|
Name |
Accession |
Description |
Interval |
E-value |
| Dynactin |
pfam12455 |
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ... |
514-792 |
1.52e-91 |
|
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: 296.45 E-value: 1.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 514 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 588
Cdd:pfam12455 1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 589 DHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 668
Cdd:pfam12455 80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 669 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMG 748
Cdd:pfam12455 156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 749 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDTRQFCKKIRRRM 792
Cdd:pfam12455 236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
29-94 |
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 1039774237 29 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 94
Cdd:pfam01302 1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
29-95 |
8.50e-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: 8.50e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 29 VGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEA-KGKNDGTVQGRKYFTCDEGHGIFVRQSQIQ 95
Cdd:smart01052 1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-527 |
1.40e-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: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLR--LKRSED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 278
Cdd:TIGR02168 170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 279 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 351
Cdd:TIGR02168 250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 352 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 427
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 428 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 507
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340
....*....|....*....|
gi 1039774237 508 RQLTAHLQDVNRELTNQQEA 527
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-502 |
3.29e-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: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 287
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 288 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDL 367
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 368 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnlNLEEKVRELRET 447
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039774237 448 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ 502
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-527 |
8.18e-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: 99.36 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 287
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 288 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEekgsdgaASSYQLKQLEEQNARLKDALVRMRDL 367
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-------ALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 368 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAL----GAEEMVEMLTDRNLNLEEKVRE 443
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 444 LRETVGDLE-AMNEMNDEL-QENARETELELREQ-------------LDMAGARVREAQKRVEAAQETVAD--------- 499
Cdd:TIGR02168 906 LESKRSELRrELEELREKLaQLELRLEGLEVRIDnlqerlseeysltLEEAEALENKIEDDEEEARRRLKRlenkikelg 985
|
330 340 350
....*....|....*....|....*....|....*..
gi 1039774237 500 ---------YQQTIKKYRQLTAHLQDVNRELTNQQEA 527
Cdd:TIGR02168 986 pvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-556 |
8.90e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 212 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTADAI 291
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELE------AELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 292 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSE 371
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 372 KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM-LTDRNLNLEEKVRELRETVGD 450
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 451 LEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNREL-TNQQEASV 529
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELaEAAARLLL 495
|
330 340
....*....|....*....|....*..
gi 1039774237 530 ERQQQPPPETFDFKIKFAETKAHAKAI 556
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
208-475 |
1.97e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.72 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQewksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 287
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 288 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK------AEIEEKGSDGAASSYQLKQLEEQNARLKDAL 361
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 362 vrmrdlssSEKQEHVKlqKLMEKKNQE-LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK 440
Cdd:PRK02224 630 --------AEKRERKR--ELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
250 260 270
....*....|....*....|....*....|....*
gi 1039774237 441 VRELRETVGDLEAMNEMNDELQENARETELELREQ 475
Cdd:PRK02224 700 REALENRVEALEALYDEAEELESMYGDLRAELRQR 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-534 |
4.41e-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: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 205 EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 284
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 ADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 364
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 365 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNLNLEEKVREL 444
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 445 RETVGDLEAMNEMNDELQENARETELELREQLDMAG--ARVREAQKRVEAA--QETVADYQQTIKKYRQ-----LTAHLQ 515
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRglAGAVAVLIGVEAAYEAaleaaLAAALQ 549
|
330
....*....|....*....
