|
Name |
Accession |
Description |
Interval |
E-value |
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
82-731 |
0e+00 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 718.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 82 RAELIETKARLSQVQDQLKQNETKRRMELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLEnSYKEEARRAKAELAG 161
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKRE-AEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 162 LKLKYDETVNKLKNEKSQQEQDARDVQLCINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMSGYEELRANFE 241
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 242 KQQQSLKVADERIKELEFEIQSYTDWKQVTKVSQERLASIPEMDSELQRLRVHNKQLNKIIGDKLLLEEQVHEYKARLDK 321
Cdd:pfam05557 160 KQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 322 EEGSRAEAAALQVKLSHTERELKEWVKVAQDHCLanTLVSPVTLRSRIEQLLQGDIVHVSEKYASESESKQMRNLVRDLE 401
Cdd:pfam05557 240 EEKYREEAATLELEKEKLEQELQSWVKLAQDTGL--NLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 402 QKIRVYLKNIEDLNMSLKRHKNFKDRLQRKLRTVSRERDFYKQMVDNFDKDLTMSNAS---------VAEMTQDMQ---- 468
Cdd:pfam05557 318 QELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSpqllerieeAEDMTQKMQahne 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 469 -VRYRVDVLERTLTGYKDLCTTLDREIQAMREQEQLSDPSS--EDYENVKKELDTLRLENDRLRRRKEEQELEIMQRCLR 545
Cdd:pfam05557 398 eMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYskEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQ 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 546 QDISPPISKVVHLVDNPAAEAYESSKNMLEKLQAEIERLKRHNKKLEDANEQhlneTTSTSTGGMTMNFKELNKLRAELE 625
Cdd:pfam05557 478 GDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQ----VLRLPETTSTMNFKEVLDLRKELE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 626 SANAKLGKTKEYFMAARKEFRDVVYMLLGYRIDrVGYKSNYRVTSMYAESPDDYFSIALSESND--LALLETPYSETLQP 703
Cdd:pfam05557 554 SAELKNQRLKEVFQAKIQEFRDVCYMLTGYQID-ITTNSQYRLTSMYAEHPDDYLLFKLSGSNGstMQLLETPFSRTLEP 632
|
650 660
....*....|....*....|....*...
gi 194113994 704 ALDQQLAANNSFPPFFSSLTLDLFQRAT 731
Cdd:pfam05557 633 LIDLHLAAQKSIPAFLSALTLELFSRQT 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-597 |
1.49e-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: 55.07 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 194 ELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMSGYEELRANFEKQQQSLKVADERIKELEFEIQSYTDwkqvtKV 273
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-----SL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 274 SQERLASIPEMDselqrlrvhnkQLNKIIGDKlllEEQVHEYKARLDKEEG--SRAEAAALQVKLSHTERELKEWVKVAQ 351
Cdd:TIGR02169 750 EQEIENVKSELK-----------ELEARIEEL---EEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 352 DhclantlvspvtlrsrIEQLLQGdiVHVSEKYAsESESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHKNFKDRLQRK 431
Cdd:TIGR02169 816 E----------------IEQKLNR--LTLEKEYL-EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 432 LRTVSRERDFYKQMVDNFDKDLTmsnasvaemtqdmQVRYRVDVLERTLTGYKDLCTTLDREIQAMREQE-QLSDPSSED 510
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLR-------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELsEIEDPKGED 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 511 YENVKKELDtlrLENDRLRRRKEEQELEIMQRclrqdisppiskvvhlVDNPAAEAYESSKNMLEKLQAEIERLKRHNKK 590
Cdd:TIGR02169 944 EEIPEEELS---LEDVQAELQRVEEEIRALEP----------------VNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
....*..
