|
Name |
Accession |
Description |
Interval |
E-value |
| Dynactin |
pfam12455 |
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ... |
507-785 |
5.56e-93 |
|
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 amino acids in length. The family is found in association with pfam01302. There is a single completely conserved residue E that may be functionally important. Dynactin has been associated with Dynein, a kinesin protein which is involved in organelle transport, mitotic spindle assembly and chromosome segregation. Dynactin anchors Dynein to specific subcellular structures.
Pssm-ID: 463591 Cd Length: 287 Bit Score: 300.30 E-value: 5.56e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 507 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 581
Cdd:pfam12455 1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 582 DHDCVLVLLLMPRLICKAELIRKQAQEKFELSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 661
Cdd:pfam12455 80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 662 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIKFTQSALDCMS 741
Cdd:pfam12455 156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 205277392 742 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDIRQFCKKIRRRM 785
Cdd:pfam12455 236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
29-94 |
1.01e-30 |
|
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 115.19 E-value: 1.01e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 29 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 94
Cdd:pfam01302 1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
29-95 |
8.43e-29 |
|
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 214997 [Multi-domain] Cd Length: 68 Bit Score: 109.98 E-value: 8.43e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 29 VGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEA-KGKNDGTVQGRKYFTCDEGHGIFVRQSQIQ 95
Cdd:smart01052 1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-520 |
5.15e-22 |
|
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: 103.21 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLR--LKRAED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 271
Cdd:TIGR02168 170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 344
Cdd:TIGR02168 250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 345 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 420
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 421 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 500
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340
....*....|....*....|
gi 205277392 501 RQLTAHLQDVNRELTNQQEA 520
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-495 |
9.14e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 9.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 280
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 281 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDL 360
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 361 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnlNLEEKVRELRET 440
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 441 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ 495
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-520 |
2.02e-21 |
|
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: 101.29 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 280
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 281 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEekgsdgaASSYQLKQLEEQNARLKDALVRMRDL 360
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-------ALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 361 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAL----GAEEMVEMLTDRNLNLEEKVRE 436
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 437 LRETVGDLE-AMNEMNDEL-QENARETELELREQ-------------LDMAGARVREAQKRVEAAQETVAD--------- 492
Cdd:TIGR02168 906 LESKRSELRrELEELREKLaQLELRLEGLEVRIDnlqerlseeysltLEEAEALENKIEDDEEEARRRLKRlenkikelg 985
|
330 340 350
....*....|....*....|....*....|....*..
gi 205277392 493 ---------YQQTIKKYRQLTAHLQDVNRELTNQQEA 520
Cdd:TIGR02168 986 pvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-527 |
9.21e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 205 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQA--------DLQRRLKEARKEAKEALEAKERYMEE 276
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAellllklrELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 277 MADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVR 356
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE-------RLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 357 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemvEMLTDRNLNLEEKVRE 436
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA---AELAAQLEELEEAEEA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 437 LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 516
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
330
....*....|.
gi 205277392 517 QQEASVERQQQ 527
Cdd:COG1196 492 RLLLLLEAEAD 502
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
201-468 |
8.95e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.88 E-value: 8.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQewksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 280
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 281 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK------AEIEEKGSDGAASSYQLKQLEEQNARLKDAL 354
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 355 vrmrdlssSEKQEHVKlqKLMEKKNQE-LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK 433
Cdd:PRK02224 630 --------AEKRERKR--ELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
250 260 270
....*....|....*....|....*....|....*
gi 205277392 434 VRELRETVGDLEAMNEMNDELQENARETELELREQ 468
Cdd:PRK02224 700 REALENRVEALEALYDEAEELESMYGDLRAELRQR 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-527 |
1.01e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 277
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 ADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 357
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 358 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNLNLEEKVREL 437
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 438 RETVGDLEAMNEMNDELQENARETELELREQLDMAG--ARVREAQKRVEAA--QETVADYQQTIKKYRQ-----LTAHLQ 508
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRglAGAVAVLIGVEAAYEAaleaaLAAALQ 549
|
330
....*....|....*....
gi 205277392 509 DVNRELTNQQEASVERQQQ 527
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKA 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-491 |
3.10e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 274
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 354
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 355 VRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKV 434
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 205277392 435 RELRETvgDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 491
Cdd:COG1196 490 AARLLL--LLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
195-484 |
3.92e-19 |
|
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: 93.98 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR----KEAKEALEAK 270
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 271 ERYMEEMADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 349
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 350 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnln 429
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----------- 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 430 LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 484
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
195-527 |
1.33e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.03 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAE--DKAKLKELEKhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 272
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDllAEAGLDDADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 YMEEMADTADaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 352
Cdd:PRK02224 347 LREDADDLEE-------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 353 ALVRMRdlsSSEKQEHVKLQKLMEK--KNQEL----------------------EVVRQQRERLQEELSQAESTIDELKE 408
Cdd:PRK02224 420 ERDELR---EREAELEATLRTARERveEAEALleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 409 QVDAA---LGAEEMVEMLTDRNLNLEEKVRELRETVGD----LEAMNEMNDELQENARETE---LELREQLDMAGARV-- 476
Cdd:PRK02224 497 RLERAedlVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKReaaAEAEEEAEEAREEVae 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 477 -----------REAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 527
Cdd:PRK02224 577 lnsklaelkerIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-488 |
1.75e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRAQV-----RDLEEKLETLRLKRAEDKAKLKELEKHKIQLeqvqewkskmqeqqadlqrrlKEARKEAKEALEAKER 272
Cdd:PRK02224 190 DQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQA---------------------RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 352
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 353 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemltdrnlnLEE 432
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-----------------LEE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 433 KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQE 488
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-514 |
2.10e-18 |
|
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: 91.66 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQvqewksKMQEQQADLQRrLKEARKEAKEALEAKErym 274
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA------EIEELEAQIEQ-LKEELKALREALDELR--- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 354
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 355 VRMRD-LSSSEKQEHVKLQKLMEKKnQELEVVRQQRERLQEELSQAESTIDELKEQV-----DAALGAEEMVEMLTDRNL 428
Cdd:TIGR02168 890 ALLRSeLEELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 429 NLEEKVRELRETVGDLEAMNEMN-DELQE-NARETELEL-REQLDMAGARVREAQKRVEAaqETVADYQQTIKKYRQlta 505
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAiEEYEElKERYDFLTAqKEDLTEAKETLEEAIEEIDR--EARERFKDTFDQVNE--- 1043
|
....*....
gi 205277392 506 HLQDVNREL 514
Cdd:TIGR02168 1044 NFQRVFPKL 1052
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
196-526 |
8.82e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 86.25 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLR----LKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 271
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 RYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-----------------KGSDGA 334
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 335 AS-----------SYQLKQLEEQNARLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRERLQEELSQAES-- 401
Cdd:PRK02224 468 ETieedrerveelEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELIAERRETIEEKRERAEElr 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 402 --------------------------------TIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETvgdLEAMNE 449
Cdd:PRK02224 544 eraaeleaeaeekreaaaeaeeeaeeareevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK---REALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 450 MNDELQE---NARETELELREQLDmaGARVREAQ---KRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEASV 522
Cdd:PRK02224 621 LNDERRErlaEKRERKRELEAEFD--EARIEEARedkERAEEYLEQVEEKLDELREERdDLQAEIGAVENELEELEELRE 698
|
....
gi 205277392 523 ERQQ 526
Cdd:PRK02224 699 RREA 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
234-557 |
1.61e-16 |
|
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: 85.50 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 234 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALeakerymeemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVD 313
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS--------------QELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 314 ELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALvrmRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQ 393
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 394 eELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEA-MNEMNDELQE-NARETELE-----LR 466
Cdd:TIGR02169 816 -EIEQKLNRLTLEKEY------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEElEAALRDLEsrlgdLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 467 EQLDMAGARVREAQKRVEAAQETVADYQQTIKkyrQLTAHLQDVNRELTnQQEASVERQQQPPPETFDFKikfaETKAHA 546
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLS---ELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE----DVQAEL 960
|
330
....*....|.
gi 205277392 547 KAIEMELRQME 557
Cdd:TIGR02169 961 QRVEEEIRALE 971
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-527 |
2.36e-16 |
|
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: 84.73 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKR-AEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEakeaLEAKER 272
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKReYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 YMEEMADTADAI---EMATLDKEMAEERAE--SLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQN 347
Cdd:TIGR02169 273 LLEELNKKIKDLgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE---REIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 348 ARlKDALvrMRDLSSSEKQEHVKLQKLME--KKNQELevvRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTD 425
Cdd:TIGR02169 350 KR-RDKL--TEEYAELKEELEDLRAELEEvdKEFAET---RDELKDYREKLEKLKREINELKRELDR----------LQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 426 RNLNLEEKVRELRETVGDLEamnemndelqenARETELElrEQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQLTA 505
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIE------------AKINELE--EEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE 476
|
330 340
....*....|....*....|....
gi 205277392 506 HLQDVNRELTNQQE--ASVERQQQ 527
Cdd:TIGR02169 477 EYDRVEKELSKLQRelAEAEAQAR 500
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
27-405 |
2.90e-15 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 80.88 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 27 LRVGSRVEVIGKghRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRqsqiqvfedgadttsp 106
Cdd:COG5244 4 LSVNDRVLLGDK--FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIR---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 107 etPDSSAskVLKREGTDTTAKTsklptrpASTGVAGASSSLGPSGSASAGELSSSEPStpaqtpLAAPIIPTPVLTSPGA 186
Cdd:COG5244 66 --PDDDS--LLNGNAAYEKIKG-------GLVCESKGMDKDGEIKQENHEDRIHFEES------KIRRLEETIEALKSTE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 187 VPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 266
Cdd:COG5244 129 KEEIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMVELVSDISETLNRNGSIQRSS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 267 LEAKERymeemadtadaiematldkemaeeraeslqqevealKERVDELTTDLEILKAEIEEKGsdgaassyqlKQLEeq 346
Cdd:COG5244 208 VRECER------------------------------------SNIHDVLFLVNGILDGVIDELN----------GELE-- 239
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 347 naRLKDALVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAESTIDE 405
Cdd:COG5244 240 --RLRRQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYE 297
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-437 |
7.04e-15 |
|
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: 80.10 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQrRLKEARKEAKEALEAKERYM 274
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELE------AQLEELESKLDELAEELA-ELEEKLEELKEELESLEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 354
Cdd:TIGR02168 361 EELEA----------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 355 VRMRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKV 434
Cdd:TIGR02168 431 EEAELKELQAELE--ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
...
gi 205277392 435 REL 437
Cdd:TIGR02168 509 KAL 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-557 |
2.16e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRA-QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQqadlQRRLKEARKEAKEALEAKERY 273
Cdd:PTZ00121 1273 KAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEI-LKAEIEEKGSDgaassyQLKQLEEQNARLKD 352
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKAD------ELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 353 ALVRMRDLsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEEMVEMLTDRNLNL 430
Cdd:PTZ00121 1423 AKKKAEEK---KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 431 EE--KVRELRETVGDLEAMNEMN--DELQ--ENARETElELREQLDMAGA-RVREAQKRVEAAQETVADYQQTIKKYRQL 503
Cdd:PTZ00121 1500 DEakKAAEAKKKADEAKKAEEAKkaDEAKkaEEAKKAD-EAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 205277392 504 TAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 557
Cdd:PTZ00121 1579 ALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
194-499 |
2.81e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRlKRAEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 273
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAE-EAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnaRLKDA 353
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--KKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 354 LVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAES----TIDELKEQVDAALGAEEMVEMLTDRNL 428
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 429 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 499
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-560 |
9.87e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQV--RDLEE--KLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQE-QQADlqrRLKEARKEAKEALEA 269
Cdd:PTZ00121 1373 KEEAKKKADAakKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkKKAD---EAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 270 KE-----RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQ 342
Cdd:PTZ00121 1450 KKkaeeaKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 343 LEEqnARLKDALVRMRDLSSSE---KQEHVK----LQKLMEKKNQELEvvRQQRERLQEELSQAEST---------IDEL 406
Cdd:PTZ00121 1530 AEE--AKKADEAKKAEEKKKADelkKAEELKkaeeKKKAEEAKKAEED--KNMALRKAEEAKKAEEArieevmklyEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 407 KEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLdmagARVREAQKRveAA 486
Cdd:PTZ00121 1606 KMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE----AKKAEEDKK--KA 1677
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 487 QETVADYQQTIKKYRQLTAHLQDVNR--ELTNQQEASVERQQQPPPETFDFKIKFAETKAHAkaiEMELRQMEVAQ 560
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA---EEDKKKAEEAK 1750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-560 |
1.67e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQ-VRDLEEKLETLRLKRAEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:PTZ00121 1171 KAEDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 349
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 350 LKDALVRMRDlsSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemLTDRNLN 429
Cdd:PTZ00121 1330 KADAAKKKAE--EAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 430 LEEKVRELRETvgdlEAMNEMNDELQENAREtelelREQLDMAGARVREAQKRVEAAQEtvADYQQTIKKYRQLTAHLQD 509
Cdd:PTZ00121 1403 DKKKADELKKA----AAAKKKADEAKKKAEE-----KKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 205277392 510 VNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQ 560
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-563 |
2.56e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKE--- 271
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKkae 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 --RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEAlKERVDELTTDLEILKA--EIEEKGSDGAASSYQLKQLEE 345
Cdd:PTZ00121 1429 ekKKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEE-AKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAE 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 346 QNARLKDAlvrmrdLSSSEKQEHVKLQKLMEKKNQElEVVRQQRERLQEELSQAESTID-ELKEQVDAALGAEEMVEMLT 424
Cdd:PTZ00121 1508 AKKKADEA------KKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKKAEELKKaEEKKKAEEAKKAEEDKNMAL 1580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 425 DRNLNL----EEKVRELRETVGDLEAMNEMNDELQENARETELELR---------EQLDMAGA-RVREAQKRVEAAQETV 490
Cdd:PTZ00121 1581 RKAEEAkkaeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaeeekkkvEQLKKKEAeEKKKAEELKKAEEENK 1660
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277392 491 ADYQQTIKKYRQLTAHLQDVNRELTNQQEA--SVERQQQPPPETFDFKIKFAETKAHAKAI--EMELRQMEVAQANR 563
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELkkAEEENKIKAEEAKK 1737
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-484 |
3.24e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLrlkrAEDKAKLKELEKHKIQLEqvqEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSL----KKELEKLEELKKKLAELE---KKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqlkqleeqnarlkda 353
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK---------------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 354 lvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEK 433
Cdd:PRK03918 655 --------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE----KALER 722
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 205277392 434 VRELRETVGDLEAMNEMN--DELQENARETELELREQlDMAGARVREAQKRVE 484
Cdd:PRK03918 723 VEELREKVKKYKALLKERalSKVGEIASEIFEELTEG-KYSGVRVKAEENKVK 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
194-561 |
4.60e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKI----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 269
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 270 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 349
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 350 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-QQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNL 428
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 429 NLEE---------KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 499
Cdd:COG1196 555 DDEVaaaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 500 YRQLTAHLQDVNRELTNQQEASVERQQqpppETFDFKIKFAETKAHAKAIEMELRQMEVAQA 561
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGS----LTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
195-519 |
5.01e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLR-----LKRAEDKA-----------KLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE 258
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKkaieeLKKAKGKCpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 259 ARKEAKEalEAKERYMEEMADTADAIE--MATLDKEMAEERAEslqqEVEALKERVDELTTDLEILKAEIEEKG---SDG 333
Cdd:PRK03918 485 LEKVLKK--ESELIKLKELAEQLKELEekLKKYNLEELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEKLEelkKKL 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 334 AASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAA 413
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 414 LGAEEMvemltdrnlnLEEKVRELREtvgdleamnEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADY 493
Cdd:PRK03918 639 EKRLEE----------LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
330 340
....*....|....*....|....*.
gi 205277392 494 QQTIKKYRQLTAHLQDVNRELTNQQE 519
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEE 725
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-568 |
5.28e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKmQEQQADLQRRLKEARKEA---KEALEAKERYMEE 276
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLeelRELEEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 277 MADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE------EKGSDGAASSYQLKQLEEQNAR 349
Cdd:COG4717 172 LAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEeleeelEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 350 LKDA----LVRMRDLSSSEKQEHVK---------LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGA 416
Cdd:COG4717 252 LLIAaallALLGLGGSLLSLILTIAgvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL-AALGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 417 EEMVEmltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELElrEQLDMAGARVREA-QKRVEAAQEtvadyqq 495
Cdd:COG4717 331 PPDLS-----PEELLELLDRIEELQELLREAEELEEELQLEELEQEIA--ALLAEAGVEDEEElRAALEQAEE------- 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 496 tikkYRQLTAHLQDVNRELTNQQEASVERQQQPPPEtfDFKIKFAETKAHAKAIEMELRQM--EVAQANRHMSLL 568
Cdd:COG4717 397 ----YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELreELAELEAELEQL 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
181-413 |
1.38e-12 |
|
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: 70.95 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 181 LTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR 260
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 261 KEAKEALEAKERYMEEMADTADAIEMATLDKEM-----------AEERAESLQQEVEALKERVDELTTDLEILKAEIEEK 329
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 330 gsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ 409
Cdd:COG4942 170 -------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 205277392 410 VDAA 413
Cdd:COG4942 243 TPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
195-560 |
1.73e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSK-------MQEQQADLQRRLKEARKEAKEaL 267
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegskrkLEEKIRELEERIEELKKEIEE-L 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 268 EAKERYMEEMADTADaiEMATLDKEMA---------EERAESLQQEVEALKERVDELTTDLEILKaEIEEKGSDGAASSY 338
Cdd:PRK03918 279 EEKVKELKELKEKAE--EYIKLSEFYEeyldelreiEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 339 QLKQLEEQNARLKDALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGA- 416
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAk 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 417 -----------------------------EEMVEMLTDRN-------------LNLEEKVRELRETVGDLEAMNEM---- 450
Cdd:PRK03918 436 gkcpvcgrelteehrkelleeytaelkriEKELKEIEEKErklrkelrelekvLKKESELIKLKELAEQLKELEEKlkky 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 451 -NDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP 529
Cdd:PRK03918 516 nLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430
....*....|....*....|....*....|.
gi 205277392 530 PETFDFKIKFAETKAHAKAIEMELRQMEVAQ 560
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-520 |
2.94e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTAD 282
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 AIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE--IEEKG------------------------------ 330
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerLKEARlllliaaallallglggsllsliltiagvl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 331 -------SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKL-MEKKNQELEVVRQQRERLQEELSQAEST 402
Cdd:COG4717 280 flvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEEL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 403 IDELK----EQVDAALGAEEMVEMLTD--RNLNLEEKVRELRETVGDLEAM--NEMNDELQENARETELELREQLDMAGA 474
Cdd:COG4717 360 EEELQleelEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEE 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 205277392 475 RVREAQKRVEAAQETVADYQQTIKK------YRQLTAHLQDVNRELTNQQEA 520
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQleedgeLAELLQELEELKAELRELAEE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
203-484 |
5.47e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKERYMEEMAD 279
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 TADAIEMAtldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqlkqLEEQNARLKDAlvrmrd 359
Cdd:PRK03918 236 LKEEIEEL-------EKELESLEGSKRKLEEKIRELEERIEELKKEIEE--------------LEEKVKELKEL------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 360 lsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRE 439
Cdd:PRK03918 289 --KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 440 TVGDLEAMNEMNDELQ-----------ENARETELELREQLDMAGARVREAQKRVE 484
Cdd:PRK03918 367 AKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
290-530 |
2.52e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 68.12 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 290 DKEMAEERAESLQQE--VEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQE 367
Cdd:COG3206 146 DPELAAAVANALAEAylEQNLELRREEARKALEFLEEQLPE----------LRKELEEAEAALEEFRQKNGLVDLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 368 HVklqklmekkNQELEVVRQQRERLQEELSQAESTIDELKEQVD------AALGAEEMVEMLTDRNLNLEEKVRELRETV 441
Cdd:COG3206 216 LL---------LQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalPELLQSPVIQQLRAQLAELEAELAELSARY 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 442 GD--------LEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLqDVNRE 513
Cdd:COG3206 287 TPnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV-EVARE 365
|
250 260
....*....|....*....|..