gi 1039774237 516 DVNRELTNQQEASVERQQQ 534
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKA 568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-491 |
1.41e-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: 92.05 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR----KEAKEALEAK 277
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 278 ERYMEEMADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 356
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 357 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnln 436
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----------- 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1039774237 437 LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 491
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
202-498 |
1.96e-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: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKE----LEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAK 277
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 278 ERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARL 357
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 358 KDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNL 437
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE------AALLEAALAELLEEL 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 438 EEKVRELRetvGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 498
Cdd:COG1196 487 AEAAARLL---LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
202-534 |
2.22e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSE--DKAKLKELEKhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 279
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDllAEAGLDDADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 359
Cdd:PRK02224 347 LREDADDLEE-------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 360 ALVRMRdlsSSEKQEHVKLQKLMEK--KNQEL----------------------EVVRQQRERLQEELSQAESTIDELKE 415
Cdd:PRK02224 420 ERDELR---EREAELEATLRTARERveEAEALleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 416 QVDAA---LGAEEMVEMLTDRNLNLEEKVRELRETVGD----LEAMNEMNDELQENARETELELREQLDMAGARV----- 483
Cdd:PRK02224 497 RLERAedlVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevae 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 484 -----------REAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:PRK02224 577 lnsklaelkerIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
205-495 |
3.97e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.48 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 205 EGLRAQV-----RDLEEKLETLRLKRSEDKAKLKELEKHKIQLeqvqewkskmqeqqadlqrrlKEARKEAKEALEAKER 279
Cdd:PRK02224 190 DQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQA---------------------RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 359
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 360 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemltdrnlnLEE 439
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-----------------LEE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 440 KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQE 495
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-521 |
5.64e-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: 90.12 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQvqewksKMQEQQADLQRrLKEARKEAKEALEAKErym 281
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA------EIEELEAQIEQ-LKEELKALREALDELR--- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 361
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 362 VRMRD-LSSSEKQEHVKLQKLMEKKnQELEVVRQQRERLQEELSQAESTIDELKEQV-----DAALGAEEMVEMLTDRNL 435
Cdd:TIGR02168 890 ALLRSeLEELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 436 NLEEKVRELRETVGDLEAMNEMN-DELQE-NARETELEL-REQLDMAGARVREAQKRVEAaqETVADYQQTIKKYRQlta 512
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAiEEYEElKERYDFLTAqKEDLTEAKETLEEAIEEIDR--EARERFKDTFDQVNE--- 1043
|
....*....
gi 1039774237 513 HLQDVNREL 521
Cdd:TIGR02168 1044 NFQRVFPKL 1052
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
241-564 |
2.80e-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: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 241 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALeakerymeemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVD 320
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS--------------QELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 321 ELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALvrmRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQ 400
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 401 eELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEA-MNEMNDELQE-NARETELE-----LR 473
Cdd:TIGR02169 816 -EIEQKLNRLTLEKEY------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEElEAALRDLEsrlgdLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 474 EQLDMAGARVREAQKRVEAAQETVADYQQTIKkyrQLTAHLQDVNRELTnQQEASVERQQQPPPETFDFKikfaETKAHA 553
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLS---ELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE----DVQAEL 960
|
330
....*....|.
gi 1039774237 554 KAIEMELRQME 564
Cdd:TIGR02169 961 QRVEEEIRALE 971
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
203-533 |
3.12e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.32 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLR----LKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 278
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 279 RYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-----------------KGSDGA 341
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 342 AS-----------SYQLKQLEEQNARLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRERLQEELSQAES-- 408
Cdd:PRK02224 468 ETieedrerveelEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELIAERRETIEEKRERAEElr 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 409 --------------------------------TIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETvgdLEAMNE 456
Cdd:PRK02224 544 eraaeleaeaeekreaaaeaeeeaeeareevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK---REALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 457 MNDELQE---NARETELELREQLDmaGARVREAQ---KRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEASV 529
Cdd:PRK02224 621 LNDERRErlaEKRERKRELEAEFD--EARIEEARedkERAEEYLEQVEEKLDELREERdDLQAEIGAVENELEELEELRE 698
|
....
gi 1039774237 530 ERQQ 533
Cdd:PRK02224 699 RREA 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-534 |
7.75e-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: 83.19 E-value: 7.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRS-EDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEakeaLEAKER 279
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADAI---EMATLDKEMAEERAE--SLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQN 354
Cdd:TIGR02169 273 LLEELNKKIKDLgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE---REIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 355 ARlKDALvrMRDLSSSEKQEHVKLQKLME--KKNQELevvRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTD 432
Cdd:TIGR02169 350 KR-RDKL--TEEYAELKEELEDLRAELEEvdKEFAET---RDELKDYREKLEKLKREINELKRELDR----------LQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 433 RNLNLEEKVRELRETVGDLEamnemndelqenARETELElrEQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQLTA 512
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIE------------AKINELE--EEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE 476
|
330 340
....*....|....*....|....