gi 194113994 591 LEDANEQ 597
Cdd:TIGR02169 1005 ILERIEE 1011
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-586 |
3.79e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 80 KLRAELIETKARLSQVQDQLKQNETKR---RMELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLENSYKEEARRAK 156
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELeelRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 157 AELAGLKLKYDETVNKLKNEKSQQEQDARDVQLcINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMSGYEEL 236
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 237 RANFEKQQQSLKVADERIKELEFEIQSYTDWKQVTKVSQERLASipEMDSELQRLRVHNKQLNKIIGDKLLLEEQVHEYK 316
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 317 ARLDKEEGSRAEAAALQVKLSHTERELKEWVKVAQDhclantlvspVTLRSRIEQLLQGDI--VHVSEKYASESESKQMR 394
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL----------LAGLRGLAGAVAVLIgvEAAYEAALEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 395 NLVRDLEQ---KIRVYLK-------NIEDLNMSLKRHKNFKDRLQRKLRTVSRERDFYKQMVDNFDKDL------TMSNA 458
Cdd:COG1196 550 NIVVEDDEvaaAAIEYLKaakagraTFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLgdtllgRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 459 SVAEMTQDMQVRYRVDVLERTLTG--------------YKDLCTTLDREIQAMREQEQLSDPSSEDYENVKKELDTLRLE 524
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGeggsaggsltggsrRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194113994 525 NDRLRRRKEEQELEIMQRCLRQDISPPISK--VVHLVDNPAAEAYESSKNM-LEKLQAEIERLKR 586
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEelLEEEELLEEEALEELPEPPdLEELERELERLER 774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
77-649 |
7.37e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNETKR----------RMELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLEN 146
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLeeleskldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 147 SYKEEARRAKAELAGLKLKYDETVNKLKNEKSQQEQ--DARDVQLCINNELGDYRRQAQRAELELQSTLKE--------- 215
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERleDRRERLQQEIEELLKKLEEAELKELQAELEELEeeleelqee 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 216 -------LECIRQR--------------HDEYKARMSGYEELRANFEKQQQSLKVA----------DERIKELefeIQSY 264
Cdd:TIGR02168 456 lerleeaLEELREEleeaeqaldaaereLAQLQARLDSLERLQENLEGFSEGVKALlknqsglsgiLGVLSEL---ISVD 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 265 TDWKQ-VTKVSQERLASIPEMDSELQRLRVHNKQLNKIIGDKLLLEEQVHEYKARLDKEEGSRAEAAALQVKLSHTEREL 343
Cdd:TIGR02168 533 EGYEAaIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 344 KewVKVAQDHCLANTLVSPvTLRSRIEQL-----------LQGDIVHVSEKYASESESKQM-----RNLVRDLEQKIRVY 407
Cdd:TIGR02168 613 K--LRKALSYLLGGVLVVD-DLDNALELAkklrpgyrivtLDGDLVRPGGVITGGSAKTNSsilerRREIEELEEKIEEL 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 408 LKNIEDLNMSLKRHKNFKDRLQRKLRTVSRERDFYKQMVDNFDKDLTMSNASVAemtqdmQVRYRVDVLERTLTGYKDLC 487
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE------QLEERIAQLSKELTELEAEI 763
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 488 TTLDREI----QAMREQEQLSDPSSEDYENVKKELDTLRLENDRLRRRKEEQELEIMQRCLRQDISppiSKVVHLVDNPA 563
Cdd:TIGR02168 764 EELEERLeeaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL---ERRIAATERRL 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 564 AEAYESSKNM---LEKLQAEIERLKRHNKKLEDANEQHLNETTSTSTGGMTMNfKELNKLRAELESANAKLGKTKEYFMA 640
Cdd:TIGR02168 841 EDLEEQIEELsedIESLAAEIEELEELIEELESELEALLNERASLEEALALLR-SELEELSEELRELESKRSELRRELEE 919
|
....*....