gi 205277392 514 -----LTNQQEASVERQQQPPP 530
Cdd:COG3206 366 lyeslLQRLEEARLAEALTVGN 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-470 |
5.39e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 222 KAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARkEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAES 300
Cdd:COG4913 609 RAKLAALEA---ELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAErEIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 301 lqQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvkLQKLMEKKNQ 380
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 381 ElEVVRQQRERLQEELSQAESTIDELKEQVDAAL-------------------GAEEMVEMLTD-RNLNLEEKVRELRET 440
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadleSLPEYLALLDRlEEDGLPEYEERFKEL 839
|
250 260 270
....*....|....*....|....*....|
gi 205277392 441 VgdLEAMNEMNDELQENARETELELREQLD 470
Cdd:COG4913 840 L--NENSIEFVADLLSKLRRAIREIKERID 867
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-567 |
5.77e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQ-VRDLEE--KLETLRLKR-AEDKAKLKELEKHKI-QLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEA 266
Cdd:PTZ00121 1238 DAEEAKKAEeERNNEEirKFEEARMAHfARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 267 LEAKERyMEEMADTADAI----EMATLDKEMAEERAESLQQEVEALKER--VDELTTDLEILKAEIEEKGSDGAASSYQL 340
Cdd:PTZ00121 1318 DEAKKK-AEEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKaeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 341 KQLEEQNARlkdalvrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEE 418
Cdd:PTZ00121 1397 KKKAEEDKK---------------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 419 MVEMLTDRnlnleEKVRELRETVGDLEAMNEMNDELQENARETElELREQLDmAGARVREAQKRVEAAQETVADYQQTIK 498
Cdd:PTZ00121 1462 AKKKAEEA-----KKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 499 KYRQL-TAHLQDVNRELTNQQEASVERQQQPPPEtfdfKIKFAETKAHAKAIEMELRQMEVAQANRHMSL 567
Cdd:PTZ00121 1535 KADEAkKAEEKKKADELKKAEELKKAEEKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-484 |
6.55e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARK--EAKEALEAK 270
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKaeEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 271 ERYMEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLE--ILKAEIEEKGSDGAASSYQLKQLEEQNA 348
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAKKAEEdeKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 349 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgAEEMVEMLTDRNL 428
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI-EEELDEEDEKRRM 1794
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 429 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 484
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
203-525 |
1.09e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 64.16 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL-EQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADta 281
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELnEELKELAEKRDE----LNAQVKELREEAQELREKRDELNEKVKE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 282 daiematldkemaeeraesLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassYQLKQLEEQNARLKDALVRmRDLS 361
Cdd:COG1340 76 -------------------LKEERDELNEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEWRQQT-EVLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 362 SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQaestIDELKEQVDAalgaeemvemltdrnlnLEEKVRELRetv 441
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAE----LKELRKEAEE-----------------IHKKIKELA--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 442 gdlEAMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEA 520
Cdd:COG1340 188 ---EEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRkELKKLRKKQRALKREKEKE 263
|
....*
gi 205277392 521 SVERQ 525
Cdd:COG1340 264 ELEEK 268
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
205-557 |
1.37e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.15 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 205 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvqewKSKMQEQQAdlQRRLKEarKEAKEALEAKERYMEEMADTADAI 284
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKA--LEYYQL--KEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 285 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSE 364
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----LLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 365 KQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDL 444
Cdd:pfam02463 316 LKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 445 EAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 524
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350
....*....|....*....|....*....|...
gi 205277392 525 QQQpppETFDFKIKFAETKAHAKAIEMELRQME 557
Cdd:pfam02463 473 LLK---ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
200-525 |
1.87e-10 |
|
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: 65.43 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 279
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRD 359
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-------EIKDLTNQDSVKELIIKNLDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 360 LSSSEKQ-------EHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeEMVEMLTDRNLNLEE 432
Cdd:TIGR04523 462 TRESLETqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKES 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 433 KVRELRETVgdleamNEMNDELQENARETE-LELREQLDmagaRVREAQKRVEAAQETVadyQQTIKKYrqlTAHLQDVN 511
Cdd:TIGR04523 539 KISDLEDEL------NKDDFELKKENLEKEiDEKNKEIE----ELKQTQKSLKKKQEEK---QELIDQK---EKEKKDLI 602
|
330
....*....|....*.
gi 205277392 512 RELTN--QQEASVERQ 525
Cdd:TIGR04523 603 KEIEEkeKKISSLEKE 618
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-500 |
3.46e-10 |
|
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: 64.66 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 192 SPSKEEEGLRAQVRDLEEKLEtlrlkRAEDKAKLKElekhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKe 271
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQ-----NQEKLNQQKD-----EQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQ- 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 rymeemaDTADAIEMATLDKemaeeRAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLK 351
Cdd:TIGR04523 449 -------DSVKELIIKNLDN-----TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 352 D----ALVRMRDLSSSEKQEHVKLQKL---MEKKNQELevvrqQRERLQEELSQAESTIDELKEQVDAALGA----EEMV 420
Cdd:TIGR04523 517 KkissLKEKIEKLESEKKEKESKISDLedeLNKDDFEL-----KKENLEKEIDEKNKEIEELKQTQKSLKKKqeekQELI 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 421 EMLTDRNLNL-------EEKVRELRETVGDLEAMNE------MNDELQENARETELEL-REQLDMAGARVREAQKRVEAA 486
Cdd:TIGR04523 592 DQKEKEKKDLikeieekEKKISSLEKELEKAKKENEklssiiKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKES 671
|
330
....*....|....
gi 205277392 487 QETVADYQQTIKKY 500
Cdd:TIGR04523 672 KTKIDDIIELMKDW 685
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
195-463 |
4.51e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 63.70 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKakLKELEKhKI-----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 269
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQE-RIdqlydILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 270 KERYMEEMADTADAIEmatldkemaeeRAESLQQEVEALKERVDELTTDLE-------ILKAEIEEkgsdgaaSSYQLKQ 342
Cdd:PRK04778 333 IDRVKQSYTLNESELE-----------SVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEE-------ILKQLEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 343 LEEQNARLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaE 417
Cdd:PRK04778 395 IEKEQEKLSEMLQGLR------KDELEAREKLERYRNKLHEIKRYlEKSNLpglpEDYLEMFFEVSDEI----------E 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 205277392 418 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 463
Cdd:PRK04778 459 ALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
196-1015 |
9.70e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 9.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEqqadlqRRLKEARKEAKEALEAKERYME 275
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKRE------YEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELT--------TDLEILKAEIEEKGSDGAASSYQLKQLEEQN 347
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 348 ARLK----DALVRMRDLSSSEKQEHVKLQKLMEkknqELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEML 423
Cdd:TIGR02169 325 AKLEaeidKLLAEIEELEREIEEERKRRDKLTE----EYAELKEELEDLRAELEEVDKEFAETRDELKDY---REKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 424 TDRNLNLEEKVRELRETVGDL-EAMNEMNDELqENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQ 502
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLsEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 503 LTAHLQDVNRELTNQQE--ASVE-RQQQPPPETFDFKIKFAETKAHAKAIEMELRQM-----------EVAQANRHMSLL 568
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRelAEAEaQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryataiEVAAGNRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 569 TafmpdsflrpggDHDCV---LVLLLMPRLICKAELI--RKQAQEKFELSencseRPGLRGAAGEQLS-------FAAGL 636
Cdd:TIGR02169 554 V------------EDDAVakeAIELLKRRKAGRATFLplNKMRDERRDLS-----ILSEDGVIGFAVDlvefdpkYEPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 637 VYSL-------SLLQATLHRYEHALSQCSVDVYKKVGSlypeMSAHERSLDFLIellhKDQLDETVNVEPLTKAIKYYQH 709
Cdd:TIGR02169 617 KYVFgdtlvveDIEAARRLMGKYRMVTLEGELFEKSGA----MTGGSRAPRGGI----LFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 710 LYSIHLAEQPEdctmqLADHIKFTQSALDCMSVEVGRLRAflqggqeatDIALLLRDLETSCSDIRQFCKKIRrrmpgtd 789
Cdd:TIGR02169 689 ELSSLQSELRR-----IENRLDELSQELSDASRKIGEIEK---------EIEQLEQEEEKLKERLEELEEDLS------- 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 790 apgipaalafgpQVSDTLLDCRKHLTWVVAVLQEvaaaaaqliaplaeneglLVAALEELAfKASEQIYGTPSSSPYECL 869
Cdd:TIGR02169 748 ------------SLEQEIENVKSELKELEARIEE------------------LEEDLHKLE-EALNDLEARLSHSRIPEI 796
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 870 RQSCNILISTMNKLATAMQEGEYDAERppskpppVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEA 949
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNR-------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 950 NVRLSLLEKKLDSAAKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQ 1015
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
203-538 |
1.02e-09 |
|
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: 62.83 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLkRAEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADL---QRRLKEARKEAKE--ALEAKERYMEEM 277
Cdd:pfam17380 288 QQQEKFEKMEQERL-RQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIyaeQERMAMERERELEriRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 ADTADAIEMATLdKEMaeeraESLQQEVEALKERVdelttdleilKAEIEekgsdgAASSYQLKQlEEQNARLKDALVRM 357
Cdd:pfam17380 366 RQEEIAMEISRM-REL-----ERLQMERQQKNERV----------RQELE------AARKVKILE-EERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 358 RDL-SSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERL-QEELSQAESTIDELKEQVDAALGAEEmvemltdRNL 428
Cdd:pfam17380 423 EQIrAEQEEARQREVRRLEEERAREMERVRleeqerqQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQ-------RRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 429 NLEEKVRELRETVgdleamneMNDELQENARETELELREQLDMAGARVREA--QKRVEAAQETVADYQQTIKKYRQLTAH 506
Cdd:pfam17380 496 ILEKELEERKQAM--------IEEERKRKLLEKEMEERQKAIYEEERRREAeeERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340 350
....*....|....*....|....*....|....
gi 205277392 507 LQ--DVNRELTNQQEASVERQQQPPPETFDFKIK 538
Cdd:pfam17380 568 LEamEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
235-476 |
2.12e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.96 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 235 LEQVQEWKSKMQEQQAD-LQRRLKEARKEAKEALEAKERYMEEMadtadAIEMATLDKEMAEERAESLQQEVEALKERVD 313
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 314 ELTTDLEILKAEIEEkGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQ-RERL 392
Cdd:COG3206 237 EAEARLAALRAQLGS-GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL----RAQIAALRAQlQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 393 QEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQenARETELELREQLDMA 472
Cdd:COG3206 312 QRILASLEAELEALQAREAS---LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEALTVG 386
|
....
gi 205277392 473 GARV 476
Cdd:COG3206 387 NVRV 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
279-523 |
2.34e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 279 DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILkAEIEEKGSDgaasSYQLKQLEEQNARLKDALVRMr 358
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWD----EIDVASAEREIAELEAELERL- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 359 DLSSSEKQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML--TDRNLNLEEKVRE 436
Cdd:COG4913 681 DASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarLELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 437 LRetvgdleamnemndeLQENARETELELREQLDMAGARVREAQKRVEAAQE---------------TVADYQQTIKKYR 501
Cdd:COG4913 758 AL---------------GDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldaDLESLPEYLALLD 822
|
250 260
....*....|....*....|....*..
gi 205277392 502 QLTA-----HLQDVNRELTNQQEASVE 523
Cdd:COG4913 823 RLEEdglpeYEERFKELLNENSIEFVA 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
196-399 |
2.44e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARKEAKEALEAKERY 273
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAiEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS---------YQLKQLE 344
Cdd:COG4717 411 LEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllqeleelkAELRELA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 345 EQNARLK---DALVRMRDLSSSEKQEHV--------------KLQKLMEKKNQELEVVRQQRERLQ-EELSQA 399
Cdd:COG4717 490 EEWAALKlalELLEEAREEYREERLPPVleraseyfsrltdgRYRLIRIDEDLSLKVDTEDGRTRPvEELSRG 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
294-524 |
2.50e-09 |
|
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: 60.93 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 294 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLssseKQEHVKLQK 373
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRAL----EQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 374 LMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--------VDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLE 445
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 446 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 524
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
289-516 |
2.78e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 289 LDKEMAEERAESLQQEVEALkervDELTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSE---- 364
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDL----ERAHEALEDAREQIE-----------LLEPIRELAERYAAARERLAELEYLRaalr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 365 ----KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemVEMLTDRnlnLEEKVRELRET 440
Cdd:COG4913 283 lwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR--LEQLERE---IERLERELEER 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 441 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQEtvaDYQQTIKKYRQLTAHLQDVNRELTN 516
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIAS 430
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
235-519 |
4.50e-09 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 60.74 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 235 LEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADaIEMATLDKEMAEERAEsLQQEVEALKErvdE 314
Cdd:COG5185 259 VEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID-IKKATESLEEQLAAAE-AEQELEESKR---E 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 315 LTTDLEILKAEIEEKGSDgaassyQLKQLEEQNARlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQE 394
Cdd:COG5185 334 TETGIQNLTAEIEQGQES------LTENLEAIKEE-IENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 395 ELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETVGDL-----EAMNEMNDELQENARETELELREQL 469
Cdd:COG5185 407 ILATLEDTLKAADRQI------EELQRQIEQATSSNEEVSKLLNELISELnkvmrEADEESQSRLEEAYDEINRSVRSKK 480
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 205277392 470 DmagarvrEAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQE 519
Cdd:COG5185 481 E-------DLNEELTQIESRVSTLKATLEKLRaKLERQLEGVRSKLDQVAE 524
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
206-463 |
4.50e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 60.64 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQ---RRLKEARKEAKEALEAKERYMEEMADTAD 282
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYdllEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 AI--EMATLDK-----EMAEERAESLQQEVEALKERVDELTTDLE-------ILKAEIEEKGSdgaassyQLKQLEEQNA 348
Cdd:pfam06160 309 ELkeELERVQQsytlnENELERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILE-------QLEEIEEEQE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 349 RLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaEEMVEML 423
Cdd:pfam06160 382 EFKESLQSLR------KDELEAREKLDEFKLELREIKRLvEKSNLpglpESYLDYFFDVSDEI----------EDLADEL 445
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 205277392 424 TDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 463
Cdd:pfam06160 446 NEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ 485
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
201-526 |
5.14e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.12 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEA---KEALEAKERymee 276
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEeVDSLKS----QLADYQQALDVQQTRAiqyQQAVQALEK---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 277 madtADAI-EMATLDKEMAEERAESLQQEVEALKERVDELttdleilkaeiEEKGSDGAASSYQLKQLEEQNARLKDALV 355
Cdd:COG3096 425 ----ARALcGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-----------EQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 356 RmrdlssseKQEHVKLQKLMEKkNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgAEEMVEML---TDRNLNLEE 432
Cdd:COG3096 490 R--------SQAWQTARELLRR-YRSQQALAQRLQQLRAQLAELEQRLRQQQN-------AERLLEEFcqrIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 433 KVRELRETvgdLEAMNEMNDELQENARETELELREQLDMAGARVRE----------AQKRVEAAQETVAdyqQTIKKYRQ 502
Cdd:COG3096 554 ELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlaAQDALERLREQSG---EALADSQE 627
|
330 340
....*....|....*....|....
gi 205277392 503 LTAHLQDVnreLTNQQEASVERQQ 526
Cdd:COG3096 628 VTAAMQQL---LEREREATVERDE 648
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
195-527 |
5.73e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkIQLEQVQEWKSKMQEQqadlqRRLKEARKEAKEALEAKERYM 274
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLE---QDYQAASDHLNLVQTA-----LRQQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEmadTADAIEMATLDKEMAEERAESLQQEVEALK-------ERVDELTTD----------LEILK-----AEIEEKGSD 332
Cdd:PRK04863 365 EE---QNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqQALDVQQTRaiqyqqavqaLERAKqlcglPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 333 GAASSYQlKQLEEQNARLKDALVRMRDlSSSEKQEHVKLQKLMEK----------KNQELEVVRQQRER--LQEELSQAE 400
Cdd:PRK04863 442 DWLEEFQ-AKEQEATEELLSLEQKLSV-AQAAHSQFEQAYQLVRKiagevsrseaWDVARELLRRLREQrhLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 401 STIDELKEQVDAALGAEEMV---EMLTDRNLNLEEKVRELREtvgDLEAMNEMNDELQENARETELELREQLDMAGARVR 477
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLaefCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 478 E----------AQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 527
Cdd:PRK04863 597 RlaarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
284-446 |
6.97e-09 |
|
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: 57.63 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 284 IEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKdalvrmrdls 361
Cdd:COG1579 10 LDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 362 ssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETV 441
Cdd:COG1579 80 --EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL------AELEAELAELEAELEEKKAELDEEL 151
|
....*
gi 205277392 442 GDLEA 446
Cdd:COG1579 152 AELEA 156
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
222-417 |
8.82e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 222 KAKLKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAE 295
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 296 ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAAssyqlkQLEEQNArlkDALVRMRDLSSSEKQEHVKLQKLM 375
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAA-----RAPAWLAAQDALA------RLREQSG---EEFEDSQDVTEYMQQLLERERELT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 205277392 376 EKKNQelevVRQQRERLQEE---LSQAESTIDE----LKEQVDAALGAE 417
Cdd:PRK04863 645 VERDE----LAARKQALDEEierLSQPGGSEDPrlnaLAERFGGVLLSE 689
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-557 |
9.69e-09 |
|
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: 60.13 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLKRAEDKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtad 282
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 aiEMATLDKEMAEERAESLQ--QEVEALKERVDELTTDLEilKAEIEekgsdgaassyqLKQLEEQNARLKDalvrmRDL 360
Cdd:pfam15921 350 --QLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLH--KREKE------------LSLEKEQNKRLWD-----RDT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 361 SSSEKQEHvkLQKLMEKKNQELE----VVRQQRERLQEELSQAESTIDELKEQVD--AALGAE---------EMVEMLTD 425
Cdd:pfam15921 409 GNSITIDH--LRRELDDRNMEVQrleaLLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQlestkemlrKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 426 RNLNLEEKVRELRETVGDLE----AMNEMNDELQENARETELELRE--QLDMAGARVREAQKRVEAAQETVADYQQTIKK 499
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQekerAIEATNAEITKLRSRVDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 500 YRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 557
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-443 |
1.56e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.16 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRAQVRDLEEKLETLRlkraEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQR---RLKEARKEAKEALEAKERYM 274
Cdd:COG4913 664 ASAEREIAELEAELERLD----ASSDDLAALEE---QLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRL 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEK----------------GSDGAASS 337
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAmrafnrewpaetadldADLESLPE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 338 YQ--LKQLEEQN-----ARLKDALVR-----MRDLSSSEKQEHVKLQKLMEKKNQELE--------------------VV 385
Cdd:COG4913 817 YLalLDRLEEDGlpeyeERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSLKripfgpgrylrlearprpdpEV 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 386 RQQRERLQEELSQAESTIDELKEQVDAALgaEEMVEMLTDRNlnlEEKVRELRETVGD 443
Cdd:COG4913 897 REFRQELRAVTSGASLFDEELSEARFAAL--KRLIERLRSEE---EESDRRWRARVLD 949
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
212-528 |
1.95e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 212 ETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 291
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 292 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHV-- 369
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQELQALSEAEAeq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 370 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNE 449
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 450 MNDELQE-NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQP 528
Cdd:COG4372 264 ELAILVEkDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-487 |
2.05e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLE-EKLETLRLKRAEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARK--------EAKE 265
Cdd:PTZ00121 1068 QDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEArKAEEAKKKAEDARKAEEARKaedarkaeEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 266 ALEAKERYMEEMADTADAIEMAtldkemaeERAESLQQEVEAlkERVDELTTDLEILKAEiEEKGSDGAASSYQLKQLEE 345
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAEEA--------RKAEDAKKAEAA--RKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 346 qnarlkdalvrMRDLSSSEKQEHVKlqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTD 425
Cdd:PTZ00121 1217 -----------ARKAEDAKKAEAVK--KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 426 RNLNLEEKVRELR--ETVGDLEAMNEMNDELQ--ENARETELELREQLDMAGARVREAQKRVEAAQ 487
Cdd:PTZ00121 1284 KKAEEKKKADEAKkaEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-1019 |
2.28e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 252 LQRRLKEARKEAKEALEAKEryMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgs 331
Cdd:COG1196 198 LERQLEPLERQAEKAERYRE--LKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 332 dgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVD 411
Cdd:COG1196 272 -------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 412 AALGAEEMvemltdrnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 491
Cdd:COG1196 341 ELEEELEE----------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 492 DYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikFAETKAHAKAIEMELRQMEVAQANRHMSLLTAf 571
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----------AAEEEAELEEEEEALLELLAELLEEAALLEAA- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 572 mpdsflrpggdhdcvlvlllmpRLICKAELIRKQAQEKFELSENCSERPGLRGA-AGEQLSFAAGLVYSLSLLQATLHRY 650
Cdd:COG1196 479 ----------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAY 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 651 EHALSQCSVdvykkvGSLYPEMSAHERSLDFLIELLhKDQLDETVNVEPLTKaikyyqhlysIHLAEQPEdctmqladhi 730
Cdd:COG1196 537 EAALEAALA------AALQNIVVEDDEVAAAAIEYL-KAAKAGRATFLPLDK----------IRARAALA---------- 589
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 731 kftqsaldcmsvevgRLRAFLQGGQEATDIALLLRDLEtscsdirqfckkirrrmpgtdapgIPAALAFGPQVSDTLLDC 810
Cdd:COG1196 590 ---------------AALARGAIGAAVDLVASDLREAD------------------------ARYYVLGDTLLGRTLVAA 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 811 RKHLTWVVAVLQEVAAAAAQLIAPLAENEGLLVAALEELafkaseqiygtpssspyeclrqscnilistmnklatamqeg 890
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE----------------------------------------- 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 891 eydaerppskpppvelRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 970
Cdd:COG1196 670 ----------------LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 205277392 971 IEKVQTRLEETQALLRKKEKEFEETMdalqADIDQLEAEKAELKQRLNS 1019
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEP----PDLEELERELERLEREIEA 778
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
200-410 |
2.60e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 58.05 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETlRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmad 279
Cdd:COG5185 287 LIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE--- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 tADAIEmATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDG-AASSYQLKQLE----------EQNA 348
Cdd:COG5185 363 -IENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEELQrqieqatssnEEVS 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 349 RLKDALVRMRDLSSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQV 410
Cdd:COG5185 441 KLLNELISELNKVMREADEESQ-SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
195-492 |
3.35e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.06 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLE---QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 271
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 RYMEEMADTADAI--EMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAA----SSYQ 339
Cdd:pfam02463 261 EKEEEKLAQVLKEnkEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKekeeIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 340 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 419
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE----SERLSSAAKLKEEELELKSEEEKEAQLLLELARQ 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277392 420 VEMLTDRNLN-LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 492
Cdd:pfam02463 417 LEDLLKEEKKeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
195-407 |
4.20e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 56.46 E-value: 4.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQ-------------------- 253
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELnEKLNELREELDELRKELAelnkaggsidklrkeierle 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 254 --------------------RRLKEARKEAKEALEAKERYMEEMADTADA-IEMATLDKEMAE--ERAESLQQEVEALKE 310
Cdd:COG1340 123 wrqqtevlspeeekelvekiKELEKELEKAKKALEKNEKLKELRAELKELrKEAEEIHKKIKElaEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 311 RVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmeKKNQELEVVRQQRE 390
Cdd:COG1340 203 EADELRKEADELHKEIVEAQ----------EKADELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAE 270
|
250
....*....|....*...
