|
Name |
Accession |
Description |
Interval |
E-value |
| Dynactin |
pfam12455 |
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ... |
504-782 |
3.04e-92 |
|
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: 298.37 E-value: 3.04e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 504 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 578
Cdd:pfam12455 1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 579 DHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 658
Cdd:pfam12455 80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 659 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMG 738
Cdd:pfam12455 156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568940563 739 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDTRQFCKKIRRRM 782
Cdd:pfam12455 236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
12-77 |
1.02e-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: 1.02e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 12 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 77
Cdd:pfam01302 1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
12-78 |
8.46e-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: 8.46e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 12 VGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEA-KGKNDGTVQGRKYFTCDEGHGIFVRQSQIQ 78
Cdd:smart01052 1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-517 |
1.18e-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: 102.06 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLR--LKRSED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 268
Cdd:TIGR02168 170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 269 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 341
Cdd:TIGR02168 250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 342 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 417
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 418 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 497
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340
....*....|....*....|
gi 568940563 498 RQLTAHLQDVNRELTNQQEA 517
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-492 |
3.19e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 100.78 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 277
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 278 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDL 357
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 358 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnlNLEEKVRELRET 437
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568940563 438 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ 492
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-517 |
7.16e-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: 99.75 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 277
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 278 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEekgsdgaASSYQLKQLEEQNARLKDALVRMRDL 357
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-------ALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 358 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAL----GAEEMVEMLTDRNLNLEEKVRE 433
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 434 LRETVGDLE-AMNEMNDEL-QENARETELELREQ-------------LDMAGARVREAQKRVEAAQETVAD--------- 489
Cdd:TIGR02168 906 LESKRSELRrELEELREKLaQLELRLEGLEVRIDnlqerlseeysltLEEAEALENKIEDDEEEARRRLKRlenkikelg 985
|
330 340 350
....*....|....*....|....*....|....*..
gi 568940563 490 ---------YQQTIKKYRQLTAHLQDVNRELTNQQEA 517
Cdd:TIGR02168 986 pvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
202-546 |
8.41e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 202 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTADAI 281
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELE------AELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 282 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSE 361
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 362 KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM-LTDRNLNLEEKVRELRETVGD 440
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 441 LEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNREL-TNQQEASV 519
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELaEAAARLLL 495
|
330 340
....*....|....*....|....*..
gi 568940563 520 ERQQQPPPETFDFKIKFAETKAHAKAI 546
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-465 |
1.71e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQewksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 277
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 278 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK------AEIEEKGSDGAASSYQLKQLEEQNARLKDAL 351
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 352 vrmrdlssSEKQEHVKlqKLMEKKNQE-LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK 430
Cdd:PRK02224 630 --------AEKRERKR--ELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
250 260 270
....*....|....*....|....*....|....*
gi 568940563 431 VRELRETVGDLEAMNEMNDELQENARETELELREQ 465
Cdd:PRK02224 700 REALENRVEALEALYDEAEELESMYGDLRAELRQR 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
195-524 |
4.20e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 93.85 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 195 EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 274
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 ADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 354
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 355 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNLNLEEKVREL 434
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 435 RETVGDLEAMNEMNDELQENARETELELREQLDMAG--ARVREAQKRVEAA--QETVADYQQTIKKYRQ-----LTAHLQ 505
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRglAGAVAVLIGVEAAYEAaleaaLAAALQ 549
|
330
....*....|....*....
gi 568940563 506 DVNRELTNQQEASVERQQQ 524
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKA 568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-481 |
1.27e-18 |
|
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: 92.44 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR----KEAKEALEAK 267
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 268 ERYMEEMADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 346
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 347 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnln 426
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----------- 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 568940563 427 LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 481
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
192-524 |
1.73e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSE--DKAKLKELEKhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 269
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDllAEAGLDDADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 349
Cdd:PRK02224 347 LREDADDLEE-------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 350 ALVRMRdlsSSEKQEHVKLQKLMEK--KNQEL----------------------EVVRQQRERLQEELSQAESTIDELKE 405
Cdd:PRK02224 420 ERDELR---EREAELEATLRTARERveEAEALleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 406 QVDAA---LGAEEMVEMLTDRNLNLEEKVRELRETVGD----LEAMNEMNDELQENARETELELREQLDMAGARV----- 473
Cdd:PRK02224 497 RLERAedlVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevae 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 474 -----------REAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:PRK02224 577 lnsklaelkerIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
192-488 |
1.90e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.54 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKE----LEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAK 267
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 268 ERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARL 347
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 348 KDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNL 427
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE------AALLEAALAELLEEL 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 428 EEKVRELRetvGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 488
Cdd:COG1196 487 AEAAARLL---LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
195-485 |
3.63e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.48 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 195 EGLRAQV-----RDLEEKLETLRLKRSEDKAKLKELEKHKIQLeqvqewkskmqeqqadlqrrlKEARKEAKEALEAKER 269
Cdd:PRK02224 190 DQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQA---------------------RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 349
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 350 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemltdrnlnLEE 429
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-----------------LEE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 430 KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQE 485
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-511 |
4.98e-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: 90.50 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQvqewksKMQEQQADLQRrLKEARKEAKEALEAKErym 271
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA------EIEELEAQIEQ-LKEELKALREALDELR--- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 351
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 352 VRMRD-LSSSEKQEHVKLQKLMEKKnQELEVVRQQRERLQEELSQAESTIDELKEQV-----DAALGAEEMVEMLTDRNL 425
Cdd:TIGR02168 890 ALLRSeLEELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 426 NLEEKVRELRETVGDLEAMNEMN-DELQE-NARETELEL-REQLDMAGARVREAQKRVEAaqETVADYQQTIKKYRQlta 502
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAiEEYEElKERYDFLTAqKEDLTEAKETLEEAIEEIDR--EARERFKDTFDQVNE--- 1043
|
....*....
gi 568940563 503 HLQDVNREL 511
Cdd:TIGR02168 1044 NFQRVFPKL 1052
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
231-554 |
2.37e-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: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 231 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALeakerymeemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVD 310
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS--------------QELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 311 ELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALvrmRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQ 390
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 391 eELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEA-MNEMNDELQE-NARETELE-----LR 463
Cdd:TIGR02169 816 -EIEQKLNRLTLEKEY------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEElEAALRDLEsrlgdLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 464 EQLDMAGARVREAQKRVEAAQETVADYQQTIKkyrQLTAHLQDVNRELTnQQEASVERQQQPPPETFDFKikfaETKAHA 543
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLS---ELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE----DVQAEL 960
|
330
....*....|.
gi 568940563 544 KAIEMELRQME 554
Cdd:TIGR02169 961 QRVEEEIRALE 971
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
193-523 |
2.69e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLR----LKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 268
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 269 RYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-----------------KGSDGA 331
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 332 AS-----------SYQLKQLEEQNARLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRERLQEELSQAES-- 398
Cdd:PRK02224 468 ETieedrerveelEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELIAERRETIEEKRERAEElr 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 399 --------------------------------TIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETvgdLEAMNE 446
Cdd:PRK02224 544 eraaeleaeaeekreaaaeaeeeaeeareevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK---REALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 447 MNDELQE---NARETELELREQLDmaGARVREAQ---KRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEASV 519
Cdd:PRK02224 621 LNDERRErlaEKRERKRELEAEFD--EARIEEARedkERAEEYLEQVEEKLDELREERdDLQAEIGAVENELEELEELRE 698
|
....
gi 568940563 520 ERQQ 523
Cdd:PRK02224 699 RREA 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-524 |
6.45e-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: 83.58 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRS-EDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEakeaLEAKER 269
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADAI---EMATLDKEMAEERAE--SLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQN 344
Cdd:TIGR02169 273 LLEELNKKIKDLgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE---REIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 345 ARlKDALvrMRDLSSSEKQEHVKLQKLME--KKNQELevvRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTD 422
Cdd:TIGR02169 350 KR-RDKL--TEEYAELKEELEDLRAELEEvdKEFAET---RDELKDYREKLEKLKREINELKRELDR----------LQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 423 RNLNLEEKVRELRETVGDLEamnemndelqenARETELElrEQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQLTA 502
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIE------------AKINELE--EEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE 476
|
330 340
....*....|....*....|....
gi 568940563 503 HLQDVNRELTNQQE--ASVERQQQ 524
Cdd:TIGR02169 477 EYDRVEKELSKLQRelAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-434 |
7.45e-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: 7.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKL----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 268
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIeelqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 269 RYMEEMADTADAIEMAtldkemaEERAESLQQEVE-------ALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 341
Cdd:TIGR02168 334 ELAEELAELEEKLEEL-------KEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 342 EQNARLKDALVRM--------RDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA 409
Cdd:TIGR02168 407 ARLERLEDRRERLqqeieellKKLEEAELKELqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250 260
....*....|....*....|....*
gi 568940563 410 ALGAEEMVEMLTDRNLNLEEKVREL 434
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKAL 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-554 |
3.76e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 3.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRA-QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQqadlQRRLKEARKEAKEALEAKERY 270
Cdd:PTZ00121 1273 KAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEI-LKAEIEEKGSDgaassyQLKQLEEQNARLKD 349
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKAD------ELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 350 ALVRMRDLsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEEMVEMLTDRNLNL 427
Cdd:PTZ00121 1423 AKKKAEEK---KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 428 EE--KVRELRETVGDLEAMNEMN--DELQ--ENARETElELREQLDMAGA-RVREAQKRVEAAQETVADYQQTIKKYRQL 500
Cdd:PTZ00121 1500 DEakKAAEAKKKADEAKKAEEAKkaDEAKkaEEAKKAD-EAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568940563 501 TAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 554
Cdd:PTZ00121 1579 ALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
10-402 |
7.27e-14 |
|
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: 76.26 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 10 LRVGSRVEVIGKghRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEdgadttsp 89
Cdd:COG5244 4 LSVNDRVLLGDK--FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLN-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 90 etpDSSASKVLKREGADAAAKTSKLRGLKPKktttrrpkptrpastgvagpssslgpsgsasagelsSSEPSTPAQTPLA 169
Cdd:COG5244 74 ---GNAAYEKIKGGLVCESKGMDKDGEIKQE------------------------------------NHEDRIHFEESKI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 170 APIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIqLEQVQEWKSKMQEQQADL 249
Cdd:COG5244 115 RRLEETIEALKSTEKEEIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMVELVSDI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 250 QRRLKEARKEAKEALEAKERymeemadtadaiematldkemaeeraeslqqevealKERVDELTTDLEILKAEIEEKGsd 329
Cdd:COG5244 194 SETLNRNGSIQRSSVRECER------------------------------------SNIHDVLFLVNGILDGVIDELN-- 235
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568940563 330 gaassyqlKQLEeqnaRLKDALVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAESTIDE 402
Cdd:COG5244 236 --------GELE----RLRRQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYE 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-557 |
9.12e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQE----------------------QQADL 249
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkkkadelkkaaaakkkadeakKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 250 QRRLKEARK---EAKEALEAKE-----RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEALKERVDELTTDLEIL 319
Cdd:PTZ00121 1430 KKKADEAKKkaeEAKKADEAKKkaeeaKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 320 KAEIEEKGSDGAASSYQLKQLEEqnARLKDALVRMRDLSSSE---KQEHVK----LQKLMEKKNQELEvvRQQRERLQEE 392
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAEEKKKADelkKAEELKkaeeKKKAEEAKKAEED--KNMALRKAEE 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 393 LSQAEST---------IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELR 463
Cdd:PTZ00121 1586 AKKAEEArieevmklyEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 464 EQLdmagARVREAQKRveAAQETVADYQQTIKKYRQLTAHLQDVNR--ELTNQQEASVERQQQPPPETFDFKIKFAETKA 541
Cdd:PTZ00121 1664 AEE----AKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
410
....*....|....*.
gi 568940563 542 HAkaiEMELRQMEVAQ 557
Cdd:PTZ00121 1738 EA---EEDKKKAEEAK 1750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
191-496 |
9.27e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRlKRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 270
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAE-EAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnaRLKDA 350
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--KKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 351 LVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAES----TIDELKEQVDAALGAEEMVEMLTDRNL 425
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 426 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 496
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
177-410 |
4.90e-13 |
|
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: 72.49 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 177 ALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEA 256
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 257 RKEAKEALEAKERYMEEMADTADAIEMATLDKEM-----------AEERAESLQQEVEALKERVDELTTDLEILKAEIEE 325
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 326 KgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 405
Cdd:COG4942 169 L-------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 568940563 406 QVDAA 410
Cdd:COG4942 242 RTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
191-481 |
6.78e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 6.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRlkrsEDKAKLKELEKHKIQLEqvqEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELE---KKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqlkqleeqnarlkda 350
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK---------------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 351 lvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEK 430
Cdd:PRK03918 655 --------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE----KALER 722
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 568940563 431 VRELRETVGDLEAMNEMN--DELQENARETELELREQlDMAGARVREAQKRVE 481
Cdd:PRK03918 723 VEELREKVKKYKALLKERalSKVGEIASEIFEELTEG-KYSGVRVKAEENKVK 774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-557 |
6.91e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQ-VRDLEEKLETLRLKRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:PTZ00121 1171 KAEDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 346
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 347 LKDALVRMRDlsSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemLTDRNLN 426
Cdd:PTZ00121 1330 KADAAKKKAE--EAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 427 LEEKVRELRETvgdlEAMNEMNDELQENAREtelelREQLDMAGARVREAQKRVEAAQEtvADYQQTIKKYRQLTAHLQD 506
Cdd:PTZ00121 1403 DKKKADELKKA----AAAKKKADEAKKKAEE-----KKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 568940563 507 VNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQ 557
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
191-558 |
1.35e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKI----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 266
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 267 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 346
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 347 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-QQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNL 425
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 426 NLEE---------KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 496
Cdd:COG1196 555 DDEVaaaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 497 YRQLTAHLQDVNRELTNQQEASVERQQqpppETFDFKIKFAETKAHAKAIEMELRQMEVAQA 558
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGS----LTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
191-516 |
1.83e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHK-----------------------IQLEQVQEWKSKMQEQQA 247
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytAELKRIEKELKEIEEKER 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 248 DLQRRLKEARKEAKEalEAKERYMEEMADTADAIE--MATLDKEMAEERAEslqqEVEALKERVDELTTDLEILKAEIEE 325
Cdd:PRK03918 477 KLRKELRELEKVLKK--ESELIKLKELAEQLKELEekLKKYNLEELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 326 KG---SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE 402
Cdd:PRK03918 551 LEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 403 LKEQVDAALGAEEMvemltdrnlnLEEKVRELREtvgdleamnEMNDELQENARETELELREQLDMAGARVREAQKRVEA 482
Cdd:PRK03918 631 AFEELAETEKRLEE----------LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
330 340 350
....*....|....*....|....*....|....
gi 568940563 483 AQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 516
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
192-557 |
3.16e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSK-------MQEQQADLQRRLKEARKEAKEaL 264
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegskrkLEEKIRELEERIEELKKEIEE-L 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 265 EAKERYMEEMADTADaiEMATLDKEMA---------EERAESLQQEVEALKERVDELTTDLEILKaEIEEKGSDGAASSY 335
Cdd:PRK03918 279 EEKVKELKELKEKAE--EYIKLSEFYEeyldelreiEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 336 QLKQLEEQNARLKDALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGA- 413
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAk 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 414 -----------------------------EEMVEMLTDRN-------------LNLEEKVRELRETVGDLEAMNEM---- 447
Cdd:PRK03918 436 gkcpvcgrelteehrkelleeytaelkriEKELKEIEEKErklrkelrelekvLKKESELIKLKELAEQLKELEEKlkky 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 448 -NDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP 526
Cdd:PRK03918 516 nLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430
....*....|....*....|....*....|.
gi 568940563 527 PETFDFKIKFAETKAHAKAIEMELRQMEVAQ 557
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
200-481 |
7.09e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKERYMEEMAD 276
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 TADAIEMAtldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqlkqLEEQNARLKDAlvrmrd 356
Cdd:PRK03918 236 LKEEIEEL-------EKELESLEGSKRKLEEKIRELEERIEELKKEIEE--------------LEEKVKELKEL------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 357 lsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRE 436
Cdd:PRK03918 289 --KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 437 TVGDLEAMNEMNDELQ-----------ENARETELELREQLDMAGARVREAQKRVE 481
Cdd:PRK03918 367 AKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
200-517 |
1.05e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTAD 279
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 AIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE--IEEKG------------------------------ 327
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerLKEARlllliaaallallglggsllsliltiagvl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 328 -------SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKL-MEKKNQELEVVRQQRERLQEELSQAEST 399
Cdd:COG4717 280 flvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEEL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 400 IDELK----EQVDAALGAEEMVEMLTD--RNLNLEEKVRELRETVGDLEAM--NEMNDELQENARETELELREQLDMAGA 471
Cdd:COG4717 360 EEELQleelEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEE 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 568940563 472 RVREAQKRVEAAQETVADYQQTIKK------YRQLTAHLQDVNRELTNQQEA 517
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQleedgeLAELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
287-527 |
3.50e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.73 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 287 DKEMAEERAESLQQE--VEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQE 364
Cdd:COG3206 146 DPELAAAVANALAEAylEQNLELRREEARKALEFLEEQLPE----------LRKELEEAEAALEEFRQKNGLVDLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 365 HVklqklmekkNQELEVVRQQRERLQEELSQAESTIDELKEQVD------AALGAEEMVEMLTDRNLNLEEKVRELRETV 438
Cdd:COG3206 216 LL---------LQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalPELLQSPVIQQLRAQLAELEAELAELSARY 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 439 GD--------LEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLqDVNRE 510
Cdd:COG3206 287 TPnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV-EVARE 365
|
250 260
....*....|....*....|..
gi 568940563 511 -----LTNQQEASVERQQQPPP 527
Cdd:COG3206 366 lyeslLQRLEEARLAEALTVGN 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-467 |
9.65e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 219 KAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARkEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAES 297
Cdd:COG4913 609 RAKLAALEA---ELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAErEIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 298 lqQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvkLQKLMEKKNQ 377
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 378 ElEVVRQQRERLQEELSQAESTIDELKEQVDAAL-------------------GAEEMVEMLTD-RNLNLEEKVRELRET 437
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadleSLPEYLALLDRlEEDGLPEYEERFKEL 839
|
250 260 270
....*....|....*....|....*....|
gi 568940563 438 VgdLEAMNEMNDELQENARETELELREQLD 467
Cdd:COG4913 840 L--NENSIEFVADLLSKLRRAIREIKERID 867
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
197-522 |
1.30e-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: 65.81 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 276
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRD 356
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-------EIKDLTNQDSVKELIIKNLDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 357 LSSSEKQ-------EHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeEMVEMLTDRNLNLEE 429
Cdd:TIGR04523 462 TRESLETqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKES 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 430 KVRELRETVgdleamNEMNDELQENARETE-LELREQLDmagaRVREAQKRVEAAQETVadyQQTIKKYrqlTAHLQDVN 508
Cdd:TIGR04523 539 KISDLEDEL------NKDDFELKKENLEKEiDEKNKEIE----ELKQTQKSLKKKQEEK---QELIDQK---EKEKKDLI 602
|
330
....*....|....*.
gi 568940563 509 RELTN--QQEASVERQ 522
Cdd:TIGR04523 603 KEIEEkeKKISSLEKE 618
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
202-554 |
1.43e-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: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 202 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEqvqewKSKMQEQQAdlQRRLKEarKEAKEALEAKERYMEEMADTADAI 281
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKA--LEYYQL--KEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 282 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSE 361
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----LLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 362 KQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDL 441
Cdd:pfam02463 316 LKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 442 EAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 521
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350
....*....|....*....|....*....|...