gi 194113994 641 ARKEFRDVV 649
Cdd:TIGR02168 920 LREKLAQLE 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-517 |
9.74e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 130 KLLDLTKDMENRRGLENSYKEEARRAKAELAGLKLKYDETVNKLKNEKSQQEQdardvqlcINNELGDYRRQAQRAELEL 209
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ--------LEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 210 QSTLKELECIRQRHDEYKARMSGYEELRANFEKQQQSLK--VADERIKELEFEIQSytdwkqVTKVSQERLASIPEMDSE 287
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSK------LEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 288 LQRLRVHNKQLNKIIGDkllLEEQVHEYKARLDKEegsRAEAAALQVKLSHTERELKEwvkvaqdhclantlvspvtLRS 367
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQE---LQEQRIDLKEQIKSI---EKEIENLNGKKEELEEELEE-------------------LEA 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 368 RIEQLlqgdivhvsekyasESESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHKNFKDRLQRKLRTVSRERDFYKQMV- 446
Cdd:TIGR02169 876 ALRDL--------------ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKg 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 447 -DNFDKDLTMSNASVAEMTQDMQVRYR---------VDVLERTLTGYKDLCTTLDReiqAMREQEQLSDpSSEDYENVKK 516
Cdd:TIGR02169 942 eDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaIQEYEEVLKRLDELKEKRAK---LEEERKAILE-RIEEYEKKKR 1017
|
.
gi 194113994 517 E 517
Cdd:TIGR02169 1018 E 1018
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
77-263 |
1.12e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAE--LIETKARLSQVQDQLKQNETKR---RMELSLAESKVSALKTQCDFTSQKLLDLTKDmenrrGLENSYKEE 151
Cdd:COG3206 197 ALEEFRQKngLVDLSEEAKLLLQQLSELESQLaeaRAELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 152 ARRAKAELAGLKLKYDETVNKLKNEKSQQEQDARDVQLCINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMS 231
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA 351
|
170 180 190
....*....|....*....|....*....|..
gi 194113994 232 GYEELRANFEKQQQSLKVADERIKELEFEIQS 263
Cdd:COG3206 352 ELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-644 |
1.97e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 194 ELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMSGYEELRANFEKQQQSLKVADERIKELEFEIQSYTDWKQVTKV 273
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 274 SQERLASIPEMDSELQRLRV----HNKQLNKIIGDKLLLEEQVHEYKARLDKEEGSRAEAAALQVKLSHTER---ELKEW 346
Cdd:PRK03918 281 KVKELKELKEKAEEYIKLSEfyeeYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKrleELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 347 VKVAQDhcLANTLVSPVTLRSRIEQLLQGDIVHVSEKyaSESESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHKNFKD 426
Cdd:PRK03918 361 HELYEE--AKAKKEELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 427 RLQRKLRTVSRERDfyKQMVDNFDKDLTMSNASVAEMT-QDMQVRYRVDVLERTLTGYKDLCT--TLDREIQAMREQ--- 500
Cdd:PRK03918 437 KCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEeKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKlkk 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 501 ---EQLSDpSSEDYENVKKELDTLRLENDRLRRR-KEEQELEIMQRCLRQDISPPISKVVHLVDNPAAEAYESSKNMLEK 576
Cdd:PRK03918 515 ynlEELEK-KAEEYEKLKEKLIKLKGEIKSLKKElEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194113994 577 LQaEIERLKRHNKKLEDAnEQHLNETTststggmtmnfKELNKLRAELESANAKLGKTKEYFMAARKE 644
Cdd:PRK03918 594 LK-ELEPFYNEYLELKDA-EKELEREE-----------KELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-345 |
2.25e-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: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 80 KLRAELIETKARLSQVQDQLKQNEtkrrmeLSLAESKVSALKTQcdftsqkLLDLTKDMENRRGLENSYKEEARRAKAEL 159
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAE------LEELEAELEELEAE-------LEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 160 AGLKlkydETVNKLKNEKSQQEQDARDVQLcinnELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMSG----YEE 235
Cdd:COG1196 284 EEAQ----AEEYELLAELARLEQDIARLEE----RRRELEERLEELEEELAELEEELEELEEELEELEEELEEaeeeLEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 236 LRANFEKQQQSLKVADERIKELEFEIQSytDWKQVTKVSQERLASIPEMDSELQRLRVHNKQLNKIIGDKLLLEEQVHEY 315
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEE--LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270
....*....|....*....|....*....|
gi 194113994 316 KARLDKEEGSRAEAAALQVKLSHTERELKE 345
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-594 |
5.93e-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: 46.59 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 187 VQLCINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARMsgyEELRANFEKQQQSLKVADERIKELEFEIQSYTD 266
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL---EQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 267 wkQVTKVSQERLASIPEMDSELQRLRVHNKQLNKIIGDKLLLEEQVHEYKARLDKeegSRAEAAALQVKLSHTERELKEw 346
Cdd:TIGR02168 748 --RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA---LREALDELRAELTLLNEEAAN- 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 347 vkvaqdhclantlvspvtLRSRIEQLlqgdivhvsekyasESESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHKNFKD 426
Cdd:TIGR02168 822 ------------------LRERLESL--------------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 427 RLQRKLRTVSRERDFYKQMVDNFDKDLTMSNASVAEMTQdmqvryRVDVLERTLTGYKDLCTTLDREIQAMRE-----QE 501
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELES------KRSELRRELEELREKLAQLELRLEGLEVridnlQE 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 502 QLSDPSSEDYENVKKELDTLRLENDRLRRRKEEQELEImqrclrQDISPpiskvvhlVDNPAAEAYESSKNMLEKLQAEI 581
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI------KELGP--------VNLAAIEEYEELKERYDFLTAQK 1009
|
410
....*....|...