gi 205277392 391 RLQEELSQAES-TIDELK 407
Cdd:COG1340 271 EIFEKLKKGEKlTTEELK 288
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
203-527 |
5.46e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKealeakerymeemadtad 282
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-----KEKLNIQKNIDKIKNKLLKLELL------------------ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 aieMATLDKEmaEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLeeqnarlkdalvrmrdlss 362
Cdd:TIGR04523 203 ---LSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 363 seKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvEMLTDRNLNLEEKVRELRETVG 442
Cdd:TIGR04523 259 --KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--------DWNKELKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 443 DL----EAMNEMNDELQ------ENARETELELREQLdmagarvREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNR 512
Cdd:TIGR04523 329 QIsqnnKIISQLNEQISqlkkelTNSESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKN---LESQINDLES 398
|
330
....*....|....*
gi 205277392 513 ELTNQQEASVERQQQ 527
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQ 413
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
194-499 |
5.75e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 57.22 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRA-QVRDLEEKLE-----TLRLkraeDKAKLKELEkhkiQLEQVQEWKSKMQEQQADLQRRLKEArkEAKEAL 267
Cdd:PLN02939 119 SKDGEQLSDfQLEDLVGMIQnaeknILLL----NQARLQALE----DLEKILTEKEALQGKINILEMRLSET--DARIKL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 268 EAKERYMEEMADTadaiEMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQLK 341
Cdd:PLN02939 189 AAQEKIHVEILEE----QLEKLRNELLIRGAteglcvHSLSKELDVLKEENMLLKDDIQFLKAELIEV----AETEERVF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 342 QLEEQNARLKDALvrmRDLSSsekqehvklqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeemve 421
Cdd:PLN02939 261 KLEKERSLLDASL---RELES----------KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAA------- 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 422 MLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETELELREQLDMAGArvrEAQKRVEAAQETVADYQQTIKK 499
Cdd:PLN02939 321 LVLDQNQDLRDKVDKLEASLKEAN-VSKFSSYKVELLQQKLKLLEERLQASDH---EIHSYIQLYQESIKEFQDTLSK 394
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
206-495 |
6.05e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAEDKAKLKELEK----HKIQLEQVQEWKSKMQE--------QQADLQRRLKEARKEAKEALEAKeRY 273
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESqeqqQRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAEEAK-RF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIE--MATLDKEmaEERAESLQQEVEALKErvdelttdleilkaeieekgsdgaassyQLKQLEEQNARLK 351
Cdd:PRK04863 913 VQQHGNALAQLEpiVSVLQSD--PEQFEQLKQDYQQAQQ----------------------------TQRDAKQQAFALT 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 352 DALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAE--------------STIDELKEQVDAAlgA 416
Cdd:PRK04863 963 EVVQRRAHFSYEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslkSSYDAKRQMLQEL--K 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 417 EEMVEMLTDRNLNLEEKVRELREtvgdleamnEMNDELQEN-ARETELELreQLDMAGARVREAQKRVEAAQEtvaDYQQ 495
Cdd:PRK04863 1041 QELQDLGVPADSGAEERARARRD---------ELHARLSANrSRRNQLEK--QLTFCEAEMDNLTKKLRKLER---DYHE 1106
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
206-475 |
6.49e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQR---------------RLKEARKEAKEALEAk 270
Cdd:COG3096 833 DPEAELAALRQRRSELER---ELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELDAAQEA- 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 271 ERYMEEMADTADAIE--MATLDKEMAEEraESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQ-----LKQL 343
Cdd:COG3096 909 QAFIQQHGKALAQLEplVAVLQSDPEQF--EQLQADYLQAKEQQRRLKQQIFALSEVVQRR----PHFSYEdavglLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 344 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeEMVEML 423
Cdd:COG3096 983 SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-----EAEERA 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 424 TDRNLNLEEKVRELRETVGDLEAM-----NEMnDELQENARETELE---LREQLDMAGAR 475
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQltrceAEM-DSLQKRLRKAERDykqEREQVVQAKAG 1116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-570 |
6.70e-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: 57.37 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKL------------------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLK 257
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIeelqkelyalaneisrleQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 258 EARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS 337
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 338 YQLKQLEEQNARLKDALVR--MRDLS---SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--- 409
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEaeLKELQaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARlds 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 410 ---------------------------------------------VDAALG-------------AEEMVEMLT------- 424
Cdd:TIGR02168 494 lerlqenlegfsegvkallknqsglsgilgvlselisvdegyeaaIEAALGgrlqavvvenlnaAKKAIAFLKqnelgrv 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 --------------------------------------------------------------------------------
Cdd:TIGR02168 574 tflpldsikgteiqgndreilkniegflgvakdlvkfdpklrkalsyllggvlvvddldnalelakklrpgyrivtldgd 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 425 -------------DRNLNLEEKVRELRETVGDLEAMNEMNDELQEN---ARETELELREQLDMAGARVREAQKRVEAAQE 488
Cdd:TIGR02168 654 lvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKAlaeLRKELEELEEELEQLRKELEELSRQISALRK 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 489 TVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikfAETKAHAKAIEMELRQMEVAQANRHMSLL 568
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE------------AEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
..
gi 205277392 569 TA 570
Cdd:TIGR02168 802 RE 803
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
199-557 |
7.48e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 56.62 E-value: 7.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 199 GLRAQVRDLEEklETLRLKRAEDKAKLK--ELEKhkiqleqvqewkskmqeQQADLQRRLKEARKEAKEALEAKERyMEE 276
Cdd:pfam05622 63 LLQKQLEQLQE--ENFRLETARDDYRIKceELEK-----------------EVLELQHRNEELTSLAEEAQALKDE-MDI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 277 MADTADAIEM--ATLD--KEMAEERAEsLQQEVEALKERvdelTTDLEILKAEIEEKGSDGAASSYQL----KQLEEQNA 348
Cdd:pfam05622 123 LRESSDKVKKleATVEtyKKKLEDLGD-LRRQVKLLEER----NAEYMQRTLQLEEELKKANALRGQLetykRQVQELHG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 349 RLkdalvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTD 425
Cdd:pfam05622 198 KL-----------SEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELRcaqLQQAELSQADALLSPSSD 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 426 R--NLNLEEKVRELRETVGDLEAMNEM---NDELQENARETEL------------ELREQLDMAGARVREAQKRVE---- 484
Cdd:pfam05622 267 PgdNLAAEIMPAEIREKLIRLQHENKMlrlGQEGSYRERLTELqqlledanrrknELETQNRLANQRILELQQQVEelqk 346
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 485 AAQETVADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQqqpPPETFDFKIKFAETKAHAKAIEMELRQME 557
Cdd:pfam05622 347 ALQEQGSKAEDSSLLKQKLEEHLEklhEAQSELQKKKEQIEELE---PKQDSNLAQKIDELQEALRKKDEDMKAME 419
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
276-530 |
7.95e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQNARLKDALV 355
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 356 RMRD-----------LSSSEKQEHVK----LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmv 420
Cdd:COG3883 94 ALYRsggsvsyldvlLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 421 emltdrnlNLEEKVRELRETVGDLEAmnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 500
Cdd:COG3883 172 --------ELEAQQAEQEALLAQLSA-----EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|
gi 205277392 501 RQLTAHLQDVNRELTNQQEASVERQQQPPP 530
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
200-502 |
8.26e-08 |
|
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: 57.11 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME 275
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRdlgeELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADT-ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL---KAEIEEKGSDGAAssyqlkQLEEQNARLK 351
Cdd:pfam01576 349 EMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEG------QLQELQARLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 352 DAlvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaaLGAEEmvemlTDRNLNL 430
Cdd:pfam01576 423 ES-----ERQRAELAEKLsKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE-----LLQEE-----TRQKLNL 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 431 EEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 502
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
196-553 |
9.47e-08 |
|
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: 56.90 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 275
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP-LCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALV 355
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 356 RMRDL----SSSEKQEHVKLQKLMEKKNQELEV--VRQQRERLQEELSQAESTIDEL------KEQVDAALGAEEMVEML 423
Cdd:TIGR00618 595 RLQDLteklSEAEDMLACEQHALLRKLQPEQDLqdVRLHLQQCSQELALKLTALHALqltltqERVREHALSIRVLPKEL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 424 TDRNLNLEEKVRELRETV-GDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ---T 496
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLtYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqarT 754
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 497 IKKYR---------------QLTAHLQDVNRELTNQQEASVERQQQpppetfdFKIKFAETKAHAKAIEMEL 553
Cdd:TIGR00618 755 VLKARteahfnnneevtaalQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEIGQEIPSDEDIL 819
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
200-360 |
1.06e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEqvQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---- 275
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRARLEAllaa 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 -EMADTADAIEMATLdKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDAL 354
Cdd:COG4913 371 lGLPLPASAEEFAAL-RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA-------EIASLERRKSNIPARL 442
|
....*.
gi 205277392 355 VRMRDL 360
Cdd:COG4913 443 LALRDA 448
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
200-483 |
1.16e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.28 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeema 278
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 279 DTADAIEMATL-----DKEMAEERAESL------------QQEVEALK------ERVDELTTDLEILKAEIEEKGSDGAA 335
Cdd:pfam15921 407 DTGNSITIDHLrreldDRNMEVQRLEALlkamksecqgqmERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 336 SSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQeelsQAESTIDELKEQVdaaLG 415
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR----NVQTECEALKLQM---AE 559
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 416 AEEMVEMLTDRNLNLEEKVRELRETVGdleAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRV 483
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAG---AMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARV 627
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
198-527 |
1.51e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.91 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRAQVRDLEEKL-----ETLRLKRA-EDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 266
Cdd:pfam07111 334 KQLRGQVAELQEQVtsqsqEQAILQRAlQDKAAEVEVERMsakglQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 267 LEAKERYMEEMADTADAI------------EMATLDKEMAEERA-ESLQQEVEALKERVDELTTDLeilkaeieekgsdg 333
Cdd:pfam07111 414 QIWLETTMTRVEQAVARIpslsnrlsyavrKVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADL-------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 334 aasSYQLKQLEEQNARLKDALvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDA 412
Cdd:pfam07111 480 ---SLELEQLREERNRLDAEL----QLSAHLIQQEVgRAREQGEAERQQLSEVAQQ---LEQELQRAQESLASVGQQLEV 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 413 ALGAEEMVemlTDRNLNLEEKVRELRETVGDleamnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 492
Cdd:pfam07111 550 ARQGQQES---TEEAASLRQELTQQQEIYGQ---------ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQ 617
|
330 340 350
....*....|....*....|....*....|....*
gi 205277392 493 YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 527
Cdd:pfam07111 618 IQHRATQEKERNQELRRLQDEARKEEGQRLARRVQ 652
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
206-358 |
1.52e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.78 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADA-- 283
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE---AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNke 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 284 -------IEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDALVR 356
Cdd:COG1579 91 yealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAELEE 160
|
..
gi 205277392 357 MR 358
Cdd:COG1579 161 LE 162
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-499 |
1.99e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.39 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 339 QLKQLEEQNARLKDALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 418
Cdd:COG1579 18 ELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 419 M------VEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDmagARVREAQKRVEAAQETVAD 492
Cdd:COG1579 91 YealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167
|
....*..
gi 205277392 493 YQQTIKK 499
Cdd:COG1579 168 LAAKIPP 174
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
197-491 |
2.15e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 197 EEGLRAQVRDLEEKLETLRLKRAE-----DKAKLK-------------ELEKH-------KIQLEQVQEWKSKMQEQQAD 251
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIEltahcDKLLLEnkeltqeasdmtlELKKHqediincKKQEERMLKQIENLEEKEMN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 252 LQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEmaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKGS 331
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE---KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 332 DGAASSYQLKQLEEQNARLKDALvrmrdlsSSEKQehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE---LKE 408
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELEL-------ASAKQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQK 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 409 QVDAALGAE--EMVEMLtDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL--------ELREQLDMagaRVRE 478
Cdd:pfam05483 693 EIDKRCQHKiaEMVALM-EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELsnikaellSLKKQLEI---EKEE 768
|
330
....*....|...
gi 205277392 479 AQKRVEAAQETVA 491
Cdd:pfam05483 769 KEKLKMEAKENTA 781
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
200-502 |
2.50e-07 |
|
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: 55.18 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLE-QVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKERYMEEMA 278
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEEKA 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 279 DTADAIEMAT------------------------------LDKEMAEERAESLQQEVEalKERVDelttdleilkAEIEE 328
Cdd:pfam01576 566 AAYDKLEKTKnrlqqelddllvdldhqrqlvsnlekkqkkFDQMLAEEKAISARYAEE--RDRAE----------AEARE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 329 KGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEEL-SQAESTIDELK 407
Cdd:pfam01576 634 KETRALSLARALEEALEA----KEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMkTQLEELEDELQ 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 408 EQVDAALGAEEMVEMLT---DRNLNL-----EEKVRELRETVGDLEAmnEMNDELQENA------RETELELRE---QLD 470
Cdd:pfam01576 710 ATEDAKLRLEVNMQALKaqfERDLQArdeqgEEKRRQLVKQVRELEA--ELEDERKQRAqavaakKKLELDLKEleaQID 787
|
330 340 350
....*....|....*....|....*....|..
gi 205277392 471 MAGARVREAQKRVEAAQETVADYQQTIKKYRQ 502
Cdd:pfam01576 788 AANKGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-328 |
2.65e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKH--KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 272
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 273 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 328
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
268-561 |
2.73e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 268 EAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQN 347
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 348 ARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRN 427
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE---LEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 428 LNLEEKVRELRETVGDlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrQLTAHL 507
Cdd:COG4372 167 AALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA--LLDALE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 205277392 508 QDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQA 561
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
195-570 |
2.85e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---------- 264
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvls 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 265 EALEAKERY---MEE----------MADTADAIEMATLDKEMAEERA-------------ESLQQEVEALKERVDELTTD 318
Cdd:TIGR02168 527 ELISVDEGYeaaIEAalggrlqavvVENLNAAKKAIAFLKQNELGRVtflpldsikgteiQGNDREILKNIEGFLGVAKD 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 319 LEILKAEIEEKGS------------DGAASSYQLKQLEEQNARLKDALVRMRDLSS--SEKQEHVKLQKlmekkNQELEV 384
Cdd:TIGR02168 607 LVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSILER-----RREIEE 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 385 VRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELE 464
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 465 LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR----QLTAHLQDVNRELTNQQEASVERQqqpppetfdFKIKFA 540
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLR---------ERLESL 829
|
410 420 430
....*....|....*....|....*....|
gi 205277392 541 ETKAHAKAIEMELRQMEVAQANRHMSLLTA 570
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
196-504 |
2.89e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.52 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---EALEAKER 272
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKtltQRVLERET 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 YMEEMADTADaiEMATLDKEMAEERaESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKD 352
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT-------QVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 353 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdAALGAEEMVEMLTDRNLNL-E 431
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ---ARLQAAQLTLQLADASLALrE 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 432 EKVRELRETVGDLEAMNEMNDELQENARETeleLREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLT 504
Cdd:pfam07888 298 GRARWAQERETLQQSAEADKDRIEKLSAEL---QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
321-526 |
3.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 321 ILKAEIEEKGSD-----GAASSYQLKQLEEQNARLKDAlvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEE 395
Cdd:COG4717 46 MLLERLEKEADElfkpqGRKPELNLKELKELEEELKEA--------EEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 396 LSQAEsTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEamnEMNDELQENARETELELREQLDMAGAR 475
Cdd:COG4717 118 LEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE---ELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 205277392 476 VREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 526
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
281-436 |
3.65e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 281 ADAIEMATLDKEMAEERAESLQQEVEA-LKERVDELTTDLEilkAEIEEKGSDgaassyqLKQLEEQNARLKDALvrmrd 359
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE---KELRERRNE-------LQKLEKRLLQKEENL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 360 lssSEKQEhvklqkLMEKKNQELEVVRQQRERLQEELSQAESTIDEL-KEQVD-----AALGAEEMVEMLTDrnlNLEEK 433
Cdd:PRK12704 99 ---DRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQeleriSGLTAEEAKEILLE---KVEEE 166
|
...
gi 205277392 434 VRE 436
Cdd:PRK12704 167 ARH 169
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
196-422 |
5.17e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWK-SKMQEQQADLQRRLKEARKEAKEALEAKERYM 274
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMATLDKEMAEERAES--LQQEVEALKERVDELTTD-------LEILKAEIEEKGSDGAASSYQLK---Q 342
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESgkAQAEVERLLGILREVENEkndkdkkIAELESLTLRQMKEQNKKVANIKhgqQ 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 343 LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaEEM 419
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADNSQQLQLEELMgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL--EEI 706
|
...
gi 205277392 420 VEM 422
Cdd:pfam10174 707 LEM 709
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
292-527 |
5.41e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 292 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKG---------SDGAASSYQLKQLEEQnarlKDALVRMRDLSS 362
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlngleSELAELDEEIERYEEQ----REQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 363 SEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgaeemVEMLTDRNLNLEEKVRELRETVG 442
Cdd:PRK02224 241 EVLEEH-------EERREELETLEAEIEDLRETIAETEREREELAEE----------VRDLRERLEELEEERDDLLAEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 443 DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDvnrELTNQQEASV 522
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES---ELEEAREAVE 380
|
....*
gi 205277392 523 ERQQQ 527
Cdd:PRK02224 381 DRREE 385
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
189-555 |
5.48e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 189 PLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE 268
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 269 AKERymeemADTadaiematldkemaeERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyQLKQLEEQNA 348
Cdd:COG4913 331 QIRG-----NGG---------------DRLEQLEREIERLERELEERERRRARLEA--------------LLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 349 RLKDALVRMRDlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNL 428
Cdd:COG4913 377 ASAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS----------LERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 429 NLEEKVRELRetvgdleamnemnDELQENARETELELR---EQLDmagarVREAQKRVEAAQETV------------ADY 493
Cdd:COG4913 437 NIPARLLALR-------------DALAEALGLDEAELPfvgELIE-----VRPEEERWRGAIERVlggfaltllvppEHY 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277392 494 QQTIKKYRQ--LTAHLQdVNRELTNQQEAsveRQQQPPPETFDFKIKFAETKAHAkAIEMELRQ 555
Cdd:COG4913 499 AAALRWVNRlhLRGRLV-YERVRTGLPDP---ERPRLDPDSLAGKLDFKPHPFRA-WLEAELGR 557
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
201-484 |
7.19e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEAKEALEAKERYmeemaD 279
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEeVDELKS----QLADYQQALDVQQTRAIQYQQAVQAL-----E 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 TADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKA-----------------------------EIEEK 329
Cdd:PRK04863 425 RAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevsrseawdvarELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 330 GSDGAASSYQLKQLE------EQNARLKDALVRMRD---------LSSSE--KQEHVKLQKLMEKKNQELEVVRQQRERL 392
Cdd:PRK04863 505 LREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLAefckrlgknLDDEDelEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 393 QEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQLDMA 472
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALA--------------RLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
330
....*....|..
gi 205277392 473 GARVREAQKRVE 484
Cdd:PRK04863 651 AARKQALDEEIE 662
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
186-418 |
8.23e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 186 AVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE 265
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 266 ALeakeRYMEEMADTADAIEMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgaassyqlkQL 343
Cdd:COG3883 91 RA----RALYRSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKA---------------------EL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 344 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 418
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
262-513 |
8.41e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.90 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 262 EAKEALEAKERYMEEMADTADAIEM-ATLDKEMAEERAESLQQEVE-ALKERVDELTTDLEILKAEIEEKGS----DGAA 335
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKnKELFEQYKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 336 SSYQLKQLEEQNARLKDalvrmrDLSSSEKQEH--VKLQKLMEKKNQELEVVRQQRERLQEELSQAES--------TID- 404
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIED------DAAKNDKSNKaaIDIQLSLENFENKFLKISDIKKKINDCLKETESiekkissfSIDs 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 405 ---ELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAM-NEMNDE-------LQENARETELELREQLDMAG 473
Cdd:TIGR01612 1641 qdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIeIDVDQHkknyeigIIEKIKEIAIANKEEIESIK 1720
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 474 ARVREAQKRVEAAQET------------------VAD-YQQTIKKYRQLTAHLQDVNRE 513
Cdd:TIGR01612 1721 ELIEPTIENLISSFNTndlegidpnekleeynteIGDiYEEFIELYNIIAGCLETVSKE 1779
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
191-501 |
8.45e-07 |
|
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: 53.69 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 191 PSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKL-----------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEA 259
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangelekasREETFARTALKNARLDLRRLFDEKQSEKDKKNKA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 260 RKEAKEALEAKERYMEEMADTADAIEMATLDkEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAAssyQ 339
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLE-EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA---E 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 340 LKQLEEQNARLKDAL----VRMRDLSSSEKQEHVKLQKLmEKKNQEL--------EVVRQQRERLQEELSQAESTIDELK 407
Cdd:pfam12128 749 LKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERI-AVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQ 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 408 EQvdaaLGAEEMVEMLTDRNLNLEEKVRE-----LRETVGDLEAMNEMNDELQE--NARETELELREQLDMAGARVREAQ 480
Cdd:pfam12128 828 QQ----LARLIADTKLRRAKLEMERKASEkqqvrLSENLRGLRCEMSKLATLKEdaNSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340
....*....|....*....|.