gi 568940563 522 QQQpppETFDFKIKFAETKAHAKAIEMELRQME 554
Cdd:pfam02463 473 LLK---ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-564 |
2.14e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQ-VRDLEE--KLETLRLKR-SEDKAKLKELEKHKI-QLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEA 263
Cdd:PTZ00121 1238 DAEEAKKAEeERNNEEirKFEEARMAHfARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 264 LEAKERyMEEMADTADAI----EMATLDKEMAEERAESLQQEVEALKER--VDELTTDLEILKAEIEEKGSDGAASSYQL 337
Cdd:PTZ00121 1318 DEAKKK-AEEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKaeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 338 KQLEEQNARlkdalvrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEE 415
Cdd:PTZ00121 1397 KKKAEEDKK---------------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 416 MVEMLTDRnlnleEKVRELRETVGDLEAMNEMNDELQENARETElELREQLDmAGARVREAQKRVEAAQETVADYQQTIK 495
Cdd:PTZ00121 1462 AKKKAEEA-----KKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 496 KYRQL-TAHLQDVNRELTNQQEASVERQQQPPPEtfdfKIKFAETKAHAKAIEMELRQMEVAQANRHMSL 564
Cdd:PTZ00121 1535 KADEAkKAEEKKKADELKKAEELKKAEEKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
200-522 |
2.26e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.39 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADta 278
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELnEELKELAEKRDE----LNAQVKELREEAQELREKRDELNEKVKE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 279 daiematldkemaeeraesLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassYQLKQLEEQNARLKDALVRmRDLS 358
Cdd:COG1340 76 -------------------LKEERDELNEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEWRQQT-EVLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 359 SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQaestIDELKEQVDAalgaeemvemltdrnlnLEEKVRELRetv 438
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAE----LKELRKEAEE-----------------IHKKIKELA--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 439 gdlEAMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEA 517
Cdd:COG1340 188 ---EEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRkELKKLRKKQRALKREKEKE 263
|
....*
gi 568940563 518 SVERQ 522
Cdd:COG1340 264 ELEEK 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-481 |
2.81e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARK--EAKEALEAK 267
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKaeEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 268 ERYMEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLE--ILKAEIEEKGSDGAASSYQLKQLEEQNA 345
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAKKAEEdeKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 346 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgAEEMVEMLTDRNL 425
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI-EEELDEEDEKRRM 1794
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 426 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 481
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
192-565 |
3.89e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRR--LKEARKEAKEALEAKER 269
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLK 348
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 349 DALVRMRDLSSSEKQE---------HVKLQKLMEKKNQELEV-------------VRQQRERLQEELSQAESTIDELKEQ 406
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 407 vdAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ-----LDMAGARVREA-QKRV 480
Cdd:COG4717 314 --EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiaalLAEAGVEDEEElRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 481 EAAQEtvadyqqtikkYRQLTAHLQDVNRELTNQQEASVERQQQPPPEtfDFKIKFAETKAHAKAIEMELRQM--EVAQA 558
Cdd:COG4717 392 EQAEE-----------YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELreELAEL 458
|
....*..
gi 568940563 559 NRHMSLL 565
Cdd:COG4717 459 EAELEQL 465
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
200-535 |
1.34e-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: 62.45 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLkRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADL---QRRLKEARKEAKE--ALEAKERYMEEM 274
Cdd:pfam17380 288 QQQEKFEKMEQERL-RQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIyaeQERMAMERERELEriRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 ADTADAIEMATLdKEMaeeraESLQQEVEALKERVdelttdleilKAEIEekgsdgAASSYQLKQlEEQNARLKDALVRM 354
Cdd:pfam17380 366 RQEEIAMEISRM-REL-----ERLQMERQQKNERV----------RQELE------AARKVKILE-EERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 355 RDL-SSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERL-QEELSQAESTIDELKEQVDAALGAEEmvemltdRNL 425
Cdd:pfam17380 423 EQIrAEQEEARQREVRRLEEERAREMERVRleeqerqQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQ-------RRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 426 NLEEKVRELRETVgdleamneMNDELQENARETELELREQLDMAGARVREA--QKRVEAAQETVADYQQTIKKYRQLTAH 503
Cdd:pfam17380 496 ILEKELEERKQAM--------IEEERKRKLLEKEMEERQKAIYEEERRREAeeERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340 350
....*....|....*....|....*....|....
gi 568940563 504 LQ--DVNRELTNQQEASVERQQQPPPETFDFKIK 535
Cdd:pfam17380 568 LEamEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
232-473 |
2.78e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 232 LEQVQEWKSKMQEQQAD-LQRRLKEARKEAKEALEAKERYMEEMadtadAIEMATLDKEMAEERAESLQQEVEALKERVD 310
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 311 ELTTDLEILKAEIEEkGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQ-RERL 389
Cdd:COG3206 237 EAEARLAALRAQLGS-GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL----RAQIAALRAQlQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 390 QEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQenARETELELREQLDMA 469
Cdd:COG3206 312 QRILASLEAELEALQAREAS---LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEALTVG 386
|
....
gi 568940563 470 GARV 473
Cdd:COG3206 387 NVRV 390
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
203-460 |
2.97e-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: 61.02 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 203 DLEEKLETLRLKRSEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQ---RRLKEARKEAKEALEAKERYMEEMADTAD 279
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYdllEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 AI--EMATLDK-----EMAEERAESLQQEVEALKERVDELTTDLE-------ILKAEIEEKGSdgaassyQLKQLEEQNA 345
Cdd:pfam06160 309 ELkeELERVQQsytlnENELERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILE-------QLEEIEEEQE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 346 RLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaEEMVEML 420
Cdd:pfam06160 382 EFKESLQSLR------KDELEAREKLDEFKLELREIKRLvEKSNLpglpESYLDYFFDVSDEI----------EDLADEL 445
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 568940563 421 TDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 460
Cdd:pfam06160 446 NEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ 485
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
192-460 |
3.98e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.62 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKakLKELEKhKI-----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 266
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQE-RIdqlydILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 267 KERYMEEMADTADAIEmatldkemaeeRAESLQQEVEALKERVDELTTDLE-------ILKAEIEEkgsdgaaSSYQLKQ 339
Cdd:PRK04778 333 IDRVKQSYTLNESELE-----------SVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEE-------ILKQLEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 340 LEEQNARLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaE 414
Cdd:PRK04778 395 IEKEQEKLSEMLQGLR------KDELEAREKLERYRNKLHEIKRYlEKSNLpglpEDYLEMFFEVSDEI----------E 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568940563 415 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 460
Cdd:PRK04778 459 ALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-520 |
4.12e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 276 DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILkAEIEEKGSDgaasSYQLKQLEEQNARLKDALVRMr 355
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWD----EIDVASAEREIAELEAELERL- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 356 DLSSSEKQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML--TDRNLNLEEKVRE 433
Cdd:COG4913 681 DASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarLELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 434 LRetvgdleamnemndeLQENARETELELREQLDMAGARVREAQKRVEAAQE---------------TVADYQQTIKKYR 498
Cdd:COG4913 758 AL---------------GDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldaDLESLPEYLALLD 822
|
250 260
....*....|....*....|....*..
gi 568940563 499 QLTA-----HLQDVNRELTNQQEASVE 520
Cdd:COG4913 823 RLEEdglpeYEERFKELLNENSIEFVA 849
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
291-521 |
4.23e-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: 60.16 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 291 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLssseKQEHVKLQK 370
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRAL----EQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 371 LMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--------VDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLE 442
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 443 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 521
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-513 |
4.41e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 286 LDKEMAEERAESLQQEVEALkervDELTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSE---- 361
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDL----ERAHEALEDAREQIE-----------LLEPIRELAERYAAARERLAELEYLRaalr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 362 ----KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemVEMLTDRnlnLEEKVRELRET 437
Cdd:COG4913 283 lwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR--LEQLERE---IERLERELEER 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 438 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQEtvaDYQQTIKKYRQLTAHLQDVNRELTN 513
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
193-396 |
4.57e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARKEAKEALEAKERY 270
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAiEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS---------YQLKQLE 341
Cdd:COG4717 411 LEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllqeleelkAELRELA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568940563 342 EQNARLK---DALVRMRDLSSSEKQEHV--------------KLQKLMEKKNQELEVVRQQRERLQ-EELSQA 396
Cdd:COG4717 490 EEWAALKlalELLEEAREEYREERLPPVleraseyfsrltdgRYRLIRIDEDLSLKVDTEDGRTRPvEELSRG 562
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
200-554 |
5.38e-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: 60.90 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtad 279
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 aiEMATLDKEMAEERAESLQ--QEVEALKERVDELTTDLEilKAEIEekgsdgaassyqLKQLEEQNARLKDalvrmRDL 357
Cdd:pfam15921 350 --QLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLH--KREKE------------LSLEKEQNKRLWD-----RDT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 358 SSSEKQEHvkLQKLMEKKNQELE----VVRQQRERLQEELSQAESTIDELKEQVD--AALGAE---------EMVEMLTD 422
Cdd:pfam15921 409 GNSITIDH--LRRELDDRNMEVQrleaLLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQlestkemlrKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 423 RNLNLEEKVRELRETVGDLE----AMNEMNDELQENARETELELRE--QLDMAGARVREAQKRVEAAQETVADYQQTIKK 496
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQekerAIEATNAEITKLRSRVDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 497 YRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 554
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
205-516 |
5.60e-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: 60.36 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 205 EEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADaIEMA 284
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID-IKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 285 TLDKEMAEERAEsLQQEVEALKErvdELTTDLEILKAEIEEKGSDgaassyQLKQLEEQNARlKDALVRMRDLSSSEKQE 364
Cdd:COG5185 311 TESLEEQLAAAE-AEQELEESKR---ETETGIQNLTAEIEQGQES------LTENLEAIKEE-IENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 365 HVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETVGDL--- 441
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI------EELQRQIEQATSSNEEVSKLLNELISELnkv 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 442 --EAMNEMNDELQENARETELELREQLDmagarvrEAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQE 516
Cdd:COG5185 454 mrEADEESQSRLEEAYDEINRSVRSKKE-------DLNEELTQIESRVSTLKATLEKLRaKLERQLEGVRSKLDQVAE 524
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
219-414 |
1.11e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 219 KAKLKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAE 292
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 293 ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAAssyqlkQLEEQNArlkDALVRMRDLSSSEKQEHVKLQKLM 372
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAA-----RAPAWLAAQDALA------RLREQSG---EEFEDSQDVTEYMQQLLERERELT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 568940563 373 EKKNQelevVRQQRERLQEE---LSQAESTIDE----LKEQVDAALGAE 414
Cdd:PRK04863 645 VERDE----LAARKQALDEEierLSQPGGSEDPrlnaLAERFGGVLLSE 689
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
281-443 |
1.13e-08 |
|
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: 57.24 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 281 IEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKdalvrmrdls 358
Cdd:COG1579 10 LDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 359 ssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETV 438
Cdd:COG1579 80 --EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL------AELEAELAELEAELEEKKAELDEEL 151
|
....*
gi 568940563 439 GDLEA 443
Cdd:COG1579 152 AELEA 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
301-560 |
1.36e-08 |
|
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: 59.70 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 301 EVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQnarlKDALVRMRDLSSsEKQEHVKLQKLMEKKN--QE 378
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRRE----REKAERYQALLK-EKREYEGYELLKEKEAleRQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 379 LEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNL-EEKVRELRETVGDLEAMnemndelQENARE 457
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAE-------IASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 458 TELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFA 537
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAETRD 385
|
250 260
....*....|....*....|...
gi 568940563 538 ETKAHAKAIEMELRQMEVAQANR 560
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKREL 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
192-524 |
2.13e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkIQLEQVQEWKSKMQEQqadlqRRLKEARKEAKEALEAKERYM 271
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLE---QDYQAASDHLNLVQTA-----LRQQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEmadTADAIEMATLDKEMAEERAESLQQEVEALK-------ERVDELTTD----------LEILK-----AEIEEKGSD 329
Cdd:PRK04863 365 EE---QNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqQALDVQQTRaiqyqqavqaLERAKqlcglPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 330 GAASSYQlKQLEEQNARLKDALVRMRDlSSSEKQEHVKLQKLMEK----------KNQELEVVRQQRER--LQEELSQAE 397
Cdd:PRK04863 442 DWLEEFQ-AKEQEATEELLSLEQKLSV-AQAAHSQFEQAYQLVRKiagevsrseaWDVARELLRRLREQrhLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 398 STIDELKEQVDAALGAEEMV---EMLTDRNLNLEEKVRELREtvgDLEAMNEMNDELQENARETELELREQLDMAGARVR 474
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLaefCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 475 E----------AQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:PRK04863 597 RlaarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
198-523 |
2.25e-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: 58.81 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEA---KEALEAKERymee 273
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEeVDSLKS----QLADYQQALDVQQTRAiqyQQAVQALEK---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 274 madtADAI-EMATLDKEMAEERAESLQQEVEALKERVDELttdleilkaeiEEKGSDGAASSYQLKQLEEQNARLKDALV 352
Cdd:COG3096 425 ----ARALcGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-----------EQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 353 RmrdlssseKQEHVKLQKLMEKkNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgAEEMVEML---TDRNLNLEE 429
Cdd:COG3096 490 R--------SQAWQTARELLRR-YRSQQALAQRLQQLRAQLAELEQRLRQQQN-------AERLLEEFcqrIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 430 KVRELRETvgdLEAMNEMNDELQENARETELELREQLDMAGARVRE----------AQKRVEAAQETVAdyqQTIKKYRQ 499
Cdd:COG3096 554 ELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlaAQDALERLREQSG---EALADSQE 627
|
330 340
....*....|....*....|....
gi 568940563 500 LTAHLQDVnreLTNQQEASVERQQ 523
Cdd:COG3096 628 VTAAMQQL---LEREREATVERDE 648
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
192-489 |
2.79e-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: 58.44 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE---QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 268
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 269 RYMEEMADTADAI--EMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL 340
Cdd:pfam02463 261 EKEEEKLAQVLKEnkEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 341 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML 420
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDL 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 421 TDRNLN-LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 489
Cdd:pfam02463 421 LKEEKKeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
195-440 |
3.04e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 195 EGLRAQVRDLEEKLETLRlkrsEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQR---RLKEARKEAKEALEAKERYM 271
Cdd:COG4913 664 ASAEREIAELEAELERLD----ASSDDLAALEE---QLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRL 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEK----------------GSDGAASS 334
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAmrafnrewpaetadldADLESLPE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 335 YQ--LKQLEEQN-----ARLKDALVR-----MRDLSSSEKQEHVKLQKLMEKKNQELE--------------------VV 382
Cdd:COG4913 817 YLalLDRLEEDGlpeyeERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSLKripfgpgrylrlearprpdpEV 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 383 RQQRERLQEELSQAESTIDELKEQVDAALgaEEMVEMLTDRNlnlEEKVRELRETVGD 440
Cdd:COG4913 897 REFRQELRAVTSGASLFDEELSEARFAAL--KRLIERLRSEE---EESDRRWRARVLD 949
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
197-407 |
3.47e-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: 57.66 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETlRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmad 276
Cdd:COG5185 287 LIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE--- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 tADAIEmATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDG-AASSYQLKQLE----------EQNA 345
Cdd:COG5185 363 -IENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEELQrqieqatssnEEVS 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 346 RLKDALVRMRDLSSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQV 407
Cdd:COG5185 441 KLLNELISELNKVMREADEESQ-SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
200-524 |
3.52e-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: 58.11 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKealeakerymeemadtad 279
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-----KEKLNIQKNIDKIKNKLLKLELL------------------ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 aieMATLDKEmaEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLeeqnarlkdalvrmrdlss 359
Cdd:TIGR04523 203 ---LSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 360 seKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvEMLTDRNLNLEEKVRELRETVG 439
Cdd:TIGR04523 259 --KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--------DWNKELKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 440 DL----EAMNEMNDELQ------ENARETELELREQLdmagarvREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNR 509
Cdd:TIGR04523 329 QIsqnnKIISQLNEQISqlkkelTNSESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKN---LESQINDLES 398
|
330
....*....|....*
gi 568940563 510 ELTNQQEASVERQQQ 524
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQ 413
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
203-492 |
3.89e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 203 DLEEKLETLRLKRSEDKAKLKELEK----HKIQLEQVQEWKSKMQE--------QQADLQRRLKEARKEAKEALEAKeRY 270
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESqeqqQRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAEEAK-RF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIE--MATLDKEmaEERAESLQQEVEALKErvdelttdleilkaeieekgsdgaassyQLKQLEEQNARLK 348
Cdd:PRK04863 913 VQQHGNALAQLEpiVSVLQSD--PEQFEQLKQDYQQAQQ----------------------------TQRDAKQQAFALT 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 349 DALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAE--------------STIDELKEQVDAAlgA 413
Cdd:PRK04863 963 EVVQRRAHFSYEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslkSSYDAKRQMLQEL--K 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 414 EEMVEMLTDRNLNLEEKVRELREtvgdleamnEMNDELQEN-ARETELELreQLDMAGARVREAQKRVEAAQEtvaDYQQ 492
Cdd:PRK04863 1041 QELQDLGVPADSGAEERARARRD---------ELHARLSANrSRRNQLEK--QLTFCEAEMDNLTKKLRKLER---DYHE 1106
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
209-525 |
5.40e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 209 ETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 288
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 289 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHV-- 366
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQELQALSEAEAeq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 367 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNE 446
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 447 MNDELQE-NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQP 525
Cdd:COG4372 264 ELAILVEkDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
193-484 |
5.80e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLE-EKLETLRLKRSEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARK--------EAKE 262
Cdd:PTZ00121 1068 QDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEArKAEEAKKKAEDARKAEEARKaedarkaeEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 263 ALEAKERYMEEMADTADAIEMAtldkemaeERAESLQQEVEAlkERVDELTTDLEILKAEiEEKGSDGAASSYQLKQLEE 342
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAEEA--------RKAEDAKKAEAA--RKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 343 qnarlkdalvrMRDLSSSEKQEHVKlqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTD 422
Cdd:PTZ00121 1217 -----------ARKAEDAKKAEAVK--KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 423 RNLNLEEKVRELR--ETVGDLEAMNEMNDELQ--ENARETELELREQLDMAGARVREAQKRVEAAQ 484
Cdd:PTZ00121 1284 KKAEEKKKADEAKkaEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
203-472 |
5.99e-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: 57.65 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 203 DLEEKLETLRLKRSEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQR---------------RLKEARKEAKEALEAk 267
Cdd:COG3096 833 DPEAELAALRQRRSELER---ELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELDAAQEA- 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 268 ERYMEEMADTADAIE--MATLDKEMAEEraESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQ-----LKQL 340
Cdd:COG3096 909 QAFIQQHGKALAQLEplVAVLQSDPEQF--EQLQADYLQAKEQQRRLKQQIFALSEVVQRR----PHFSYEdavglLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 341 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeEMVEML 420
Cdd:COG3096 983 SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-----EAEERA 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 421 TDRNLNLEEKVRELRETVGDLEAM-----NEMnDELQENARETELE---LREQLDMAGAR 472
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQltrceAEM-DSLQKRLRKAERDykqEREQVVQAKAG 1116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
249-1016 |
6.13e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 249 LQRRLKEARKEAKEALEAKEryMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgs 328
Cdd:COG1196 198 LERQLEPLERQAEKAERYRE--LKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 329 dgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVD 408
Cdd:COG1196 272 -------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 409 AALGAEEMvemltdrnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 488
Cdd:COG1196 341 ELEEELEE----------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 489 DYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikFAETKAHAKAIEMELRQMEVAQANRHMSLLTAf 568
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----------AAEEEAELEEEEEALLELLAELLEEAALLEAA- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 569 mpdsflrpggdhdcvlvlllmpRLICKAELIRKQAQEKFDLSENCSERPGLRGA-AGEQLSFAAGLVYSLSLLQATLHRY 647
Cdd:COG1196 479 ----------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAY 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 648 EHALSQCSVdvykkvGSLYPEMSAHERSLDFLIELLhKDQLDETVNVEPLTKaikyyqhlysIHLAEQPEDSTMQLADhi 727
Cdd:COG1196 537 EAALEAALA------AALQNIVVEDDEVAAAAIEYL-KAAKAGRATFLPLDK----------IRARAALAAALARGAI-- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 728 kftqsaldcmgvevgrlraflqgGQEATDIALLLRDLEtscsdtrqfckkirrrmpgtdapgiPAALAFGSQVSDTLLDC 807
Cdd:COG1196 598 -----------------------GAAVDLVASDLREAD-------------------------ARYYVLGDTLLGRTLVA 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 808 RKHLTWVVavlqevaaaaaqliaplaenegLPVAALEELAFKASEQIYGSPSSSpyeclrqsctilistmnklataMQEG 887
Cdd:COG1196 630 ARLEAALR----------------------RAVTLAGRLREVTLEGEGGSAGGS----------------------LTGG 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 888 EydaerppskpppVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 967
Cdd:COG1196 666 S------------RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 568940563 968 IEKVQTRLDETQTLLRKKEKDFEETMdalqADIDQLEAEKAELKQRLNS 1016
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEP----PDLEELERELERLEREIEA 778
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
191-496 |
6.24e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 57.22 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRA-QVRDLEEKLE-----TLRLkrseDKAKLKELEkhkiQLEQVQEWKSKMQEQQADLQRRLKEArkEAKEAL 264
Cdd:PLN02939 119 SKDGEQLSDfQLEDLVGMIQnaeknILLL----NQARLQALE----DLEKILTEKEALQGKINILEMRLSET--DARIKL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 265 EAKERYMEEMADTadaiEMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQLK 338
Cdd:PLN02939 189 AAQEKIHVEILEE----QLEKLRNELLIRGAteglcvHSLSKELDVLKEENMLLKDDIQFLKAELIEV----AETEERVF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 339 QLEEQNARLKDALvrmRDLSSsekqehvklqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeemve 418
Cdd:PLN02939 261 KLEKERSLLDASL---RELES----------KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAA------- 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 419 MLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETELELREQLDMAGArvrEAQKRVEAAQETVADYQQTIKK 496
Cdd:PLN02939 321 LVLDQNQDLRDKVDKLEASLKEAN-VSKFSSYKVELLQQKLKLLEERLQASDH---EIHSYIQLYQESIKEFQDTLSK 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
273-527 |
7.99e-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: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQNARLKDALV 352
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 353 RMRD-----------LSSSEKQEHVK----LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmv 417
Cdd:COG3883 94 ALYRsggsvsyldvlLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 418 emltdrnlNLEEKVRELRETVGDLEAmnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 497
Cdd:COG3883 172 --------ELEAQQAEQEALLAQLSA-----EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|
gi 568940563 498 RQLTAHLQDVNRELTNQQEASVERQQQPPP 527
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
192-404 |
9.33e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.30 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQ-------------------- 250
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELnEKLNELREELDELRKELAelnkaggsidklrkeierle 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 251 --------------------RRLKEARKEAKEALEAKERYMEEMADTADA-IEMATLDKEMAE--ERAESLQQEVEALKE 307
Cdd:COG1340 123 wrqqtevlspeeekelvekiKELEKELEKAKKALEKNEKLKELRAELKELrKEAEEIHKKIKElaEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 308 RVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmeKKNQELEVVRQQRE 387
Cdd:COG1340 203 EADELRKEADELHKEIVEAQ----------EKADELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAE 270
|
250
....*....|....*...