gi 1039774237 513 HLQDVNRELTNQQE--ASVERQQQ 534
Cdd:TIGR02169 477 EYDRVEKELSKLQRelAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-444 |
7.75e-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: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKL----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 278
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIeelqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 279 RYMEEMADTADAIEMAtldkemaEERAESLQQEVE-------ALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 351
Cdd:TIGR02168 334 ELAEELAELEEKLEEL-------KEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 352 EQNARLKDALVRM--------RDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA 419
Cdd:TIGR02168 407 ARLERLEDRRERLqqeieellKKLEEAELKELqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250 260
....*....|....*....|....*
gi 1039774237 420 ALGAEEMVEMLTDRNLNLEEKVREL 444
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKAL 511
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
27-412 |
2.87e-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: 77.80 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 27 LRVGSRVEVIGKghRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSP 106
Cdd:COG5244 4 LSVNDRVLLGDK--FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGNAAYEKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 107 ETPDSSASKVlkregadaAAKTSKLTTTRRPKPTrpastgvagpssslgpsgsasagelsSSEPStpaqtpLAAPIIPTP 186
Cdd:COG5244 82 KGGLVCESKG--------MDKDGEIKQENHEDRI--------------------------HFEES------KIRRLEETI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 187 ALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIqLEQVQEWKSKMQEQQADLQRRLKEA 266
Cdd:COG5244 122 EALKSTEKEEIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMVELVSDISETLNRN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 267 RKEAKEALEAKERymeemadtadaiematldkemaeeraeslqqevealKERVDELTTDLEILKAEIEEKGsdgaassyq 346
Cdd:COG5244 201 GSIQRSSVRECER------------------------------------SNIHDVLFLVNGILDGVIDELN--------- 235
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039774237 347 lKQLEeqnaRLKDALVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAESTIDE 412
Cdd:COG5244 236 -GELE----RLRRQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYE 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-564 |
3.88e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRA-QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQqadlQRRLKEARKEAKEALEAKERY 280
Cdd:PTZ00121 1273 KAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEI-LKAEIEEKGSDgaassyQLKQLEEQNARLKD 359
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKAD------ELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 360 ALVRMRDLsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEEMVEMLTDRNLNL 437
Cdd:PTZ00121 1423 AKKKAEEK---KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 438 EE--KVRELRETVGDLEAMNEMN--DELQ--ENARETElELREQLDMAGA-RVREAQKRVEAAQETVADYQQTIKKYRQL 510
Cdd:PTZ00121 1500 DEakKAAEAKKKADEAKKAEEAKkaDEAKkaEEAKKAD-EAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1039774237 511 TAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 564
Cdd:PTZ00121 1579 ALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
201-506 |
9.01e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRlKRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 280
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAE-EAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnaRLKDA 360
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--KKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 361 LVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAES----TIDELKEQVDAALGAEEMVEMLTDRNL 435
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 436 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 506
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-567 |
9.48e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQE----------------------QQADL 259
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkkkadelkkaaaakkkadeakKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 260 QRRLKEARK---EAKEALEAKE-----RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEALKERVDELTTDLEIL 329
Cdd:PTZ00121 1430 KKKADEAKKkaeEAKKADEAKKkaeeaKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 330 KAEIEEKGSDGAASSYQLKQLEEqnARLKDALVRMRDLSSSE---KQEHVK----LQKLMEKKNQELEvvRQQRERLQEE 402
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAEEKKKADelkKAEELKkaeeKKKAEEAKKAEED--KNMALRKAEE 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 403 LSQAEST---------IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELR 473
Cdd:PTZ00121 1586 AKKAEEArieevmklyEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 474 EQLdmagARVREAQKRveAAQETVADYQQTIKKYRQLTAHLQDVNR--ELTNQQEASVERQQQPPPETFDFKIKFAETKA 551
Cdd:PTZ00121 1664 AEE----AKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
410
....*....|....*.