gi 194113994 582 ERLKRHNKKLEDA 594
Cdd:TIGR02168 1010 EDLTEAKETLEEA 1022
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
77-592 |
1.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNEtKRRMELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLENSYKEEARRAK 156
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 157 aELAGLKLKYdETVNKLKNEKSQQEQDardvqlcINNELGDYRRQAQ----------RAELELQSTLKELECIRQRHDEY 226
Cdd:PRK03918 287 -ELKEKAEEY-IKLSEFYEEYLDELRE-------IEKRLSRLEEEINgieerikeleEKEERLEELKKKLKELEKRLEEL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 227 KARMSGYEELRANF-EKQQQSLKVADERIKELEFEIQSYTDWK-QVTKVSQERLASIPEMDSELQRLRVHNKQLNKIIGD 304
Cdd:PRK03918 358 EERHELYEEAKAKKeELERLKKRLTGLTPEKLEKELEELEKAKeEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 305 -----KLLLEEQVHEYKARLDKE-EGSRAEAAALQVKLSHTERELKEWVKVAQDHCLANTLVSPVTLRSRIEQLLQGdiV 378
Cdd:PRK03918 438 cpvcgRELTEEHRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKK--Y 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 379 HVSEKYASESESKQMRNLVRDLEQKIRVYLKNIEdlnmSLKRHKNFKDRLQRKLRTVSRERdfyKQMVDNFDKDLTMSNA 458
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEEL---AELLKELEELGFESVE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 459 SVAEMTQDMQVRYR--------VDVLERTLTGYKDLCTTLDR----------EIQAMREQ--EQLSDPSSEDYENVKKEL 518
Cdd:PRK03918 589 ELEERLKELEPFYNeylelkdaEKELEREEKELKKLEEELDKafeelaetekRLEELRKEleELEKKYSEEEYEELREEY 668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194113994 519 DTLRLENDRLRRRKEEQEleimqrCLRQDISPPISKVVHLVDN--PAAEAYESSKNMLEKLQAEIERLKRHNKKLE 592
Cdd:PRK03918 669 LELSRELAGLRAELEELE------KRREEIKKTLEKLKEELEEreKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
150-352 |
1.20e-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: 45.14 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 150 EEARRAKAELAGLKLKYDETVNKLKNEKSQQEQdardvqlcINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKAR 229
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA--------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 230 MsgyEELRANFEKQQQSLK---VADERIKELEFEI---------QSYTDWKQVTKVSQERLASIPEMDSELQRLRVHNKQ 297
Cdd:COG4942 92 I---AELRAELEAQKEELAellRALYRLGRQPPLAlllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 194113994 298 LNKIIGDKLLLEEQVHEYKARLDKEEGSRAEA-AALQVKLSHTERELKEWVKVAQD 352
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLlARLEKELAELAAELAELQQEAEE 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-444 |
1.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 154 RAKAELAGLKLKYDETVNKLknEKSQQEQDARDVQLCINNELGDYrrqaQRAELELQSTLKELECIRQRHDEYKARMSGY 233
Cdd:COG4913 614 ALEAELAELEEELAEAEERL--EALEAELDALQERREALQRLAEY----SWDEIDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 234 EELRANFEKQQQSLKVADERIKELEFEI----QSYTDWKQVTKVSQERLASIPEMDSELQRLRVhNKQLnkiigDKLLLE 309
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIgrleKELEQAEEELDELQDRLEAAEDLARLELRALL-EERF-----AAALGD 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 310 EQVHEYKARLDKE-EGSRAEAAALQVKLSHTERE-LKEWVKVAQDhcLANTLVSPVTLRSRIEQLLQGDIVHVSEK---Y 384
Cdd:COG4913 762 AVERELRENLEERiDALRARLNRAEEELERAMRAfNREWPAETAD--LDADLESLPEYLALLDRLEEDGLPEYEERfkeL 839