gi 568940563 388 RLQEELSQAES-TIDELK 404
Cdd:COG1340 271 EIFEKLKKGEKlTTEELK 288
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-499 |
1.50e-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: 55.95 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME 272
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRdlgeELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMADT-ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL---KAEIEEKGSDGAAssyqlkQLEEQNARLK 348
Cdd:pfam01576 349 EMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEG------QLQELQARLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 349 DAlvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaaLGAEEmvemlTDRNLNL 427
Cdd:pfam01576 423 ES-----ERQRAELAEKLsKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE-----LLQEE-----TRQKLNL 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 428 EEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 499
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
191-497 |
1.69e-07 |
|
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: 55.80 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQvqewkskmqeQQADLQRRLKEARKEakeaLEAKERy 270
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----------QLKVLSRSINKIKQN----LEQKQK- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 meEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDElttdLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDA 350
Cdd:TIGR04523 490 --ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----LESEKKEKESK----------ISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 351 LVRMrdlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLNLEEK 430
Cdd:TIGR04523 554 LKKE------------NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK-DLIKE--IEEKEKKISSLEKE 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 431 VRELRETVGDLEAMnEMNDELQENARETELEL-REQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 497
Cdd:TIGR04523 619 LEKAKKENEKLSSI-IKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDW 685
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
197-480 |
1.79e-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: 55.89 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeema 275
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 276 DTADAIEMATL-----DKEMAEERAESL------------QQEVEALK------ERVDELTTDLEILKAEIEEKGSDGAA 332
Cdd:pfam15921 407 DTGNSITIDHLrreldDRNMEVQRLEALlkamksecqgqmERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 333 SSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQeelsQAESTIDELKEQVdaaLG 412
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR----NVQTECEALKLQM---AE 559
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 413 AEEMVEMLTDRNLNLEEKVRELRETVGdleAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRV 480
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAG---AMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARV 627
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
196-554 |
1.92e-07 |
|
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: 55.47 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 196 GLRAQVRDLEEklETLRLKRSEDKAKLK--ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA--LEAK-ERY 270
Cdd:pfam05622 63 LLQKQLEQLQE--ENFRLETARDDYRIKceELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVkkLEATvETY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADaiematldkemaeeraesLQQEVEALKERvdelTTDLEILKAEIEEKGSDGAASSYQL----KQLEEQNAR 346
Cdd:pfam05622 141 KKKLEDLGD------------------LRRQVKLLEER----NAEYMQRTLQLEEELKKANALRGQLetykRQVQELHGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 347 LkdalvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDR 423
Cdd:pfam05622 199 L-----------SEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELRcaqLQQAELSQADALLSPSSDP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 424 NLNLEEKVR--ELRETVGDLEAMNEM---NDELQENARETEL------------ELREQLDMAGARVREAQKRVE----A 482
Cdd:pfam05622 268 GDNLAAEIMpaEIREKLIRLQHENKMlrlGQEGSYRERLTELqqlledanrrknELETQNRLANQRILELQQQVEelqkA 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568940563 483 AQETVADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQqqpPPETFDFKIKFAETKAHAKAIEMELRQME 554
Cdd:pfam05622 348 LQEQGSKAEDSSLLKQKLEEHLEklhEAQSELQKKKEQIEELE---PKQDSNLAQKIDELQEALRKKDEDMKAME 419
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
195-524 |
2.44e-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: 55.14 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 195 EGLRAQVRDLEEKL-----ETLRLKRS-EDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 263
Cdd:pfam07111 334 KQLRGQVAELQEQVtsqsqEQAILQRAlQDKAAEVEVERMsakglQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 264 LEAKERYMEEMADTADAI------------EMATLDKEMAEERA-ESLQQEVEALKERVDELTTDLeilkaeieekgsdg 330
Cdd:pfam07111 414 QIWLETTMTRVEQAVARIpslsnrlsyavrKVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADL-------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 331 aasSYQLKQLEEQNARLKDALvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDA 409
Cdd:pfam07111 480 ---SLELEQLREERNRLDAEL----QLSAHLIQQEVgRAREQGEAERQQLSEVAQQ---LEQELQRAQESLASVGQQLEV 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 410 ALGAEEMVemlTDRNLNLEEKVRELRETVGDleamnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 489
Cdd:pfam07111 550 ARQGQQES---TEEAASLRQELTQQQEIYGQ---------ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQ 617
|
330 340 350
....*....|....*....|....*....|....*
gi 568940563 490 YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:pfam07111 618 IQHRATQEKERNQELRRLQDEARKEEGQRLARRVQ 652
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
164-551 |
2.52e-07 |
|
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: 55.44 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 164 AQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKiqleqvQEWKSKMQ 243
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR------DEMLGLAP 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 244 EQQADLQRRLKEArKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALkERVDELTTDLE--ILKA 321
Cdd:TIGR00606 734 GRQSIIDLKEKEI-PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM-ERFQMELKDVErkIAQQ 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 322 EIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERLQEEL- 393
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKlqigtnlQRRQQFEEQLv 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 394 ---SQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----------EEKVRELRETVGDLEA-MNEMNDELQENARET 458
Cdd:TIGR00606 892 elsTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsnkkaQDKVNDIKEKVKNIHGyMKDIENKIQDGKDDY 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 459 ELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQD-VNRELTNQQEASVERQqqppPETFDFKI--- 534
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDnLTLRKRENELKEVEEE----LKQHLKEMgqm 1047
|
410
....*....|....*..
gi 568940563 535 KFAETKAHAKAIEMELR 551
Cdd:TIGR00606 1048 QVLQMKQEHQKLEENID 1064
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
194-488 |
2.61e-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: 55.11 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 194 EEGLRAQVRDLEEKLETLRLKRSE-----DKAKLK-------------ELEKH-------KIQLEQVQEWKSKMQEQQAD 248
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIEltahcDKLLLEnkeltqeasdmtlELKKHqediincKKQEERMLKQIENLEEKEMN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 249 LQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEmaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKGS 328
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE---KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 329 DGAASSYQLKQLEEQNARLKDALvrmrdlsSSEKQehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE---LKE 405
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELEL-------ASAKQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQK 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 406 QVDAALGAE--EMVEMLtDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL--------ELREQLDMagaRVRE 475
Cdd:pfam05483 693 EIDKRCQHKiaEMVALM-EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELsnikaellSLKKQLEI---EKEE 768
|
330
....*....|...
gi 568940563 476 AQKRVEAAQETVA 488
Cdd:pfam05483 769 KEKLKMEAKENTA 781
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
193-524 |
2.81e-07 |
|
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: 55.36 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 272
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP-LCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALV 352
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 353 RMRDL----SSSEKQEHVKLQKLMEKKNQELEV--VRQQRERLQEELSQAESTIDEL------KEQVDAALGAEEMVEML 420
Cdd:TIGR00618 595 RLQDLteklSEAEDMLACEQHALLRKLQPEQDLqdVRLHLQQCSQELALKLTALHALqltltqERVREHALSIRVLPKEL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 421 TDRNLNLEEKVRELRETV-GDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ---T 493
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLtYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqarT 754
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 568940563 494 IKKYR---------------QLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:TIGR00618 755 VLKARteahfnnneevtaalQTGAELSHLAAEIQFFNRLREEDTHL 800
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
336-496 |
3.26e-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: 52.62 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 336 QLKQLEEQNARLKDALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 415
Cdd:COG1579 18 ELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 416 M------VEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDmagARVREAQKRVEAAQETVAD 489
Cdd:COG1579 91 YealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167
|
....*..
gi 568940563 490 YQQTIKK 496
Cdd:COG1579 168 LAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
193-501 |
3.31e-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: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---EALEAKER 269
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKtltQRVLERET 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADaiEMATLDKEMAEERaESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKD 349
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT-------QVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 350 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdAALGAEEMVEMLTDRNLNL-E 428
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ---ARLQAAQLTLQLADASLALrE 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568940563 429 EKVRELRETVGDLEAMNEMNDELQENARETeleLREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLT 501
Cdd:pfam07888 298 GRARWAQERETLQQSAEADKDRIEKLSAEL---QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-499 |
3.38e-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: 54.80 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE-QVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKERYMEEMA 275
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEEKA 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 276 DTADAIEMA------------------------------TLDKEMAEERAESLQQEVE---ALKERVDELTTDLEILKAE 322
Cdd:pfam01576 566 AAYDKLEKTknrlqqelddllvdldhqrqlvsnlekkqkKFDQMLAEEKAISARYAEErdrAEAEAREKETRALSLARAL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 323 IEEKGsdgaassyQLKQLEEQNARLK---DALVRMRDLSSSEKQEHVKLQKLMEkknQELEVVRQQRERLQEELSQAEST 399
Cdd:pfam01576 646 EEALE--------AKEELERTNKQLRaemEDLVSSKDDVGKNVHELERSKRALE---QQVEEMKTQLEELEDELQATEDA 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 400 IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAmnEMNDELQENA------RETELELRE---QLDMAG 470
Cdd:pfam01576 715 KLRLEVNMQALKAQFE--RDLQARDEQGEEKRRQLVKQVRELEA--ELEDERKQRAqavaakKKLELDLKEleaQIDAAN 790
|
330 340
....*....|....*....|....*....
gi 568940563 471 ARVREAQKRVEAAQETVADYQQTIKKYRQ 499
Cdd:pfam01576 791 KGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
192-355 |
3.64e-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: 52.62 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRlkrsedkaklKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErym 271
Cdd:COG1579 24 HRLKELPAELAELEDELAALE----------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 eeMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDAL 351
Cdd:COG1579 91 --YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAEL 158
|
....
gi 568940563 352 VRMR 355
Cdd:COG1579 159 EELE 162
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
193-419 |
3.82e-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: 54.44 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWK-SKMQEQQADLQRRLKEARKEAKEALEAKERYM 271
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMATLDKEMAEERAES--LQQEVEALKERVDELTTD-------LEILKAEIEEKGSDGAASSYQLK---Q 339
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESgkAQAEVERLLGILREVENEkndkdkkIAELESLTLRQMKEQNKKVANIKhgqQ 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 340 LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaEEM 416
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADNSQQLQLEELMgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL--EEI 706
|
...
gi 568940563 417 VEM 419
Cdd:pfam10174 707 LEM 709
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
278-433 |
4.14e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 278 ADAIEMATLDKEMAEERAESLQQEVEA-LKERVDELTTDLEilkAEIEEKGSDgaassyqLKQLEEQNARLKDALvrmrd 356
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE---KELRERRNE-------LQKLEKRLLQKEENL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 357 lssSEKQEhvklqkLMEKKNQELEVVRQQRERLQEELSQAESTIDEL-KEQVD-----AALGAEEMVEMLTDrnlNLEEK 430
Cdd:PRK12704 99 ---DRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQeleriSGLTAEEAKEILLE---KVEEE 166
|
...
gi 568940563 431 VRE 433
Cdd:PRK12704 167 ARH 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-325 |
4.65e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKH--KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 269
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 270 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 325
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
318-523 |
5.75e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 318 ILKAEIEEKGSD-----GAASSYQLKQLEEQNARLKDAlvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEE 392
Cdd:COG4717 46 MLLERLEKEADElfkpqGRKPELNLKELKELEEELKEA--------EEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 393 LSQAEsTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEamnEMNDELQENARETELELREQLDMAGAR 472
Cdd:COG4717 118 LEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE---ELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568940563 473 VREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 523
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
265-558 |
5.92e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 265 EAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQN 344
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 345 ARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRN 424
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE---LEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 425 LNLEEKVRELRETVGDlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrQLTAHL 504
Cdd:COG4372 167 AALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA--LLDALE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 568940563 505 QDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQA 558
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
197-481 |
6.93e-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: 53.96 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLET--LRLKRSEDKAKL--KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---------EAKEA 263
Cdd:pfam05483 354 FEATTCSLEELLRTeqQRLEKNEDQLKIitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkqfeKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 264 LEAKERYM--------EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSY 335
Cdd:pfam05483 434 LKGKEQELifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 336 QLKQLEEqnarlkdalvrmrDLSSSEKQEHVKLQK---LMEKKNQ---ELEVVR----QQRERLQEELSQAESTIDELKE 405
Cdd:pfam05483 514 ELKKHQE-------------DIINCKKQEERMLKQienLEEKEMNlrdELESVReefiQKGDEVKCKLDKSEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 406 QVdaaLGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEM------NDELQENARET-----ELELREQLDMAGARVR 474
Cdd:pfam05483 581 EV---LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsAENKQLNAYEIkvnklELELASAKQKFEEIID 657
|
....*..
gi 568940563 475 EAQKRVE 481
Cdd:pfam05483 658 NYQKEIE 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
289-524 |
7.64e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 289 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKG---------SDGAASSYQLKQLEEQnarlKDALVRMRDLSS 359
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlngleSELAELDEEIERYEEQ----REQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 360 SEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgaeemVEMLTDRNLNLEEKVRELRETVG 439
Cdd:PRK02224 241 EVLEEH-------EERREELETLEAEIEDLRETIAETEREREELAEE----------VRDLRERLEELEEERDDLLAEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 440 DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDvnrELTNQQEASV 519
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES---ELEEAREAVE 380
|
....*
gi 568940563 520 ERQQQ 524
Cdd:PRK02224 381 DRREE 385
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
259-510 |
8.45e-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: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 259 EAKEALEAKERYMEEMADTADAIEM-ATLDKEMAEERAESLQQEVE-ALKERVDELTTDLEILKAEIEEKGS----DGAA 332
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKnKELFEQYKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 333 SSYQLKQLEEQNARLKDalvrmrDLSSSEKQEH--VKLQKLMEKKNQELEVVRQQRERLQEELSQAES--------TID- 401
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIED------DAAKNDKSNKaaIDIQLSLENFENKFLKISDIKKKINDCLKETESiekkissfSIDs 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 402 ---ELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAM-NEMNDE-------LQENARETELELREQLDMAG 470
Cdd:TIGR01612 1641 qdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIeIDVDQHkknyeigIIEKIKEIAIANKEEIESIK 1720
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 471 ARVREAQKRVEAAQET------------------VAD-YQQTIKKYRQLTAHLQDVNRE 510
Cdd:TIGR01612 1721 ELIEPTIENLISSFNTndlegidpnekleeynteIGDiYEEFIELYNIIAGCLETVSKE 1779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-567 |
1.11e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---------- 261
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvls 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 262 EALEAKERY---MEE----------MADTADAIEMATLDKEMAEERA-------------ESLQQEVEALKERVDELTTD 315
Cdd:TIGR02168 527 ELISVDEGYeaaIEAalggrlqavvVENLNAAKKAIAFLKQNELGRVtflpldsikgteiQGNDREILKNIEGFLGVAKD 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 316 LEILKAEIEEKGS------------DGAASSYQLKQLEEQNARLKDALVRMRDLSS--SEKQEHVKLQKlmekkNQELEV 381
Cdd:TIGR02168 607 LVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSILER-----RREIEE 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 382 VRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELE 461
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 462 LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR----QLTAHLQDVNRELTNQQEASVERQqqpppetfdFKIKFA 537
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLR---------ERLESL 829
|
410 420 430
....*....|....*....|....*....|
gi 568940563 538 ETKAHAKAIEMELRQMEVAQANRHMSLLTA 567
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-418 |
1.15e-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: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 239 KSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL------ 312
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 313 ----TTDLEILkaeieeKGSDGAAS----SYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvrQ 384
Cdd:COG3883 98 sggsVSYLDVL------LGSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE---A 168
|
170 180 190
....*....|....*....|....*....|....
gi 568940563 385 QRERLQEELSQAESTIDELKEQVDAALGAEEMVE 418
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
231-411 |
1.87e-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: 50.69 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 231 QLEQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD 310
Cdd:COG1579 8 ALLDLQELDSELDR----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 311 ELTT--DLEILKAEIEekgsdgaassyqlkQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRE- 387
Cdd:COG1579 84 NVRNnkEYEALQKEIE--------------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDe 149
|
170 180
....*....|....*....|....*..
