIESLKRRISDLEDEILELMERI---EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|
gi 28573859 558 MV--IDQKLL 565
Cdd:COG1579 168 LAakIPPELL 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-587 |
9.58e-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: 45.43 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 408 VAKLKTVKEQMVKRLEEADKGLER---ARNSVDKNLKHID--------YLE--GELKEArELIVhLEQRPDAMDAGVKEK 474
Cdd:TIGR02168 167 ISKYKERRKETERKLERTRENLDRledILNELERQLKSLErqaekaerYKElkAELREL-ELAL-LVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 475 DLIIADLKLQLQSLEQHKKVMNKQVANTIKQHA----DFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKE 550
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSeleeEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190
....*....|....*....|....*....|....*..
gi 28573859 551 VSKMREQMVIDQKLLNARSELIATLQKNEEDSRTKLD 587
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
349-583 |
1.63e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 349 IELDAKLKQELASR-----DQIIVELRKSLRRSEDMLSE--QSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKR 421
Cdd:COG3206 162 LEQNLELRREEARKaleflEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 422 LEEADKGLERARNSVDKNLKHidyleGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEQHKKVMNKQVAN 501
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 502 TIKQhadfeelggNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRK---EVSKMREQMvidQKLLNARSELIATLQKN 578
Cdd:COG3206 317 SLEA---------ELEALQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELY---ESLLQRLEEARLAEALT 384
|
....*
gi 28573859 579 EEDSR 583
Cdd:COG3206 385 VGNVR 389
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-473 |
2.45e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 264 QRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRYFDAQKEHTE- 342
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 343 --QMNQLRIELDaKLKQELASRDQIIVELR-----------------KSLRRSEDMLSEQSIRLAENNSKLLTE------ 397
Cdd:TIGR02169 342 erEIEEERKRRD-KLTEEYAELKEELEDLRaeleevdkefaetrdelKDYREKLEKLKREINELKRELDRLQEElqrlse 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 398 -----DSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERARNSVDK------NLKH-IDYLEGELKEARELIVHLEQRPD 465
Cdd:TIGR02169 421 eladlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKyeqelyDLKEeYDRVEKELSKLQRELAEAEAQAR 500
|
....*...
gi 28573859 466 AMDAGVKE 473
Cdd:TIGR02169 501 ASEERVRG 508
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
262-574 |
2.62e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEasekreETQKKLsNLVEEKMNLIVEEIEQLcgacSKQESPNKSLYREM----SELRSQKQAMEVRYFDAQ 337
Cdd:PRK04778 99 RFRKAKHEIN------EIESLL-DLIEEDIEQILEELQEL----LESEEKNREEVEQLkdlyRELRKSLLANRFSFGPAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 338 KEHTEQMNQLRIELD--AKLKQE---LASRDqIIVELRKSLRRSEDMLseqsirlaENNSKLLTEDSTieVLRSEVAKLK 412
Cdd:PRK04778 168 DELEKQLENLEEEFSqfVELTESgdyVEARE-ILDQLEEELAALEQIM--------EEIPELLKELQT--ELPDQLQELK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 413 TVKEQMVK---RLEEA--DKGLERARNSVDKNLKHIDYLEgeLKEARELIVHLEQRPDAM--------DAG--VKEKDLI 477
Cdd:PRK04778 237 AGYRELVEegyHLDHLdiEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLydilerevKARkyVEKNSDT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 478 IAD-----------LKLQLQSLEQHKKVMNKQVANTIKQHADFEELGGNYKEALQQI-------SDLRETLSVTNAKLEM 539
Cdd:PRK04778 315 LPDflehakeqnkeLKEEIDRVKQSYTLNESELESVRQLEKQLESLEKQYDEITERIaeqeiaySELQEELEEILKQLEE 394
|
330 340 350
....*....|....*....|....*....|....*.
gi 28573859 540 QSKLEVQLRKEVSKMR-EQMVIDQKLLNARSELIAT 574
Cdd:PRK04778 395 IEKEQEKLSEMLQGLRkDELEAREKLERYRNKLHEI 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
262-463 |
3.15e-04 |
|
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: 43.21 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEASEKREETQKKLSNLVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRYFD----AQ 337
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllraLY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 338 KehTEQMNQLRIELDAKLKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEvakLKTVKEQ 417
Cdd:COG4942 115 R--LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE---LEEERAA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 28573859 418 MVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQR 463
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
262-452 |
5.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEASEKREETQKKLSNLV--EEKMNLIVEEIEQlcgacskqespnksLYREMSELRSQKQAMEVRYFDAQKe 339
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVdlSEEAKLLLQQLSE--------------LESQLAEARAELAEAEARLAALRA- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 340 hteQMNQLRIELDAklkqelASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRS----EVAKLKTVK 415
Cdd:COG3206 248 ---QLGSGPDALPE------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAqlqqEAQRILASL 318
|
170 180 190
....*....|....*....|....*....|....*..