gi 1039774237 552 HAkaiEMELRQMEVAQ 567
Cdd:PTZ00121 1738 EA---EEDKKKAEEAK 1750
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
187-420 |
4.62e-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: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 187 ALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEA 266
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 267 RKEAKEALEAKERYMEEMADTADAIEMATLDKEM-----------AEERAESLQQEVEALKERVDELTTDLEILKAEIEE 335
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 336 KgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 415
Cdd:COG4942 169 L-------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 1039774237 416 QVDAA 420
Cdd:COG4942 242 RTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-491 |
6.70e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRlkrsEDKAKLKELEKHKIQLEqvqEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELE---KKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqlkqleeqnarlkda 360
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK---------------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 361 lvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEK 440
Cdd:PRK03918 655 --------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE----KALER 722
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 441 VRELRETVGDLEAMNEMN--DELQENARETELELREQlDMAGARVREAQKRVE 491
Cdd:PRK03918 723 VEELREKVKKYKALLKERalSKVGEIASEIFEELTEG-KYSGVRVKAEENKVK 774
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-567 |
7.37e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQ-VRDLEEKLETLRLKRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:PTZ00121 1171 KAEDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 356
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 357 LKDALVRMRDlsSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemLTDRNLN 436
Cdd:PTZ00121 1330 KADAAKKKAE--EAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 437 LEEKVRELRETvgdlEAMNEMNDELQENAREtelelREQLDMAGARVREAQKRVEAAQEtvADYQQTIKKYRQLTAHLQD 516
Cdd:PTZ00121 1403 DKKKADELKKA----AAAKKKADEAKKKAEE-----KKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 517 VNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQ 567
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-568 |
1.43e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKI----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 276
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 277 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 356
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 357 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-QQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNL 435
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 436 NLEE---------KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 506
Cdd:COG1196 555 DDEVaaaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 507 YRQLTAHLQDVNRELTNQQEASVERQQqpppETFDFKIKFAETKAHAKAIEMELRQMEVAQA 568
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGS----LTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-526 |
1.84e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHK-----------------------IQLEQVQEWKSKMQEQQA 257
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytAELKRIEKELKEIEEKER 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 258 DLQRRLKEARKEAKEalEAKERYMEEMADTADAIE--MATLDKEMAEERAEslqqEVEALKERVDELTTDLEILKAEIEE 335
Cdd:PRK03918 477 KLRKELRELEKVLKK--ESELIKLKELAEQLKELEekLKKYNLEELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 336 KG---SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE 412
Cdd:PRK03918 551 LEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 413 LKEQVDAALGAEEMvemltdrnlnLEEKVRELREtvgdleamnEMNDELQENARETELELREQLDMAGARVREAQKRVEA 492
Cdd:PRK03918 631 AFEELAETEKRLEE----------LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
330 340 350
....*....|....*....|....*....|....
gi 1039774237 493 AQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 526
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
202-567 |
3.02e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSK-------MQEQQADLQRRLKEARKEAKEaL 274
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegskrkLEEKIRELEERIEELKKEIEE-L 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 275 EAKERYMEEMADTADaiEMATLDKEMA---------EERAESLQQEVEALKERVDELTTDLEILKaEIEEKGSDGAASSY 345
Cdd:PRK03918 279 EEKVKELKELKEKAE--EYIKLSEFYEeyldelreiEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 346 QLKQLEEQNARLKDALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGA- 423
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAk 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 424 -----------------------------EEMVEMLTDRN-------------LNLEEKVRELRETVGDLEAMNEM---- 457
Cdd:PRK03918 436 gkcpvcgrelteehrkelleeytaelkriEKELKEIEEKErklrkelrelekvLKKESELIKLKELAEQLKELEEKlkky 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 458 -NDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP 536
Cdd:PRK03918 516 nLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430
....*....|....*....|....*....|.