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194113994 385 ASESESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHK-NFKDRLQRKLRTVSRE--RDFYKQ 444
Cdd:COG4913 840 LNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPfGPGRYLRLEARPRPDPevREFRQE 902
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
77-374 |
3.30e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNETKRRMELSLAESKVSALKTQCDFTSQKLLDLTKDM------------------ 138
Cdd:PRK01156 385 NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlge 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 139 ENRRGLENSYKEEARRAKAELAGLKLKYDETVNKLKNEKSQQEQ-DARDVQLCIN--NELGDYRRQAQRAELELqSTLKE 215
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINeyNKIESARADLEDIKIKI-NELKD 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 216 ----------------LECIRQRHDEYKARMS-----GYEELRANFEKQQQSLKVADERIKELEFE---IQSYTDwkqvt 271
Cdd:PRK01156 544 khdkyeeiknrykslkLEDLDSKRTSWLNALAvisliDIETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYID----- 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 272 kvsqerlASIPEMDSELQRLRVHNKQL--NKIIGDKllLEEQVHEYKARLDKEEGSRAEAAALQVKLSHTERELKEWVKV 349
Cdd:PRK01156 619 -------KSIREIENEANNLNNKYNEIqeNKILIEK--LRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKA 689
|
330 340
....*....|....*....|....*
gi 194113994 350 AQDhclanTLVSPVTLRSRIEQLLQ 374
Cdd:PRK01156 690 LDD-----AKANRARLESTIEILRT 709
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-335 |
3.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 198 YRRQAQRAEL---ELQSTLKELECIRQRHDEYKARMSGYEELRANFEKQQQSLKVADERIKELEFEIQSYTDWKQVTKVs 274
Cdd:COG4717 59 FKPQGRKPELnlkELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL- 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194113994 275 QERLASIPEmdsELQRLRVHNKQLNKIIGDKLLLEEQVHEYKARLDKEEGSRAEAAALQVK 335
Cdd:COG4717 138 EAELAELPE---RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-438 |
3.85e-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: 43.90 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 163 KLKYDETVNKLKN----EKSQQEQDARDVQLCINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARmsgyeeLRA 238
Cdd:TIGR02169 210 AERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK------IKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 239 NFEKQQQSLKvadERIKELEFEIQSYTDWKQVTKVSQERLAS-IPEMDSELQRLRVHNKQLNKIIGDKLLLEEQV-HEYK 316
Cdd:TIGR02169 284 LGEEEQLRVK---EKIGELEAEIASLERSIAEKERELEDAEErLAKLEAEIDKLLAEIEELEREIEEERKRRDKLtEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 317 ARLDKEEGSRAEAAALQVKLSHTERELKEWVKVAQD---------HCLANTLVSPVTLRSRIEQLLQGDIVHVSEKYASE 387
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 194113994 388 SESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHKNFKDRLQRKLRTVSRE 438
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-404 |
1.09e-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: 42.74 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 106 RRMELSLAESKVSALKTQCDFTSQKLLDLTKDMENrrglensYKEEARRAKAELAGLKLKYDETVNKLKNEKSQQEQDAR 185
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 186 DVQlcinnelgDYRRQAQRAELELQSTLKELECIRQRHDEYKARMsgyEELRANFEKQQQSLKVADERIKELEFEIQ--- 262