gi 205277392 481 KRVEAAQETVADYQQTIKKYR 501
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHS 924
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-484 |
8.53e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLET--LRLKRAEDKAKL--KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---------EAKEA 266
Cdd:pfam05483 354 FEATTCSLEELLRTeqQRLEKNEDQLKIitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkqfeKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 267 LEAKERYM--------EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSY 338
Cdd:pfam05483 434 LKGKEQELifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 339 QLKQLEEqnarlkdalvrmrDLSSSEKQEHVKLQK---LMEKKNQ---ELEVVR----QQRERLQEELSQAESTIDELKE 408
Cdd:pfam05483 514 ELKKHQE-------------DIINCKKQEERMLKQienLEEKEMNlrdELESVReefiQKGDEVKCKLDKSEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 409 QVdaaLGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEM------NDELQENARET-----ELELREQLDMAGARVR 477
Cdd:pfam05483 581 EV---LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsAENKQLNAYEIkvnklELELASAKQKFEEIID 657
|
....*..
gi 205277392 478 EAQKRVE 484
Cdd:pfam05483 658 NYQKEIE 664
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
242-421 |
1.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 242 KSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL------ 315
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 316 ----TTDLEILkaeieeKGSDGAAS----SYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvrQ 387
Cdd:COG3883 98 sggsVSYLDVL------LGSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE---A 168
|
170 180 190
....*....|....*....|....*....|....
gi 205277392 388 QRERLQEELSQAESTIDELKEQVDAALGAEEMVE 421
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
227-519 |
1.83e-06 |
|
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: 52.44 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 227 ELEKHKIQLEQVQEWKSKMQEQQadlqrrlKEARKEAKEALEAKERYMEEMADtadaiematldkemaeeRAESLQQEVE 306
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH-------KRARIELEKKASALKRQLDRESD-----------------RNQELQKRIR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 307 ALKERVDELTtdlEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQEL---- 382
Cdd:pfam05557 59 LLEKREAEAE---EALREQAELNRLKKKYLEALNKKLNEKESQLADA----REVISCLKNELSELRRQIQRAELELqstn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 383 ---EVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNLNLEEKVRELRETVGDLEAMNEMNDELqenAR 459
Cdd:pfam05557 132 selEELQERLDLLKAKASEAEQLRQNLEKQQSS----------LAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL---AR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 460 ETELE-LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 519
Cdd:pfam05557 199 IPELEkELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
197-324 |
1.83e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 50.21 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 197 EEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLE-QVQEWkskmqEQQADLQrrLKEARKE-AKEALEAKERYM 274
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEaEAEKW-----EEKARLA--LEKGREDlAREALERKAELE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIematldkEMAEERAESLQQEVEALKERVDELTTDLEILKA 324
Cdd:COG1842 98 AQAEALEAQL-------AQLEEQVEKLKEALRQLESKLEELKAKKDTLKA 140
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
190-527 |
1.90e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 190 LPSPSKEEE-GLRAQVRDLEEKLETLrlkraedKAKLKELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALE 268
Cdd:pfam10174 172 LPKKSGEEDwERTRRIAEAEMQLGHL-------EVLLDQKEKENIHLREELHRRNQLQPDPAKT-----KALQTVIEMKD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 269 AKERYMEEM-ADTADAIEMATLDKEM-AEERAESLQQeVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 346
Cdd:pfam10174 240 TKISSLERNiRDLEDEVQMLKTNGLLhTEDREEEIKQ-MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 347 NAR-------LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEM 419
Cdd:pfam10174 319 NSDckqhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 420 VEMLTDRNLNLEEKVR-------ELRETVGDLE--------AMNEMNDELQENARETElELREQldmagaRVREAQKRve 484
Cdd:pfam10174 396 INVLQKKIENLQEQLRdkdkqlaGLKERVKSLQtdssntdtALTTLEEALSEKERIIE-RLKEQ------REREDRER-- 466
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 205277392 485 aaQETVADYQQTIKKYRQLTAHLQdvnRELTNQQEASVERQQQ 527
Cdd:pfam10174 467 --LEELESLKKENKDLKEKVSALQ---PELTEKESSLIDLKEH 504
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
194-467 |
1.94e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 52.28 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKM----QEQQADLQRRLKEARKEAKEALEA 269
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 270 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEI--EEKGSDGAASSYQLKQLEEQN 347
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 348 ARLKDALVRMRDLSSSEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRN 427
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSED-------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 205277392 428 LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE 467
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
203-310 |
2.45e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 52.14 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRlKRAEDKAKlkELEKHKIQLEQV-QEWKSKMQEQQADLQRRLKEARKEAKEAL-EAKE--------- 271
Cdd:PRK00409 517 KLNELIASLEELE-RELEQKAE--EAEALLKEAEKLkEELEEKKEKLQEEEDKLLEEAEKEAQQAIkEAKKeadeiikel 593
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 205277392 272 RYMEEMADTA----DAIEMATLDKEMAEERAESLQQEVEALKE 310
Cdd:PRK00409 594 RQLQKGGYASvkahELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
206-470 |
2.59e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 51.78 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---------- 275
Cdd:pfam06160 71 EAEELNDKYRFKKA--KKALDEIE------ELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRElrktllanrf 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAIE--MATLDKE---------------------MAEERAESLQQEVEALKERVDELTTD----LEILKAEIEE 328
Cdd:pfam06160 143 SYGPAIDELEkqLAEIEEEfsqfeeltesgdylearevleKLEEETDALEELMEDIPPLYEELKTElpdqLEELKEGYRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 329 KGSDGAASSY-----QLKQLEEQNARLKDALVRMRDLSSSEKQEHVK-----LQKLMEKKNQELEVVRQQRERLQEELSQ 398
Cdd:pfam06160 223 MEEEGYALEHlnvdkEIQQLEEQLEENLALLENLELDEAEEALEEIEeridqLYDLLEKEVDAKKYVEKNLPEIEDYLEH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 399 AESTIDELKEQVD--------------AALGAEEMVEMLTDRNLNLEEKVRE-----------LRETVGDLEAMNEMNDE 453
Cdd:pfam06160 303 AEEQNKELKEELErvqqsytlneneleRVRGLEKQLEELEKRYDEIVERLEEkevayselqeeLEEILEQLEEIEEEQEE 382
|
330 340
....*....|....*....|
gi 205277392 454 LQE---NARETELELREQLD 470
Cdd:pfam06160 383 FKEslqSLRKDELEAREKLD 402
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
297-441 |
3.20e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.62 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 297 RAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME 376
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDE------ASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 377 KKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAE-----------EMVEMLTDRNLNLEEkvrELRETV 441
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEvvsrwtgipvgKLLEGEREKLLNLEE---ELHERV 551
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
207-345 |
3.44e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 207 LEEKLETLRLKRAEDKAK--LKELEK--HKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadtad 282
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKeaEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEE------ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 283 aiemaTLDKEMaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaaSSYQLKQLEE 345
Cdd:PRK12704 97 -----NLDRKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELER 146
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
200-563 |
3.46e-06 |
|
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: 51.71 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETL--RLKRAEDKAKLKELEKHKIQlEQVQEWKSKMQEQQADLQRRLKEarkeaKEALEAKERYMEEm 277
Cdd:pfam01576 66 LAARKQELEEILHELesRLEEEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQKLQLE-----KVTTEAKIKKLEE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 adtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLeilkAEIEEKgsdgAASSYQLKQLEEqnARLKDALVRM 357
Cdd:pfam01576 139 ------------DILLLEDQNSKLSKERKLLEERISEFTSNL----AEEEEK----AKSLSKLKNKHE--AMISDLEERL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 358 RdlssSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNlNLEEKVREL 437
Cdd:pfam01576 197 K----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKN-NALKKIREL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 438 RETVGDLEAMNEMNDELQENARETELELREQLdmagarvrEAQK-RVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 516
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEEL--------EALKtELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 205277392 517 QQEASVERQQQpppetfdfkikfaetkAHAKAIEMELRQMEVAQANR 563
Cdd:pfam01576 342 SHEAQLQEMRQ----------------KHTQALEELTEQLEQAKRNK 372
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
185-472 |
3.97e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 185 GAVPPLPSpskeEEGLRAQVrdleEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMqeqqADLQRRLKEARKEAK 264
Cdd:PRK11281 30 ASNGDLPT----EADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEET----EQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 265 EALEAKERYMEEmADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLe 344
Cdd:PRK11281 98 QAQAELEALKDD-NDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQI- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 345 eqNARLKDALVRMRDLSSSEKQ----EHVKLQKLMEKKNQELEVVRQ-------QRE-------RLQEE----------- 395
Cdd:PRK11281 176 --RNLLKGGKVGGKALRPSQRVllqaEQALLNAQNDLQRKSLEGNTQlqdllqkQRDyltariqRLEHQlqllqeainsk 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 396 -LSQAESTIDELKEQVDAA-LGAEEMVEMLTDRNLNLEEKVrelretvgdLEAMNEMNDELQENareteLELREQLDMA 472
Cdd:PRK11281 254 rLTLSEKTVQEAQSQDEAArIQANPLVAQELEINLQLSQRL---------LKATEKLNTLTQQN-----LRVKNWLDRL 318
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-532 |
4.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 294 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDAlvrmrdlssseKQEHVKLQK 373
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----------EEYNELQAELEAL-----------QAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 374 LMEKKNQELEvvrQQRERLQEELSQA------ESTIDELK--EQVDAALGAEEMVEMLTDRNLNLeekVRELRETVGDLE 445
Cdd:COG3883 73 EIAEAEAEIE---ERREELGERARALyrsggsVSYLDVLLgsESFSDFLDRLSALSKIADADADL---LEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 446 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 525
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*..
gi 205277392 526 QQPPPET 532
Cdd:COG3883 227 AAAAAAA 233
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-470 |
4.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 243 SKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL 322
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADA---RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 323 KAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST 402
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 403 IDELKEQVDAALGAEEMVEMLTDRNLN-LEEKVRELREtvgDLEAMNEMN----DELQEnARETELELREQLD 470
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEeLERELERLER---EIEALGPVNllaiEEYEE-LEERYDFLSEQRE 805
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
196-399 |
4.30e-06 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 49.26 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEARKEAKEALEake 271
Cdd:pfam00261 37 EVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrkvLENRALKDEEKMEILEAQLKEAKEIAEEADR--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 RYMEemadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEiEEKGSDgAASSYQLkQLEEQNARLK 351
Cdd:pfam00261 114 KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEAS-EEKASE-REDKYEE-QIRFLTEKLK 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 205277392 352 DALVRMRDlsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA 399
Cdd:pfam00261 187 EAETRAEF----AERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
906-1026 |
5.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 906 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLEE 980
Cdd:COG1196 213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 205277392 981 TQALLRKKEKEF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1026
Cdd:COG1196 293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-561 |
5.53e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQ-VRDLEEKLETLRLKRAEDkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 273
Cdd:PTZ00121 1123 KAEDARKAEeARKAEDARKAEEARKAED-AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-AEELRKAEDAR 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADaiematldkemAEERAESLQQEVEAlkERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEqnARLKDA 353
Cdd:PTZ00121 1201 KAEAARKAE-----------EERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE--ARMAHF 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 354 LVRMRDLSSSEKQEHVKLQKLMEKKNqelevvrqqrerlQEELSQAEST--IDELKEQVDAALGAEEmvemLTDRNLNLE 431
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKK-------------ADEAKKAEEKkkADEAKKKAEEAKKADE----AKKKAEEAK 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 432 EKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ---ETVADYQQTIKKYRQLTAHLQ 508
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 205277392 509 DVNRELTNQQEASVERQQQPPPETFDFKIKFAETKahAKAIEMELRQMEVAQA 561
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKA 1459
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
907-1016 |
5.55e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 907 RAAALRAEITDAE----GLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA------------------- 963
Cdd:COG1579 25 RLKELPAELAELEdelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeieslkrr 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 964 -------AKDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQR 1016
Cdd:COG1579 105 isdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
905-1026 |
5.64e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 905 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLEETQAL 984
Cdd:COG1196 252 EAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 205277392 985 LRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1026
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
201-514 |
6.99e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 50.24 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLR-LKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEaKERYMEEMAD 279
Cdd:pfam06160 9 YKEIDELEERKNELMnLPVQEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELND-KYRFKKAKKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 TADAiematldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEE---------------KGSDGAAssyqLKQLE 344
Cdd:pfam06160 88 LDEI-----------EELLDDIEEDIKQILEELDELLESEEKNREEVEElkdkyrelrktllanRFSYGPA----IDELE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 345 EQNARLKDALVRMRDLSSSekQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST----IDELKEqvdaalGAEEMV 420
Cdd:pfam06160 153 KQLAEIEEEFSQFEELTES--GDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTElpdqLEELKE------GYREME 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 421 EM---LTDRNL-----NLEEKVRELRETV--GDLEAMNEMNDELQENAreteLELREQLdmagarvreaQKRVEAAQEtv 490
Cdd:pfam06160 225 EEgyaLEHLNVdkeiqQLEEQLEENLALLenLELDEAEEALEEIEERI----DQLYDLL----------EKEVDAKKY-- 288
|
330 340
....*....|....*....|....
gi 205277392 491 adYQQTIKKYRQLTAHLQDVNREL 514
Cdd:pfam06160 289 --VEKNLPEIEDYLEHAEEQNKEL 310
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
190-550 |
9.19e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 190 LPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE---- 265
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQraml 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 266 --ALEAKERYMEEMAD--------------TADAIEMATLDKE----MAEERAESLQQEVEALKERVDELTTDLEILKAE 325
Cdd:TIGR00606 659 agATAVYSQFITQLTDenqsccpvcqrvfqTEAELQEFISDLQsklrLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 326 IEEKgsdgaasSYQLKQLEEQNARLKDALVRMR-DLSSSEKQEHVKLQKLMEKKNQELEVVRQQreRLQEELSQAESTID 404
Cdd:TIGR00606 739 IDLK-------EKEIPELRNKLQKVNRDIQRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIME--RFQMELKDVERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 405 ELKEQVDAALGAEEMVEMltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE------QLDMAGARVRE 478
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseklQIGTNLQRRQQ 885
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 479 AQKRVEAAQETVADYQQTIKKYR-------QLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFAETKAHAKAIE 550
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKeqdspleTFLEKDQQEKEELISSKETSNKKAQD---KVNDIKEKVKNIHGYMKDIE 961
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
198-511 |
9.65e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRAQVRDLEE---KLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQ---EQQADLQRRLKEARKEAKEALEAKE 271
Cdd:PRK01156 315 SNIDAEINKYHAiikKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNsylKSIESLKKKIEEYSKNIERMSAFIS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 272 RYMEEMADTADAI--EMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKA----------------------- 324
Cdd:PRK01156 395 EILKIQEIDPDAIkkELNEINVKLQDisSKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvcgttlgeeksnhiinhy 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 325 ------------EIEEKGSDGAASSYQLKQLEEQNA------------RLKDALVRMRDLSSSE---KQEHVKLQKLMEK 377
Cdd:PRK01156 475 nekksrleekirEIEIEVKDIDEKIVDLKKRKEYLEseeinksineynKIESARADLEDIKIKInelKDKHDKYEEIKNR 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 378 -KNQELEVVRQQRERLQEELSQA--------ESTIDELKEQV-DAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEam 447
Cdd:PRK01156 555 yKSLKLEDLDSKRTSWLNALAVIslidietnRSRSNEIKKQLnDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLN-- 632
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277392 448 NEMNdELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVN 511
Cdd:PRK01156 633 NKYN-EIQENKILIE-KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
195-408 |
9.74e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKErY 273
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAREDALNQSLKELMHQARTVLKART-E 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEmaeeraESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassyqlkqleEQNARLKDA 353
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAEL------SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD-----------EDILNLQCE 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 354 LVrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 408
Cdd:TIGR00618 825 TL---------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-315 |
1.01e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 192 SPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 271
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 205277392 272 RYMEEMADTADAIEMATLDKEMAEERAEsLQQEVEALKERVDEL 315
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEE-LERELERLEREIEAL 779
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
285-521 |
1.30e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 48.80 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 285 EMATLDKEMA--EERAESLQQEVEALKERVDELTT---DLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRD 359
Cdd:pfam09728 33 EMKRLQKDLKklKKKQDQLQKEKDQLQSELSKAILaksKLEKLCRELQK----------QNKKLKEESKKLAKEEEEKRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 360 LSSSEKQEHVK-LQKLMEKKNQELEVVRQQRERLQEELsqaESTID--ELKE-QVDAALGAEEMVEMLTDRNLNLEEKVR 435
Cdd:pfam09728 103 ELSEKFQSTLKdIQDKMEEKSEKNNKLREENEELREKL---KSLIEqyELRElHFEKLLKTKELEVQLAEAKLQQATEEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 436 ELRETVGDLEAMNEMNDELQEnARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELT 515
Cdd:pfam09728 180 EKKAQEKEVAKARELKAQVQT-LSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWK 258
|
....*.
gi 205277392 516 NQQEAS 521
Cdd:pfam09728 259 RKWEKS 264
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
248-487 |
1.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 248 QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTtdlEILKAEIE 327
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 328 EKGSDGAASSYQLKQLEEQNarLKDALVRMRDLSSSEKQEhvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 407
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 408 EQVDAALGAEEMVEMLTDRnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 487
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
218-417 |
1.40e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 218 RAEDKAK--LKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERyMEEMADTADAiEMATL 289
Cdd:COG3096 492 QAWQTARelLRRYRSQQALAQRLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEA-QLEEL 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 290 DKEMAE--ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDgaassyQLKQLEEQ-NARLKDalvrmrdlsSSEKQ 366
Cdd:COG3096 570 EEQAAEavEQRSELRQQLEQLRARIKELAA-----RAPAWLAAQD------ALERLREQsGEALAD---------SQEVT 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 367 EHvkLQKLMEKK---NQELEVVRQQRERLQ---EELSQAESTID----ELKEQVDAALGAE 417
Cdd:COG3096 630 AA--MQQLLEREreaTVERDELAARKQALEsqiERLSQPGGAEDprllALAERLGGVLLSE 688
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
197-373 |
1.49e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.65 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 197 EEGLRAQVRDLEEKLETLRLKR-AEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKER 272
Cdd:pfam15905 147 EDGTQKKMSSLSMELMKLRNKLeAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKekiEEKSETEKLLE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 YMEEMADTADAIEMATLD----KEMAEERA---ESLQQEVEA----LKERVDELTTDLEILKAEIEEKgsdgaassyqLK 341
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDiaqlEELLKEKNdeiESLKQSLEEkeqeLSKQIKDLNEKCKLLESEKEEL----------LR 296
|
170 180 190
....*....|....*....|....*....|..
gi 205277392 342 QLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 373
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
203-519 |
1.65e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 203 QVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeemadTAD 282
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL-------CAA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 AIEMATLDKEMAEERAESLQQeveALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSS 362
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 363 SE---------KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST-------IDELKEQVDAALGAEEMVEMLTDR 426
Cdd:TIGR00618 523 PGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcDNRSKEDIPNLQNITVRLQDLTEK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 427 NLNLEEKVR--------ELRETVGDLEAMNEMNDELQENARE------TELEL-REQLDMAGARVREAQKRVEAAQETVA 491
Cdd:TIGR00618 603 LSEAEDMLAceqhallrKLQPEQDLQDVRLHLQQCSQELALKltalhaLQLTLtQERVREHALSIRVLPKELLASRQLAL 682
|
330 340
....*....|....*....|....*...
gi 205277392 492 DYQQTikKYRQLTAHLQDVNRELTNQQE 519
Cdd:TIGR00618 683 QKMQS--EKEQLTYWKEMLAQCQTLLRE 708
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
200-554 |
1.93e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRD---LEEKLETLRLKRAEDKAKLKELEK-HKIQLEQVQEWKSKMQEQQADLQrRLKEARKEAKEALEAKERYME 275
Cdd:PRK01156 178 LRAEISNidyLEEKLKSSNLELENIKKQIADDEKsHSITLKEIERLSIEYNNAMDDYN-NLKSALNELSSLEDMKNRYES 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAIEMATLD----KEMAEERAESLQQEVEALKERVDE---LTTDLEILKAEIEekGSDGAASSYQ--LKQLEEQ 346
Cdd:PRK01156 257 EIKTAESDLSMELEKnnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILS--NIDAEINKYHaiIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 347 NARLKDALV---RMRDLS---SSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTidelkeqvdAALGAE 417
Cdd:PRK01156 335 QKDYNDYIKkksRYDDLNnqiLELEGYEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKI---------QEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 418 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENAR-----------ETELELREQLDMAGARVREAQKRVEAA 486
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKI 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 487 QETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETK-AHAKAIEMELR 554
Cdd:PRK01156 486 REIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdKHDKYEEIKNR 554
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
215-498 |
2.10e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 215 RLKRAEDKAKL---KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 291
Cdd:COG4372 3 RLGEKVGKARLslfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 292 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKL 371
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 372 QKLMEKKNQELEVVRQQRERLQEELSQAestidELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN 451
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 205277392 452 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIK 498
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
206-572 |
2.14e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.68 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYmEEM-------- 277
Cdd:PRK04778 90 EAEELNDKFRFRKA--KHEINEIE------SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLY-RELrksllanr 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 ---ADTADAIE--MATLDKEMAEerAESLQQE---------VEALKERVDELTTDLEILKAEIEEKGSDGAAssyQLKQL 343
Cdd:PRK04778 161 fsfGPALDELEkqLENLEEEFSQ--FVELTESgdyveareiLDQLEEELAALEQIMEEIPELLKELQTELPD---QLQEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 344 EEQNARLKDA---------LVRMRDLssseKQEHVKLQKLMEkkNQELEVVRQQRERLQEELSQ--------------AE 400
Cdd:PRK04778 236 KAGYRELVEEgyhldhldiEKEIQDL----KEQIDENLALLE--ELDLDEAEEKNEEIQERIDQlydilerevkarkyVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 401 STIDELKEQVDAAlgaEEMVEML---TDR-------NLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLD 470
Cdd:PRK04778 310 KNSDTLPDFLEHA---KEQNKELkeeIDRvkqsytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 471 MAGARVREAQKRVEAAQETVADY-------QQTIKKYRQLtahLQDVNREltnqqeasVERQQQPP-PEtfDFKIKFAET 542
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNK---LHEIKRY--------LEKSNLPGlPE--DYLEMFFEV 453
|
410 420 430
....*....|....*....|....*....|..