gi 1039774237 537 PETFDFKIKFAETKAHAKAIEMELRQMEVAQ 567
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
210-491 |
7.19e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKERYMEEMAD 286
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 TADAIEMAtldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqlkqLEEQNARLKDAlvrmrd 366
Cdd:PRK03918 236 LKEEIEEL-------EKELESLEGSKRKLEEKIRELEERIEELKKEIEE--------------LEEKVKELKEL------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 367 lsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRE 446
Cdd:PRK03918 289 --KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 447 TVGDLEAMNEMNDELQ-----------ENARETELELREQLDMAGARVREAQKRVE 491
Cdd:PRK03918 367 AKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
210-527 |
1.25e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTAD 289
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 AIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE--IEEKG------------------------------ 337
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerLKEARlllliaaallallglggsllsliltiagvl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 338 -------SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKL-MEKKNQELEVVRQQRERLQEELSQAEST 409
Cdd:COG4717 280 flvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEEL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 410 IDELK----EQVDAALGAEEMVEMLTD--RNLNLEEKVRELRETVGDLEAM--NEMNDELQENARETELELREQLDMAGA 481
Cdd:COG4717 360 EEELQleelEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEE 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 482 RVREAQKRVEAAQETVADYQQTIKK------YRQLTAHLQDVNRELTNQQEA 527
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQleedgeLAELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
282-537 |
4.79e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.35 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAI------EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYqLKQLEEQNA 355
Cdd:COG3206 148 ELAAAVANALaeayleQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLL-LQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 356 RLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRE--RLQEELSQAESTIDELKEQvdaalgaeemvemLTDR 433
Cdd:COG3206 227 QLAEARAELAEAEARLAA----LRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAELSAR-------------YTPN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 434 NlnleEKVRELRETVGDLEAmnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAH 513
Cdd:COG3206 290 H----PDVIALRAQIAALRA------QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
250 260
....*....|....*....|....*....
gi 1039774237 514 LqDVNRE-----LTNQQEASVERQQQPPP 537
Cdd:COG3206 360 V-EVARElyeslLQRLEEARLAEALTVGN 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
229-464 |
1.18e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 229 KAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARkEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAES 307
Cdd:COG4913 609 RAKLAALEA---ELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAErEIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 308 lqQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvkLQKLMEKKNQ 387
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALG 760
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039774237 388 ElEVVRQQRERLQEELSQAESTIDELkeqvdaalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQEN 464
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRA---------EEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED 827
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
207-532 |
1.48e-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: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 286
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRD 366
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-------EIKDLTNQDSVKELIIKNLDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 367 LSSSEKQ-------EHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeEMVEMLTDRNLNLEE 439
Cdd:TIGR04523 462 TRESLETqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKES 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 440 KVRELRETVgdleamNEMNDELQENARETE-LELREQLDmagaRVREAQKRVEAAQETVadyQQTIKKYrqlTAHLQDVN 518
Cdd:TIGR04523 539 KISDLEDEL------NKDDFELKKENLEKEiDEKNKEIE----ELKQTQKSLKKKQEEK---QELIDQK---EKEKKDLI 602
|
330
....*....|....*.
gi 1039774237 519 RELTN--QQEASVERQ 532
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 ... |
212-564 |
1.59e-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: 65.76 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 212 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEqvqewKSKMQEQQAdlQRRLKEarKEAKEALEAKERYMEEMADTADAI 291
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKA--LEYYQL--KEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 292 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSE 371
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----LLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 372 KQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDL 451
Cdd:pfam02463 316 LKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 452 EAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 531
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350
....*....|....*....|....*....|...