gi 568940563 388 ---RLQEELSQAESTIDELKEQVDAAL 411
Cdd:COG1579 150 elaELEAELEELEAEREELAAKIPPEL 176
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
224-516 |
2.58e-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: 51.67 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 224 ELEKHKIQLEQVQEWKSKMQEQQadlqrrlKEARKEAKEALEAKERYMEEMADtadaiematldkemaeeRAESLQQEVE 303
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH-------KRARIELEKKASALKRQLDRESD-----------------RNQELQKRIR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 304 ALKERVDELTtdlEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQEL---- 379
Cdd:pfam05557 59 LLEKREAEAE---EALREQAELNRLKKKYLEALNKKLNEKESQLADA----REVISCLKNELSELRRQIQRAELELqstn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 380 ---EVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNLNLEEKVRELRETVGDLEAMNEMNDELqenAR 456
Cdd:pfam05557 132 selEELQERLDLLKAKASEAEQLRQNLEKQQSS----------LAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL---AR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 457 ETELE-LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 516
Cdd:pfam05557 199 IPELEkELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
200-415 |
2.62e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD--- 276
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 -------TADAIEMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgaassyqlkQLEEQNARL 347
Cdd:COG3883 94 alyrsggSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKA---------------------ELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 348 KDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 415
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
198-481 |
2.70e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEAKEALEAKERYmeemaD 276
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEeVDELKS----QLADYQQALDVQQTRAIQYQQAVQAL-----E 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 TADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKA-----------------------------EIEEK 326
Cdd:PRK04863 425 RAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevsrseawdvarELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 327 GSDGAASSYQLKQLE------EQNARLKDALVRMRD---------LSSSE--KQEHVKLQKLMEKKNQELEVVRQQRERL 389
Cdd:PRK04863 505 LREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLAefckrlgknLDDEDelEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 390 QEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQLDMA 469
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALA--------------RLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
330
....*....|..
gi 568940563 470 GARVREAQKRVE 481
Cdd:PRK04863 651 AARKQALDEEIE 662
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
188-498 |
2.75e-06 |
|
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: 52.15 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 188 PSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKL-----------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEA 256
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangelekasREETFARTALKNARLDLRRLFDEKQSEKDKKNKA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 257 RKEAKEALEAKERYMEEMADTADAIEMATLDkEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAAssyQ 336
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLE-EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA---E 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 337 LKQLEEQNARLKDAL----VRMRDLSSSEKQEHVKLQKLmEKKNQEL--------EVVRQQRERLQEELSQAESTIDELK 404
Cdd:pfam12128 749 LKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERI-AVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQ 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 405 EQvdaaLGAEEMVEMLTDRNLNLEEKVRE-----LRETVGDLEAMNEMNDELQE--NARETELELREQLDMAGARVREAQ 477
Cdd:pfam12128 828 QQ----LARLIADTKLRRAKLEMERKASEkqqvrLSENLRGLRCEMSKLATLKEdaNSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340
....*....|....*....|.
gi 568940563 478 KRVEAAQETVADYQQTIKKYR 498
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHS 924
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
191-466 |
2.83e-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: 51.90 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKM----QEQQADLQRRLKEARKEAKEALEA 266
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 267 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEI--EEKGSDGAASSYQLKQLEEQN 344
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 345 ARLKDALVRMRDLSSSEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRN 424
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSED-------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568940563 425 LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQL 466
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
186-552 |
3.07e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 186 PLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE 265
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 266 AKERymeemADTadaiematldkemaeERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyQLKQLEEQNA 345
Cdd:COG4913 331 QIRG-----NGG---------------DRLEQLEREIERLERELEERERRRARLEA--------------LLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 346 RLKDALVRMRDlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNL 425
Cdd:COG4913 377 ASAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS----------LERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 426 NLEEKVRELRetvgdleamnemnDELQENARETELELR---EQLDmagarVREAQKRVEAAQETV------------ADY 490
Cdd:COG4913 437 NIPARLLALR-------------DALAEALGLDEAELPfvgELIE-----VRPEEERWRGAIERVlggfaltllvppEHY 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568940563 491 QQTIKKYRQ--LTAHLQdVNRELTNQQEAsveRQQQPPPETFDFKIKFAETKAHAkAIEMELRQ 552
Cdd:COG4913 499 AAALRWVNRlhLRGRLV-YERVRTGLPDP---ERPRLDPDSLAGKLDFKPHPFRA-WLEAELGR 557
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
187-524 |
3.55e-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: 51.36 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 187 LPSPSKEEE-GLRAQVRDLEEKLETLrlkrsedKAKLKELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALE 265
Cdd:pfam10174 172 LPKKSGEEDwERTRRIAEAEMQLGHL-------EVLLDQKEKENIHLREELHRRNQLQPDPAKT-----KALQTVIEMKD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 266 AKERYMEEM-ADTADAIEMATLDKEM-AEERAESLQQeVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 343
Cdd:pfam10174 240 TKISSLERNiRDLEDEVQMLKTNGLLhTEDREEEIKQ-MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 344 NAR-------LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEM 416
Cdd:pfam10174 319 NSDckqhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 417 VEMLTDRNLNLEEKVR-------ELRETVGDLE--------AMNEMNDELQENARETElELREQldmagaRVREAQKRve 481
Cdd:pfam10174 396 INVLQKKIENLQEQLRdkdkqlaGLKERVKSLQtdssntdtALTTLEEALSEKERIIE-RLKEQ------REREDRER-- 466
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 568940563 482 aaQETVADYQQTIKKYRQLTAHLQdvnRELTNQQEASVERQQQ 524
Cdd:pfam10174 467 --LEELESLKKENKDLKEKVSALQ---PELTEKESSLIDLKEH 504
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
294-438 |
3.80e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.24 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 294 RAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME 373
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDE------ASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 374 KKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAE-----------EMVEMLTDRNLNLEEkvrELRETV 438
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEvvsrwtgipvgKLLEGEREKLLNLEE---ELHERV 551
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
182-469 |
4.02e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 182 GAAPPLPSpskeEEGLRAQVrdleEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMqeqqADLQRRLKEARKEAK 261
Cdd:PRK11281 30 ASNGDLPT----EADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEET----EQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 262 EALEAKERYMEEmADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLe 341
Cdd:PRK11281 98 QAQAELEALKDD-NDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQI- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 342 eqNARLKDALVRMRDLSSSEKQ----EHVKLQKLMEKKNQELEVVRQ-------QRE-------RLQEE----------- 392
Cdd:PRK11281 176 --RNLLKGGKVGGKALRPSQRVllqaEQALLNAQNDLQRKSLEGNTQlqdllqkQRDyltariqRLEHQlqllqeainsk 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 393 -LSQAESTIDELKEQVDAA-LGAEEMVEMLTDRNLNLEEKVrelretvgdLEAMNEMNDELQENareteLELREQLDMA 469
Cdd:PRK11281 254 rLTLSEKTVQEAQSQDEAArIQANPLVAQELEINLQLSQRL---------LKATEKLNTLTQQN-----LRVKNWLDRL 318
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
291-529 |
4.05e-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: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 291 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDAlvrmrdlssseKQEHVKLQK 370
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----------EEYNELQAELEAL-----------QAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 371 LMEKKNQELEvvrQQRERLQEELSQA------ESTIDELK--EQVDAALGAEEMVEMLTDRNLNLeekVRELRETVGDLE 442
Cdd:COG3883 73 EIAEAEAEIE---ERREELGERARALyrsggsVSYLDVLLgsESFSDFLDRLSALSKIADADADL---LEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 443 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 522
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*..
gi 568940563 523 QQPPPET 529
Cdd:COG3883 227 AAAAAAA 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-560 |
5.21e-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: 50.94 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETL--RLKRSEDKAKLKELEKHKIQlEQVQEWKSKMQEQQADLQRRLKEarkeaKEALEAKERYMEEm 274
Cdd:pfam01576 66 LAARKQELEEILHELesRLEEEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQKLQLE-----KVTTEAKIKKLEE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 adtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLeilkAEIEEKgsdgAASSYQLKQLEEqnARLKDALVRM 354
Cdd:pfam01576 139 ------------DILLLEDQNSKLSKERKLLEERISEFTSNL----AEEEEK----AKSLSKLKNKHE--AMISDLEERL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 355 RdlssSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNlNLEEKVREL 434
Cdd:pfam01576 197 K----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKN-NALKKIREL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 435 RETVGDLEAMNEMNDELQENARETELELREQLdmagarvrEAQK-RVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 513
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEEL--------EALKtELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 568940563 514 QQEASVERQQQpppetfdfkikfaetkAHAKAIEMELRQMEVAQANR 560
Cdd:pfam01576 342 SHEAQLQEMRQ----------------KHTQALEELTEQLEQAKRNK 372
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
192-324 |
5.35e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEdkaKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYM 271
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQ---LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQ 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568940563 272 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE 324
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
195-307 |
5.76e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 195 EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwkSKMQEQQADLQRRLKEARKEAKEALeAKERYMEEM 274
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED--KLLEEAEKEAQQAIKEAKKEADEII-KELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*..
gi 568940563 275 ADTA----DAIEMATLDKEMAEERAESLQQEVEALKE 307
Cdd:PRK00409 600 GYASvkahELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
319-554 |
6.06e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 319 LKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRD-------LSSSEKQEHVKLQKLMEKKNQ-------------- 377
Cdd:TIGR02169 644 LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQelsdasrkigeiek 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 378 ELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN--DELQENA 455
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 456 RETELELREQldmaGARVREAQKRVEAAQETVADYQQTIKkyrqltaHLQDVNRELTNqQEASVERQQQpppetfDFKIK 535
Cdd:TIGR02169 801 SKLEEEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQ-------ELQEQRIDLKE-QIKSIEKEIE------NLNGK 862
|
250
....*....|....*....
gi 568940563 536 FAETKAHAKAIEMELRQME 554
Cdd:TIGR02169 863 KEELEEELEELEAALRDLE 881
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-467 |
6.17e-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: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 240 SKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL 319
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADA---RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 320 KAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST 399
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568940563 400 IDELKEQVDAALGAEEMVEMLTDRNLN-LEEKVRELREtvgDLEAMNEMN----DELQEnARETELELREQLD 467
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEeLERELERLER---EIEALGPVNllaiEEYEE-LEERYDFLSEQRE 805
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
187-547 |
8.06e-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: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 187 LPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE---- 262
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQraml 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 263 --ALEAKERYMEEMAD--------------TADAIEMATLDKE----MAEERAESLQQEVEALKERVDELTTDLEILKAE 322
Cdd:TIGR00606 659 agATAVYSQFITQLTDenqsccpvcqrvfqTEAELQEFISDLQsklrLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 323 IEEKgsdgaasSYQLKQLEEQNARLKDALVRMR-DLSSSEKQEHVKLQKLMEKKNQELEVVRQQreRLQEELSQAESTID 401
Cdd:TIGR00606 739 IDLK-------EKEIPELRNKLQKVNRDIQRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIME--RFQMELKDVERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 402 ELKEQVDAALGAEEMVEMltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE------QLDMAGARVRE 475
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseklQIGTNLQRRQQ 885
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 476 AQKRVEAAQETVADYQQTIKKYR-------QLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFAETKAHAKAIE 547
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKeqdspleTFLEKDQQEKEELISSKETSNKKAQD---KVNDIKEKVKNIHGYMKDIE 961
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
203-467 |
1.02e-05 |
|
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: 49.85 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 203 DLEEKLETLRLKRSedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---------- 272
Cdd:pfam06160 71 EAEELNDKYRFKKA--KKALDEIE------ELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRElrktllanrf 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMADTADAIE--MATLDKE---------------------MAEERAESLQQEVEALKERVDELTTD----LEILKAEIEE 325
Cdd:pfam06160 143 SYGPAIDELEkqLAEIEEEfsqfeeltesgdylearevleKLEEETDALEELMEDIPPLYEELKTElpdqLEELKEGYRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 326 KGSDGAASSY-----QLKQLEEQNARLKDALVRMRDLSSSEKQEHVK-----LQKLMEKKNQELEVVRQQRERLQEELSQ 395
Cdd:pfam06160 223 MEEEGYALEHlnvdkEIQQLEEQLEENLALLENLELDEAEEALEEIEeridqLYDLLEKEVDAKKYVEKNLPEIEDYLEH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 396 AESTIDELKEQVD--------------AALGAEEMVEMLTDRNLNLEEKVRE-----------LRETVGDLEAMNEMNDE 450
Cdd:pfam06160 303 AEEQNKELKEELErvqqsytlneneleRVRGLEKQLEELEKRYDEIVERLEEkevayselqeeLEEILEQLEEIEEEQEE 382
|
330 340
....*....|....*....|
gi 568940563 451 LQE---NARETELELREQLD 467
Cdd:pfam06160 383 FKEslqSLRKDELEAREKLD 402
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
192-405 |
1.14e-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: 49.97 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKErY 270
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAREDALNQSLKELMHQARTVLKART-E 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEmaeeraESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassyqlkqleEQNARLKDA 350
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAEL------SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD-----------EDILNLQCE 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568940563 351 LVrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 405
Cdd:TIGR00618 825 TL---------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
245-484 |
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 568940563 245 QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTtdlEILKAEIE 324
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 325 EKGSDGAASSYQLKQLEEQNarLKDALVRMRDLSSSEKQEhvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 404
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 405 EQVDAALGAEEMVEMLTDRnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 484
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
198-511 |
1.41e-05 |
|
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: 49.47 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLrLKRS--EDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEaKERYMEEMA 275
Cdd:pfam06160 9 YKEIDELEERKNEL-MNLPvqEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELND-KYRFKKAKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 276 DTADAiematldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEE---------------KGSDGAAssyqLKQL 340
Cdd:pfam06160 87 ALDEI-----------EELLDDIEEDIKQILEELDELLESEEKNREEVEElkdkyrelrktllanRFSYGPA----IDEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 341 EEQNARLKDALVRMRDLSSSekQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST----IDELKEqvdaalGAEEM 416
Cdd:pfam06160 152 EKQLAEIEEEFSQFEELTES--GDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTElpdqLEELKE------GYREM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 417 VEM---LTDRNL-----NLEEKVRELRETV--GDLEAMNEMNDELQENAreteLELREQLdmagarvreaQKRVEAAQEt 486
Cdd:pfam06160 224 EEEgyaLEHLNVdkeiqQLEEQLEENLALLenLELDEAEEALEEIEERI----DQLYDLL----------EKEVDAKKY- 288
|
330 340
....*....|....*....|....*
gi 568940563 487 vadYQQTIKKYRQLTAHLQDVNREL 511
Cdd:pfam06160 289 ---VEKNLPEIEDYLEHAEEQNKEL 310
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
193-396 |
1.56e-05 |
|
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: 47.72 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEARKEAKEALEake 268
Cdd:pfam00261 37 EVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrkvLENRALKDEEKMEILEAQLKEAKEIAEEADR--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 269 RYMEemadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEiEEKGSDgAASSYQLkQLEEQNARLK 348
Cdd:pfam00261 114 KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEAS-EEKASE-REDKYEE-QIRFLTEKLK 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568940563 349 DALVRMRDlsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA 396
Cdd:pfam00261 187 EAETRAEF----AERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
200-516 |
1.70e-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: 49.20 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeemadTAD 279
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL-------CAA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 AIEMATLDKEMAEERAESLQQeveALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSS 359
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 360 SE---------KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST-------IDELKEQVDAALGAEEMVEMLTDR 423
Cdd:TIGR00618 523 PGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcDNRSKEDIPNLQNITVRLQDLTEK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 424 NLNLEEKVR--------ELRETVGDLEAMNEMNDELQENARE------TELEL-REQLDMAGARVREAQKRVEAAQETVA 488
Cdd:TIGR00618 603 LSEAEDMLAceqhallrKLQPEQDLQDVRLHLQQCSQELALKltalhaLQLTLtQERVREHALSIRVLPKELLASRQLAL 682
|
330 340
....*....|....*....|....*...
gi 568940563 489 DYQQTikKYRQLTAHLQDVNRELTNQQE 516
Cdd:TIGR00618 683 QKMQS--EKEQLTYWKEMLAQCQTLLRE 708
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
192-524 |
1.87e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDK--AKLKELEKHKIQLEQvqewkskmQEQQADLQRRLKEARKEAKEALEA-KE 268
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENRMTLEAIRvtQSDRDLFKHLITEST--------NYVAADYMRHANERRVHLEEALELrRE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 269 RYMEEmadtadaiemATLDKEmaEERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgAASSYQlkQLEEQNARLK 348
Cdd:PRK04863 295 LYTSR----------RQLAAE--QYRLVEMARELAELNEAESDLEQDYQ-------------AASDHL--NLVQTALRQQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 349 DALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ---VDAALgaeemvEMLTDRNL 425
Cdd:PRK04863 348 EKIERYQA-------DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQAL------DVQQTRAI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 426 NLEEKVRELRETvgdlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHL- 504
Cdd:PRK04863 415 QYQQAVQALERA----KQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVs 490
|
330 340
....*....|....*....|....*..
gi 568940563 505 ----QDVNRELTNQ---QEASVERQQQ 524
Cdd:PRK04863 491 rseaWDVARELLRRlreQRHLAEQLQQ 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
903-1023 |
1.99e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 903 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLDE 977
Cdd:COG1196 213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568940563 978 TQTLLRKKEKDF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1023
Cdd:COG1196 293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
197-441 |
2.04e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHkiqleqVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 276
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 tadaiematLDKEMaEERAESLQ---QEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALVR 353
Cdd:PHA02562 246 ---------LVMDI-EDPSAALNklnTAAAKIKSKIEQFQKVIKMYE--------KGGVCPTCTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 354 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTDRNLNLEEKVR 432
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNKISTNKQSLITLVDKAKKVKAAiEELQAEFVDNAEELAKLQD 386
|
....*....
gi 568940563 433 ELRETVGDL 441
Cdd:PHA02562 387 ELDKIVKTK 395
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
377-560 |
2.05e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 377 QELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--------EEKVRELRETVGDLEAMNEMN 448
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELlllklrelEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 449 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 528
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE---- 334
|
170 180 190
....*....|....*....|....*....|..
gi 568940563 529 tFDFKIKFAETKAHAKAIEMELRQMEVAQANR 560
Cdd:COG1196 335 -LEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
282-518 |
2.09e-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: 48.03 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 282 EMATLDKEMA--EERAESLQQEVEALKERVDELTT---DLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRD 356
Cdd:pfam09728 33 EMKRLQKDLKklKKKQDQLQKEKDQLQSELSKAILaksKLEKLCRELQK----------QNKKLKEESKKLAKEEEEKRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 357 LSSSEKQEHVK-LQKLMEKKNQELEVVRQQRERLQEELsqaESTID--ELKE-QVDAALGAEEMVEMLTDRNLNLEEKVR 432
Cdd:pfam09728 103 ELSEKFQSTLKdIQDKMEEKSEKNNKLREENEELREKL---KSLIEqyELRElHFEKLLKTKELEVQLAEAKLQQATEEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 433 ELRETVGDLEAMNEMNDELQEnARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELT 512
Cdd:pfam09728 180 EKKAQEKEVAKARELKAQVQT-LSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWK 258
|
....*.