gi 205277392 543 KAHAKAIEMEL--RQMEVAQANRHMSLLTAFM 572
Cdd:PRK04778 454 SDEIEALAEELeeKPINMEAVNRLLEEATEDV 485
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
194-409 |
2.20e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEqvqewksKMQEQQADLQRRLKEARKEAKEaLEAKERY 273
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE---ELE-------ELEAALRDLESRLGDLKKERDE-LEAQLRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqLKQLEEQNARLKDA 353
Cdd:TIGR02169 901 LE------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--------LEDVQAELQRVEEE 966
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 354 LVRMRDLSSSEKQEHvklqKLMEKKNQELEvvrQQRERLQEELSQAESTIDELKEQ 409
Cdd:TIGR02169 967 IRALEPVNMLAIQEY----EEVLKRLDELK---EKRAKLEEERKAILERIEEYEKK 1015
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-534 |
2.37e-05 |
|
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: 48.81 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 206 DLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEW---KSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadTAD 282
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltqKREAQEEQLKKQQLLKQLRARIEE-LRAQEAVLEE---TQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 AIEMATLDKEMAEEraeslQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlkdalvrmRDLSS 362
Cdd:TIGR00618 285 RINRARKAAPLAAH-----IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----------RRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 363 SEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAES-TIDELKEQVDAALGAEEMVEMLTDRNLNLEEkvRELRETV 441
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 442 GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEAS 521
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330
....*....|...
gi 205277392 522 VERQQQPPPETFD 534
Cdd:TIGR00618 507 CGSCIHPNPARQD 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
866-1023 |
2.61e-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: 48.90 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 866 YECLRQSCNILISTMNKLATAMQEGEYDAERPPSKPPPVELRAAALRAEItdaEGLGLKLEDRETVIKELKKSLKIKGEE 945
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL---YALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 946 LSEANVRLSLLEKKLDSAAKDA---DERIEKVQTRLEETQALL---RKKEKEFEETMDALQADIDQLEAEKAELKQRLNS 1019
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELaelEEKLEELKEELESLEAELeelEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
....
gi 205277392 1020 QSKR 1023
Cdd:TIGR02168 398 LNNE 401
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
241-404 |
2.78e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.17 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 241 WKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAiematLDKEMAEERAESLQQEVEALKERVDELTTDLE 320
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-----QQRQEARREREELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 321 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQehvklQKLMEKKNQELEVVRQQRERLQEELSQAE 400
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR-----KLLLKLLDAELEEEKAQRVKKIEEEADLE 173
|
....
gi 205277392 401 STID 404
Cdd:PRK12705 174 AERK 177
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
195-492 |
3.01e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLK-RAEDKAKLKELEKHKIQLEQVQEWKSKMqEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEMLRKVVEELTAKKMTLESSERT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMAT-------------LDKEMAE--------ERAESLQQEVEALKERVDELTTDLEILKAEIE----- 327
Cdd:pfam15921 498 VSDLTASLQEKERAIeatnaeitklrsrVDLKLQElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtql 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 328 --EKGSDGAASSYQLKQLEEQ--NARL-----------KDALVRMRDLSSSEKQ-EHVKLQKLMEKKNQELEVVRQQRER 391
Cdd:pfam15921 578 vgQHGRTAGAMQVEKAQLEKEinDRRLelqefkilkdkKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 392 LQEELSQAESTIDELKEQVDAAL-----GAEEMvEMLTDR-NLNLEEKVRELRETVGDLEAMNEMNDelqeNARETELEL 465
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEM-ETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDG----HAMKVAMGM 732
|
330 340
....*....|....*....|....*..
gi 205277392 466 REQLDMAGARVREAQKRVEAAQETVAD 492
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTN 759
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
250-525 |
3.29e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 250 ADLQRRLKEArKEAKEALEAKERYMEEMADTadaieMATLDK-EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 328
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQT-----LALLDKiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 329 KgSDGAASSYQLKQLEEQNARLKDALvrmrdlsssekQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 408
Cdd:PRK11281 113 E-TRETLSTLSLRQLESRLAQTLDQL-----------QN---AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 409 QVDAALGAEEmvemltdrNLNLEEKVRELRETVGdLEAMNEMN-DELQENARETELeLREQLDMAGARVREAQKRVEAAQ 487
Cdd:PRK11281 178 LLKGGKVGGK--------ALRPSQRVLLQAEQAL-LNAQNDLQrKSLEGNTQLQDL-LQKQRDYLTARIQRLEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 205277392 488 ETV-----ADYQQTIKKYRQltahLQDVNRELTN---QQEASVERQ 525
Cdd:PRK11281 248 EAInskrlTLSEKTVQEAQS----QDEAARIQANplvAQELEINLQ 289
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
256-411 |
3.36e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 256 LKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEeraesLQQEVEALKERVDElttdleiLKAEIEEKgsdgaa 335
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR-----LEEQVERLEAEVEE-------LEAELEEK------ 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 336 ssyqlkqlEEQNARLKDALVRMRdlsSSEKQEHvklqklmeKKNQELEVVRQQRERLQEELSQAESTIDELKEQVD 411
Cdd:COG2433 440 --------DERIERLERELSEAR---SEERREI--------RKDREISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
195-468 |
3.41e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEK-------LETLR--LKRAEDKAKLKeLEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEake 265
Cdd:pfam05483 527 KQEERMLKQIENLEEKemnlrdeLESVReeFIQKGDEVKCK-LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 266 aLEAKERYMEEMADTADAIEmatldkemAEERAESLQQEVEALKerVDELTTDLEILKAEIEEKgSDGAASSYQLKQLEE 345
Cdd:pfam05483 603 -IENKNKNIEELHQENKALK--------KKGSAENKQLNAYEIK--VNKLELELASAKQKFEEI-IDNYQKEIEDKKISE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 346 QNarlkdaLVRMRDLSSSEKQEHVKLQKLMEKKNQE--------LEVVRQQRERLQEElSQAESTIDELKEQVDAALGAE 417
Cdd:pfam05483 671 EK------LLEEVEKAKAIADEAVKLQKEIDKRCQHkiaemvalMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKAA 743
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 205277392 418 EMVEMLTDRNlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQ 468
Cdd:pfam05483 744 LEIELSNIKA--------ELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
200-517 |
3.46e-05 |
|
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: 48.20 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLK---RAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQA---DLQRRLKEAR------------- 260
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAripELEKELERLRehnkhlnenienk 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 261 ---KEAKEALEAKERYMEEMADTADAIEM--------------------ATLDKEMA-EERAESLQQEVEALKERVDELT 316
Cdd:pfam05557 224 lllKEEVEDLKRKLEREEKYREEAATLELekekleqelqswvklaqdtgLNLRSPEDlSRRIEQLQQREIVLKEENSSLT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 317 TDLEILKAEIEEKGSDGAAssyQLKQLEEQNARLK--DALVRM-----------RDL----------------SSSEKQE 367
Cdd:pfam05557 304 SSARQLEKARRELEQELAQ---YLKKIEDLNKKLKrhKALVRRlqrrvllltkeRDGyrailesydkeltmsnYSPQLLE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 368 HVK-LQKLMEKKNQELEVVRQQRERLQEEL-------SQAESTIDELKEQVDAA--LGAEEMVEMLTDRNLNLEEKVREL 437
Cdd:pfam05557 381 RIEeAEDMTQKMQAHNEEMEAQLSVAEEELggykqqaQTLERELQALRQQESLAdpSYSKEEVDSLRRKLETLELERQRL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 438 RETVGDLEA---------MNEMND----ELQEN----ARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTI--- 497
Cdd:pfam05557 461 REQKNELEMelerrclqgDYDPKKtkvlHLSMNpaaeAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTstm 540
|
410 420
....*....|....*....|..
gi 205277392 498 --KKYRQLTAHLQDvnRELTNQ 517
Cdd:pfam05557 541 nfKEVLDLRKELES--AELKNQ 560
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
207-531 |
4.18e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 48.02 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 207 LEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTAD-AIE 285
Cdd:pfam15818 9 LLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQlATE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 286 MATLDKEMAEERAESLQQEVEALKERVDELTTDLEI--LKAEIEEKGSDGAASSY-----QLKQLEEQNARL----KDAL 354
Cdd:pfam15818 89 IKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLhlLAKEDHHKQLNEIEKYYatitgQFGLVKENHGKLeqnvQEAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 355 VRMRDLSS-SEKQE--------------------HVKLQKLMEKKNQELEVVRQQRERLQEELS---------QAEST-I 403
Cdd:pfam15818 169 QLNKRLSAlNKKQEseicslkkelkkvtsdliksKVTCQYKMGEENINLTIKEQKFQELQERLNmelelnkkiNEEIThI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 404 DELKEQVDAALG-AEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAgarVREAQKR 482
Cdd:pfam15818 249 QEEKQDIIISFQhMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA---LGTWKKH 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 205277392 483 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPE 531
Cdd:pfam15818 326 VEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPE 374
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
195-519 |
4.75e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 47.34 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRlkRAEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELR--RRDQKRQETLERERRLLLQQSQEqWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEKGSDgAASSYQLKQLEEQNarlkda 353
Cdd:pfam15558 96 WREQAEDQENQRQEKLERARQEAEQRKQCQE-QRLKEKEEELQALREQNSLQLQERLEE-ACHKRQLKEREEQK------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 354 lvRMRDLSSSEKQEHVKLQKLMEKKNQElevvrqqrERLQEELSQaestidELKEQVdaalgAEEMVEMLtdrnlnLEEK 433
Cdd:pfam15558 168 --KVQENNLSELLNHQARKVLVDCQAKA--------EELLRRLSL------EQSLQR-----SQENYEQL------VEER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 434 VRELREtvgdlEAMNEmNDELQENARETELELREQLDMAGARVREAQKRVE----AAQETVADYQQTIKKYRQLTAHLQD 509
Cdd:pfam15558 221 HRELRE-----KAQKE-EEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqarqVAHKTVQDKAQRARELNLEREKNHH 294
|
330
....*....|
gi 205277392 510 VNRELTNQQE 519
Cdd:pfam15558 295 ILKLKVEKEE 304
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
200-444 |
4.77e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHkiqleqVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 279
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 tadaiematLDKEMaEERAESLQ---QEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALVR 356
Cdd:PHA02562 246 ---------LVMDI-EDPSAALNklnTAAAKIKSKIEQFQKVIKMYE--------KGGVCPTCTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 357 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTDRNLNLEEKVR 435
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNKISTNKQSLITLVDKAKKVKAAiEELQAEFVDNAEELAKLQD 386
|
....*....
gi 205277392 436 ELRETVGDL 444
Cdd:PHA02562 387 ELDKIVKTK 395
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
200-448 |
4.85e-05 |
|
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: 47.86 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMAD 279
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEK---KLKNLEAELLQLQEDLAASERARRQAQQERDEL--ADEIASGASGK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 TADAIEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 357
Cdd:pfam01576 878 SALQDEKRRLEARIAqlEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 358 RDLSSSEKQEHV-----KLQKLMEKKNQEL-------EVVRQQRERLQEELSQAES---TIDELKEQVDAALGA------ 416
Cdd:pfam01576 958 EGTVKSKFKSSIaaleaKIAQLEEQLEQESrerqaanKLVRRTEKKLKEVLLQVEDerrHADQYKDQAEKGNSRmkqlkr 1037
|
250 260 270
....*....|....*....|....*....|....
gi 205277392 417 --EEMVEMLTDRNLNLEEKVRELRETVGDLEAMN 448
Cdd:pfam01576 1038 qlEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
194-527 |
4.99e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.91 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKlkELEKHKIQLEQVQEWKSK--------MQEQQADLQRRLKEARKEAKE 265
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 266 ALEAKERYMEEMA---DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKaeieekgsdgaassyqlKQ 342
Cdd:pfam12128 438 EEYRLKSRLGELKlrlNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR-----------------KR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 343 LEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM 422
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 423 LTDRNLNLEEKVRELRETVGDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETvadYQQTIKK 499
Cdd:pfam12128 578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEalqSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLD 654
|
330 340 350
....*....|....*....|....*....|..
gi 205277392 500 YRQLTAHLQD----VNRELTNQQEASVERQQQ 527
Cdd:pfam12128 655 LRRLFDEKQSekdkKNKALAERKDSANERLNS 686
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
194-400 |
5.00e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRlkraedkaklkelEKHKIqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFR-------------QKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAE--SLQQEVEALKER-------VDELTTDLEILKAEIEEKGSDGAASSY-QLKQL 343
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 205277392 344 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQRERLQEELSQAE 400
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRL----EREVEVARELYESLLQRLEEAR 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
196-474 |
5.35e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETlRLKRAEDkaklkELEKHKIQLEQVQEwkskmQEQQAdLQRR--LKEARKEAKEALEAKERY 273
Cdd:COG3096 974 DAVGLLGENSDLNEKLRA-RLEQAEE-----ARREAREQLRQAQA-----QYSQY-NQVLasLKSSRDAKQQTLQELEQE 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIematldkemAEERAES----LQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLKQLEEQNAR 349
Cdd:COG3096 1042 LEELGVQADAE---------AEERARIrrdeLHEELSQNRSRRSQLEKQLTRCEAEMDS-------LQKRLRKAERDYKQ 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 350 LKDALVrmrdlssSEKQEHVKLQKLMEKKNQELEVVRQqrerlqeELSQAEStiDELKEQVDAALGAEEMV----EMLTD 425
Cdd:COG3096 1106 EREQVV-------QAKAGWCAVLRLARDNDVERRLHRR-------ELAYLSA--DELRSMSDKALGALRLAvadnEHLRD 1169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 426 rNLNLEE-------KV-------RELRE--------TVGDLEAMNEMNDELqenARET-ELELREQlDMAGA 474
Cdd:COG3096 1170 -ALRLSEdprrperKVqfyiavyQHLRErirqdiirTDDPVEAIEQMEIEL---ARLTeELTSREQ-KLAIS 1236
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
196-409 |
6.03e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKH--KIQLEQVqewksKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARvsDLELEKV-----KLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDG-------------AASSYQ 339
Cdd:pfam15921 666 RNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmEGSDGhamkvamgmqkqiTAKRGQ 742
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277392 340 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME----KKNQ---ELEVVRQQRERLQEELSQAESTIDELKEQ 409
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvatEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
196-527 |
6.08e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDK--AKLKELEKHKiqleQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE----------IEEKGSDGAASSYQLK-- 341
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlqrsmstqkaLEEDLQIATKTICQLTee 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 342 ---QLEEQN-ARLKDALVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---------- 407
Cdd:pfam05483 333 keaQMEELNkAKAAHSFV-----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkevel 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 408 EQVDAALGAEemvEMLTDRNLNLEEKVRELR----ETVGDLEAM-NEMND-ELQENARETELE--LREQLDMAGARVREA 479
Cdd:pfam05483 408 EELKKILAED---EKLLDEKKQFEKIAEELKgkeqELIFLLQAReKEIHDlEIQLTAIKTSEEhyLKEVEDLKTELEKEK 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 205277392 480 QKRVeaaqETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 527
Cdd:pfam05483 485 LKNI----ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
195-527 |
6.48e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDK--AKLKELEKHKIQLEQVQEWKSKMQ---EQQADLQRRLkEARKE---AKEA 266
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENRMTLEAIRvtQSDRDLFKHLITESTNYVAADYMRhanERRVHLEEAL-ELRRElytSRRQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 267 LEAKERYMEEMADTADAIematldkemaEERAESLQQEVEALKERVDELTTDLeILKAEIEEKGSDGAASSYqlkQLEEQ 346
Cdd:PRK04863 302 LAAEQYRLVEMARELAEL----------NEAESDLEQDYQAASDHLNLVQTAL-RQQEKIERYQADLEELEE---RLEEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 347 NARLKDA--LVRMRDLSSSEKQEHVK-LQKLMEKKNQELEVvrQQRERLQEElsQAESTIDELKEQVD----AALGAEEM 419
Cdd:PRK04863 368 NEVVEEAdeQQEENEARAEAAEEEVDeLKSQLADYQQALDV--QQTRAIQYQ--QAVQALERAKQLCGlpdlTADNAEDW 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 420 VEMLTDRNLNLEEKVRELRETVGDLEAMNEMND----------------ELQENARETELELREQLDMAG------ARVR 477
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrsEAWDVARELLRRLREQRHLAEqlqqlrMRLS 523
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 478 EAQKRVE---AAQETVADYQQTIKK-----------YRQLTAHLQDVNRELTNQQE-ASVERQQQ 527
Cdd:PRK04863 524 ELEQRLRqqqRAERLLAEFCKRLGKnlddedeleqlQEELEARLESLSESVSEARErRMALRQQL 588
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
263-416 |
7.06e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.21 E-value: 7.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 263 AKEALEAKERYMEEMADTADAIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaas 336
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEELEEakktikALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK-------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 337 syQLKQLEEQNARLKDALvrMRDLSSSEKQEHVKLQKLMEKKNQEL------------------EVVRQQRERLQEELSQ 398
Cdd:cd22656 154 --DQTALETLEKALKDLL--TDEGGAIARKEIKDLQKELEKLNEEYaaklkakidelkaliaddEAKLAAALRLIADLTA 229
|
170
....*....|....*...
gi 205277392 399 AESTIDELKEQVDAALGA 416
Cdd:cd22656 230 ADTDLDNLLALIGPAIPA 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
195-558 |
7.14e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRaedkaklkelekhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 274
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMER-----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEieekgSDGAASSYQLKQLEEQNARLKDAL 354
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 355 VRMRDlsssekqehvKLQKLMEKKNQELEVVRQQ-RERLQEELSQAESTIDELKEQVDAALGA--------EEMVEMLTD 425
Cdd:pfam15921 241 FPVED----------QLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGLTEKASSARSQansiqsqlEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 426 RNLNLEEKVRELRETVGDLEAmnemndELQENARETE---LELREQLDMAGARVREAqkRVEAAQETvadyQQTIKKYRQ 502
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRS------ELREAKRMYEdkiEELEKQLVLANSELTEA--RTERDQFS----QESGNLDDQ 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 503 LTAHLQDVNREltnQQEASVERQQQppPETFDFKIKFAETKAHAKAiEMELRQMEV 558
Cdd:pfam15921 379 LQKLLADLHKR---EKELSLEKEQN--KRLWDRDTGNSITIDHLRR-ELDDRNMEV 428
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
208-516 |
7.25e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 208 EEKLETLRLKRAE----------DKAKLKELEKHKIQL--EQVQEW--------KSKMQEQQADLQRRLKEARKEAKEAL 267
Cdd:COG3096 784 EKRLEELRAERDElaeqyakasfDVQKLQRLHQAFSQFvgGHLAVAfapdpeaeLAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 268 EAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELT------TDLEILKAEIEEKGSDGAASSYQL 340
Cdd:COG3096 864 QQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQAFIQqhgkalAQLEPLVAVLQSDPEQFEQLQADY 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 341 KQLEEQNARLKDALVRMRDLssSEKQEHVKLQKL--MEKKNQELEvvrqqrERLQEELSQAESTIDELKEQVDAALG-AE 417
Cdd:COG3096 944 LQAKEQQRRLKQQIFALSEV--VQRRPHFSYEDAvgLLGENSDLN------EKLRARLEQAEEARREAREQLRQAQAqYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 418 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMND-ELQENARETELELREQLDMAGARVREAQK---RVEAAQETVAdy 493
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEELGVQADaEAEERARIRRDELHEELSQNRSRRSQLEKqltRCEAEMDSLQ-- 1093
|
330 340
....*....|....*....|...
gi 205277392 494 qqtiKKYRQLTAHLQDVNRELTN 516
Cdd:COG3096 1094 ----KRLRKAERDYKQEREQVVQ 1112
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
208-348 |
8.30e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 208 EEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMADTADAIEMA 287
Cdd:PRK09510 86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA--AKAKAEAEAKRAAAAAKKA 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 288 TLDKEMAEERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAASSYQLKQLEEQNA 348
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-----KAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
904-1017 |
9.03e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 904 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLE----------KKLDSAAKDADERIEK 973
Cdd:TIGR02169 376 VDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieakiNELEEEKEDKALEIKK 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 205277392 974 VQTRLEETQALLRKKEKEFEetmdALQADIDQLEAEKAELKQRL 1017
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELY----DLKEEYDRVEKELSKLQREL 492
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
234-329 |
9.36e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 44.01 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 234 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTA--DAIEMATLDKEMAEERAESLQQE-VEALKE 310
Cdd:COG0711 39 GLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAkaEAEAEAERIIAQAEAEIEQERAKaLAELRA 118
|
90 100
....*....|....*....|.
gi 205277392 311 RVDELTTDL--EILKAEIEEK 329
Cdd:COG0711 119 EVADLAVAIaeKILGKELDAA 139
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
372-563 |
9.94e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 372 QKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEmn 451
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 452 dELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 531
Cdd:COG4942 94 -ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---- 168
|
170 180 190
....*....|....*....|....*....|..