gi 1039774237 532 QQQpppETFDFKIKFAETKAHAKAIEMELRQME 564
Cdd:pfam02463 473 LLK---ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-574 |
2.21e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQ-VRDLEE--KLETLRLKR-SEDKAKLKELEKHKI-QLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEA 273
Cdd:PTZ00121 1238 DAEEAKKAEeERNNEEirKFEEARMAHfARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 274 LEAKERyMEEMADTADAI----EMATLDKEMAEERAESLQQEVEALKER--VDELTTDLEILKAEIEEKGSDGAASSYQL 347
Cdd:PTZ00121 1318 DEAKKK-AEEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKaeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 348 KQLEEQNARlkdalvrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEE 425
Cdd:PTZ00121 1397 KKKAEEDKK---------------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 426 MVEMLTDRnlnleEKVRELRETVGDLEAMNEMNDELQENARETElELREQLDmAGARVREAQKRVEAAQETVADYQQTIK 505
Cdd:PTZ00121 1462 AKKKAEEA-----KKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 506 KYRQL-TAHLQDVNRELTNQQEASVERQQQPPPEtfdfKIKFAETKAHAKAIEMELRQMEVAQANRHMSL 574
Cdd:PTZ00121 1535 KADEAkKAEEKKKADELKKAEELKKAEEKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
210-532 |
2.67e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.01 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADta 288
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELnEELKELAEKRDE----LNAQVKELREEAQELREKRDELNEKVKE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 289 daiematldkemaeeraesLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassYQLKQLEEQNARLKDALVRmRDLS 368
Cdd:COG1340 76 -------------------LKEERDELNEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEWRQQT-EVLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 369 SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQaestIDELKEQVDAalgaeemvemltdrnlnLEEKVRELRetv 448
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAE----LKELRKEAEE-----------------IHKKIKELA--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 449 gdlEAMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEA 527
Cdd:COG1340 188 ---EEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRkELKKLRKKQRALKREKEKE 263
|
....*
gi 1039774237 528 SVERQ 532
Cdd:COG1340 264 ELEEK 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-491 |
2.78e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARK--EAKEALEAK 277
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKaeEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 278 ERYMEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLE--ILKAEIEEKGSDGAASSYQLKQLEEQNA 355
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAKKAEEdeKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 356 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgAEEMVEMLTDRNL 435
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI-EEELDEEDEKRRM 1794
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 436 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 491
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
202-575 |
4.60e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRR--LKEARKEAKEALEAKER 279
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLK 358
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 359 DALVRMRDLSSSEKQE---------HVKLQKLMEKKNQELEV-------------VRQQRERLQEELSQAESTIDELKEQ 416
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 417 vdAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ-----LDMAGARVREA-QKRV 490
Cdd:COG4717 314 --EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiaalLAEAGVEDEEElRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 491 EAAQEtvadyqqtikkYRQLTAHLQDVNRELTNQQEASVERQQQPPPEtfDFKIKFAETKAHAKAIEMELRQM--EVAQA 568
Cdd:COG4717 392 EQAEE-----------YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELreELAEL 458
|
....*..
gi 1039774237 569 NRHMSLL 575
Cdd:COG4717 459 EAELEQL 465
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
210-545 |
1.89e-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: 62.06 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLkRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADL---QRRLKEARKEAKE--ALEAKERYMEEM 284
Cdd:pfam17380 288 QQQEKFEKMEQERL-RQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIyaeQERMAMERERELEriRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 ADTADAIEMATLdKEMaeeraESLQQEVEALKERVdelttdleilKAEIEekgsdgAASSYQLKQlEEQNARLKDALVRM 364
Cdd:pfam17380 366 RQEEIAMEISRM-REL-----ERLQMERQQKNERV----------RQELE------AARKVKILE-EERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 365 RDL-SSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERL-QEELSQAESTIDELKEQVDAALGAEEmvemltdRNL 435
Cdd:pfam17380 423 EQIrAEQEEARQREVRRLEEERAREMERVRleeqerqQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQ-------RRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 436 NLEEKVRELRETVgdleamneMNDELQENARETELELREQLDMAGARVREA--QKRVEAAQETVADYQQTIKKYRQLTAH 513
Cdd:pfam17380 496 ILEKELEERKQAM--------IEEERKRKLLEKEMEERQKAIYEEERRREAeeERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340 350
....*....|....*....|....*....|....