Cdd:TIGR02168 748 RIA--------QLSKELTELEAEIEELEERLEEAEEELAEAEAEI---EELEAQIEQLKEELKALREALDELRAELTlln 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 263 -SYTDWKQVTKVSQERLA----SIPEMDSELQRLRVHNKQLNKIIGDKLLLEEQVHEYKARLDKEEGSRAEA-AALQVKL 336
Cdd:TIGR02168 817 eEAANLRERLESLERRIAaterRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAlALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 337 SHTERELKEWVKVA----QDHCLANTLVSPVTLR-SRIEQLLQGDIVHVSEKY------------ASESESKQMRNLVRD 399
Cdd:TIGR02168 897 EELSEELRELESKRselrRELEELREKLAQLELRlEGLEVRIDNLQERLSEEYsltleeaealenKIEDDEEEARRRLKR 976
|
....*
gi 194113994 400 LEQKI 404
Cdd:TIGR02168 977 LENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
193-532 |
1.49e-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: 41.98 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 193 NELGDYRRQAQRAELELQSTLKELEcirqRHDEYKARMSGYEELRANFEKQQQSLKV-----ADERIKELEFEIQSYTdw 267
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLE----RLRREREKAERYQALLKEKREYEGYELLkekeaLERQKEAIERQLASLE-- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 268 KQVTKVSQERLASIPEMDSELQRLRVHNKQLNKIIGDKLL-LEEQVHEYKARLDKEEGSRAEAAALQVKLSHTERELKEW 346
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 347 vkvaqdhcLANTLVSPVTLRSRIEQLlQGDIVHVSEKYASESEskQMRNLVRDLEQ----------KIRVYLKNIEDLNM 416
Cdd:TIGR02169 331 --------IDKLLAEIEELEREIEEE-RKRRDKLTEEYAELKE--ELEDLRAELEEvdkefaetrdELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 417 SLKRHKNFKDRLQRKLRTVSRERDFYKQmvdnfdkDLTMSNASVAEMTQDMQ-VRYRVDVLERTLTGYKDLCTTLDREIQ 495
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNA-------AIAGIEAKINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350
....*....|....*....|....*....|....*..
gi 194113994 496 AMReqeqlsdpssEDYENVKKELDTLRLENDRLRRRK 532
Cdd:TIGR02169 473 DLK----------EEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
77-453 |
1.72e-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: 41.93 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNE---TKRRMELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLENSYKEEAR 153
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQqeiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 154 RAKAELAGLKLKYDETVNK-LKNEKSQQEQDARDVQLCINN-----------------ELGDYRRQAQRAELELQSTLKE 215
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKeLKSELKNQEKKLEEIQNQISQnnkiisqlneqisqlkkELTNSESENSEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 216 LECIRQRHDEYKARM----SGYEELRANFEKQQQSLKVADERIKELEFEIQsytdwkqvtkvsqerlasipEMDSELQRL 291
Cdd:TIGR04523 372 IEKLKKENQSYKQEIknleSQINDLESKIQNQEKLNQQKDEQIKKLQQEKE--------------------LLEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 292 RVHNKQLNKIIGDkllLEEQVHEYKARLDKEEGSRAEaaaLQVKLSHTERELKEwvkvaqdhclantlvspvtLRSRIEQ 371
Cdd:TIGR04523 432 KETIIKNNSEIKD---LTNQDSVKELIIKNLDNTRES---LETQLKVLSRSINK-------------------IKQNLEQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 372 LLQGDIVHVSEKYASESESKQMRNLVRDLEQKIRVYLKNIEDLNMSLKRHKNFKDRLQRKLRTVSRE--RDFYKQMVDNF 449
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEK 566
|
....