gi 28573859 416 EQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKE 452
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-580 |
6.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 263 IQRAKNDLEASEKREETqkklsnlVEEKMNLIVEEIEQLcgacskqESPNKSLYREMSELRSQKQAMEVRYFDAQKEHTE 342
Cdd:PRK03918 386 PEKLEKELEELEKAKEE-------IEEEISKITARIGEL-------KKEIKELKKAIEELKKAKGKCPVCGRELTEEHRK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 343 Q-MNQLRIELdAKLKQELASRDQIIVELRKSLRRSEDMLSEQSirlaennsKLLTEDSTIEVLRSEVAKLKTV-KEQMVK 420
Cdd:PRK03918 452 ElLEEYTAEL-KRIEKELKEIEEKERKLRKELRELEKVLKKES--------ELIKLKELAEQLKELEEKLKKYnLEELEK 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 421 RLEEADKGLERARN------SVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEKDL-IIADLKLQLQSLEQHKK 493
Cdd:PRK03918 523 KAEEYEKLKEKLIKlkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFeSVEELEERLKELEPFYN 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 494 VMNKQVantiKQHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKmREQMVIDQKLLNARSELIA 573
Cdd:PRK03918 603 EYLELK----DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-EEYEELREEYLELSRELAG 677
|
....*..
gi 28573859 574 TLQKNEE 580
Cdd:PRK03918 678 LRAELEE 684
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
307-588 |
8.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 307 KQESPNKSLYREMSELRSQkqamevryfdaQKEHTEQMNQLRIELDaKLKQELASRDQIIVELRKSLRRSEDMLSEQSIR 386
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQ-----------NNQLKDNIEKKQQEIN-EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 387 LAENNSKLLTEDSTIEVLRSEVAKLKTVKEQ-----MVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLE 461
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 462 QRPDAMDAGVKEKDLIIADLK-------LQLQSLEQHKKVMNKQVANTIKQHADFEE----LGGNYKEALQQISDLRETL 530
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKkenqsykQEIKNLESQINDLESKIQNQEKLNQQKDEqikkLQQEKELLEKEIERLKETI 435
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 28573859 531 SVTNAKLEMQSKLEVQLRKEVSKMREQMVIDQKLLNARSELIATLQKNEEDSRTKLDQ 588
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
262-469 |
1.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDLEAS---EKREETQKKLSNLVEEKMNLIVEEIEQlcgACSKQESPNKsLYREMSELRSQKQAMEVRYfDAQK 338
Cdd:PRK02224 497 RLERAEDLVEAEdriERLEERREDLEELIAERRETIEEKRER---AEELRERAAE-LEAEAEEKREAAAEAEEEA-EEAR 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 339 EHTEQMNQLRIELDAKLKQ---------ELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVA 409
Cdd:PRK02224 572 EEVAELNSKLAELKERIESlerirtllaAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEA 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28573859 410 KLKtvKEQMVKRLEEADKGLERARNSVDKNLKHIDYLEGELKEAREL---IVHLEQRPDAMDA 469
Cdd:PRK02224 652 RED--KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELrerREALENRVEALEA 712
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
408-588 |
1.24e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 408 VAKLKTVKEQMVKRLEEADKGLERA---RNSVDKNLKHI--------DYL----EGELKEARELIVHLEQRpdamDAGVK 472
Cdd:COG1196 167 ISKYKERKEEAERKLEATEENLERLediLGELERQLEPLerqaekaeRYRelkeELKELEAELLLLKLREL----EAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 473 EKDLIIADLKLQLQSLEQHKKVMNKQVANTIKQHAD----FEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLR 548
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEEleleLEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 28573859 549 KEVSKMREQMVIDQKLLNARSELIATLQKNEEDSRTKLDQ 588
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
270-544 |
1.79e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 270 LEASEKREETQKKLSNlveEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRYFDAQKEHTEQMNQLRI 349
Cdd:pfam12128 645 RTALKNARLDLRRLFD---EKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 350 ELDAKLKQELASRDQIIVELRKSLRRSEDMLSEQSIRlaENNSKLLTEDStievlrseVAKLKTVKEQMVKRLEEADKGL 429
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAARRSGAKAELKALETWYKR--DLASLGVDPDV--------IAKLKREIRTLERKIERIAVRR 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 430 ERARNSVD----KNLKHIDYLEGELKEARELIVHLEQrpdamdagvkEKDLIIADLKLQLQSLEQHKKVMNKQVA----- 500
Cdd:pfam12128 792 QEVLRYFDwyqeTWLQRRPRLATQLSNIERAISELQQ----------QLARLIADTKLRRAKLEMERKASEKQQVrlsen 861