gi 1039774237 514 LQ--DVNRELTNQQEASVERQQQPPPETFDFKIK 545
Cdd:pfam17380 568 LEamEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
213-470 |
3.51e-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: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 213 DLEEKLETLRLKRSEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQ---RRLKEARKEAKEALEAKERYMEEMADTAD 289
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYdllEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 AI--EMATLDK-----EMAEERAESLQQEVEALKERVDELTTDLE-------ILKAEIEEKGSdgaassyQLKQLEEQNA 355
Cdd:pfam06160 309 ELkeELERVQQsytlnENELERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILE-------QLEEIEEEQE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 356 RLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaEEMVEML 430
Cdd:pfam06160 382 EFKESLQSLR------KDELEAREKLDEFKLELREIKRLvEKSNLpglpESYLDYFFDVSDEI----------EDLADEL 445
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1039774237 431 TDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 470
Cdd:pfam06160 446 NEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ 485
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
242-483 |
3.57e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 242 LEQVQEWKSKMQEQQAD-LQRRLKEARKEAKEALEAKERYMEEMadtadAIEMATLDKEMAEERAESLQQEVEALKERVD 320
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 321 ELTTDLEILKAEIEEkGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQ-RERL 399
Cdd:COG3206 237 EAEARLAALRAQLGS-GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL----RAQIAALRAQlQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 400 QEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQenARETELELREQLDMA 479
Cdd:COG3206 312 QRILASLEAELEALQAREAS---LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEALTVG 386
|
....
gi 1039774237 480 GARV 483
Cdd:COG3206 387 NVRV 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
301-531 |
3.99e-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: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 301 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLssseKQEHVKLQK 380
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRAL----EQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 381 LMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--------VDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLE 452
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 453 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 531
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
202-470 |
4.59e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 60.62 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKakLKELEKhKI-----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 276
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQE-RIdqlydILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 277 KERYMEEMADTADAIEmatldkemaeeRAESLQQEVEALKERVDELTTDLE-------ILKAEIEEkgsdgaaSSYQLKQ 349
Cdd:PRK04778 333 IDRVKQSYTLNESELE-----------SVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEE-------ILKQLEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 350 LEEQNARLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaE 424
Cdd:PRK04778 395 IEKEQEKLSEMLQGLR------KDELEAREKLERYRNKLHEIKRYlEKSNLpglpEDYLEMFFEVSDEI----------E 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039774237 425 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 470
Cdd:PRK04778 459 ALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-530 |
4.66e-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: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 286 DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILkAEIEEKGSDgaasSYQLKQLEEQNARLKDALVRMr 365
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWD----EIDVASAEREIAELEAELERL- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 366 DLSSSEKQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML--TDRNLNLEEKVRE 443
Cdd:COG4913 681 DASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarLELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 444 LRetvgdleamnemndeLQENARETELELREQLDMAGARVREAQKRVEAAQE---------------TVADYQQTIKKYR 508
Cdd:COG4913 758 AL---------------GDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldaDLESLPEYLALLD 822
|
250 260
....*....|....*....|....*..