gi 194113994 450 DKDL 453
Cdd:TIGR04523 567 NKEI 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
77-291 |
2.29e-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: 40.90 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNETKRR---MELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLENSYKEEAR 153
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKallKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 154 RAKAELAGLKLKYDET--VNKLKNEKSQQE--QDARDVQLcinneLGDYRRQAQRAELELQSTLKELECIRQRHDEYKAR 229
Cdd:COG4942 101 AQKEELAELLRALYRLgrQPPLALLLSPEDflDAVRRLQY-----LKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194113994 230 MsgyEELRANFEKQQQSLKVADERIKELEFEIQsytdwkQVTKVSQERLASIPEMDSELQRL 291
Cdd:COG4942 176 L---EALLAELEEERAALEALKAERQKLLARLE------KELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
77-345 |
2.59e-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: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNETKRR-----MELSLAESKVSALKTQCDFTSQKLLDLTKDMENRRGLEnsykEE 151
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE----EQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 152 ARRAKAELAGLKLKYDETVNKLKNEKSQQEQDARDVQLCINNELGDYRRQAQRAELELQSTLKELECIRQRhdeykarms 231
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE--------- 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 232 gyEELRANFEKQQQSLKVADERI-KELEFEIQSYT-DWKQVTKVSQERLASIPEMDSELQRLRvhnkqlnkiigdklllE 309
Cdd:COG4913 765 --RELRENLEERIDALRARLNRAeEELERAMRAFNrEWPAETADLDADLESLPEYLALLDRLE----------------E 826
|
250 260 270
....*....|....*....|....*....|....*...
gi 194113994 310 EQVHEYKARLD--KEEGSRAEAAALQVKLSHTERELKE 345
Cdd:COG4913 827 DGLPEYEERFKelLNENSIEFVADLLSKLRRAIREIKE 864
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
270-631 |
3.76e-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: 40.81 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 270 VTKVSQERLASIPEMDSELQRLRvhnKQLNKIIGDKLLLEEQVHEYKARLDKEEGSRAEAAALQVKLSHTERELKEWVKV 349
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELE---EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 350 AQDHClaNTLVSPVTLRSRIEQLLQGDIVHVSEKYASESESKQMRNLVR-DLEQKIRVYLKNIEDLNMSLKRHKNFKDRL 428
Cdd:TIGR02168 738 LEAEV--EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 429 QRKLRTVSRERDFYKQMVDNFDKDLTMSNASVAEMTQDMQVryrvdvLERTLTGYKDLCTTLDREIQA----MREQEQLS 504
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES------LAAEIEELEELIEELESELEAllneRASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 505 DPSSEDYENVKKELDTLRLENDRLRRRKEEQELEIMQRCLRQD--------ISPPISKVVHLVDNPAAEAYESSKNMLEK 576
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEglevridnLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 194113994 577 LQAEIERLKRHNKKLEDANEQHLNETTSTSTGgmtmnFKELNKLRAELESANAKL 631
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEELKER-----YDFLTAQKEDLTEAKETL 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
97-548 |
3.94e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 97 DQLKQNETKRRMELSLAESKVSALKTQCDFtsqkllDLTKDMENRRGlENSYKEEARRAKAELAGLKLKYDETVNKLKNE 176
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSECQG------QMERQMAAIQG-KNESLEKVSSLTAQLESTKEMLRKVVEELTAK 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 177 KSQQEQDARDVQlcinnelgDYRRQAQRAELELQSTLKELECIRQRHDeykarmSGYEELranfekqqQSLKVADERIKE 256
Cdd:pfam15921 488 KMTLESSERTVS--------DLTASLQEKERAIEATNAEITKLRSRVD------LKLQEL--------QHLKNEGDHLRN 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 257 LEFEIQS----YTDWKQVTKVSQERLASIPEMDSELQR----LRVHNKQLNKIIGDKLLleeQVHEYKARLDKEEgsrAE 328
Cdd:pfam15921 546 VQTECEAlklqMAEKDKVIEILRQQIENMTQLVGQHGRtagaMQVEKAQLEKEINDRRL---ELQEFKILKDKKD---AK 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 329 AAALQVKLSHTERELKEWVKVAQDHclantLVSPVTLRSRIEQLLqgdivhvsekyaseSESKQMRNLVRDLEQKIRVYL 408