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 28573859 501 -----------NTIKQHADFEELGGNYKEALQQISDLRETLSvtNAKLEMQSKLE 544
Cdd:pfam12128 862 lrglrcemsklATLKEDANSEQAQGSIGERLAQLEDLKLKRD--YLSESVKKYVE 914
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
380-554 |
1.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 380 LSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKRLEEADKglerarnsvdknlkhidylegELKEARELIVH 459
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEK---------------------ELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 460 LEQRPDAMDAGVKEKDliiADLKLQLQSLEQHKKVMNKQVANTIKQHADFEELGGNYKEALQQISDlretLSVTNAKLEM 539
Cdd:PRK12704 87 LEKRLLQKEENLDRKL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG----LTAEEAKEIL 159
|
170
....*....|....*
gi 28573859 540 QSKLEVQLRKEVSKM 554
Cdd:PRK12704 160 LEKVEEEARHEAAVL 174
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
263-479 |
2.33e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 263 IQRAKNDLEASEKREETQ-----------KKLSNLVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQamev 331
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQlqelqarlsesERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQ---- 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 332 ryfDAQKEHTEQMNQlRIELDAKLKQ---ELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEV 408
Cdd:pfam01576 472 ---DTQELLQEETRQ-KLNLSTRLRQledERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28573859 409 AKLKTVKEQMVKRLEE---ADKGLERARNSVDKNLkhiDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIA 479
Cdd:pfam01576 548 KRLQRELEALTQQLEEkaaAYDKLEKTKNRLQQEL---DDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA 618
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
262-426 |
3.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 262 RIQRAKNDL-EASEKREETQKKLSNLvEEKMNLIVEEIEQLcgacsKQESPNKSLYREMSELRSQKQAMEVRYFDAQ--- 337
Cdd:COG3206 220 QLSELESQLaEARAELAEAEARLAAL-RAQLGSGPDALPEL-----LQSPVIQQLRAQLAELEAELAELSARYTPNHpdv 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 338 KEHTEQMNQLRIELDAKLKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLltedSTIEVLRSEVAKLKTVKEQ 417
Cdd:COG3206 294 IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE----AELRRLEREVEVARELYES 369
|
....*....
gi 28573859 418 MVKRLEEAD 426
Cdd:COG3206 370 LLQRLEEAR 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
273-546 |
3.03e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 273 SEKREETQKKLSNLVEEKmnlivEEIEQLCGACSKQeSPNKSLYREMSELRSQKQAMEVRYFDAQKEHTEQMNQLRIELD 352
Cdd:PRK03918 465 EKELKEIEEKERKLRKEL-----RELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 353 AKLKQeLASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTED-STIEVLRSEVAKLKTVKEQMV------KRLEEA 425
Cdd:PRK03918 539 GEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLelkdaeKELERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 426 DKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLI-----IADLKLQLQSLEQHKKVMNKQVA 500
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLelsreLAGLRAELEELEKRREEIKKTLE 697
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 28573859 501 NTIKQHADFEELG---GNYKEALQQISDLRETLSVTNAKLEMQSKLEVQ 546
Cdd:PRK03918 698 KLKEELEEREKAKkelEKLEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
358-490 |
3.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 358 ELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERARNSVD 437
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 28573859 438 -KNLKH-IDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQSLEQ 490
Cdd:COG1579 91 yEALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
264-434 |
3.65e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 264 QRAKNDLEASEKREETQKKlsnlveEKMNLIVEEIEQLcgacsKQEspnksLYREMSELRSQKQAMEVRYfdAQKEHT-- 341
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKK------EALLEAKEEIHKL-----RNE-----FEKELRERRNELQKLEKRL--LQKEENld 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 342 ---EQMNQLRIELDAKlKQELASRDQIIVELRKSLrrsEDMLSEQSIRLaENNSKLLTEDSTIEVLRSEVAKLKTVKEQM 418
Cdd:PRK12704 100 rklELLEKREEELEKK-EKELEQKQQELEKKEEEL---EELIEEQLQEL-ERISGLTAEEAKEILLEKVEEEARHEAAVL 174
|
170 180
....*....|....*....|.