gi 568940563 513 NQQEAS 518
Cdd:pfam09728 259 RKWEKS 264
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
192-558 |
2.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQ-VRDLEEKLETLRLKRSEDkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 270
Cdd:PTZ00121 1123 KAEDARKAEeARKAEDARKAEEARKAED-AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-AEELRKAEDAR 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADaiematldkemAEERAESLQQEVEAlkERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEqnARLKDA 350
Cdd:PTZ00121 1201 KAEAARKAE-----------EERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE--ARMAHF 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 351 LVRMRDLSSSEKQEHVKLQKLMEKKNqelevvrqqrerlQEELSQAEST--IDELKEQVDAALGAEEmvemLTDRNLNLE 428
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKK-------------ADEAKKAEEKkkADEAKKKAEEAKKADE----AKKKAEEAK 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 429 EKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ---ETVADYQQTIKKYRQLTAHLQ 505
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 568940563 506 DVNRELTNQQEASVERQQQPPPETFDFKIKFAETKahAKAIEMELRQMEVAQA 558
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKA 1459
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
204-342 |
2.51e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 204 LEEKLETLRLKRSEDKAK--LKELEK--HKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadtad 279
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKeaEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEE------ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568940563 280 aiemaTLDKEMaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaaSSYQLKQLEE 342
Cdd:PRK12704 97 -----NLDRKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELER 146
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
176-414 |
2.56e-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: 48.80 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 176 PALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKL-----------ETLRL--------KRSE--DKAK--LKELEKHKIQL 232
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvadaarrqfeKAYELvckiagevERSQawQTARelLRRYRSQQALA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 233 EQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERyMEEMADTADAiEMATLDKEMAE--ERAESLQQEVEA 304
Cdd:COG3096 512 QRLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEA-QLEELEEQAAEavEQRSELRQQLEQ 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 305 LKERVDELTTdleilKAEIEEKGSDgaassyQLKQLEEQ-NARLKDalvrmrdlsSSEKQEHvkLQKLMEKK---NQELE 380
Cdd:COG3096 590 LRARIKELAA-----RAPAWLAAQD------ALERLREQsGEALAD---------SQEVTAA--MQQLLEREreaTVERD 647
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568940563 381 VVRQQRERLQ---EELSQAESTID----ELKEQVDAALGAE 414
Cdd:COG3096 648 ELAARKQALEsqiERLSQPGGAEDprllALAERLGGVLLSE 688
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-312 |
2.67e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 187 LPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEA 266
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER---ELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568940563 267 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL 312
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
191-524 |
2.68e-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: 48.68 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKlkELEKHKIQLEQVQEWKSK--------MQEQQADLQRRLKEARKEAKE 262
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 263 ALEAKERYMEEMA---DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKaeieekgsdgaassyqlKQ 339
Cdd:pfam12128 438 EEYRLKSRLGELKlrlNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR-----------------KR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 340 LEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM 419
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 420 LTDRNLNLEEKVRELRETVGDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETvadYQQTIKK 496
Cdd:pfam12128 578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEalqSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLD 654
|
330 340 350
....*....|....*....|....*....|..
gi 568940563 497 YRQLTAHLQD----VNRELTNQQEASVERQQQ 524
Cdd:pfam12128 655 LRRLFDEKQSekdkKNKALAERKDSANERLNS 686
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
238-401 |
3.02e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.17 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 238 WKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAiematLDKEMAEERAESLQQEVEALKERVDELTTDLE 317
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-----QQRQEARREREELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 318 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQehvklQKLMEKKNQELEVVRQQRERLQEELSQAE 397
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR-----KLLLKLLDAELEEEKAQRVKKIEEEADLE 173
|
....
gi 568940563 398 STID 401
Cdd:PRK12705 174 AERK 177
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
194-370 |
3.06e-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: 47.50 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 194 EEGLRAQVRDLEEKLETLRLKR-SEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKER 269
Cdd:pfam15905 147 EDGTQKKMSSLSMELMKLRNKLeAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKekiEEKSETEKLLE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADAIEMATLD----KEMAEERA---ESLQQEVEA----LKERVDELTTDLEILKAEIEEKgsdgaassyqLK 338
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDiaqlEELLKEKNdeiESLKQSLEEkeqeLSKQIKDLNEKCKLLESEKEEL----------LR 296
|
170 180 190
....*....|....*....|....*....|..
gi 568940563 339 QLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 370
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
194-321 |
3.29e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 194 EEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE-QVQEWkskmqEQQADLQrrLKEARKE-AKEALEAKERYM 271
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEaEAEKW-----EEKARLA--LEKGREDlAREALERKAELE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIematldkEMAEERAESLQQEVEALKERVDELTTDLEILKA 321
Cdd:COG1842 98 AQAEALEAQL-------AQLEEQVEKLKEALRQLESKLEELKAKKDTLKA 140
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
204-528 |
3.52e-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: 48.40 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 204 LEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTAD-AIE 282
Cdd:pfam15818 9 LLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQlATE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 283 MATLDKEMAEERAESLQQEVEALKERVDELTTDLEI--LKAEIEEKGSDGAASSY-----QLKQLEEQNARL----KDAL 351
Cdd:pfam15818 89 IKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLhlLAKEDHHKQLNEIEKYYatitgQFGLVKENHGKLeqnvQEAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 352 VRMRDLSS-SEKQE--------------------HVKLQKLMEKKNQELEVVRQQRERLQEELS---------QAEST-I 400
Cdd:pfam15818 169 QLNKRLSAlNKKQEseicslkkelkkvtsdliksKVTCQYKMGEENINLTIKEQKFQELQERLNmelelnkkiNEEIThI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 401 DELKEQVDAALG-AEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAgarVREAQKR 479
Cdd:pfam15818 249 QEEKQDIIISFQhMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA---LGTWKKH 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 568940563 480 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPE 528
Cdd:pfam15818 326 VEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPE 374
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
902-1023 |
3.59e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 902 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLDETQTL 981
Cdd:COG1196 252 EAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568940563 982 LRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1023
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-489 |
3.62e-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: 48.19 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLK-RSEDKAKLKELEKHKIQLEQVQEWKSKMqEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEMLRKVVEELTAKKMTLESSERT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMAT-------------LDKEMAE--------ERAESLQQEVEALKERVDELTTDLEILKAEIE----- 324
Cdd:pfam15921 498 VSDLTASLQEKERAIeatnaeitklrsrVDLKLQElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtql 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 325 --EKGSDGAASSYQLKQLEEQ--NARL-----------KDALVRMRDLSSSEKQ-EHVKLQKLMEKKNQELEVVRQQRER 388
Cdd:pfam15921 578 vgQHGRTAGAMQVEKAQLEKEinDRRLelqefkilkdkKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 389 LQEELSQAESTIDELKEQVDAAL-----GAEEMvEMLTDR-NLNLEEKVRELRETVGDLEAMNEMNDelqeNARETELEL 462
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEM-ETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDG----HAMKVAMGM 732
|
330 340
....*....|....*....|....*..
gi 568940563 463 REQLDMAGARVREAQKRVEAAQETVAD 489
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTN 759
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
192-465 |
3.83e-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: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLR---------LKRSEDKAKLKeLEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEake 262
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRdelesvreeFIQKGDEVKCK-LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 263 aLEAKERYMEEMADTADAIEmatldkemAEERAESLQQEVEALKerVDELTTDLEILKAEIEEKgSDGAASSYQLKQLEE 342
Cdd:pfam05483 603 -IENKNKNIEELHQENKALK--------KKGSAENKQLNAYEIK--VNKLELELASAKQKFEEI-IDNYQKEIEDKKISE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 343 QNarlkdaLVRMRDLSSSEKQEHVKLQKLMEKKNQE--------LEVVRQQRERLQEElSQAESTIDELKEQVDAALGAE 414
Cdd:pfam05483 671 EK------LLEEVEKAKAIADEAVKLQKEIDKRCQHkiaemvalMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKAA 743
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568940563 415 EMVEMLTDRNlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQ 465
Cdd:pfam05483 744 LEIELSNIKA--------ELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
197-514 |
4.01e-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: 47.81 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKA---KLKELEKHKIQLEQVQEWKSKMQEQQA---DLQRRLKEAR------------- 257
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKNSKSELAripELEKELERLRehnkhlnenienk 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 258 ---KEAKEALEAKERYMEEMADTADAIEM--------------------ATLDKEMA-EERAESLQQEVEALKERVDELT 313
Cdd:pfam05557 224 lllKEEVEDLKRKLEREEKYREEAATLELekekleqelqswvklaqdtgLNLRSPEDlSRRIEQLQQREIVLKEENSSLT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 314 TDLEILKAEIEEKGSDGAAssyQLKQLEEQNARLK--DALVRM-----------RDL----------------SSSEKQE 364
Cdd:pfam05557 304 SSARQLEKARRELEQELAQ---YLKKIEDLNKKLKrhKALVRRlqrrvllltkeRDGyrailesydkeltmsnYSPQLLE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 365 HVK-LQKLMEKKNQELEVVRQQRERLQEEL-------SQAESTIDELKEQVDAA--LGAEEMVEMLTDRNLNLEEKVREL 434
Cdd:pfam05557 381 RIEeAEDMTQKMQAHNEEMEAQLSVAEEELggykqqaQTLERELQALRQQESLAdpSYSKEEVDSLRRKLETLELERQRL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 435 RETVGDLEA---------MNEMND----ELQEN----ARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTI--- 494
Cdd:pfam05557 461 REQKNELEMelerrclqgDYDPKKtkvlHLSMNpaaeAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTstm 540
|
410 420
....*....|....*....|..
gi 568940563 495 --KKYRQLTAHLQDvnRELTNQ 514
Cdd:pfam05557 541 nfKEVLDLRKELES--AELKNQ 560
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
212-495 |
4.02e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 212 RLKRSEDKAKL---KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 288
Cdd:COG4372 3 RLGEKVGKARLslfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 289 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKL 368
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 369 QKLMEKKNQELEVVRQQRERLQEELSQAestidELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN 448
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 568940563 449 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIK 495
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
247-522 |
4.02e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 247 ADLQRRLKEArKEAKEALEAKERYMEEMADTadaieMATLDK-EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 325
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQT-----LALLDKiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 326 KgSDGAASSYQLKQLEEQNARLKDALvrmrdlsssekQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 405
Cdd:PRK11281 113 E-TRETLSTLSLRQLESRLAQTLDQL-----------QN---AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 406 QVDAALGAEEmvemltdrNLNLEEKVRELRETVGdLEAMNEMN-DELQENARETELeLREQLDMAGARVREAQKRVEAAQ 484
Cdd:PRK11281 178 LLKGGKVGGK--------ALRPSQRVLLQAEQAL-LNAQNDLQrKSLEGNTQLQDL-LQKQRDYLTARIQRLEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568940563 485 ETV-----ADYQQTIKKYRQltahLQDVNRELTN---QQEASVERQ 522
Cdd:PRK11281 248 EAInskrlTLSEKTVQEAQS----QDEAARIQANplvAQELEINLQ 289
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
193-406 |
4.11e-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: 48.19 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKH--KIQLEQVqewksKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARvsDLELEKV-----KLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDG-------------AASSYQ 336
Cdd:pfam15921 666 RNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmEGSDGhamkvamgmqkqiTAKRGQ 742
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568940563 337 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME----KKNQ---ELEVVRQQRERLQEELSQAESTIDELKEQ 406
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvatEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
253-408 |
4.14e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 253 LKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEeraesLQQEVEALKERVDElttdleiLKAEIEEKgsdgaa 332
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR-----LEEQVERLEAEVEE-------LEAELEEK------ 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 333 ssyqlkqlEEQNARLKDALVRMRdlsSSEKQEHvklqklmeKKNQELEVVRQQRERLQEELSQAESTIDELKEQVD 408
Cdd:COG2433 440 --------DERIERLERELSEAR---SEERREI--------RKDREISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
191-406 |
4.31e-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: 48.14 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRlkrsedkaklKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERY 270
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIE----------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-LEAQLRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqLKQLEEQNARLKDA 350
Cdd:TIGR02169 901 LE------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--------LEDVQAELQRVEEE 966
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 351 LVRMRDLSSSEKQEHvklqKLMEKKNQELEvvrQQRERLQEELSQAESTIDELKEQ 406
Cdd:TIGR02169 967 IRALEPVNMLAIQEY----EEVLKRLDELK---EKRAKLEEERKAILERIEEYEKK 1015
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
904-1013 |
5.00e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 904 RAAALRAEITDAE----GLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA------------------- 960
Cdd:COG1579 25 RLKELPAELAELEdelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeieslkrr 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 961 -------AKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQR 1013
Cdd:COG1579 105 isdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-445 |
5.58e-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: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMAD 276
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEK---KLKNLEAELLQLQEDLAASERARRQAQQERDEL--ADEIASGASGK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 TADAIEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 354
Cdd:pfam01576 878 SALQDEKRRLEARIAqlEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 355 RDLSSSEKQEHV-----KLQKLMEKKNQEL-------EVVRQQRERLQEELSQAES---TIDELKEQVDAALGA------ 413
Cdd:pfam01576 958 EGTVKSKFKSSIaaleaKIAQLEEQLEQESrerqaanKLVRRTEKKLKEVLLQVEDerrHADQYKDQAEKGNSRmkqlkr 1037
|
250 260 270
....*....|....*....|....*....|....
gi 568940563 414 --EEMVEMLTDRNLNLEEKVRELRETVGDLEAMN 445
Cdd:pfam01576 1038 qlEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
192-516 |
5.93e-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: 46.95 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRlkRSEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELR--RRDQKRQETLERERRLLLQQSQEqWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEKGSDgAASSYQLKQLEEQNarlkda 350
Cdd:pfam15558 96 WREQAEDQENQRQEKLERARQEAEQRKQCQE-QRLKEKEEELQALREQNSLQLQERLEE-ACHKRQLKEREEQK------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 351 lvRMRDLSSSEKQEHVKLQKLMEKKNQElevvrqqrERLQEELSQaestidELKEQVdaalgAEEMVEMLtdrnlnLEEK 430
Cdd:pfam15558 168 --KVQENNLSELLNHQARKVLVDCQAKA--------EELLRRLSL------EQSLQR-----SQENYEQL------VEER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 431 VRELREtvgdlEAMNEmNDELQENARETELELREQLDMAGARVREAQKRVE----AAQETVADYQQTIKKYRQLTAHLQD 506
Cdd:pfam15558 221 HRELRE-----KAQKE-EEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqarqVAHKTVQDKAQRARELNLEREKNHH 294
|
330
....*....|
gi 568940563 507 VNRELTNQQE 516
Cdd:pfam15558 295 ILKLKVEKEE 304
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
191-397 |
6.38e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRlkrsedkaklkelEKHKIqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFR-------------QKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAE--SLQQEVEALKER-------VDELTTDLEILKAEIEEKGSDGAASSY-QLKQL 340
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568940563 341 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQRERLQEELSQAE 397
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRL----EREVEVARELYESLLQRLEEAR 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
205-513 |
6.58e-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: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 205 EEKLETLRLKRSE----------DKAKLKELEKHKIQL--EQVQEW--------KSKMQEQQADLQRRLKEARKEAKEAL 264
Cdd:COG3096 784 EKRLEELRAERDElaeqyakasfDVQKLQRLHQAFSQFvgGHLAVAfapdpeaeLAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 265 EAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELT------TDLEILKAEIEEKGSDGAASSYQL 337
Cdd:COG3096 864 QQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQAFIQqhgkalAQLEPLVAVLQSDPEQFEQLQADY 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 338 KQLEEQNARLKDALVRMRDLssSEKQEHVKLQKL--MEKKNQELEvvrqqrERLQEELSQAESTIDELKEQVDAALG-AE 414
Cdd:COG3096 944 LQAKEQQRRLKQQIFALSEV--VQRRPHFSYEDAvgLLGENSDLN------EKLRARLEQAEEARREAREQLRQAQAqYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 415 EMVEMLTDRNLNLEEKVRELRETVGDLEAMN-EMNDELQENARETELELREQLDMAGARVREAQK---RVEAAQETVAdy 490
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEELGvQADAEAEERARIRRDELHEELSQNRSRRSQLEKqltRCEAEMDSLQ-- 1093
|
330 340
....*....|....*....|...
gi 568940563 491 qqtiKKYRQLTAHLQDVNRELTN 513
Cdd:COG3096 1094 ----KRLRKAERDYKQEREQVVQ 1112
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
203-531 |
6.63e-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: 47.27 E-value: 6.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 203 DLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEW---KSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadTAD 279
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltqKREAQEEQLKKQQLLKQLRARIEE-LRAQEAVLEE---TQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 AIEMATLDKEMAEEraeslQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlkdalvrmRDLSS 359
Cdd:TIGR00618 285 RINRARKAAPLAAH-----IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----------RRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 360 SEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAES-TIDELKEQVDAALGAEEMVEMLTDRNLNLEEkvRELRETV 438
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 439 GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEAS 518
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330
....*....|...
gi 568940563 519 VERQQQPPPETFD 531
Cdd:TIGR00618 507 CGSCIHPNPARQD 519
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-555 |
7.36e-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: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRsedkaklkelekhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 271
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMER-----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEieekgSDGAASSYQLKQLEEQNARLKDAL 351
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 352 VRMRDlsssekqehvKLQKLMEKKNQELEVVRQQ-RERLQEELSQAESTIDELKEQVDAALGA--------EEMVEMLTD 422
Cdd:pfam15921 241 FPVED----------QLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGLTEKASSARSQansiqsqlEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 423 RNLNLEEKVRELRETVGDLEAmnemndELQENARETE---LELREQLDMAGARVREAqkRVEAAQETvadyQQTIKKYRQ 499
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRS------ELREAKRMYEdkiEELEKQLVLANSELTEA--RTERDQFS----QESGNLDDQ 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 500 LTAHLQDVNREltnQQEASVERQQQppPETFDFKIKFAETKAHAKAiEMELRQMEV 555
Cdd:pfam15921 379 LQKLLADLHKR---EKELSLEKEQN--KRLWDRDTGNSITIDHLRR-ELDDRNMEV 428
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
193-524 |
7.81e-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: 47.02 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDK--AKLKELEKHKiqleQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE----------IEEKGSDGAASSYQLK-- 338
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlqrsmstqkaLEEDLQIATKTICQLTee 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 339 ---QLEEQN-ARLKDALVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---------- 404
Cdd:pfam05483 333 keaQMEELNkAKAAHSFV-----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkevel 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 405 EQVDAALGAEemvEMLTDRNLNLEEKVRELR----ETVGDLEAM-NEMND-ELQENARETELE--LREQLDMAGARVREA 476
Cdd:pfam05483 408 EELKKILAED---EKLLDEKKQFEKIAEELKgkeqELIFLLQAReKEIHDlEIQLTAIKTSEEhyLKEVEDLKTELEKEK 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568940563 477 QKRVeaaqETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:pfam05483 485 LKNI----ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
192-462 |
8.76e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.77 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKA---------------KLKELEKHKI-----------QLEQVQEWKSKMQEQ 245
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKEssskpselalnemieKLKKEIDLEYteaviamglqeRLENLREEFSKANSQ 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 246 QADLQRRLKEA----RKEAKEALEAKERYmEEMADTADAIEMATLDKEMAE--ERAESLQQEV-EALKERVD--ELTTDL 316
Cdd:PLN03229 502 DQLMHPVLMEKieklKDEFNKRLSRAPNY-LSLKYKLDMLNEFSRAKALSEkkSKAEKLKAEInKKFKEVMDrpEIKEKM 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 317 EILKAEIEEKGS------DGAASSYQLKQLEEQNARLKDAL---------VRMRDLSSSEKQE----HVKLQKLMEKKNQ 377
Cdd:PLN03229 581 EALKAEVASSGAssgdelDDDLKEKVEKMKKEIELELAGVLksmglevigVTKKNKDTAEQTPppnlQEKIESLNEEINK 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 378 ELEVV------RQQRERLQEELSQAESTID------------ELKEQVDAALGAEEMVEmltdRNLNLEEKVRELRETVG 439
Cdd:PLN03229 661 KIERVirssdlKSKIELLKLEVAKASKTPDvtekekiealeqQIKQKIAEALNSSELKE----KFEELEAELAAARETAA 736
|
330 340
....*....|....*....|...
gi 568940563 440 DLEAMNEMNDELQENARETELEL 462
Cdd:PLN03229 737 ESNGSLKNDDDKEEDSKEDGSRV 759
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
260-413 |
9.57e-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: 45.82 E-value: 9.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 260 AKEALEAKERYMEEMADTADAIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaas 333
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEELEEakktikALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK-------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 334 syQLKQLEEQNARLKDALvrMRDLSSSEKQEHVKLQKLMEKKNQEL------------------EVVRQQRERLQEELSQ 395
Cdd:cd22656 154 --DQTALETLEKALKDLL--TDEGGAIARKEIKDLQKELEKLNEEYaaklkakidelkaliaddEAKLAAALRLIADLTA 229
|
170
....*....|....*...