gi 205277392 532 tfdFKIKFAETKAHAKAIEMELRQMEVAQANR 563
Cdd:COG4942 169 ---LEAERAELEALLAELEEERAALEALKAER 197
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
283-512 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 AIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqLKQLEEQNARLKDALVR 356
Cdd:COG4717 45 AMLLERLEKEADElfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEE-----------LEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 357 MRdlsssekQEHVKLQKLmekknQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnlnLEEKVRE 436
Cdd:COG4717 114 LR-------EELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 437 LRETVgdleamnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNR 512
Cdd:COG4717 179 LEELL----------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
224-465 |
1.11e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.39 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 224 KLKELEKHKIQLEQvqewKSKMQEQQADLQRRLKEA--RKEAKEALEA-KERYMEEMADTADaiemaTLDKEMAEErAES 300
Cdd:PLN03229 539 MLNEFSRAKALSEK----KSKAEKLKAEINKKFKEVmdRPEIKEKMEAlKAEVASSGASSGD-----ELDDDLKEK-VEK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 301 LQQEVEA-LKERVDELTTDLEILKAEIEEKGSDGAASSYQLK--QLEEQNARLKDALVRMRDLSSSekqehVKLQKLmek 377
Cdd:PLN03229 609 MKKEIELeLAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKieSLNEEINKKIERVIRSSDLKSK-----IELLKL--- 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 378 knqelEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdRNLNLEEKVRELRETVGDLEAMNEMNDELQEN 457
Cdd:PLN03229 681 -----EVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKE----KFEELEAELAAARETAAESNGSLKNDDDKEED 751
|
....*...
gi 205277392 458 ARETELEL 465
Cdd:PLN03229 752 SKEDGSRV 759
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
194-312 |
1.15e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.61 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEE-EGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAker 272
Cdd:COG0542 438 SFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--- 514
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 205277392 273 ymeemADTADAIEMAT---LDKeMAEERAESLQQEVEALKERV 312
Cdd:COG0542 515 -----EDIAEVVSRWTgipVGK-LLEGEREKLLNLEEELHERV 551
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
229-526 |
1.16e-04 |
|
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: 46.76 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 229 EKHKIQLEQVQEWkskMQEQQAdLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMATLDKE-MAEERAESLQQEveA 307
Cdd:pfam12128 214 PKSRLNRQQVEHW---IRDIQA-IAGIMKIRPEFTKLQQEFNTLESAEL-------RLSHLHFGyKSDETLIASRQE--E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 308 LKERVDELTTDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDAlvrmrDLSSSEKQEHVKLqkLMEKKNQELEVVRQ 387
Cdd:pfam12128 281 RQETSAELNQLLRTLDDQWKEK-------------RDELNGELSAA-----DAAVAKDRSELEA--LEDQHGAFLDADIE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 388 QRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--EEKVRELRETVGDLEAMNEMNDELQENARET---- 461
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqal 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 462 ELELREQLDMAGARVREAQKRVEAAQET----VADYQQTIKKYRQLTAHLQDVN--RELTNQQEASVERQQ 526
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGElklrLNQATATPELLLQLENFDERIEraREEQEAANAEVERLQ 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
386-546 |
1.22e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 386 RQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnLNL-------EEKVRELREtvgDLEAMNEMNDElQENA 458
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrqQEKIERYQE---DLEELTERLEE-QEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 459 REtelELREQLDMAGARVREAQKRVEAAQETVADYQQTIK-------KYRQLTAHLQDVNR-----ELT-----NQQEAS 521
Cdd:COG3096 370 VE---EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARAlcglpDLTpenaeDYLAAF 446
|
170 180
....*....|....*....|....*
gi 205277392 522 VERQQQPPPETFDFKIKFAETKAHA 546
Cdd:COG3096 447 RAKEQQATEEVLELEQKLSVADAAR 471
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
200-469 |
1.31e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKL-----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 274
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLeilkaeieekgsdgaasSYQLKQLEEQNARL 350
Cdd:pfam00038 103 NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheEEVRELQAQV-----------------SDTQVNVEMDAARK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 351 KDALVRMRDLSSS-EKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLN 429
Cdd:pfam00038 166 LDLTSALAEIRAQyEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQ-SLEIE--LQSLKKQKAS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 205277392 430 LEEKVRELRET-VGDLEAMNEMNDELQENARETELELREQL 469
Cdd:pfam00038 243 LERQLAETEERyELQLADYQELISELEAELQETRQEMARQL 283
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
207-482 |
1.43e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.68 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 207 LEEKLETLRLKRAEDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadta 281
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEEreralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 282 daieMATLDKEMAEERAESLQQ--EVEALKERVDELTTDLEILKAE--IEEKGSDGAASSYQLKQLEEQNARLKdalvRM 357
Cdd:pfam13868 104 ----DEIVERIQEEDQAEAEEKleKQRQLREEIDEFNEEQAEWKELekEEEREEDERILEYLKEKAEREEEREA----ER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 358 RDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDE-LKEQVDAALGAEEMVEMLTDRNLNLEEKVRE 436
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDE----KAERDELRAKLYQEEQERKErQKEREEAEKKARQRQELQQAREEQIELKERR 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 205277392 437 LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKR 482
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
223-351 |
1.54e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 43.01 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 223 AKLKELEKHKIQLEQVQEwkskmqEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLdkemAEERAESLQ 302
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAA------DAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQA----LREELNELK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 205277392 303 QEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLK 351
Cdd:pfam07926 71 AEIAELKAEAESAKAELEESEESWEE----------QKKELEKELSELE 109
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
370-527 |
1.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 370 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlNLEEKVRELRETVGDLEAMNE 449
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 450 MNDELQENAretelELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 527
Cdd:COG4717 127 LLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
925-1015 |
1.80e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 925 LEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADE----RIEKVQTRLEETQALLRKKEKEFEETMDALQ 1000
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAELEELEKRREEIK 693
|
90
....*....|....*
gi 205277392 1001 ADIDQLEAEKAELKQ 1015
Cdd:PRK03918 694 KTLEKLKEELEEREK 708
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
216-520 |
1.84e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.79 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 216 LKRAEDkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE--ARKEAKEALEAKERYMEEMADTADAIEMATLDKEM 293
Cdd:pfam05701 228 LKQAEE-----ELQRLNQQLLSAKDLKSKLETASALLLDLKAElaAYMESKLKEEADGEGNEKKTSTSIQAALASAKKEL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 294 AEERA--ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD--ALVRMRDLSSSEKQehV 369
Cdd:pfam05701 303 EEVKAniEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAVSSLEAELNRTKSeiALVQAKEKEAREKM--V 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 370 KLQKLMEKKNQELE----VVRQQRERL---QEELSQA-------ESTIDELKEQVDAALGAEEMVemLTDRNLNLEEKVR 435
Cdd:pfam05701 381 ELPKQLQQAAQEAEeaksLAQAAREELrkaKEEAEQAkaaastvESRLEAVLKEIEAAKASEKLA--LAAIKALQESESS 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 436 ELRETVGDLEAM----NEMNDELQENARETElelreqlDMAGARVREAQKRVEAAQETvadyqqtikKYRQLtAHLQDVN 511
Cdd:pfam05701 459 AESTNQEDSPRGvtlsLEEYYELSKRAHEAE-------ELANKRVAEAVSQIEEAKES---------ELRSL-EKLEEVN 521
|
....*....
gi 205277392 512 RELTNQQEA 520
Cdd:pfam05701 522 REMEERKEA 530
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
236-474 |
1.85e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.84 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 236 EQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERY---MEEMaDTAD--AIEMATLDKEM-----AEERAESLQQEV 305
Cdd:COG0497 155 ELLEEYREAYRAWRA-LKKELEELRADEAERARELDLLrfqLEEL-EAAAlqPGEEEELEEERrrlsnAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 306 EALKERVDELTTDLEILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMRDLSSS------------EKQEHV---- 369
Cdd:COG0497 233 EALSGGEGGALDLLGQALRALER------LAEYD-PSLAELAERLESALIELEEAASElrryldslefdpERLEEVeerl 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 370 -KLQKLMEKKNQELEVVRQQRERLQEELSQ---AESTIDELKEQVDAALGAeemvemltdrnlnLEEKVREL----RETV 441
Cdd:COG0497 306 aLLRRLARKYGVTVEELLAYAEELRAELAElenSDERLEELEAELAEAEAE-------------LLEAAEKLsaarKKAA 372
|
250 260 270
....*....|....*....|....*....|....*...
gi 205277392 442 GDLEAmnEMNDELQ----ENAR-ETELELREQLDMAGA 474
Cdd:COG0497 373 KKLEK--AVTAELAdlgmPNARfEVEVTPLEEPGPNGA 408
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
207-322 |
1.87e-04 |
|
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439986 [Multi-domain] Cd Length: 356 Bit Score: 45.38 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 207 LEEKLETLrlkraedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 274
Cdd:COG0216 2 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKKLLEDIEEA-------- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 205277392 275 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 322
Cdd:COG0216 63 KELLEEESDPEM----REMAKE-------ELEELEARLEELEEELKIL 99
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
200-418 |
1.88e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETL--RLKRAEDKaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALEAKERYMEEM 277
Cdd:pfam12128 313 ADAAVAKDRSELEALedQHGAFLDA----DIETAAADQEQLPSWQSELENLEERL-----KALTGKHQDVTAKYNRRRSK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 ADTADAIEMATLDKEMA---EERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLK-QLEEQNARLKDA 353
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLAkirEARDRQLAVAEDDLQALESELREQLEAGKLEFNE-------EEYRLKsRLGELKLRLNQA 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 205277392 354 LVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAestiDELKEQVDAALGAEE 418
Cdd:pfam12128 457 TA-----TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA----RKRRDQASEALRQAS 512
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
299-409 |
2.07e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 299 ESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGAASSYQlKQLEEQNARLKdALVRMRDLSSSEKQEHVKLQKLME 376
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNYE-RELVLHAEDIK-ALQALREELNELKAEIAELKAEAE 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 205277392 377 KKNQELEVVR----QQRERLQEELSQAESTIDELKEQ 409
Cdd:pfam07926 82 SAKAELEESEesweEQKKELEKELSELEKRIEDLNEQ 118
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
321-516 |
2.87e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 321 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAE 400
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 401 STIDE--------------LKEQVDAALG--------------------AEEMVEMLTDRNLNLEEKVRELRETVGDLEA 446
Cdd:PHA02562 248 MDIEDpsaalnklntaaakIKSKIEQFQKvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277392 447 -MNEMND---ELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNRELTN 516
Cdd:PHA02562 328 iMDEFNEqskKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-557 |
2.96e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 382 LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----EEKVRELRETVGDLEAMNEMNDELQE 456
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 457 NARETELELrEQLDmagARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP------- 529
Cdd:TIGR02168 261 ELQELEEKL-EELR---LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldela 336
|
170 180 190
....*....|....*....|....*....|....*
gi 205277392 530 -------PETFDFKIKFAETKAHAKAIEMELRQME 557
Cdd:TIGR02168 337 eelaeleEKLEELKEELESLEAELEELEAELEELE 371
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
886-1019 |
3.53e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 886 AMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKgeeLSEANVRLSLLEKKLDSaak 965
Cdd:TIGR02169 654 AMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKIGEIEKEIEQ--- 727
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 205277392 966 dADERIEKVQTRLEETQALLRKKEKEFEE---TMDALQADIDQLEAEKAELKQRLNS 1019
Cdd:TIGR02169 728 -LEQEEEKLKERLEELEEDLSSLEQEIENvksELKELEARIEELEEDLHKLEEALND 783
|
|
| CASP_C |
pfam08172 |
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ... |
294-435 |
3.71e-04 |
|
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.
Pssm-ID: 462392 [Multi-domain] Cd Length: 247 Bit Score: 43.81 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 294 AEERAESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGA-ASSYQLKQLEEQNARLKDALVrmrdLSSSEKQEHVK 370
Cdd:pfam08172 2 LQEELSSLNAELEEQQELNAKLENDLLKVQDEASNafSFNDASsAGSGVSRYPPSGGRRSPTSSI----ISGFEPSESSS 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 371 LQKlmekkNQELEVVRQQRER-------LQEELSQAESTIDELKEQVDAalgaeemveMLTDrNLNLEEKVR 435
Cdd:pfam08172 78 SSD-----SSILPIVTSQRDRfrqrnaeLEEELRKQFETISSLRQEIAS---------LQKD-NLKLYEKTR 134
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
214-491 |
3.84e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 214 LRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEM 293
Cdd:pfam05701 126 LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 294 AEER----AESLQQEVEALKERVDELTTDLEILKAEI----EEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEK 365
Cdd:pfam05701 206 AEEHrigaALAREQDKLNWEKELKQAEEELQRLNQQLlsakDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEK 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 366 QEHVKLQKLMEKKNQELEVVRQQRER--------------LQEELSQAESTIDELKEQVDAALGAEemvemltdrnLNLE 431
Cdd:pfam05701 286 KTSTSIQAALASAKKELEEVKANIEKakdevnclrvaaasLRSELEKEKAELASLRQREGMASIAV----------SSLE 355
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 432 EkvrELRETVGDLEAMNEMNDElqenARETELELREQLDMAGARVREAQKRVEAAQETVA 491
Cdd:pfam05701 356 A---ELNRTKSEIALVQAKEKE----AREKMVELPKQLQQAAQEAEEAKSLAQAAREELR 408
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
905-1023 |
3.97e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 905 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSaakdADERIEKVQTRLEETQAL 984
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANE 296
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 205277392 985 LRKKEKEFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1023
Cdd:TIGR02168 297 ISRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEE 338
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
177-402 |
4.11e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 177 PTPVLTSPGAVPPLPSPSKEE--EGLRAQVRDLEEKLETLRLKRAEDKA-----KLKELEKHKIQLEQVQEWKSKMQEQQ 249
Cdd:pfam15709 299 PTQTFVVTGNMESEEERSEEDpsKALLEKREQEKASRDRLRAERAEMRRleverKRREQEEQRRLQQEQLERAEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 250 ADLQRRLKEARKEAKEALEAKERYMEEMAdtadaiEMATLDKEMAEERAESLQQEVEalkervdelTTDLEILKAEIEEK 329
Cdd:pfam15709 379 ELEQQRRFEEIRLRKQRLEEERQRQEEEE------RKQRLQLQAAQERARQQQEEFR---------RKLQELQRKKQQEE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 330 GSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEhvKLQKLMEKKNQELEvVRQQRERLQEELSQAEST 402
Cdd:pfam15709 444 AERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQR--QKQEAEEKARLEAE-ERRQKEEEAARLALEEAM 513
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
237-556 |
4.15e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 237 QVQEWKSKMQEQQADLQRRLKEARKEAKEaleaKERYMEEMADTAD--AIEMATLDKEMAE--ERAESLQQEVEALKERV 312
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKK----KEKRRDEMLGLAPgrQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 313 DELTTDLEILKAEiEEKGSDGAASSYQLKQLEEQnarLKDALVRMRDL-----SSSEKQEHVKLQKLMEKKNQELEVVRQ 387
Cdd:TIGR00606 768 EEQETLLGTIMPE-EESAKVCLTDVTIMERFQME---LKDVERKIAQQaaklqGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 388 QRERLQEELSQAESTIDELKEQVDaALGAEEM-VEMLTDRNLNLEEKVRELRETVgdleamNEMNDELQEnARETELELR 466
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTN-ELKSEKLqIGTNLQRRQQFEEQLVELSTEV------QSLIREIKD-AKEQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 467 EQLDMAGARVREAQKRVEAAQETVADYQQTIK-KYRQLTAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAH 545
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKeKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKH 992
|
330
....*....|.
gi 205277392 546 AKAIEMELRQM 556
Cdd:TIGR00606 993 QEKINEDMRLM 1003
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
217-346 |
4.25e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 217 KRAEDKAKLKELE------KHKIQLEQ-VQEWKSKMQEQQADLQRRlKEARKEAKEALEAKERYMEEMADTADAiEMATL 289
Cdd:PRK12704 49 KEAEAIKKEALLEakeeihKLRNEFEKeLRERRNELQKLEKRLLQK-EENLDRKLELLEKREEELEKKEKELEQ-KQQEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 290 DKEmaEERAESLQQEVEALKERVDELTTD--LEILKAEIEEKGSDGAASsyQLKQLEEQ 346
Cdd:PRK12704 127 EKK--EEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAV--LIKEIEEE 181
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
187-412 |
4.28e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 187 VPPLPSPSKEEEGLRAQVRDLEEKLetlRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQ---QADLQRRLKEARKEA 263
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEEN---KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkEAEEAKKAEELKKKE 1711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 264 KEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQL 343
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRK----------EKEAV 1780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 344 EEQNARLKDALVRMrDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA 412
Cdd:PTZ00121 1781 IEEELDEEDEKRRM-EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
194-312 |
4.82e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.89 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKlkelekhkiqlEQVQEWKSKMQEQQADLQrrlkeaRKEAKEALEAKERY 273
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKAR-----------AKAAKAQEKVNEALSGID------SDDATSALERMEEK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 205277392 274 MEEMADTADAI-EMA---TLDKEMAE-ERAESLQQEVEALKERV 312
Cdd:COG1842 174 IEEMEARAEAAaELAagdSLDDELAElEADSEVEDELAALKAKM 217
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
194-299 |
4.92e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEalEAKERY 273
Cdd:PRK12704 85 QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ---KQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEIL 159
|
90 100
....*....|....*....|....*.
gi 205277392 274 MEEMADTADAiEMATLDKEMaEERAE 299
Cdd:PRK12704 160 LEKVEEEARH-EAAVLIKEI-EEEAK 183
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
888-1018 |
5.21e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 888 QEGEYDAERPPSKPPPVELRAAALRAEITDA----EGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA 963
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 964 AKD---ADERIEKVQTRLEETQALLRKKEKEFEET-MDALQADIDQLEAEKAELKQRLN 1018
Cdd:TIGR02168 399 NNEierLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELE 457
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
924-1023 |
5.49e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 924 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERI-EKVQTRLEETQALLRKKEkEFEETMDALQAD 1002
Cdd:smart00787 162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIMIKVKKLE-ELEEELQELESK 240
|
90 100
....*....|....*....|.
gi 205277392 1003 IDQLEAEKAELKQRLNSQSKR 1023
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKK 261
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-463 |
5.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 225 LKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAieMATLDKEMAEERAESLQQE 304
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL--LREAEELEEELQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 305 VEALKERVDelTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKlmEKKNQELEV 384
Cdd:COG4717 372 IAALLAEAG--VEDEEELRAALE-----------QAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 385 VRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNlNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 463
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
205-527 |
5.57e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 205 RDLEEKLETLRLKRAEDKAKL--KELEKHKIQL-EQVQEWKSKMQEQQ------ADLQRRLKEARKEAKEALEAKERYME 275
Cdd:PRK10929 82 AELRQQLNNERDEPRSVPPNMstDALEQEILQVsSQLLEKSRQAQQEQdrareiSDSLSQLPQQQTEARRQLNEIERRLQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAIEMATLdkemaeeraESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSYQlKQLEEQNARLKDALV 355
Cdd:PRK10929 162 TLGTPNTPLAQAQL---------TALQAESAALKALVDEL--ELAQLSANNRQELARLRSELAK-KRSQQLDAYLQALRN 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 356 RMRDLSSSEKQEHVKLQKLMEKKNQEL-----EVVRQQRErLQEELSQAESTIDELKEQVDAAlgaeemvemlTDRNLNL 430
Cdd:PRK10929 230 QLNSQRQREAERALESTELLAEQSGDLpksivAQFKINRE-LSQALNQQAQRMDLIASQQRQA----------ASQTLQV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 431 EEKVRELRETVGDLEAMNEMNDELQEN-ARETELELREQLD--MAGARVreaqKRVEaaqetvadYQQTIKKYRQLTAHL 507
Cdd:PRK10929 299 RQALNTLREQSQWLGVSNALGEALRAQvARLPEMPKPQQLDteMAQLRV----QRLR--------YEDLLNKQPQLRQIR 366
|
330 340
....*....|....*....|
gi 205277392 508 QDVNRELTNQQEASVERQQQ 527
Cdd:PRK10929 367 QADGQPLTAEQNRILDAQLR 386
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
195-527 |
5.74e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLR--LKRAEDkAKLK---ELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARK 261
Cdd:pfam01576 685 RSKRALEQQVEEMKTQLEELEdeLQATED-AKLRlevNMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 262 EAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTT---DLEILKAEIEEKGSDGAASSY 338
Cdd:pfam01576 764 QRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAsrdEILAQSKESEKKLKNLEAELL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 339 QLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV-VRQQRERLQEELSQAESTIDELK------EQVD 411
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRkstlqvEQLT 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 412 AALGAEE-MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL-ELREQLD-------MAGARVREAQKR 482
Cdd:pfam01576 924 TELAAERsTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIaQLEEQLEqesrerqAANKLVRRTEKK 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 205277392 483 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 527
Cdd:pfam01576 1004 LKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR 1048
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
207-457 |
6.41e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 207 LEEKLETLRLKRAEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEarkeaKEA-LEAKERYMEEMAD--TADA 283
Cdd:pfam10174 308 LQTKLETLTNQNSDCKQHIEVL---KESLTAKEQRAAILQTEVDALRLRLEE-----KESfLNKKTKQLQDLTEekSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 284 IEMATLdKEM---AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA---RLKDALVRM 357
Cdd:pfam10174 380 GEIRDL-KDMldvKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 358 RDLSSSEKQEHVklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA-ALGAEEMVEMLTDRNLNLEEKVRE 436
Cdd:pfam10174 459 REREDRERLEEL------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKSLEIAVEQKKEE 532
|
250 260
....*....|....*....|.
gi 205277392 437 LRETVGDLEAMNEMNDELQEN 457
Cdd:pfam10174 533 CSKLENQLKKAHNAEEAVRTN 553
|
|
| PCRF |
pfam03462 |
PCRF domain; This domain is found in peptide chain release factors. |
222-315 |
6.84e-04 |
|
PCRF domain; This domain is found in peptide chain release factors.