gi 28573859 419 VKRLE-----EADKgleRARN 434
Cdd:PRK12704 175 IKEIEeeakeEADK---KAKE 192
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-588 |
3.67e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 365 IIVELRKSLRRsedmLSEQSiRLAENNSKLLTEDSTIEVlrsevAKLKTVKEQMVKRLEEADKGLERARNSVDKNLKHID 444
Cdd:TIGR02168 194 ILNELERQLKS----LERQA-EKAERYKELKAELRELEL-----ALLVLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 445 YLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQLQ-------SLEQHKKVMNKQVANT----IKQHADFEELG 513
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlaNLERQLEELEAQLEELesklDELAEELAELE 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28573859 514 GNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMRE---QMVIDQKLLNARSELIATLQKNEEDSRTKLDQ 588
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
317-510 |
7.07e-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: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 317 REMSELRSQKQAMEVRYFDA----QKEHTEQMNQLRIELDAKLKQELASRD------QIIVELRKSLRRSEDMLSEQSIR 386
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRElerlQMERQQKNERVRQELEAARKVKILEEErqrkiqQQKVEMEQIRAEQEEARQREVRR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 387 LAENNSKLL--------TEDSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLERARNSVDKNLKH-----------IDYLE 447
Cdd:pfam17380 440 LEEERAREMervrleeqERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEErkqamieeerkRKLLE 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28573859 448 GELKEARELIVHLEQRPDAMDAGVKEKDL-----------IIADLKLQLQSLEQHKKVMnKQVANTIKQHADFE 510
Cdd:pfam17380 520 KEMEERQKAIYEEERRREAEEERRKQQEMeerrriqeqmrKATEERSRLEAMEREREMM-RQIVESEKARAEYE 592
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
355-485 |
8.19e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.79 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 355 LKQELASRDQIIVELRKSLRRSEDMLS---EQSIRLAENNSKLLTEDSTIEVLRSEVAKLKTVKEQMVKRLEEADKGLER 431
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSlerQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 28573859 432 ARNSVDK----NLKHIDYLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADLKLQL 485
Cdd:PRK09039 124 ELDSEKQvsarALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRL 181
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
263-547 |
9.79e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.00 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 263 IQRAKNDLEASEKR-EETQKKLSNLVEEKmNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVRYFD----AQ 337
Cdd:pfam01576 14 LQKVKERQQKAESElKELEKKHQQLCEEK-NALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEeeerSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 338 KEHTE--QMNQLRIELDAKLKQELASRDQIIVElRKSLRRSEDMLSEQSIRLAENNSKLLTEDSTIEVLRSEV------- 408
Cdd:pfam01576 93 QLQNEkkKMQQHIQDLEEQLDEEEAARQKLQLE-KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFtsnlaee 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 409 -------AKLKTVKEQMVKRLEEADKGLERARNSVDKNLKHidyLEGELKEARELIVHLEQRPDAMDAGVKEKDLIIADL 481
Cdd:pfam01576 172 eekakslSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK---LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 482 KLQLQSLEQHKKVMNKQVANTIKQHA----DFEELGGNYKEALQQISDLRE-----------TLSVTNAKLEMQSKLEVQ 546
Cdd:pfam01576 249 LARLEEETAQKNNALKKIRELEAQISelqeDLESERAARNKAEKQRRDLGEelealkteledTLDTTAAQQELRSKREQE 328
|
.
gi 28573859 547 L 547
Cdd:pfam01576 329 V 329
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
267-581 |
9.83e-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: 38.85 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 267 KNDLEASEKR-EETQKKLSNlVEEKMNLIVEEIEQLCGACSKQESPNKSLYREMSELRSQKQAMEVR---YFDAQKEHTE 342
Cdd:TIGR04523 313 KSELKNQEKKlEEIQNQISQ-NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsYKQEIKNLES 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 343 QMNQLRIELD--AKLKQELASRDQIIVELRKSLRRSEDMLSEQSIRLAENNSKLLTEDStieVLRSEVAKLKTVKEQMVK 420
Cdd:TIGR04523 392 QINDLESKIQnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS---VKELIIKNLDNTRESLET 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 421 RLEEADKGLERARNSVDKNLKHIDYLEGELKEARELIVHLEQRpdamdagVKEKDLIIADLKLQLQSLEQHKKVMNKQVA 500
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK-------VKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28573859 501 ------NTIKQHADFEELGGNYKEALQQISDLRETLSVTNAKLEMQSKLEVQLRKEVSKMREQMVIDQKLLNARSELIAT 574
Cdd:TIGR04523 542 dledelNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
....*..
gi 28573859 575 LQKNEED 581
Cdd:TIGR04523 622 AKKENEK 628
|
|
| |