gi 568940563 396 AESTIDELKEQVDAALGA 413
Cdd:cd22656 230 ADTDLDNLLALIGPAIPA 247
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
197-466 |
1.02e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKL-----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 271
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLeilkaeieekgsdgaasSYQLKQLEEQNARL 347
Cdd:pfam00038 103 NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheEEVRELQAQV-----------------SDTQVNVEMDAARK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 348 KDALVRMRDLSSS-EKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLN 426
Cdd:pfam00038 166 LDLTSALAEIRAQyEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQ-SLEIE--LQSLKKQKAS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568940563 427 LEEKVRELRET-VGDLEAMNEMNDELQENARETELELREQL 466
Cdd:pfam00038 243 LERQLAETEERyELQLADYQELISELEAELQETRQEMARQL 283
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
200-569 |
1.18e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 200 QVRDLEEKLETLRLKRSedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYmEEM----- 274
Cdd:PRK04778 87 QLFEAEELNDKFRFRKA--KHEINEIE------SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLY-RELrksll 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 ------ADTADAIE--MATLDKEMAEerAESLQQE---------VEALKERVDELTTDLEILKAEIEEKGSDGAAssyQL 337
Cdd:PRK04778 158 anrfsfGPALDELEkqLENLEEEFSQ--FVELTESgdyveareiLDQLEEELAALEQIMEEIPELLKELQTELPD---QL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 338 KQLEEQNARLKDA---------LVRMRDLssseKQEHVKLQKLMEkkNQELEVVRQQRERLQEELSQ------------- 395
Cdd:PRK04778 233 QELKAGYRELVEEgyhldhldiEKEIQDL----KEQIDENLALLE--ELDLDEAEEKNEEIQERIDQlydilerevkark 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 396 -AESTIDELKEQVDAAlgaEEMVEML---TDR-------NLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE 464
Cdd:PRK04778 307 yVEKNSDTLPDFLEHA---KEQNKELkeeIDRvkqsytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 465 QLDMAGARVREAQKRVEAAQETVADY-------QQTIKKYRQLtahLQDVNREltnqqeasVERQQQPP-PEtfDFKIKF 536
Cdd:PRK04778 384 ELEEILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNK---LHEIKRY--------LEKSNLPGlPE--DYLEMF 450
|
410 420 430
....*....|....*....|....*....|....*
gi 568940563 537 AETKAHAKAIEMEL--RQMEVAQANRHMSLLTAFM 569
Cdd:PRK04778 451 FEVSDEIEALAEELeeKPINMEAVNRLLEEATEDV 485
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
193-524 |
1.32e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERYME 272
Cdd:PRK04863 559 LQEELEARLESLSESVSEARERRMALRQQLEQLQ------ARIQRLAARAPAWLA-AQDALARLREQSGEEFEDSQDVTE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMADTADAIEMATLDKEMAEERAESLQQEVE--------------ALKER-----VDELTTDLEILKAEIEEKGSDGAAS 333
Cdd:PRK04863 632 YMQQLLERERELTVERDELAARKQALDEEIErlsqpggsedprlnALAERfggvlLSEIYDDVSLEDAPYFSALYGPARH 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 334 -------SYQLKQLEEQNARLKDALV------RMRD-LSSSEKQEHVKLQKLMEK-----------------KNQELEVV 382
Cdd:PRK04863 712 aivvpdlSDAAEQLAGLEDCPEDLYLiegdpdSFDDsVFSVEELEKAVVVKIADRqwrysrfpevplfgraaREKRIEQL 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 383 RQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQ---ENAR 456
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRsqlEQAK 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 457 ETELELREQLDMA--------GARVREAQKRVEAAQET---VADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQ 522
Cdd:PRK04863 872 EGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQ 951
|
..
gi 568940563 523 QQ 524
Cdd:PRK04863 952 RD 953
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
231-326 |
1.34e-04 |
|
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: 43.62 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 231 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTA--DAIEMATLDKEMAEERAESLQQE-VEALKE 307
Cdd:COG0711 39 GLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAkaEAEAEAERIIAQAEAEIEQERAKaLAELRA 118
|
90 100
....*....|....*....|.
gi 568940563 308 RVDELTTDL--EILKAEIEEK 326
Cdd:COG0711 119 EVADLAVAIaeKILGKELDAA 139
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
369-560 |
1.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 369 QKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEmn 448
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 449 dELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 528
Cdd:COG4942 94 -ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---- 168
|
170 180 190
....*....|....*....|....*....|..
gi 568940563 529 tfdFKIKFAETKAHAKAIEMELRQMEVAQANR 560
Cdd:COG4942 169 ---LEAERAELEALLAELEEERAALEALKAER 197
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
383-543 |
1.57e-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: 46.10 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 383 RQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnLNL-------EEKVRELREtvgDLEAMNEMNDElQENA 455
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrqQEKIERYQE---DLEELTERLEE-QEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 456 REtelELREQLDMAGARVREAQKRVEAAQETVADYQQTIK-------KYRQLTAHLQDVNR-----ELT-----NQQEAS 518
Cdd:COG3096 370 VE---EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARAlcglpDLTpenaeDYLAAF 446
|
170 180
....*....|....*....|....*
gi 568940563 519 VERQQQPPPETFDFKIKFAETKAHA 543
Cdd:COG3096 447 RAKEQQATEEVLELEQKLSVADAAR 471
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
226-523 |
1.58e-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: 46.37 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 226 EKHKIQLEQVQEWkskMQEQQAdLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMATLDKE-MAEERAESLQQEveA 304
Cdd:pfam12128 214 PKSRLNRQQVEHW---IRDIQA-IAGIMKIRPEFTKLQQEFNTLESAEL-------RLSHLHFGyKSDETLIASRQE--E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 305 LKERVDELTTDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDAlvrmrDLSSSEKQEHVKLqkLMEKKNQELEVVRQ 384
Cdd:pfam12128 281 RQETSAELNQLLRTLDDQWKEK-------------RDELNGELSAA-----DAAVAKDRSELEA--LEDQHGAFLDADIE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 385 QRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--EEKVRELRETVGDLEAMNEMNDELQENARET---- 458
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqal 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 459 ELELREQLDMAGARVREAQKRVEAAQET----VADYQQTIKKYRQLTAHLQDVN--RELTNQQEASVERQQ 523
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGElklrLNQATATPELLLQLENFDERIEraREEQEAANAEVERLQ 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
280-509 |
1.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 280 AIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqLKQLEEQNARLKDALVR 353
Cdd:COG4717 45 AMLLERLEKEADElfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEE-----------LEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 354 MRdlsssekQEHVKLQKLmekknQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnlnLEEKVRE 433
Cdd:COG4717 114 LR-------EELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 434 LRETVgdleamnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNR 509
Cdd:COG4717 179 LEELL----------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
220-348 |
1.96e-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: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 220 AKLKELEKHKIQLEQVQEwkskmqEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLdkemAEERAESLQ 299
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAA------DAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQA----LREELNELK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568940563 300 QEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLK 348
Cdd:pfam07926 71 AEIAELKAEAESAKAELEESEESWEE----------QKKELEKELSELE 109
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
191-309 |
2.00e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEE-EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAker 269
Cdd:COG0542 438 SFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--- 514
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 568940563 270 ymeemADTADAIEMAT---LDKeMAEERAESLQQEVEALKERV 309
Cdd:COG0542 515 -----EDIAEVVSRWTgipVGK-LLEGEREKLLNLEEELHERV 551
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
204-319 |
2.08e-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: 44.99 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 204 LEEKLETLrlkrsedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 271
Cdd:COG0216 2 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKKLLEDIEEA-------- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568940563 272 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 319
Cdd:COG0216 63 KELLEEESDPEM----REMAKE-------ELEELEARLEELEEELKIL 99
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
204-454 |
2.21e-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: 45.58 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 204 LEEKLETLRLKRSEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEarkeaKEA-LEAKERYMEEMAD--TADA 280
Cdd:pfam10174 308 LQTKLETLTNQNSDCKQHIEVL---KESLTAKEQRAAILQTEVDALRLRLEE-----KESfLNKKTKQLQDLTEekSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 281 IEMATLdKEM---AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA---RLKDALVRM 354
Cdd:pfam10174 380 GEIRDL-KDMldvKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 355 RDLSSSEKQEHVklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA-ALGAEEMVEMLTDRNLNLEEKVRE 433
Cdd:pfam10174 459 REREDRERLEEL------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKSLEIAVEQKKEE 532
|
250 260
....*....|....*....|.
gi 568940563 434 LRETVGDLEAMNEMNDELQEN 454
Cdd:pfam10174 533 CSKLENQLKKAHNAEEAVRTN 553
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-415 |
2.22e-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: 45.60 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETL--RLKRSEDKaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALEAKERYMEEM 274
Cdd:pfam12128 313 ADAAVAKDRSELEALedQHGAFLDA----DIETAAADQEQLPSWQSELENLEERL-----KALTGKHQDVTAKYNRRRSK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 ADTADAIEMATLDKEMA---EERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLK-QLEEQNARLKDA 350
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLAkirEARDRQLAVAEDDLQALESELREQLEAGKLEFNE-------EEYRLKsRLGELKLRLNQA 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568940563 351 LVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAestiDELKEQVDAALGAEE 415
Cdd:pfam12128 457 TA-----TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA----RKRRDQASEALRQAS 512
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
233-471 |
2.26e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 233 EQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERY---MEEMaDTAD--AIEMATLDKEM-----AEERAESLQQEV 302
Cdd:COG0497 155 ELLEEYREAYRAWRA-LKKELEELRADEAERARELDLLrfqLEEL-EAAAlqPGEEEELEEERrrlsnAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 303 EALKERVDELTTDLEILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMRDLSSS------------EKQEHV---- 366
Cdd:COG0497 233 EALSGGEGGALDLLGQALRALER------LAEYD-PSLAELAERLESALIELEEAASElrryldslefdpERLEEVeerl 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 367 -KLQKLMEKKNQELEVVRQQRERLQEELSQ---AESTIDELKEQVDAALGAeemvemltdrnlnLEEKVREL----RETV 438
Cdd:COG0497 306 aLLRRLARKYGVTVEELLAYAEELRAELAElenSDERLEELEAELAEAEAE-------------LLEAAEKLsaarKKAA 372
|
250 260 270
....*....|....*....|....*....|....*...
gi 568940563 439 GDLEAmnEMNDELQ----ENAR-ETELELREQLDMAGA 471
Cdd:COG0497 373 KKLEK--AVTAELAdlgmPNARfEVEVTPLEEPGPNGA 408
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
296-406 |
2.52e-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: 42.24 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 296 ESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGAASSYQlKQLEEQNARLKdALVRMRDLSSSEKQEHVKLQKLME 373
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNYE-RELVLHAEDIK-ALQALREELNELKAEIAELKAEAE 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 568940563 374 KKNQELEVVR----QQRERLQEELSQAESTIDELKEQ 406
Cdd:pfam07926 82 SAKAELEESEesweEQKKELEKELSELEKRIEDLNEQ 118
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-524 |
2.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 367 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlNLEEKVRELRETVGDLEAMNE 446
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 447 MNDELQENAretelELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:COG4717 127 LLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
191-517 |
2.60e-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: 45.02 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEE-EGLRAQVRDLEEKLETLRLKRSEDKAKLK--------ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE--ARKE 259
Cdd:pfam05701 192 TKESlESAHAAHLEAEEHRIGAALAREQDKLNWEkelkqaeeELQRLNQQLLSAKDLKSKLETASALLLDLKAElaAYME 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 260 AKEALEAKERYMEEMADTADAIEMATLDKEMAEERA--ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQL 337
Cdd:pfam05701 272 SKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKAniEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 338 KQLEEQNARLKD--ALVRMRDLSSSEKQehVKLQKLMEKKNQELE----VVRQQRERL---QEELSQA-------ESTID 401
Cdd:pfam05701 352 SSLEAELNRTKSeiALVQAKEKEAREKM--VELPKQLQQAAQEAEeaksLAQAAREELrkaKEEAEQAkaaastvESRLE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 402 ELKEQVDAALGAEEMVemLTDRNLNLEEKVRELRETVGDLEAM----NEMNDELQENARETElelreqlDMAGARVREAQ 477
Cdd:pfam05701 430 AVLKEIEAAKASEKLA--LAAIKALQESESSAESTNQEDSPRGvtlsLEEYYELSKRAHEAE-------ELANKRVAEAV 500
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568940563 478 KRVEAAQETvadyqqtikKYRQLtAHLQDVNRELTNQQEA 517
Cdd:pfam05701 501 SQIEEAKES---------ELRSL-EKLEEVNREMEERKEA 530
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
205-476 |
2.74e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 205 EEKLETLRLKRSEDKAKLKElEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMA 284
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEE-KIREIEIE-----VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-------RAD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 285 TLDKEMAEERAESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSY-----QLKQLEEQNARLKDALVRMRDL-- 357
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRYKSL--KLEDLDSKRTSWLNALAVISLidietNRSRSNEIKKQLNDLESRLQEIei 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 358 ---------SSSEKQEHVKLQKLMEKKNqELEVVRQQRERLQEelsqaesTIDELKEQVDAALGAEEMVEMLTDRNLNLE 428
Cdd:PRK01156 609 gfpddksyiDKSIREIENEANNLNNKYN-EIQENKILIEKLRG-------KIDNYKKQIAEIDSIIPDLKEITSRINDIE 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 429 EKVRELRETVGDLEA---------------MNEMNDELQEnaRETELELREQLDMAGA---RVREA 476
Cdd:PRK01156 681 DNLKKSRKALDDAKAnrarlestieilrtrINELSDRIND--INETLESMKKIKKAIGdlkRLREA 744
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
318-513 |
3.12e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 318 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAE 397
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 398 STIDE--------------LKEQVDAALG--------------------AEEMVEMLTDRNLNLEEKVRELRETVGDLEA 443
Cdd:PHA02562 248 MDIEDpsaalnklntaaakIKSKIEQFQKvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568940563 444 -MNEMND---ELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNRELTN 513
Cdd:PHA02562 328 iMDEFNEqskKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSE 397
|
|
| CASP_C |
pfam08172 |
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ... |
291-432 |
3.22e-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: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 291 AEERAESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGA-ASSYQLKQLEEQNARLKDALVrmrdLSSSEKQEHVK 367
Cdd:pfam08172 2 LQEELSSLNAELEEQQELNAKLENDLLKVQDEASNafSFNDASsAGSGVSRYPPSGGRRSPTSSI----ISGFEPSESSS 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 368 LQKlmekkNQELEVVRQQRER-------LQEELSQAESTIDELKEQVDAalgaeemveMLTDrNLNLEEKVR 432
Cdd:pfam08172 78 SSD-----SSILPIVTSQRDRfrqrnaeLEEELRKQFETISSLRQEIAS---------LQKD-NLKLYEKTR 134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
379-554 |
3.83e-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: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 379 LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----EEKVRELRETVGDLEAMNEMNDELQE 453
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 454 NARETELELrEQLDmagARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP------- 526
Cdd:TIGR02168 261 ELQELEEKL-EELR---LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldela 336
|
170 180 190
....*....|....*....|....*....|....*
gi 568940563 527 -------PETFDFKIKFAETKAHAKAIEMELRQME 554
Cdd:TIGR02168 337 eelaeleEKLEELKEELESLEAELEELEAELEELE 371
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
193-471 |
4.01e-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: 44.94 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETlRLKRSEDkaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlKEARKEAKEALEAKERYME 272
Cdd:COG3096 974 DAVGLLGENSDLNEKLRA-RLEQAEE-----ARREAREQLRQAQAQYSQYNQVLASL----KSSRDAKQQTLQELEQELE 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMADTADAIematldkemAEERAES----LQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLKQLEEQNARLK 348
Cdd:COG3096 1044 ELGVQADAE---------AEERARIrrdeLHEELSQNRSRRSQLEKQLTRCEAEMDS-------LQKRLRKAERDYKQER 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 349 DALVrmrdlssSEKQEHVKLQKLMEKKNQELEVVRQqrerlqeELSQAEStiDELKEQVDAALGAEEMV----EMLTDrN 424
Cdd:COG3096 1108 EQVV-------QAKAGWCAVLRLARDNDVERRLHRR-------ELAYLSA--DELRSMSDKALGALRLAvadnEHLRD-A 1170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 425 LNLEE-------KV-------RELRE--------TVGDLEAMNEMNDELqenARET-ELELREQlDMAGA 471
Cdd:COG3096 1171 LRLSEdprrperKVqfyiavyQHLRErirqdiirTDDPVEAIEQMEIEL---ARLTeELTSREQ-KLAIS 1236
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
188-524 |
4.13e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 188 PSPSKEeegLRAQVRDLEEKLETLRLKRSEDkaklkELEKHKIQL-EQVQEWKSKMQEQQ------ADLQRRLKEARKEA 260
Cdd:PRK10929 78 PKLSAE---LRQQLNNERDEPRSVPPNMSTD-----ALEQEILQVsSQLLEKSRQAQQEQdrareiSDSLSQLPQQQTEA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 261 KEALEAKERYMEEMADTADAIEMATLdkemaeeraESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSYQlKQL 340
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQAQL---------TALQAESAALKALVDEL--ELAQLSANNRQELARLRSELAK-KRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 341 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-----EVVRQQRErLQEELSQAESTIDELKEQVDAAlgaee 415
Cdd:PRK10929 218 QQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLpksivAQFKINRE-LSQALNQQAQRMDLIASQQRQA----- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 416 mvemlTDRNLNLEEKVRELRETVGDLEAMNEMNDELQEN-ARETELELREQLD--MAGARVreaqKRVEaaqetvadYQQ 492
Cdd:PRK10929 292 -----ASQTLQVRQALNTLREQSQWLGVSNALGEALRAQvARLPEMPKPQQLDteMAQLRV----QRLR--------YED 354
|
330 340 350
....*....|....*....|....*....|..
gi 568940563 493 TIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:PRK10929 355 LLNKQPQLRQIRQADGQPLTAEQNRILDAQLR 386
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
205-345 |
4.44e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 205 EEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMADTADAIEMA 284
Cdd:PRK09510 86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA--AKAKAEAEAKRAAAAAKKA 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 285 TLDKEMAEERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAASSYQLKQLEEQNA 345
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-----KAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
234-553 |
4.98e-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: 44.65 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 234 QVQEWKSKMQEQQADLQRRLKEARKEAKEaleaKERYMEEMADTAD--AIEMATLDKEMAE--ERAESLQQEVEALKERV 309
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKK----KEKRRDEMLGLAPgrQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 310 DELTTDLEILKAEiEEKGSDGAASSYQLKQLEEQnarLKDALVRMRDL-----SSSEKQEHVKLQKLMEKKNQELEVVRQ 384
Cdd:TIGR00606 768 EEQETLLGTIMPE-EESAKVCLTDVTIMERFQME---LKDVERKIAQQaaklqGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 385 QRERLQEELSQAESTIDELKEQVDaALGAEEM-VEMLTDRNLNLEEKVRELRETVgdleamNEMNDELQEnARETELELR 463
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTN-ELKSEKLqIGTNLQRRQQFEEQLVELSTEV------QSLIREIKD-AKEQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 464 EQLDMAGARVREAQKRVEAAQETVADYQQTIK-KYRQLTAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAH 542
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKeKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKH 992
|
330
....*....|.
gi 568940563 543 AKAIEMELRQM 553
Cdd:TIGR00606 993 QEKINEDMRLM 1003
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
191-296 |
5.67e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEalEAKERY 270
Cdd:PRK12704 85 QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ---KQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEIL 159
|
90 100
....*....|....*....|....*.