Pssm-ID: 460929 [Multi-domain] Cd Length: 192 Bit Score: 41.99 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 222 KAKLKELEKhkiQLEQVQEWKSkmqeqQADLQRRLKEaRKEAKEALEAKERYMEEMADTADAIEMATLD--KEMAEERAE 299
Cdd:pfam03462 2 EERYEELEA---LLSDPDVWDD-----QKRAQKLSKE-YSELEPIVEAYREYKQALEDLEEAKELLEDPelAELAEEELE 72
|
90
....*....|....*.
gi 205277392 300 SLQQEVEALKERVDEL 315
Cdd:pfam03462 73 ELEKRLEELEEELKLL 88
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
944-1029 |
7.01e-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: 43.60 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 944 EELSEANVRLSLLEKKLDSAAKDADERIEKVQtRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKR 1023
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
....*.
gi 205277392 1024 TIEGLR 1029
Cdd:COG4942 106 LAELLR 111
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
195-488 |
7.60e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETlrlKRAEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQadlQRRLKEARKEAKEaleakerY 273
Cdd:pfam02029 23 KEEEEPSGQVTESVEPNEH---NSYEEDSELKPSGQGGLDEEEaFLDRTAKREERR---QKRLQEALERQKE-------F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIemATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDGAASSYQlkQLEEQNARLKD 352
Cdd:pfam02029 90 DPTIADEKESV--AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnKWSTEVRQAEE--EGEEEEDKSEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 353 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMV---EMLTDRNLN 429
Cdd:pfam02029 166 AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 430 LEEKVRELRETVGDLEamNEMNDELQENARETELELREQLdmagaRVREAQKRVEAAQE 488
Cdd:pfam02029 246 AEQKLEELRRRRQEKE--SEEFEKLRQKQQEAELELEELK-----KKREERRKLLEEEE 297
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
177-330 |
8.07e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 177 PTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqleqvqewkskmqeqqadlqRRL 256
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLE------------------------REL 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 257 KEARKEAKEALEaKERYMEEMadtadaiematldkemaEERAESLQQEVEALKERVDELTTDLEILKA--EIEEKG 330
Cdd:COG2433 451 SEARSEERREIR-KDREISRL-----------------DREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
197-471 |
9.37e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 197 EEGLrAQVRDLEEKLETLRLKRAEdkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKErymE 275
Cdd:PRK05771 27 ELGV-VHIEDLKEELSNERLRKLR--SLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIE---K 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMadtadaiematldKEMAEERAEsLQQEVEALKERVDELT--TDLEI-LKAEIEEKGSDGAASSYQLKQLEEQNARLKD 352
Cdd:PRK05771 101 EI-------------KELEEEISE-LENEIKELEQEIERLEpwGNFDLdLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 353 ALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAEsTIDELKEQvdaalgaeemvemltdrnl 428
Cdd:PRK05771 167 ENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEE------------------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 205277392 429 nLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDM 471
Cdd:PRK05771 224 -LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEA 265
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
211-510 |
9.83e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 211 LETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKealeAKERYMEEMADTADAIEmATLD 290
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK----SYENELDPLKNRLKEIE-HNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 291 KEMaeeraeSLQQEVEALKERVDELTTDLEILKAEIEE--KGSDgaassYQLKQLEEQNARLkdalvrmrdlSSSEKQEH 368
Cdd:TIGR00606 263 KIM------KLDNEIKALKSRKKQMEKDNSELELKMEKvfQGTD-----EQLNDLYHNHQRT----------VREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 369 VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA--ALGAEEMVEMLTD---RNLNLEEKVRELRETV-- 441
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDgfeRGPFSERQIKNFHTLVie 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 442 ---GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDV 510
Cdd:TIGR00606 402 rqeDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
194-358 |
1.00e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 43.02 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLR----LKRAEdKAKLKELEKHkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE- 268
Cdd:pfam10498 183 SKPREIIESNVDAAEWKLELERvlpqLKVTI-KADAKDWRAH---LEQMKQHKKSIEESLPDTKSQLDKLHTDISKTLEk 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 269 --AKERY----MEEMADtadaiEMATLDKEMAEERaESLQQEVEALKERVDEL---TTDLEILKAEIEEKG---SDGAas 336
Cdd:pfam10498 259 ieSREKYinsqLEPLIQ-----EYREAQDELSEVQ-EKYKQLSEGVTERTRELaeiTEELEKVKQEMEERGssmTDGS-- 330
|
170 180
....*....|....*....|..
gi 205277392 337 syqlkqleeQNARLKDALVRMR 358
Cdd:pfam10498 331 ---------PLVKIKQALTKLK 343
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
207-322 |
1.01e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 42.76 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 207 LEEKLETLrlkraedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 274
Cdd:PRK00591 4 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKQAQEDLEEA-------- 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 205277392 275 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 322
Cdd:PRK00591 65 KEMLEEESDPEM----REMAKE-------ELKELEERLEELEEELKIL 101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
201-345 |
1.01e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 201 RAQVRDLEEKLETLRLKRAEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQ---------RRLKEARKEAKEALEAKE 271
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEA---ELAKKKAEERREAETARAEAEAAYEIAeanaerevqRQLEIAEREREIELQEKE 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 272 RYMEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERvdeLTTDLEILKAEIEEKGSDGAASSYQ--LKQLEE 345
Cdd:COG2268 299 AEREEAELEADVRKPAEAEKQAAEAEAE---AEAEAIRAK---GLAEAEGKRALAEAWNKLGDAAILLmlIEKLPE 368
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
177-441 |
1.10e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 177 PTPVLTSPGAVPPLPSPSKEEEGLRA--QVRDLEEKLETLRLKRAEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQA 250
Cdd:pfam15905 46 DASTPATARKVKSLELKKKSQKNLKEskDQKELEKEIRALVQERGEQDKRLQaleeELEKVEAKLNAAVREKTSLSASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 251 DLQRRLKEArKEAKEALEAKerymeeMADTADAIEMATLDKEMAEERA--ESLQQEVEALKE----RVDELTTDLEILKA 324
Cdd:pfam15905 126 SLEKQLLEL-TRVNELLKAK------FSEDGTQKKMSSLSMELMKLRNklEAKMKEVMAKQEgmegKLQVTQKNLEHSKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 325 EI---EEKGSD----GAASSYQLKQLEEQNARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQrerLQEELS 397
Cdd:pfam15905 199 KVaqlEEKLVStekeKIEEKSETEKLLEYITELSCV----SEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQ 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 205277392 398 QAESTIDELKEQVDAALGA-EEMVEMLTDRNLNLEEKVRELRETV 441
Cdd:pfam15905 272 ELSKQIKDLNEKCKLLESEkEELLREYEEKEQTLNAELEELKEKL 316
|
|
| PRK07994 |
PRK07994 |
DNA polymerase III subunits gamma and tau; Validated |
132-414 |
1.10e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236138 [Multi-domain] Cd Length: 647 Bit Score: 43.32 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 132 PTRPASTGVAGASSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPVLTSP--GAVPPLPS------PSKEEEGLRAQ 203
Cdd:PRK07994 369 EVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQllAARQQLQRaqgatkAKKSEPAAASR 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 204 VRDLEEKLETLRLKRAEDKAKLKELEKhkiqlEQVQEWKskmqEQQADLQRRLKEAR-KEAKEALEAkerymeemadtAD 282
Cdd:PRK07994 449 ARPVNSALERLASVRPAPSALEKAPAK-----KEAYRWK----ATNPVEVKKEPVATpKALKKALEH-----------EK 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 283 AIEMATLDKEMAEERAESLqQEVEALKerVDELTTDLeILKAEIEEKGSD----GAASSYQLKQLEEQNARLKDALvrmr 358
Cdd:PRK07994 509 TPELAAKLAAEAIERDPWA-ALVSQLG--LPGLVEQL-ALNAWKEEHDNGevclHLRPSQRHLNSPRAQQRLAEAL---- 580
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 359 dlsSSEKQEHVKLqKLMEKKNQELEVVRQQRERLQEE-LSQAES------TIDELKEQVDAAL 414
Cdd:PRK07994 581 ---SELLGRTVEL-TIEEDDNPAVETPLEWRQRIYEEkLAQAEEsiiadpNIQTLRQFFDAEL 639
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
195-309 |
1.12e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLetLRLKRAEDKAKLKELEKHkiQLEQVQEWKSKMQEqqadlqrRLKEARKEAKEALEAKERym 274
Cdd:cd16269 200 IEAERAKAEAAEQERKL--LEEQQRELEQKLEDQERS--YEEHLRQLKEKMEE-------ERENLLKEQERALESKLK-- 266
|
90 100 110
....*....|....*....|....*....|....*
gi 205277392 275 eemadtadaiEMATLDKEMAEERAESLQQEVEALK 309
Cdd:cd16269 267 ----------EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
251-325 |
1.15e-03 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 39.45 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 251 DLQRRLKEARK-----EAKEALEAKERYMEEMADTADAIEMATLD-------------------KEMAEERAESLQQEVE 306
Cdd:cd23165 1 DQQKINKFSRLnarlhELKEELKAKKKELENLEDASDELELADDDepvpykigevfvhlsleeaQERLEKAKEELEEEIE 80
|
90
....*....|....*....
gi 205277392 307 ALKERVDELTTDLEILKAE 325
Cdd:cd23165 81 KLEEEIDEIEEEMKELKVQ 99
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
205-570 |
1.19e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 205 RDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArkeAKEALEAKERYMEEMADTADAi 284
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---LTETLKKEVKSLQNEKADLDR- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 285 EMATLDKEMAE-ERAESLQQEVEALKErvDELTTDLEILKaeIEEKGSDGAASSY----QLKQLEEQNARLKDALVRMRD 359
Cdd:TIGR00606 516 KLRKLDQEMEQlNHHTTTRTQMEMLTK--DKMDKDEQIRK--IKSRHSDELTSLLgyfpNKKQLEDWLHSKSKEINQTRD 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 360 LSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA------ESTIDELKEQVD------AALGA-----EEMVEM 422
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEksskqrAMLAGatavySQFITQ 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 423 LTDRNLNLEEKVRELRETVGDLeamNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 502
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 503 LTAHLQDVNRELtnQQEASVERQQQPPPETFDFKIKFAETKAHAKAIeMELRQMEVAQANRHMSLLTA 570
Cdd:TIGR00606 749 LRNKLQKVNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAA 813
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
200-283 |
1.31e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQ----------RRLKEARK 261
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLeeklkdreEELREKRKLNQDLQDELValqlqlnmaeEKLRKLEK 155
|
90 100
....*....|....*....|..
gi 205277392 262 EAKEALEakeRYMEEMADTADA 283
Cdd:pfam08614 156 ENRELVE---RWMKRKGQEAEA 174
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
196-492 |
1.45e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLEtLRLKRAEDKAKLKELEKHKIQL------EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 269
Cdd:pfam02029 60 EEEAFLDRTAKREERRQ-KRLQEALERQKEFDPTIADEKEsvaerkENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 270 KER---YMEEMADTADAIEMATLDKEMAEERAESL----QQEVEALKERVDELTTDLEILKAE---IEEKGSDGAASSYQ 339
Cdd:pfam02029 139 EYQenkWSTEVRQAEEEGEEEEDKSEEAEEVPTENfakeEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 340 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmEKKNQELEvvRQQRERLQEELSQAESTIDELKeqvdaalgaeem 419
Cdd:pfam02029 219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEEL-RRRRQEKE--SEEFEKLRQKQQEAELELEELK------------ 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 420 vemltdrnlnleeKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 492
Cdd:pfam02029 284 -------------KKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSSE 343
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
194-509 |
1.45e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 273
Cdd:PRK01156 203 KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADA-----IEMATLDKEMAEERA--ESLQQEVEALKERVDELtTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 346
Cdd:PRK01156 283 MKIINDPVYKnrnyiNDYFKYKNDIENKKQilSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 347 NARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-------EVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 419
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 420 V----EMLTDRNL------NL-EEKVRELRETVG-DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 487
Cdd:PRK01156 442 LsrnmEMLNGQSVcpvcgtTLgEEKSNHIINHYNeKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521
|
330 340
....*....|....*....|..
gi 205277392 488 ETVADYQQTIKKYRQLTAHLQD 509
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKD 543
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
254-526 |
1.51e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 42.33 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 254 RRLKEARKEAKEALEAKERYMEE--MADTADA-IEMATLDKEM--AEERAESLQQEVEALKERVDE-LTTDLEILKAEIE 327
Cdd:COG1538 50 RARIEAAKAQAEAAEADLRAARLdlAAEVAQAyFDLLAAQEQLalAEENLALAEELLELARARYEAgLASRLDVLQAEAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 328 EkgsdgAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 407
Cdd:COG1538 130 L-----AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 408 EQVDAA-------------LGAEEMVEMLTDRN------LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ 468
Cdd:COG1538 205 AEIGVAraaflpslslsasYGYSSSDDLFSGGSdtwsvgLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 205277392 469 LDMAGARVREAQKRVEAAQETVAD----YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 526
Cdd:COG1538 285 VEDALAALRAAREQLEALEEALEAaeeaLELARARYRAGLASLLDVLDAQRELLQAQLNLIQ 346
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
195-467 |
1.60e-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: 42.80 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLE----EKLETLRLKRAEDKAKLK-ELE---KHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 266
Cdd:pfam17380 360 RELERIRQEEIAMEisrmRELERLQMERQQKNERVRqELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 267 LEakerymeemadtadaiematldkemaEERAeslqQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyQLKQLEEQ 346
Cdd:pfam17380 440 LE--------------------------EERA----REMERVRLEEQERQQQVERLRQQEEER---------KRKKLELE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 347 NARlkdalvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDR 426
Cdd:pfam17380 481 KEK--------RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 205277392 427 nlNLEEKVRELRETVGDLEAMnEMNDELQENARETELELRE 467
Cdd:pfam17380 553 --RIQEQMRKATEERSRLEAM-EREREMMRQIVESEKARAE 590
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
904-1026 |
1.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 904 VELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKkldsaAKDADERIEKVQTRLE-ETQ 982
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLTgLTP 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 205277392 983 ALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1026
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
371-561 |
1.67e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 371 LQKLMEKKNQELEVVRQQRERLQEELSQaesTIDELKEQVDAALgaeemvemltdrnLNLEEKVRELREtvgdleamnem 450
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEE---KKEKLQEEEDKLL-------------EEAEKEAQQAIK----------- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 451 ndELQENARETELELREQLDMAGARVR-----EAQKRVEAAQETVADYQQTIK------------KYRQL--TAHLQDV- 510
Cdd:PRK00409 581 --EAKKEADEIIKELRQLQKGGYASVKaheliEARKRLNKANEKKEKKKKKQKekqeelkvgdevKYLSLgqKGEVLSIp 658
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 511 -NRELTNQ--------QEASVERQQQPPPETFDfKIKFAETKAHAKAIEMELRQMEVAQA 561
Cdd:PRK00409 659 dDKEAIVQagimkmkvPLSDLEKIQKPKKKKKK-KPKTVKPKPRTVSLELDLRGMRYEEA 717
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
905-1030 |
1.67e-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: 42.74 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 905 ELRAAALRAEITDAEGLGLKLEDRE--TVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKD---ADERIEKVQTRLE 979
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESKLD 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 205277392 980 ETQALLRKKEKEFEET---MDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRG 1030
Cdd:TIGR02168 334 ELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQ-LETLRS 386
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
293-478 |
1.73e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 40.71 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 293 MAEERAESLQQEVEALKERVDElttDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDALVRMRDLSSSEkqehvkLQ 372
Cdd:pfam01442 23 VAQELVDRLEKETEALRERLQK---DLEEVRAKLEPY-------------LEELQAKLGQNVEELRQRLEPY------TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 373 KLMEKKNQELEVVRQQRERLQEEL-SQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELRETVGdleamnEMN 451
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELrERLEQNVDALRARLAPY--AEELRQ-------KLAERLEELKESLA------PYA 145
|
170 180
....*....|....*....|....*..
gi 205277392 452 DELQENARETELELREQLDMAGARVRE 478
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
891-1029 |
1.84e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 891 EYDAERPPSKPPPVELRAAALRAEITDAEGlglKLEDRETVIKELKkslkikgEELSEanvrlslLEKKLdsaaKDADER 970
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLE-------AEVEE-------LEAEL----EEKDER 442
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 971 IEKVQTRLEETQALLRKKEKEFEEtMDALQADIDQLEAEKAELKQRlNSQSKRTIEGLR 1029
Cdd:COG2433 443 IERLERELSEARSEERREIRKDRE-ISRLDREIERLERELEEERER-IEELKRKLERLK 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-394 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVqewKSKMQEQQADLQRRLKEARkeaKEALEAKERY 273
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 274 MEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERVDELTtdlEILKAEIEEkgsdgaassyqlkqLEEQNARLKDA 353
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKIKELG---PVNLAAIEE--------------YEELKERYDFL 1005
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 205277392 354 LVRMRDLSSSEKQehvkLQKLMEKKNQELevvrqqRERLQE 394
Cdd:TIGR02168 1006 TAQKEDLTEAKET----LEEAIEEIDREA------RERFKD 1036
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
200-510 |
1.89e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 200 LRAQVRDLEEK---LETLRLKR----AEDKAKLKELEKHKIQLEQvqeWKSKMQEQQADLQRRLKEARKEAKEALEAKER 272
Cdd:pfam01576 164 FTSNLAEEEEKaksLSKLKNKHeamiSDLEERLKKEEKGRQELEK---AKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD--------------ELTTDLEILKAEIEEKGSDGAASSY 338
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrDLGEELEALKTELEDTLDTTAAQQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 339 QLKQLEEQNARLKDALvrmrdlsSSEKQEH-VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGAE 417
Cdd:pfam01576 321 LRSKREQEVTELKKAL-------EEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN-AELQAE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 418 emVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAdyqqti 497
Cdd:pfam01576 393 --LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------ 464
|
330
....*....|...
gi 205277392 498 kkyrQLTAHLQDV 510
Cdd:pfam01576 465 ----SLESQLQDT 473
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
221-384 |
2.01e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 221 DKAKlKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEAleakERYMEEMADTADAIEmATLDKEMAEERaES 300
Cdd:PRK00409 505 EEAK-KLIGEDKEKLNELIA---SLEELERELEQKAEEAEALLKEA----EKLKEELEEKKEKLQ-EEEDKLLEEAE-KE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 301 LQQEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALvrmrdlssSEKQEHVKLQKlmeKKNQ 380
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQ--------KGGYASVKAHELIEARKRLNKAN--------EKKEKKKKKQK---EKQE 635
|
....
gi 205277392 381 ELEV 384
Cdd:PRK00409 636 ELKV 639
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
202-396 |
2.01e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.89 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 202 AQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQRR---LKEARKEAKEALEAKERYMEEM 277
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEELNQRweeLRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 ADTADaiematLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDalvRM 357
Cdd:cd00176 113 RDADD------LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-------EPRLKSLNELAEELLE---EG 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 205277392 358 RDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEEL 396
Cdd:cd00176 177 HPDADEEIEE--KLEELNERWEELLELAEERQKKLEEAL 213
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
190-527 |
2.07e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 190 LPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQAdLQRRLKEARKEAKEALE 268
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQArIQRLAARAPAWLA-AQDALARLREQSGEEFE 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 269 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVE--------------ALKER-----VDELTTDLEILKAEIEEK 329
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggsedprlnALAERfggvlLSEIYDDVSLEDAPYFSA 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 330 GSDGAAS-------SYQLKQLEEQNARLKDALV------RMRD-LSSSEKQEHVKLQKLMEK-----------------K 378
Cdd:PRK04863 705 LYGPARHaivvpdlSDAAEQLAGLEDCPEDLYLiegdpdSFDDsVFSVEELEKAVVVKIADRqwrysrfpevplfgraaR 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 379 NQELEVVRQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQ 455
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQR 864
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 456 ---ENARETELELREQLDMA--------GARVREAQKRVEAAQET---VADYQQTIKKYRQLTAHLQ---DVNRELTNQQ 518
Cdd:PRK04863 865 sqlEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDY 944
|
....*....
gi 205277392 519 EASVERQQQ 527
Cdd:PRK04863 945 QQAQQTQRD 953
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
171-311 |
2.30e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.30 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 171 LAAPIIPTPVLTSPGAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEkhkiqlEQVQEWKSKMQEQQ- 249
Cdd:pfam08614 26 LQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLN------EELQELEKKLREDEr 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 205277392 250 --ADLQRR---LKEARKEAKEALEAKERYMEEMADtadaiEMATLDKE--MAEERAESLQQEVEALKER 311
Cdd:pfam08614 100 rlAALEAEraqLEEKLKDREEELREKRKLNQDLQD-----ELVALQLQlnMAEEKLRKLEKENRELVER 163
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
185-346 |
2.37e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 185 GAVPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEAR 260
Cdd:COG3096 512 QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAqleeLEEQAAEAVEQRSELRQQLEQLR 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 261 KEAKEaLEAKERYMEEMADTADAIEM---ATLD--KEMAEERAESLQQEVEALKERvDELTTDLEILKAEIEEKGSDGAA 335
Cdd:COG3096 592 ARIKE-LAARAPAWLAAQDALERLREqsgEALAdsQEVTAAMQQLLEREREATVER-DELAARKQALESQIERLSQPGGA 669
|
170
....*....|.