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSER-----LRAVKDIKQERDQLL--------------NEVKTSRNELNSLSEDYEVLK 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 409 KNIEDLNMSLKRHKNfkdRLQRKLRTVSRERDFYKQMVDNFD-KDLTMSNASVAEMTQDMQVRYRVDVLERTLTGYKDLC 487
Cdd:pfam15921 681 RNFRNKSEEMETTTN---KLKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAM 757
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 488 TTLDREIQAMREQ-----EQLSDPSSEDyENVKKELDTLRLENDRLRRRKEEQELEIMQRCLR----QDI 548
Cdd:pfam15921 758 TNANKEKHFLKEEknklsQELSTVATEK-NKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaecQDI 826
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
81-546 |
5.98e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.95 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 81 LRAELIETKARLSQVQDQLKQNETKRRMELSLAESKVSALKTQCDFTSQKLLDLTKDMENrrglensyKEEARRAKAELA 160
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA--------QEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 161 GLKLKYDETVNKLKNEKSQQEQDARDVQ----LCINNELGDYRRQAQRAELELQSTLKELECIRQRhdeykarmsgyeel 236
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK-------------- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 237 RANFEKQQQSLKVADERIKELEFEIQSYTDWkqvTKVSQERLASIPEMDSELQRLRVHNKQlnkiigdKLLLEEQVHEYK 316
Cdd:TIGR00618 330 RAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA---HEVATSIREISCQQHTLTQHIHTLQQQ-------KTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 317 ARLDKEEGSRAEAAALQVKlshtERELKEWVKVAQDHCLANtlvspvtlRSRIEQLLQGDIVHVSEKYASESESKQMRNL 396
Cdd:TIGR00618 400 KELDILQREQATIDTRTSA----FRDLQGQLAHAKKQQELQ--------QRYAELCAAAITCTAQCEKLEKIHLQESAQS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 397 VRDLEQKirvyLKNIEDLNMSLKRHKnfKDRLQRKLRTVSRERDFYKQMVdNFDKDLTMSNASVAEMTQDMQVRYRVDVL 476
Cdd:TIGR00618 468 LKEREQQ----LQTKEQIHLQETRKK--AVVLARLLELQEEPCPLCGSCI-HPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194113994 477 ERTLTGYKDLCTTLDREIQAMREQEQLSDPS----SEDYENVKKELDTLRLENDRLRRRKEEQ-ELEIMQRCLRQ 546
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsilTQCDNRSKEDIPNLQNITVRLQDLTEKLsEAEDMLACEQH 615
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
425-647 |
7.42e-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: 39.65 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 425 KDRLQRKLRTVSRERDFYKQMVDNFDKDLTMSNASVAE-MTQDMQVRYRVDVLERTLTGYKDLCTTLDREIQAMREQEQL 503
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEElRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 504 SDPS----SEDYENVKKELDTLRLENDRLRRRKEEQELEIMQrcLRQDISPPISKVVHLVD---------NPAAEAYESS 570
Cdd:TIGR02168 314 LERQleelEAQLEELESKLDELAEELAELEEKLEELKEELES--LEAELEELEAELEELESrleeleeqlETLRSKVAQL 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194113994 571 KNMLEKLQAEIERLKRHNKKLEDANEQHLNETTSTSTGGMTMNFKELNKLRAELESANAKLGKTKEYFMAARKEFRD 647
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
77-277 |
7.90e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 77 KMNKLRAELIETKARLSQVQDQLKQNETKRRmELSLAESKVSALKTQCDFTSQKLL--DLTKDMENRRGLENSYKEEARR 154
Cdd:COG1340 72 KVKELKEERDELNEKLNELREELDELRKELA-ELNKAGGSIDKLRKEIERLEWRQQteVLSPEEEKELVEKIKELEKELE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194113994 155 AKAELAGLKLKYDETVNKLKNEKSQQEQdardvqlcINNELGDYRRQAQRAELELQSTLKELECIRQRHDEYKARmsgYE 234
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEE--------IHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE---IV 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 194113994 235 ELRANFEKQQQSLKVADERIKELEFEIQSYTDWKQVTKVSQER 277
Cdd:COG1340 220 EAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| |