gi 568940563 271 MEEMADTADAiEMATLDKEMaEERAE 296
Cdd:PRK12704 160 LEKVEEEARH-EAAVLIKEI-EEEAK 183
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
191-309 |
5.98e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKlkelekhkiqlEQVQEWKSKMQEQQADLQrrlkeaRKEAKEALEAKERY 270
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKAR-----------AKAAKAQEKVNEALSGID------SDDATSALERMEEK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568940563 271 MEEMADTADAI-EMA---TLDKEMAE-ERAESLQQEVEALKERV 309
Cdd:COG1842 174 IEEMEARAEAAaELAagdSLDDELAElEADSEVEDELAALKAKM 217
|
|
| PCRF |
pfam03462 |
PCRF domain; This domain is found in peptide chain release factors. |
219-312 |
7.00e-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: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 219 KAKLKELEKhkiQLEQVQEWKSkmqeqQADLQRRLKEaRKEAKEALEAKERYMEEMADTADAIEMATLD--KEMAEERAE 296
Cdd:pfam03462 2 EERYEELEA---LLSDPDVWDD-----QKRAQKLSKE-YSELEPIVEAYREYKQALEDLEEAKELLEDPelAELAEEELE 72
|
90
....*....|....*.
gi 568940563 297 SLQQEVEALKERVDEL 312
Cdd:pfam03462 73 ELEKRLEELEEELKLL 88
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
222-460 |
7.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 222 LKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAieMATLDKEMAEERAESLQQE 301
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL--LREAEELEEELQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 302 VEALKERVDelTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKlmEKKNQELEV 381
Cdd:COG4717 372 IAALLAEAG--VEDEEELRAALE-----------QAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 382 VRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNlNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 460
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
202-567 |
8.07e-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: 43.88 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 202 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArkeAKEALEAKERYMEEMADTADAi 281
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---LTETLKKEVKSLQNEKADLDR- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 282 EMATLDKEMAE-ERAESLQQEVEALKErvDELTTDLEILKaeIEEKGSDGAASSY----QLKQLEEQNARLKDALVRMRD 356
Cdd:TIGR00606 516 KLRKLDQEMEQlNHHTTTRTQMEMLTK--DKMDKDEQIRK--IKSRHSDELTSLLgyfpNKKQLEDWLHSKSKEINQTRD 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 357 LSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA------ESTIDELKEQVD------AALGA-----EEMVEM 419
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEksskqrAMLAGatavySQFITQ 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 420 LTDRNLNLEEKVRELRETVGDLeamNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 499
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 500 LTAHLQDVNRELtnQQEASVERQQQPPPETFDFKIKFAETKAHAKAIeMELRQMEVAQANRHMSLLTA 567
Cdd:TIGR00606 749 LRNKLQKVNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAA 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
883-1024 |
8.11e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 883 AMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKgeeLSEANVRLSLLEKKLDSAAK 962
Cdd:TIGR02169 654 AMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 963 DAD---ERIEKVQTRLDETQ---TLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEG 1024
Cdd:TIGR02169 731 EEEklkERLEELEEDLSSLEqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA 798
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
190-399 |
8.55e-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: 43.40 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 190 PSKEEEGLRAQVRDLEEKLETLR--LKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAK 267
Cdd:pfam15709 320 PSKALLEKREQEKASRDRLRAERaeMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 268 ERYMEEMAdtadaiEMATLDKEMAEERAESLQQEVEalkervdelTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARL 347
Cdd:pfam15709 400 RQRQEEEE------RKQRLQLQAAQERARQQQEEFR---------RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568940563 348 KDALVRMRDLSSSEKQEhvKLQKLMEKKNQELEvVRQQRERLQEELSQAEST 399
Cdd:pfam15709 465 QKRLMEMAEEERLEYQR--QKQEAEEKARLEAE-ERRQKEEEAARLALEEAM 513
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
204-479 |
8.71e-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: 42.98 E-value: 8.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 204 LEEKLETLRLKRSEDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadta 278
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEEreralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 279 daieMATLDKEMAEERAESLQQ--EVEALKERVDELTTDLEILKAE--IEEKGSDGAASSYQLKQLEEQNARLKdalvRM 354
Cdd:pfam13868 104 ----DEIVERIQEEDQAEAEEKleKQRQLREEIDEFNEEQAEWKELekEEEREEDERILEYLKEKAEREEEREA----ER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 355 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEstiDELKEQVDAALGAEEMVEMLTDRNLNLEEKVREL 434
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK---ERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 568940563 435 RETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKR 479
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
201-438 |
8.95e-04 |
|
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: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 201 VRDLEEKLETLRLKRSEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArKEAKEALEAKerymeeMAD 276
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQaleeELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAK------FSE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 TADAIEMATLDKEMAEERA--ESLQQEVEALKE----RVDELTTDLEILKAEI---EEKGSD----GAASSYQLKQLEEQ 343
Cdd:pfam15905 148 DGTQKKMSSLSMELMKLRNklEAKMKEVMAKQEgmegKLQVTQKNLEHSKGKVaqlEEKLVStekeKIEEKSETEKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 344 NARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTD 422
Cdd:pfam15905 228 ITELSCV----SEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQELSKQIKDLNEKCKLLESEkEELLREYEE 300
|
250
....*....|....*.
gi 568940563 423 RNLNLEEKVRELRETV 438
Cdd:pfam15905 301 KEQTLNAELEELKEKL 316
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
191-506 |
1.04e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 270
Cdd:PRK01156 203 KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADA-----IEMATLDKEMAEERA--ESLQQEVEALKERVDELtTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 343
Cdd:PRK01156 283 MKIINDPVYKnrnyiNDYFKYKNDIENKKQilSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 344 NARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-------EVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 416
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 417 V----EMLTDRNL------NL-EEKVRELRETVG-DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 484
Cdd:PRK01156 442 LsrnmEMLNGQSVcpvcgtTLgEEKSNHIINHYNeKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521
|
330 340
....*....|....*....|..
gi 568940563 485 ETVADYQQTIKKYRQLTAHLQD 506
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKD 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1020 |
1.04e-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: 43.51 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 902 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSaakdADERIEKVQTRLDETQTL 981
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANE 296
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 568940563 982 LRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1020
Cdd:TIGR02168 297 ISRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEE 338
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
204-319 |
1.16e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 42.76 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 204 LEEKLETLrlkrsedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 271
Cdd:PRK00591 4 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKQAQEDLEEA-------- 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 568940563 272 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 319
Cdd:PRK00591 65 KEMLEEESDPEM----REMAKE-------ELKELEERLEELEEELKIL 101
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
219-488 |
1.24e-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: 43.09 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 219 KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEER---- 294
Cdd:pfam05701 134 AAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHriga 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 295 AESLQQEVEALKERVDELTTDLEILKAEI----EEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 370
Cdd:pfam05701 214 ALAREQDKLNWEKELKQAEEELQRLNQQLlsakDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 371 LMEKKNQELEVVRQQRER--------------LQEELSQAESTIDELKEQVDAALGAEemvemltdrnLNLEEkvrELRE 436
Cdd:pfam05701 294 ALASAKKELEEVKANIEKakdevnclrvaaasLRSELEKEKAELASLRQREGMASIAV----------SSLEA---ELNR 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 568940563 437 TVGDLEAMNEMNDElqenARETELELREQLDMAGARVREAQKRVEAAQETVA 488
Cdd:pfam05701 361 TKSEIALVQAKEKE----AREKMVELPKQLQQAAQEAEEAKSLAQAAREELR 408
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
901-1026 |
1.25e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 901 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLK-IKGE--------ELSEANVRLSLLEKK---LDSAAKDADERI 968
Cdd:COG1579 50 AKTELEDLEKEIKRLE---LEIEEVEARIKKYEEQLGnVRNNkeyealqkEIESLKRRISDLEDEileLMERIEELEEEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 969 EKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLR 1026
Cdd:COG1579 127 AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
208-507 |
1.26e-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: 43.11 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 208 LETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKealeAKERYMEEMADTADAIEmATLD 287
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK----SYENELDPLKNRLKEIE-HNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 288 KEMaeeraeSLQQEVEALKERVDELTTDLEILKAEIEE--KGSDgaassYQLKQLEEQNARLkdalvrmrdlSSSEKQEH 365
Cdd:TIGR00606 263 KIM------KLDNEIKALKSRKKQMEKDNSELELKMEKvfQGTD-----EQLNDLYHNHQRT----------VREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 366 VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA--ALGAEEMVEMLTD---RNLNLEEKVRELRETV-- 438
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDgfeRGPFSERQIKNFHTLVie 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 439 ---GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDV 507
Cdd:TIGR00606 402 rqeDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
191-355 |
1.33e-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: 42.63 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLR----LKRSEdKAKLKELEKHkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE- 265
Cdd:pfam10498 183 SKPREIIESNVDAAEWKLELERvlpqLKVTI-KADAKDWRAH---LEQMKQHKKSIEESLPDTKSQLDKLHTDISKTLEk 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 266 --AKERY----MEEMADtadaiEMATLDKEMAEERaESLQQEVEALKERVDEL---TTDLEILKAEIEEKG---SDGAas 333
Cdd:pfam10498 259 ieSREKYinsqLEPLIQ-----EYREAQDELSEVQ-EKYKQLSEGVTERTRELaeiTEELEKVKQEMEERGssmTDGS-- 330
|
170 180
....*....|....*....|..
gi 568940563 334 syqlkqleeQNARLKDALVRMR 355
Cdd:pfam10498 331 ---------PLVKIKQALTKLK 343
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
64-204 |
1.34e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.98 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 64 CDEGHGIFVRQSQIQVFEDGADTtSPETpdssasKVLKREGADAAAKTSKLRGLKPKKTTTRRPKPTrpaSTGVAGPSSS 143
Cdd:pfam05109 376 CENISGAFASNRTFDITVSGLGT-APKT------LIITRTATNATTTTHKVIFSKAPESTTTSPTLN---TTGFAAPNTT 445
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 144 LGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDL 204
Cdd:pfam05109 446 TGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDM 506
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
194-551 |
1.46e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 194 EEGLRAQVRDLEEKLETLrlkrSEDKAKLKELEKHKIQLEqvQEWKSKMQEQQadlqrRLKEARKEAKEALEAKERYMEE 273
Cdd:PRK01156 189 EEKLKSSNLELENIKKQI----ADDEKSHSITLKEIERLS--IEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 274 MADTADAIEMATLD----KEMAEERAESLQQEVEALKERVDE---LTTDLEILKAEIEekGSDGAASSYQ--LKQLEEQN 344
Cdd:PRK01156 258 IKTAESDLSMELEKnnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILS--NIDAEINKYHaiIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 345 ARLKDALV---RMRDLS---SSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTidelkeqvdAALGAEE 415
Cdd:PRK01156 336 KDYNDYIKkksRYDDLNnqiLELEGYEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKI---------QEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 416 MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENAR-----------ETELELREQLDMAGARVREAQKRVEAAQ 484
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 485 ETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETK-AHAKAIEMELR 551
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdKHDKYEEIKNR 554
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
921-1020 |
1.46e-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: 42.31 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 921 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERI-EKVQTRLDETQtLLRKKEKDFEETMDALQAD 999
Cdd:smart00787 162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIM-IKVKKLEELEEELQELESK 240
|
90 100
....*....|....*....|.
gi 568940563 1000 IDQLEAEKAELKQRLNSQSKR 1020
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKK 261
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
197-280 |
1.50e-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: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQ----------RRLKEARK 258
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLeeklkdreEELREKRKLNQDLQDELValqlqlnmaeEKLRKLEK 155
|
90 100
....*....|....*....|..
gi 568940563 259 EAKEALEakeRYMEEMADTADA 280
Cdd:pfam08614 156 ENRELVE---RWMKRKGQEAEA 174
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
192-478 |
1.54e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEdkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 271
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREE------ELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMAtldkEMAEERAESLQQEVEALKERVDELTT-----------DLEILKAEIEEKGSDgaaSSYQLKQL 340
Cdd:pfam05667 384 KQYKVKKKTLDLL----PDAEENIAKLQALVDASAQRLVELAGqwekhrvplieEYRALKEAKSNKEDE---SQRKLEEI 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 341 EEQNARLKD--ALVRMRDlsssekQEHVKLQKLMEKKNQE----------LEVV---RQQRERLQEELSQaestIDELKE 405
Cdd:pfam05667 457 KELREKIKEvaEEAKQKE------ELYKQLVAEYERLPKDvsrsaytrriLEIVkniKKQKEEITKILSD----TKSLQK 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568940563 406 QVDAALGAEEMVEMLTDRNLNLEEKVRE-LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQK 478
Cdd:pfam05667 527 EINSLTGKLDRTFTVTDELVFKDAKKDEsVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
248-322 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 248 DLQRRLKEARK-----EAKEALEAKERYMEEMADTADAIEMATLD-------------------KEMAEERAESLQQEVE 303
Cdd:cd23165 1 DQQKINKFSRLnarlhELKEELKAKKKELENLEDASDELELADDDepvpykigevfvhlsleeaQERLEKAKEELEEEIE 80
|
90
....*....|....*....
gi 568940563 304 ALKERVDELTTDLEILKAE 322
Cdd:cd23165 81 KLEEEIDEIEEEMKELKVQ 99
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
192-485 |
1.57e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETlrlKRSEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQadlQRRLKEARKEAKEaleakerY 270
Cdd:pfam02029 23 KEEEEPSGQVTESVEPNEH---NSYEEDSELKPSGQGGLDEEEaFLDRTAKREERR---QKRLQEALERQKE-------F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIemATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDGAASSYQlkQLEEQNARLKD 349
Cdd:pfam02029 90 DPTIADEKESV--AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnKWSTEVRQAEE--EGEEEEDKSEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 350 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMV---EMLTDRNLN 426
Cdd:pfam02029 166 AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 427 LEEKVRELRETVGDLEamNEMNDELQENARETELELREQLdmagaRVREAQKRVEAAQE 485
Cdd:pfam02029 246 AEQKLEELRRRRQEKE--SEEFEKLRQKQQEAELELEELK-----KKREERRKLLEEEE 297
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
888-1014 |
1.64e-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: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 888 EYDAERPPSKPPPVELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 967
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 568940563 968 IEKVQ--TRLDETQTLLRKKEKDFEETMDALQADIDQL-EAEKAELKQRL 1014
Cdd:COG2433 461 IRKDReiSRLDREIERLERELEEERERIEELKRKLERLkELWKLEHSGEL 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
191-391 |
1.70e-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: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVqewKSKMQEQQADLQRRLKEARkeaKEALEAKERY 270
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 271 MEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERVDELTtdlEILKAEIEEkgsdgaassyqlkqLEEQNARLKDA 350
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKIKELG---PVNLAAIEE--------------YEELKERYDFL 1005
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568940563 351 LVRMRDLSSSEKQehvkLQKLMEKKNQELevvrqqRERLQE 391
Cdd:TIGR02168 1006 TAQKEDLTEAKET----LEEAIEEIDREA------RERFKD 1036
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
192-464 |
1.73e-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: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLE----EKLETLRLKRSEDKAKLK-ELE---KHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 263
Cdd:pfam17380 360 RELERIRQEEIAMEisrmRELERLQMERQQKNERVRqELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 264 LEakerymeemadtadaiematldkemaEERAeslqQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyQLKQLEEQ 343
Cdd:pfam17380 440 LE--------------------------EERA----REMERVRLEEQERQQQVERLRQQEEER---------KRKKLELE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 344 NARlkdalvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDR 423
Cdd:pfam17380 481 KEK--------RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568940563 424 nlNLEEKVRELRETVGDLEAMnEMNDELQENARETELELRE 464
Cdd:pfam17380 553 --RIQEQMRKATEERSRLEAM-EREREMMRQIVESEKARAE 590
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
194-468 |
1.74e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 194 EEGLrAQVRDLEEKLETLRLkrSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKErymE 272
Cdd:PRK05771 27 ELGV-VHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIE---K 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 273 EMadtadaiematldKEMAEERAEsLQQEVEALKERVDELT--TDLEI-LKAEIEEKGSDGAASSYQLKQLEEQNARLKD 349
Cdd:PRK05771 101 EI-------------KELEEEISE-LENEIKELEQEIERLEpwGNFDLdLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 350 ALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAEsTIDELKEQvdaalgaeemvemltdrnl 425
Cdd:PRK05771 167 ENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEE------------------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 568940563 426 nLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDM 468
Cdd:PRK05771 224 -LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEA 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
902-1037 |
1.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 902 ELRAAALRAEITDAEGLGLKLEDRETVIKELKkslkikgEELSEANVRLSLLEKKLDsaakDADERIEKVQTRLDETQTL 981
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLE-------AELEELRAELARLEAELE----RLEARLDALREELDELEAQ 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 982 LRKKEKDfeeTMDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRGPPPSGIATLV 1037
Cdd:COG4913 332 IRGNGGD---RLEQLEREIERLERELEERERRRARLEAL-LAALGLPLPASAEEFA 383
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
192-524 |
1.75e-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: 42.85 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLR--LKRSEDkAKLK---ELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARK 258
Cdd:pfam01576 685 RSKRALEQQVEEMKTQLEELEdeLQATED-AKLRlevNMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 259 EAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTT---DLEILKAEIEEKGSDGAASSY 335
Cdd:pfam01576 764 QRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAsrdEILAQSKESEKKLKNLEAELL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 336 QLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV-VRQQRERLQEELSQAESTIDELK------EQVD 408
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRkstlqvEQLT 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 409 AALGAEE-MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL-ELREQLD-------MAGARVREAQKR 479
Cdd:pfam01576 924 TELAAERsTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIaQLEEQLEqesrerqAANKLVRRTEKK 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 568940563 480 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 524
Cdd:pfam01576 1004 LKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR 1048
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-507 |
1.76e-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: 42.85 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 197 LRAQVRDLEEK---LETLRLKR----SEDKAKLKELEKHKIQLEQvqeWKSKMQEQQADLQRRLKEARKEAKEALEAKER 269
Cdd:pfam01576 164 FTSNLAEEEEKaksLSKLKNKHeamiSDLEERLKKEEKGRQELEK---AKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD--------------ELTTDLEILKAEIEEKGSDGAASSY 335
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrDLGEELEALKTELEDTLDTTAAQQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 336 QLKQLEEQNARLKDALvrmrdlsSSEKQEH-VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGAE 414
Cdd:pfam01576 321 LRSKREQEVTELKKAL-------EEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN-AELQAE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 415 emVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAdyqqti 494
Cdd:pfam01576 393 --LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------ 464
|
330
....*....|...
gi 568940563 495 kkyrQLTAHLQDV 507
Cdd:pfam01576 465 ----SLESQLQDT 473
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
162-308 |
1.86e-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: 40.69 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 162 TPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQvrdLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSK 241
Cdd:pfam08614 23 NAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQ---LREELAELYRSRGELAQRLVDLN------EELQELEKK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568940563 242 MQEQQ---ADLQRR---LKEARKEAKEALEAKERYMEEMADtadaiEMATLDKE--MAEERAESLQQEVEALKER 308
Cdd:pfam08614 94 LREDErrlAALEAEraqLEEKLKDREEELREKRKLNQDLQD-----ELVALQLQlnMAEEKLRKLEKENRELVER 163
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
368-558 |
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 568940563 368 LQKLMEKKNQELEVVRQQRERLQEELSQaesTIDELKEQVDAALgaeemvemltdrnLNLEEKVRELREtvgdleamnem 447
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEE---KKEKLQEEEDKLL-------------EEAEKEAQQAIK----------- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 448 ndELQENARETELELREQLDMAGARVR-----EAQKRVEAAQETVADYQQTIK------------KYRQL--TAHLQDV- 507
Cdd:PRK00409 581 --EAKKEADEIIKELRQLQKGGYASVKaheliEARKRLNKANEKKEKKKKKQKekqeelkvgdevKYLSLgqKGEVLSIp 658
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 508 -NRELTNQ--------QEASVERQQQPPPETFDfKIKFAETKAHAKAIEMELRQMEVAQA 558
Cdd:PRK00409 659 dDKEAIVQagimkmkvPLSDLEKIQKPKKKKKK-KPKTVKPKPRTVSLELDLRGMRYEEA 717
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
192-306 |
2.04e-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: 41.79 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLetLRLKRSEDKAKLKELEKHkiQLEQVQEWKSKMQEqqadlqrRLKEARKEAKEALEAKERym 271
Cdd:cd16269 200 IEAERAKAEAAEQERKL--LEEQQRELEQKLEDQERS--YEEHLRQLKEKMEE-------ERENLLKEQERALESKLK-- 266
|
90 100 110
....*....|....*....|....*....|....*
gi 568940563 272 eemadtadaiEMATLDKEMAEERAESLQQEVEALK 306
Cdd:cd16269 267 ----------EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1020 |
2.06e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 901 VELRAAALRAEITD----AEGLGLKLEDRETVIKELKKSLKIKGEE--------LSEANVRLSLLEKKLDSAA---KDAD 965
Cdd:TIGR02169 242 IERQLASLEEELEKlteeISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekIGELEAEIASLERSIAEKErelEDAE 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 966 ERIEKVQTRLDETQTLLRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1020
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
941-1026 |
2.21e-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: 42.06 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 941 EELSEANVRLSLLEKKLDSAAKDADE---RIEKVQTRLDETQTLLRKKEKDfeetMDALQADIDQLEAEKAELKQRLNSQ 1017
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQE----LAALEAELAELEKEIAELRAELEAQ 102
|
....*....