gi 205277392 336 SSYQLKQLEEQ 346
Cdd:COG3096 670 EDPRLLALAER 680
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
247-492 |
2.45e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 42.38 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 247 EQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE 325
Cdd:COG5644 331 EPRTESERKMHQALLDAGLENESALKKQEELALNKLSVeEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 326 IEEKGSDGAASSyqlkQLEEQNARLKDALVRMrdlssseKQEHVKLQKLMEKknqelevvrqqrerLQEELSQAESTIDE 405
Cdd:COG5644 411 KEKEMALIPKSE----DLENEKSEEARALERM-------TQRHKNTSSWTRK--------------MLERASHGEGTREA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 406 LKEQVDAalgAEEMVEMLTDRNLNLEEKVRElrETVGDLEamNEMNDELQENARETELELREQLDMAGARVREAQKRvEA 485
Cdd:COG5644 466 VNEQIRK---GDELMQRIHGKEIMDGEDVSE--FSDSDYD--TNEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQM-AA 537
|
....*..
gi 205277392 486 AQETVAD 492
Cdd:COG5644 538 SKISVAD 544
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
377-527 |
2.46e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 377 KKNQELevVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEKVRELRETVGDLEAMNEMNDELQE 456
Cdd:COG1566 68 KKGQVL--ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIA----AAEAQLAAAQAQLDLAQRELERYQALYK 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 205277392 457 NaretELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVnreltNQQEASVERQQQ 527
Cdd:COG1566 142 K----GAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQV-----AQAEAALAQAEL 203
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
268-495 |
2.53e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 268 EAKERYMEEMADTADAIE-MATLDKEMAEER--AESLQQEVEALKERVDELTTDLEilkaEIEEKGSDGAASSYQ--LKQ 342
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIAsLEELERELEQKAeeAEALLKEAEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQqaIKE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 343 LEEQNARLKDALVRMRDlsssEKQEHVKLQKLMEKKNQelevVRQQRERLQEELSQAESTIDELKEqvdaalGAE----- 417
Cdd:PRK00409 582 AKKEADEIIKELRQLQK----GGYASVKAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKV------GDEvkyls 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 418 -----EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRVEAA--Q 487
Cdd:PRK00409 648 lgqkgEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvslELDLRGMRYEEALERLDKYldD 727
|
....*...
gi 205277392 488 ETVADYQQ 495
Cdd:PRK00409 728 ALLAGYGE 735
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
197-500 |
2.54e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 197 EEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 275
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADLED-IKIKINELK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 276 EMADTADAI--EMATLDKEMAEERAESLQQ--------EVEALKERVDELTT---DLEILKAEIEEKGSDgaASSY---Q 339
Cdd:PRK01156 543 DKHDKYEEIknRYKSLKLEDLDSKRTSWLNalavisliDIETNRSRSNEIKKqlnDLESRLQEIEIGFPD--DKSYidkS 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 340 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAAL----G 415
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-ITSRINDIEDNLKKSRKALDDAKanraR 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 416 AEEMVEMLTDRNLNLEEKVRELREtvgDLEAMNEMndelqENARETELELREQLDMAGArvrEAQKRVEAAQETVADYQQ 495
Cdd:PRK01156 700 LESTIEILRTRINELSDRINDINE---TLESMKKI-----KKAIGDLKRLREAFDKSGV---PAMIRKSASQAMTSLTRK 768
|
....*
gi 205277392 496 TIKKY 500
Cdd:PRK01156 769 YLFEF 773
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
198-328 |
2.66e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 41.75 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRAQVRDLEEKLETLRLKRAEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 277
Cdd:COG4477 350 RNLEKQIEELEKRYDEIDERIEEEKVAYSEL---QEELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELKKKL 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 205277392 278 ADTADAIEMATL---------DKEMAEERAESLQQE-------VEALKERVDELTTDLEILKAEIEE 328
Cdd:COG4477 427 REIKRRLEKSNLpglpeeyleMFEEASDEIEELSEElnevplnMDEVNRLLEEAEEDIETLEEKTEE 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
905-1022 |
3.00e-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: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 905 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQAL 984
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
90 100 110
....*....|....*....|....*....|....*...
gi 205277392 985 LRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSK 1022
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
911-1017 |
3.18e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 911 LRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLEEtqalLRKKEK 990
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEE----LEKELE 248
|
90 100
....*....|....*....|....*..
gi 205277392 991 EFEETMDALQADIDQLEAEKAELKQRL 1017
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEI 275
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
196-350 |
3.25e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLR--LKRAEDKAkLKELEKHKIQL----EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 269
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRteLQELEAQQ-QEEAESSREQLqeleEQLATERSARREAEAELERLQEELRYLEEELRRS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 270 KERYMEEMADTADAIEMATlDKEMAEERAESLQQEVEAlkeRVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 349
Cdd:pfam09787 134 KATLQSRIKDREAEIEKLR-NQLTSKSQSSSSQSELEN---RLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKE 209
|
.
gi 205277392 350 L 350
Cdd:pfam09787 210 L 210
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
237-460 |
3.31e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 237 QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL- 315
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 316 -----------TTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV 384
Cdd:pfam05701 112 qgiadeasvaaKAQLEVAKARHAAAVAELKSVKEELESLRKE----YASLVSERDIAIKRAEEAVSASKEIEKTVEELTI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 385 vrqQRERLQEELSQAESTIDELKEQ-VDAALGAEEmvEMLT-DRNLN-LEEKVRELRETV---GDLEAMNEMNDELQENA 458
Cdd:pfam05701 188 ---ELIATKESLESAHAAHLEAEEHrIGAALAREQ--DKLNwEKELKqAEEELQRLNQQLlsaKDLKSKLETASALLLDL 262
|
..
gi 205277392 459 RE 460
Cdd:pfam05701 263 KA 264
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
195-481 |
3.33e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEdkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 274
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREE------ELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 275 EEMADTADAIEMAtldkEMAEERAESLQQEVEALKERVDELTT-----------DLEILKAEIEEKGSDgaaSSYQLKQL 343
Cdd:pfam05667 384 KQYKVKKKTLDLL----PDAEENIAKLQALVDASAQRLVELAGqwekhrvplieEYRALKEAKSNKEDE---SQRKLEEI 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 344 EEQNARLKD--ALVRMRDlsssekQEHVKLQKLMEKKNQE----------LEVV---RQQRERLQEELSQaestIDELKE 408
Cdd:pfam05667 457 KELREKIKEvaEEAKQKE------ELYKQLVAEYERLPKDvsrsaytrriLEIVkniKKQKEEITKILSD----TKSLQK 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 205277392 409 QVDAALGAEEMVEMLTDRNLNLEEKVRE-LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQK 481
Cdd:pfam05667 527 EINSLTGKLDRTFTVTDELVFKDAKKDEsVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
198-374 |
3.41e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 198 EGLRaqvRDLEEKLETLRlkraEDKAKLKElekhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErymeem 277
Cdd:smart00787 143 EGLK---EGLDENLEGLK----EDYKLLMK------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP------ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 278 adtadaiemATLDKemAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRM 357
Cdd:smart00787 204 ---------TELDR--AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKKLEQC 265
|
170 180
....*....|....*....|.
gi 205277392 358 RDLSSSE----KQEHVKLQKL 374
Cdd:smart00787 266 RGFTFKEieklKEQLKLLQSL 286
|
|
| Not3 |
pfam04065 |
Not1 N-terminal domain, CCR4-Not complex component; |
209-351 |
4.01e-03 |
|
Not1 N-terminal domain, CCR4-Not complex component;
Pssm-ID: 461155 [Multi-domain] Cd Length: 228 Bit Score: 40.22 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 209 EKLEtlrlkrAEDKAKLKELEKHKiqlEQVQEW--------KSKMQEQqadlqRRLKEARKEAKEALEakeRYMEEMADT 280
Cdd:pfam04065 40 EKLE------ADLKKEIKKLQRLR---DQIKTWlssndikdKKKLLEN-----RKLIEEAMERFKAVE---KESKTKAFS 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205277392 281 ADAIEMATLDKEMAEERAEslQQEVEALKERVDELTTDLEILKAEIE-----EKGSDGAASSYQLKQLEEQNARLK 351
Cdd:pfam04065 103 KEGLSLAAASKLDPKEKEK--AEARDWLSDSIDELNRQIEALEAEIEslqaqKKKKKKDSEKARLEELEKLIERHK 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
907-1019 |
4.04e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 907 RAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANV------------RLSLLeKKLDSAAKDADERIEKV 974
Cdd:COG3883 66 EIDKLQAEIAEAEA---EIEERREELGERARALYRSGGSVSYLDVllgsesfsdfldRLSAL-SKIADADADLLEELKAD 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 205277392 975 QTRLEETQALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNS 1019
Cdd:COG3883 142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ 186
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
195-353 |
4.45e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKhkiQLEQVQEWKSKMQEQQ--ADLQRRLKEARKE----AKEALE 268
Cdd:cd22656 128 KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK---ALKDLLTDEGGAIARKeiKDLQKELEKLNEEyaakLKAKID 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 269 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERV-------DELTTDLEILKAEIEEKGSDGAA---SSY 338
Cdd:cd22656 205 ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeklqgawQAIATDLDSLKDLLEDDISKIPAailAKL 284
|
170
....*....|....*
gi 205277392 339 QLKQLEEQNARLKDA 353
Cdd:cd22656 285 ELEKAIEKWNELAEK 299
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
228-410 |
4.52e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 228 LEKHKIQLEQVQE----WKSKMQEQQADLQRrLKEARKEAKEALEAK-ERYmeemadtadaiematldkEMAEERAESLQ 302
Cdd:pfam10168 549 LKKHDLAREEIQKrvklLKLQKEQQLQELQS-LEEERKSLSERAEKLaEKY------------------EEIKDKQEKLM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 303 QEVEALKERVDELTTDL-EILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMrdlssSEKQEHVKLQKLMEKKNqE 381
Cdd:pfam10168 610 RRCKKVLQRLNSQLPVLsDAEREMKKE------LETIN-EQLKHLANAIKQAKKKM-----NYQRYQIAKSQSIRKKS-S 676
|
170 180
....*....|....*....|....*....
gi 205277392 382 LEVVRQQRERLQEELSQAESTIDELKEQV 410
Cdd:pfam10168 677 LSLSEKQRKTIKEILKQLGSEIDELIKQV 705
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
195-439 |
4.91e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 195 KEEEGLRAQVRDLEEKLETLRLKRA---EDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARKEA 263
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQMDEIVERiqeEDQAEAEEKLEKQRQLreeidefnEEQAEWKELEKEEEREEDERILEYLKEK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 264 KEALEAKERYMEEMADtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL 343
Cdd:pfam13868 165 AEREEEREAEREEIEE----------EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 344 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMl 423
Cdd:pfam13868 235 QELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE--EIEQEEAEKRRMKRLEHRRELEKQIEE---REEQRAA- 308
|
250
....*....|....*.
gi 205277392 424 tDRNLNLEEKVRELRE 439
Cdd:pfam13868 309 -EREEELEEGERLREE 323
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
194-508 |
5.02e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 194 SKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKER 272
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 273 ymeEMADTADAI-----EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE---EKGSDGAASSYQLKQ-- 342
Cdd:TIGR00606 320 ---ELVDCQRELeklnkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRlelDGFERGPFSERQIKNfh 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 343 ---LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgaeem 419
Cdd:TIGR00606 397 tlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ----------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 420 VEMLTDRNLNLEEkvrELRETVGDLEAMNEMNDELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 499
Cdd:TIGR00606 466 LEGSSDRILELDQ---ELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
....*....
gi 205277392 500 YRQLTAHLQ 508
Cdd:TIGR00606 542 KDKMDKDEQ 550
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
209-439 |
5.10e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 209 EKLETLRLKRAEDK--AKLKELE-------KHKIQLEQVQEWKSKMQEQQADLqRRLKEARKEAKEALEAKERYmeEMAD 279
Cdd:PRK05771 7 KKVLIVTLKSYKDEvlEALHELGvvhiedlKEELSNERLRKLRSLLTKLSEAL-DKLRSYLPKLNPLREEKKKV--SVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 280 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK----------AEIEEKGSDGAASSYQLKQLEEQNAR 349
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlsLLLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 350 LKDALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERL------QEELSQAESTIDELKEQVDAALG-AEE 418
Cdd:PRK05771 164 SDVENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLLEeLKE 240
|
250 260
....*....|....*....|.
gi 205277392 419 MVEMLTDRNLNLEEKVRELRE 439
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELE 261
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
187-286 |
5.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 187 VPPlPSPSKEEEGLRAQVRDLEEKLETLRLKRAEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEA 266
Cdd:PRK11448 135 VPP-EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAA---ELEEKQQELEAQLEQLQEKAAET 210
|
90 100
....*....|....*....|.
gi 205277392 267 -LEAKERYMEEMADTADAIEM 286
Cdd:PRK11448 211 sQERKQKRKEITDQAAKRLEL 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
190-400 |
5.21e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 190 LPSPSKEEEGLRAQVRDLEEKLETLRLK-RAEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAkEALE 268
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQ 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 269 AKERYMEEmadtadAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyqlkqleeQNA 348
Cdd:pfam15921 748 SKIQFLEE------AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS---------------------QER 800
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 205277392 349 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvrQQRERLQEELSQAE 400
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQE-----SVRLKLQHTLDVKE 847
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
299-404 |
5.23e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 299 ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLkdalvrmrdlssseKQEHVKLQKlmekk 378
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL--------------EAQLEQLQE----- 205
|
90 100
....*....|....*....|....*.
gi 205277392 379 nQELEVVRQQRERLQEELSQAESTID 404
Cdd:PRK11448 206 -KAAETSQERKQKRKEITDQAAKRLE 230
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
234-325 |
5.54e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.57 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 234 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtaDAIEMATLDKEMAEERA-ESLQQEVEALKERV 312
Cdd:cd06503 38 SLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE--EILAEAKEEAERILEQAkAEIEQEKEKALAEL 115
|
90
....*....|...
gi 205277392 313 DELTTDLEILKAE 325
Cdd:cd06503 116 RKEVADLAVEAAE 128
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
164-551 |
5.74e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.90 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 164 STPAQTPLAAPIIPTPVLTSPGAVPPLPSPSKEEEglrAQVRDLEEKLETLRLKRAEDKAKLKElEKHKIQLEQVQEWKS 243
Cdd:pfam09731 71 VVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE---KEATKDAAEAKAQLPKSEQEKEKALE-EVLKEAISKAESATA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 244 KMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDEL------TT 317
Cdd:pfam09731 147 VAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEA-LAEKLKEVINLAKQSEEEAAPPLLDAApetppkLP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 318 DLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDA-LVRMRD-----LSSSEKQEHVKLQKLMEKKNQELEVVRQQRER 391
Cdd:pfam09731 226 EHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQeLVSIFPdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 392 LQ-EELSQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELREtvgDLEAMNEmnDELQENARETELELREQLD 470
Cdd:pfam09731 306 LKkREEKHIERALEKQKEELDKL--AEELSA-------RLEEVRAADEA---QLRLEFE--REREEIRESYEEKLRTELE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 471 MAGARVREAQKRVEAAQETVADYQqtikkyrqltaHLQDVNRELTNQQEAsverqqqpppetfdFKIKFAETKAHAKAIE 550
Cdd:pfam09731 372 RQAEAHEEHLKDVLVEQEIELQRE-----------FLQDIKEKVEEERAG--------------RLLKLNELLANLKGLE 426
|
.
gi 205277392 551 M 551
Cdd:pfam09731 427 K 427
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
236-526 |
6.12e-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: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 236 EQVQEWKSKMQEQQADLQRRLkearKEAKEALEAKERYMEEmadtaDAIEMATLDKEMAEERAESL------QQEVEALK 309
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRL----NESNELHEKQKFYLRQ-----SVIDLQTKLQEMQMERDAMAdirrreSQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 310 ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL----EEQNARLKDALVRMRDLSSSEKQEHVKLQKlMEKKNQELEVV 385
Cdd:pfam15921 145 NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGKKIYEHDSMST-MHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 386 RQQRErLQEELSQAESTIDELKEQVDaALGAEEM--VEMLTDRNLN---------------LEEKVRELRETVGDLEAMN 448
Cdd:pfam15921 224 KILRE-LDTEISYLKGRIFPVEDQLE-ALKSESQnkIELLLQQHQDrieqliseheveitgLTEKASSARSQANSIQSQL 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 205277392 449 EMndeLQENARETELELREQLDMAGARVREAQKRVEAAQETVADyqqtikKYRQLTAHLQDVNRELTnqqEASVERQQ 526
Cdd:pfam15921 302 EI---IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELT---EARTERDQ 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
932-1022 |
6.22e-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: 40.52 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 932 IKELKKSLKIKGEELSEANVRLSLLEKKLDSAA---KDADERIEKVQTRLEETQALLRKKEKEFEETMDALQADIDQLEA 1008
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLkqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90
....*....|....
gi 205277392 1009 EKAELKQRLNSQSK 1022
Cdd:COG4942 102 QKEELAELLRALYR 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
905-1019 |
6.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 905 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAD--------------ER 970
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaqirgnggdrlEQ 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 205277392 971 IEKVQTRLEETQALLRKKEKEFEETMDALQ----ADIDQLEAEKAELKQRLNS 1019
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEA 395
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
228-456 |
6.55e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 228 LEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadtadaiematldkemaeeraesLQQEVEA 307
Cdd:pfam13851 3 MKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSE------------------------IQQENKR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 308 LKERVDELTTDLEILKAEIEEKGSDGAAssyqlkqLEEQNARLKDALVRMRDLssseKQEHVKLQKLMEKKNQELEVVRQ 387
Cdd:pfam13851 59 LTEPLQKAQEEVEELRKQLENYEKDKQS-------LKNLKARLKVLEKELKDL----KWEHEVLEQRFEKVERERDELYD 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 205277392 388 QRERLQEELSQAEstidELKEQVdaalgAEEMVEMLTDrnlNLEEKVRELRETVG----DLEAMNEMNDELQE 456
Cdd:pfam13851 128 KFEAAIQDVQQKT----GLKNLL-----LEKKLQALGE---TLEKKEAQLNEVLAaanlDPDALQAVTEKLED 188
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
231-409 |
6.81e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 231 HKIQLEQVQ--EWKSKMQEQQADLQRRLKEARKEakEALEAKERYMEEMADTADAI------EMATLDKEMAEerAESLQ 302
Cdd:pfam03528 126 RRLEQERAQwnQYRESAEREIADLRRRLSEGQEE--ENLEDEMKKAQEDAEKLRSVvmpmekEIAALKAKLTE--AEDKI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 303 QEVEALKerVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKN-QE 381
Cdd:pfam03528 202 KELEASK--MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANdQF 279
|
170 180 190
....*....|....*....|....*....|..
gi 205277392 382 LEVVR---QQRERLQEELSQAE-STIDELKEQ 409
Cdd:pfam03528 280 LESQRllmRDMQRMESVLTSEQlRQVEEIKKK 311
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
905-1026 |
7.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 7.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 905 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQAL 984
Cdd:COG1196 315 EERLEELEEELAELEE---ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 205277392 985 LRKKEkefeetmdALQADIDQLEAEKAELKQRLNSQSKRTIE 1026
Cdd:COG1196 392 LRAAA--------ELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
903-1146 |
7.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 903 PVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTRLEETQ 982
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 983 ALLRKKEKEFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIeglrgppPSGIATLVSGIAGGAIPGQAPGSVPGPGLV 1062
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-------LLIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 1063 KDSPLLLQQISAMRLHISQLQHENSILKGAQMKASLASLPPLHVAKLSHEGPGSELPAGALYRKTSQLLETLNQLSTHTH 1142
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
....
gi 205277392 1143 VVDI 1146
Cdd:COG4717 362 ELQL 365
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
297-526 |
8.17e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 297 RAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQL----KQLEEQNARLKDALVRMRDLSSSEKQEHVKLQ 372
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWerqrRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 373 KLMEKKNQELEVVRQQRErlqeelsQAESTIDELkeqvdaalgaEEMVEMLTDRNLNLEEKVRELRETV----GDLEAMN 448
Cdd:pfam07888 108 ASSEELSEEKDALLAQRA-------AHEARIREL----------EEDIKTLTQRVLERETELERMKERAkkagAQRKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 449 EMNDELQENARETELELRE-QLDMAGARVREAQKRVEAA--QETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 525
Cdd:pfam07888 171 AERKQLQAKLQQTEEELRSlSKEFQELRNSLAQRDTQVLqlQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE 250
|
.
gi 205277392 526 Q 526
Cdd:pfam07888 251 R 251
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
901-1029 |
8.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 901 PPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKsLKIKGEELSEANVRLSLLEKKLDSAAKDADER-IEKVQTRLE 979
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAELEYLRAALRLWFAQRrLELLEAELE 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 205277392 980 ETQALLRKKEKEfeetMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLR 1029
Cdd:COG4913 299 ELRAELARLEAE----LERLEARLDALREELDELEAQIRGNGGDRLEQLE 344
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
196-337 |
9.90e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 196 EEEGLRAQVRDLEEKLETLRLKRAEDKAKLKE--LEKHKIQLEQVQ----------------EWKSKMQEQQADLQRRLK 257
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQdnADKQRDEVRQKQqeaknlpkpadtsspkEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205277392 258 EARKEAKEALEAKERYMEEMAdtadaiematldKEMAEERAESLQQEVEALKERvDELTTDLEILKAEIEEKGSDGAASS 337
Cdd:pfam05262 289 EIKKNDEEALKAKDHKAFDLK------------QESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQVEAQPTSLNEDA 355
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