gi 568940563 1018 SKRTIEGLR 1026
Cdd:COG4942 103 KEELAELLR 111
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
251-523 |
2.28e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 41.95 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 251 RRLKEARKEAKEALEAKERYMEE--MADTADA-IEMATLDKEM--AEERAESLQQEVEALKERVDE-LTTDLEILKAEIE 324
Cdd:COG1538 50 RARIEAAKAQAEAAEADLRAARLdlAAEVAQAyFDLLAAQEQLalAEENLALAEELLELARARYEAgLASRLDVLQAEAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 325 EkgsdgAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 404
Cdd:COG1538 130 L-----AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 405 EQVDAA-------------LGAEEMVEMLTDRN------LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ 465
Cdd:COG1538 205 AEIGVAraaflpslslsasYGYSSSDDLFSGGSdtwsvgLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568940563 466 LDMAGARVREAQKRVEAAQETVAD----YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 523
Cdd:COG1538 285 VEDALAALRAAREQLEALEEALEAaeeaLELARARYRAGLASLLDVLDAQRELLQAQLNLIQ 346
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
174-327 |
2.33e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 174 PTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRlkrsedkAKLKELEkhkiqleqvqewkskmqEQQADLQRRL 253
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKD-----------------ERIERLEREL 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 254 KEARKEAKEALEaKERYMEEMadtadaiematldkemaEERAESLQQEVEALKERVDELTTDLEILKA--EIEEKG 327
Cdd:COG2433 451 SEARSEERREIR-KDREISRL-----------------DREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
214-343 |
2.84e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 214 KRSEDKAKLKELE------KHKIQLEQ-VQEWKSKMQEQQADLQRRlKEARKEAKEALEAKERYMEEMADTADAiEMATL 286
Cdd:PRK12704 49 KEAEAIKKEALLEakeeihKLRNEFEKeLRERRNELQKLEKRLLQK-EENLDRKLELLEKREEELEKKEKELEQ-KQQEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 568940563 287 DKEmaEERAESLQQEVEALKERVDELTTD--LEILKAEIEEKGSDGAASsyQLKQLEEQ 343
Cdd:PRK12704 127 EKK--EEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAV--LIKEIEEE 181
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
374-524 |
2.92e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.19 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 374 KKNQELevVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEKVRELRETVGDLEAMNEMNDELQE 453
Cdd:COG1566 68 KKGQVL--ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIA----AAEAQLAAAQAQLDLAQRELERYQALYK 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940563 454 NaretELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVnreltNQQEASVERQQQ 524
Cdd:COG1566 142 K----GAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQV-----AQAEAALAQAEL 203
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
290-475 |
3.00e-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: 39.94 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 290 MAEERAESLQQEVEALKERVDElttDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDALVRMRDLSSSEkqehvkLQ 369
Cdd:pfam01442 23 VAQELVDRLEKETEALRERLQK---DLEEVRAKLEPY-------------LEELQAKLGQNVEELRQRLEPY------TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 370 KLMEKKNQELEVVRQQRERLQEEL-SQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELRETVGdleamnEMN 448
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELrERLEQNVDALRARLAPY--AEELRQ-------KLAERLEELKESLA------PYA 145
|
170 180
....*....|....*....|....*..
gi 568940563 449 DELQENARETELELREQLDMAGARVRE 475
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
199-405 |
3.06e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 199 AQVRDLEEKLETLRLKRSEDKaklKELEKHKIQLEQVQEWKSKMQEQQADLQRrlKEARKEAKEALEAKERYMEEMADTA 278
Cdd:COG5022 817 ACIIKLQKTIKREKKLRETEE---VEFSLKAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 279 DAIEMA-----TLDKEMAE---ERAESLQQEVEALKERVDELTTDLEilKAEIEEKGSDGAASSYQLKQLEEQNARLKDA 350
Cdd:COG5022 892 KSISSLklvnlELESEIIElkkSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHEVESKLKET 969
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 351 LVRMRDLSSSEKQEHVKLQK---LMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 405
Cdd:COG5022 970 SEEYEDLLKKSTILVREGNKansELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
265-492 |
3.07e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 265 EAKERYMEEMADTADAIE-MATLDKEMAEER--AESLQQEVEALKERVDELTTDLEilkaEIEEKGSDGAASSYQ--LKQ 339
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIAsLEELERELEQKAeeAEALLKEAEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQqaIKE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 340 LEEQNARLKDALVRMRDlsssEKQEHVKLQKLMEKKNQelevVRQQRERLQEELSQAESTIDELKEqvdaalGAE----- 414
Cdd:PRK00409 582 AKKEADEIIKELRQLQK----GGYASVKAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKV------GDEvkyls 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 415 -----EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRVEAA--Q 484
Cdd:PRK00409 648 lgqkgEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvslELDLRGMRYEEALERLDKYldD 727
|
....*...
gi 568940563 485 ETVADYQQ 492
Cdd:PRK00409 728 ALLAGYGE 735
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
244-489 |
3.10e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 42.00 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 244 EQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE 322
Cdd:COG5644 331 EPRTESERKMHQALLDAGLENESALKKQEELALNKLSVeEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 323 IEEKGSDGAASSyqlkQLEEQNARLKDALVRMrdlssseKQEHVKLQKLMEKknqelevvrqqrerLQEELSQAESTIDE 402
Cdd:COG5644 411 KEKEMALIPKSE----DLENEKSEEARALERM-------TQRHKNTSSWTRK--------------MLERASHGEGTREA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 403 LKEQVDAalgAEEMVEMLTDRNLNLEEKVRElrETVGDLEamNEMNDELQENARETELELREQLDMAGARVREAQKRvEA 482
Cdd:COG5644 466 VNEQIRK---GDELMQRIHGKEIMDGEDVSE--FSDSDYD--TNEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQM-AA 537
|
....*..
gi 568940563 483 AQETVAD 489
Cdd:COG5644 538 SKISVAD 544
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
193-347 |
3.38e-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: 40.90 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLETLR--LKRSEDKAkLKELEKHKIQL----EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 266
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRteLQELEAQQ-QEEAESSREQLqeleEQLATERSARREAEAELERLQEELRYLEEELRRS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 267 KERYMEEMADTADAIEMATlDKEMAEERAESLQQEVEAlkeRVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 346
Cdd:pfam09787 134 KATLQSRIKDREAEIEKLR-NQLTSKSQSSSSQSELEN---RLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKE 209
|
.
gi 568940563 347 L 347
Cdd:pfam09787 210 L 210
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
193-489 |
3.45e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 193 EEEGLRAQVRDLEEKLEtLRLKRSEDKAKLKELEKHKIQL------EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 266
Cdd:pfam02029 60 EEEAFLDRTAKREERRQ-KRLQEALERQKEFDPTIADEKEsvaerkENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 267 KER---YMEEMADTADAIEMATLDKEMAEERAE----SLQQEVEALKERVDELTTDLEILKAE---IEEKGSDGAASSYQ 336
Cdd:pfam02029 139 EYQenkWSTEVRQAEEEGEEEEDKSEEAEEVPTenfaKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 337 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmEKKNQELEvvRQQRERLQEELSQAESTIDELKeqvdaalgaeem 416
Cdd:pfam02029 219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEEL-RRRRQEKE--SEEFEKLRQKQQEAELELEELK------------ 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568940563 417 vemltdrnlnleeKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 489
Cdd:pfam02029 284 -------------KKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSSE 343
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
195-371 |
3.87e-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: 40.77 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 195 EGLRaqvRDLEEKLETLRlkrsEDKAKLKElekhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErymeem 274
Cdd:smart00787 143 EGLK---EGLDENLEGLK----EDYKLLMK------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP------ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 adtadaiemATLDKemAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRM 354
Cdd:smart00787 204 ---------TELDR--AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKKLEQC 265
|
170 180
....*....|....*....|.
gi 568940563 355 RDLSSSE----KQEHVKLQKL 371
Cdd:smart00787 266 RGFTFKEieklKEQLKLLQSL 286
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
234-457 |
3.87e-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: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 234 QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL- 312
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 313 -----------TTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV 381
Cdd:pfam05701 112 qgiadeasvaaKAQLEVAKARHAAAVAELKSVKEELESLRKE----YASLVSERDIAIKRAEEAVSASKEIEKTVEELTI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 382 vrqQRERLQEELSQAESTIDELKEQ-VDAALGAEEmvEMLT-DRNLN-LEEKVRELRETV---GDLEAMNEMNDELQENA 455
Cdd:pfam05701 188 ---ELIATKESLESAHAAHLEAEEHrIGAALAREQ--DKLNwEKELKqAEEELQRLNQQLlsaKDLKSKLETASALLLDL 262
|
..
gi 568940563 456 RE 457
Cdd:pfam05701 263 KA 264
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
199-325 |
4.38e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 41.37 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 199 AQVRDLEEKLETLRlkrSEDKAKLKELEKHKI-------QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 271
Cdd:COG4477 347 EKVRNLEKQIEELE---KRYDEIDERIEEEKVayselqeELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAIEMATL---------DKEMAEERAESLQQE-------VEALKERVDELTTDLEILKAEIEE 325
Cdd:COG4477 424 KKLREIKRRLEKSNLpglpeeyleMFEEASDEIEELSEElnevplnMDEVNRLLEEAEEDIETLEEKTEE 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1014 |
4.51e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 901 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLE----------KKLDSAAKDADERIEK 970
Cdd:TIGR02169 376 VDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieakiNELEEEKEDKALEIKK 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568940563 971 VQTRLDETQTLLRKKEKDFEetmdALQADIDQLEAEKAELKQRL 1014
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELY----DLKEEYDRVEKELSKLQREL 492
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
225-407 |
4.54e-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: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 225 LEKHKIQLEQVQE----WKSKMQEQQADLQRrLKEARKEAKEALEAK-ERYmeemadtadaiematldkEMAEERAESLQ 299
Cdd:pfam10168 549 LKKHDLAREEIQKrvklLKLQKEQQLQELQS-LEEERKSLSERAEKLaEKY------------------EEIKDKQEKLM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 300 QEVEALKERVDELTTDL-EILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMrdlssSEKQEHVKLQKLMEKKNqE 378
Cdd:pfam10168 610 RRCKKVLQRLNSQLPVLsDAEREMKKE------LETIN-EQLKHLANAIKQAKKKM-----NYQRYQIAKSQSIRKKS-S 676
|
170 180
....*....|....*....|....*....
gi 568940563 379 LEVVRQQRERLQEELSQAESTIDELKEQV 407
Cdd:pfam10168 677 LSLSEKQRKTIKEILKQLGSEIDELIKQV 705
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
206-436 |
4.75e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 206 EKLETLRLKRSEDK--AKLKELE-------KHKIQLEQVQEWKSKMQEQQADLqRRLKEARKEAKEALEAKERYmeEMAD 276
Cdd:PRK05771 7 KKVLIVTLKSYKDEvlEALHELGvvhiedlKEELSNERLRKLRSLLTKLSEAL-DKLRSYLPKLNPLREEKKKV--SVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 277 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK----------AEIEEKGSDGAASSYQLKQLEEQNAR 346
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlsLLLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 347 LKDALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERL------QEELSQAESTIDELKEQVDAALG-AEE 415
Cdd:PRK05771 164 SDVENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLLEeLKE 240
|
250 260
....*....|....*....|.
gi 568940563 416 MVEMLTDRNLNLEEKVRELRE 436
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELE 261
|
|
| Not3 |
pfam04065 |
Not1 N-terminal domain, CCR4-Not complex component; |
206-348 |
5.53e-03 |
|
Not1 N-terminal domain, CCR4-Not complex component;
Pssm-ID: 461155 [Multi-domain] Cd Length: 228 Bit Score: 39.84 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 206 EKLETLrLKRSedkakLKELEKHKiqlEQVQEW--------KSKMQEQqadlqRRLKEARKEAKEALEakeRYMEEMADT 277
Cdd:pfam04065 40 EKLEAD-LKKE-----IKKLQRLR---DQIKTWlssndikdKKKLLEN-----RKLIEEAMERFKAVE---KESKTKAFS 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 278 ADAIEMATLDKEMAEERAEslQQEVEALKERVDELTTDLEILKAEIE-----EKGSDGAASSYQLKQLEEQNARLK 348
Cdd:pfam04065 103 KEGLSLAAASKLDPKEKEK--AEARDWLSDSIDELNRQIEALEAEIEslqaqKKKKKKDSEKARLEELEKLIERHK 176
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
902-1027 |
5.68e-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: 41.20 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 902 ELRAAALRAEITDAEGLGLKLEDRE--TVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKD---ADERIEKVQTRLD 976
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESKLD 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568940563 977 ETQTLLRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRG 1027
Cdd:TIGR02168 334 ELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQ-LETLRS 386
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1023 |
5.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 901 VELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKkldsaAKDADERIEKVQTRL-DETQ 979
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLtGLTP 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568940563 980 TLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1023
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
187-397 |
6.04e-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: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 187 LPSPSKEEEGLRAQVRDLEEKLETLRLK-RSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAkEALE 265
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQ 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 266 AKERYMEEmadtadAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyqlkqleeQNA 345
Cdd:pfam15921 748 SKIQFLEE------AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS---------------------QER 800
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568940563 346 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvrQQRERLQEELSQAE 397
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQE-----SVRLKLQHTLDVKE 847
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
199-393 |
6.10e-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: 39.74 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 199 AQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQRR---LKEARKEAKEALEAKERYMEEM 274
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEELNQRweeLRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 275 ADTADaiematLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDalvRM 354
Cdd:cd00176 113 RDADD------LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-------EPRLKSLNELAEELLE---EG 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 568940563 355 RDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEEL 393
Cdd:cd00176 177 HPDADEEIEE--KLEELNERWEELLELAEERQKKLEEAL 213
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
296-401 |
6.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 296 ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLkdalvrmrdlssseKQEHVKLQKlmekk 375
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL--------------EAQLEQLQE----- 205
|
90 100
....*....|....*....|....*.
gi 568940563 376 nQELEVVRQQRERLQEELSQAESTID 401
Cdd:PRK11448 206 -KAAETSQERKQKRKEITDQAAKRLE 230
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
198-342 |
6.12e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 198 RAQVRDLEEKLETLRLKRSEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQ---------RRLKEARKEAKEALEAKE 268
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEA---ELAKKKAEERREAETARAEAEAAYEIAeanaerevqRQLEIAEREREIELQEKE 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 269 RYMEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERvdeLTTDLEILKAEIEEKGSDGAASSYQ--LKQLEE 342
Cdd:COG2268 299 AEREEAELEADVRKPAEAEKQAAEAEAE---AEAEAIRAK---GLAEAEGKRALAEAWNKLGDAAILLmlIEKLPE 368
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
191-505 |
6.13e-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: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 191 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKER 269
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 270 ymeEMADTADAI-----EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE---EKGSDGAASSYQLKQ-- 339
Cdd:TIGR00606 320 ---ELVDCQRELeklnkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRlelDGFERGPFSERQIKNfh 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 340 ---LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgaeem 416
Cdd:TIGR00606 397 tlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ----------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 417 VEMLTDRNLNLEEkvrELRETVGDLEAMNEMNDELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 496
Cdd:TIGR00606 466 LEGSSDRILELDQ---ELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
....*....
gi 568940563 497 YRQLTAHLQ 505
Cdd:TIGR00606 542 KDKMDKDEQ 550
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
233-523 |
6.30e-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: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 233 EQVQEWKSKMQEQQADLQRRLkearKEAKEALEAKERYMEEmadtaDAIEMATLDKEMAEERAESL------QQEVEALK 306
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRL----NESNELHEKQKFYLRQ-----SVIDLQTKLQEMQMERDAMAdirrreSQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 307 ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL----EEQNARLKDALVRMRDLSSSEKQEHVKLQKlMEKKNQELEVV 382
Cdd:pfam15921 145 NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGKKIYEHDSMST-MHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 383 RQQRErLQEELSQAESTIDELKEQVDaALGAEEM--VEMLTDRNLN---------------LEEKVRELRETVGDLEAMN 445
Cdd:pfam15921 224 KILRE-LDTEISYLKGRIFPVEDQLE-ALKSESQnkIELLLQQHQDrieqliseheveitgLTEKASSARSQANSIQSQL 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940563 446 EMndeLQENARETELELREQLDMAGARVREAQKRVEAAQETVADyqqtikKYRQLTAHLQDVNRELTnqqEASVERQQ 523
Cdd:pfam15921 302 EI---IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELT---EARTERDQ 367
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
909-1020 |
6.34e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 909 RAEITDAEglglklEDRETVIKELKKSLK-IKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTR-------LDETQT 980
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRllqkeenLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568940563 981 LLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKR 1020
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
192-350 |
6.52e-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: 40.05 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 192 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQ--ADLQRRLKEARKE----AKEALE 265
Cdd:cd22656 128 KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK---ALKDLLTDEGGAIARKeiKDLQKELEKLNEEyaakLKAKID 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 266 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERV-------DELTTDLEILKAEIEEKGSDGAA---SSY 335
Cdd:cd22656 205 ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeklqgawQAIATDLDSLKDLLEDDISKIPAailAKL 284
|
170
....*....|....*
gi 568940563 336 QLKQLEEQNARLKDA 350
Cdd:cd22656 285 ELEKAIEKWNELAEK 299
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
205-406 |
7.33e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 205 EEKLETLRLKRSEDKAKLKELEK-----------HKIQLEQVQ--EWKSKMQEQQADLQRRLKEARKEakEALEAKERYM 271
Cdd:pfam03528 92 QEAIDEVKSQWQEEVASLQAIMKetvreyevqfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQEE--ENLEDEMKKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 272 EEMADTADAI------EMATLDKEMAEerAESLQQEVEALKerVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA 345
Cdd:pfam03528 170 QEDAEKLRSVvmpmekEIAALKAKLTE--AEDKIKELEASK--MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAE 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568940563 346 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKN-QELEVVR---QQRERLQEELSQAE-STIDELKEQ 406
Cdd:pfam03528 246 KLRKELHEVCHLLEQERQQHNQLKHTWQKANdQFLESQRllmRDMQRMESVLTSEQlRQVEEIKKK 311
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
231-322 |
7.34e-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: 38.19 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940563 231 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtaDAIEMATLDKEMAEERA-ESLQQEVEALKERV 309
Cdd:cd06503 38 SLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE--EILAEAKEEAERILEQAkAEIEQEKEKALAEL 115
|
90
....*....|...
gi 568940563 310 DELTTDLEILKAE 322
Cdd:cd06503 116 RKEVADLAVEAAE 128
|
|
| |