gi 1039774237 509 QLTA-----HLQDVNRELTNQQEASVE 530
Cdd:COG4913 823 RLEEdglpeYEERFKELLNENSIEFVA 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
203-406 |
5.09e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARKEAKEALEAKERY 280
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAiEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS---------YQLKQLE 351
Cdd:COG4717 411 LEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllqeleelkAELRELA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 352 EQNARLK---DALVRMRDLSSSEKQEHV--------------KLQKLMEKKNQELEVVRQQRERLQ-EELSQA 406
Cdd:COG4717 490 EEWAALKlalELLEEAREEYREERLPPVleraseyfsrltdgRYRLIRIDEDLSLKVDTEDGRTRPvEELSRG 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
296-523 |
5.12e-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: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 296 LDKEMAEERAESLQQEVEALK---ERVDELTTDLEILkAEIEEKGSDgaassyqLKQLEEQNARLKDALVRMRDLSSSEK 372
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLErahEALEDAREQIELL-EPIRELAER-------YAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 373 QEhvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemVEMLTDRnlnLEEKVRELRETVGDLE 452
Cdd:COG4913 290 LE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR--LEQLERE---IERLERELEERERRRA 362
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 453 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADyqqTIKKYRQLTAHLQDVNRELTN 523
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAEIAS 430
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
215-526 |
5.97e-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: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 215 EEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADaIEMA 294
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID-IKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 295 TLDKEMAEERAEsLQQEVEALKErvdELTTDLEILKAEIEEKGSDgaassyQLKQLEEQNARlKDALVRMRDLSSSEKQE 374
Cdd:COG5185 311 TESLEEQLAAAE-AEQELEESKR---ETETGIQNLTAEIEQGQES------LTENLEAIKEE-IENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 375 HVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETVGDL--- 451
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI------EELQRQIEQATSSNEEVSKLLNELISELnkv 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 452 --EAMNEMNDELQENARETELELREQLDmagarvrEAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQE 526
Cdd:COG5185 454 mrEADEESQSRLEEAYDEINRSVRSKKE-------DLNEELTQIESRVSTLKATLEKLRaKLERQLEGVRSKLDQVAE 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
210-564 |
9.62e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.13 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtad 289
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 aiEMATLDKEMAEERAESLQ--QEVEALKERVDELTTDLEilKAEIEekgsdgaassyqLKQLEEQNARLKDalvrmRDL 367
Cdd:pfam15921 350 --QLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLH--KREKE------------LSLEKEQNKRLWD-----RDT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 368 SSSEKQEHvkLQKLMEKKNQELE----VVRQQRERLQEELSQAESTIDELKEQVD--AALGAE---------EMVEMLTD 432
Cdd:pfam15921 409 GNSITIDH--LRRELDDRNMEVQrleaLLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQlestkemlrKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 433 RNLNLEEKVRELRETVGDLE----AMNEMNDELQENARETELELRE--QLDMAGARVREAQKRVEAAQETVADYQQTIKK 506
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQekerAIEATNAEITKLRSRVDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 507 YRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 564
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
291-453 |
1.16e-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: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 291 IEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKdalvrmrdls 368
Cdd:COG1579 10 LDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 369 ssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETV 448
Cdd:COG1579 80 --EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL------AELEAELAELEAELEEKKAELDEEL 151
|
....*
gi 1039774237 449 GDLEA 453
Cdd:COG1579 152 AELEA 156
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
229-424 |
1.38e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 229 KAKLKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAE 302
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 303 ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAAssyqlkQLEEQNArlkDALVRMRDLSSSEKQEHVKLQKLM 382
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAA-----RAPAWLAAQDALA------RLREQSG---EEFEDSQDVTEYMQQLLERERELT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1039774237 383 EKKNQelevVRQQRERLQEE---LSQAESTIDE----LKEQVDAALGAE 424
Cdd:PRK04863 645 VERDE----LAARKQALDEEierLSQPGGSEDPrlnaLAERFGGVLLSE 689
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-570 |
1.46e-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: 59.31 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 311 EVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQnarlKDALVRMRDLSSsEKQEHVKLQKLMEKKN--QE 388
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRRE----REKAERYQALLK-EKREYEGYELLKEKEAleRQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 389 LEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNL-EEKVRELRETVGDLEAMnemndelQENARE 467
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAE-------IASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 468 TELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFA 547
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAETRD 385
|
250 260
....*....|....*....|...
gi 1039774237 548 ETKAHAKAIEMELRQMEVAQANR 570
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKREL 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
202-534 |
2.56e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkIQLEQVQEWKSKMQEQqadlqRRLKEARKEAKEALEAKERYM 281
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLE---QDYQAASDHLNLVQTA-----LRQQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEmadTADAIEMATLDKEMAEERAESLQQEVEALK-------ERVDELTTD----------LEILK-----AEIEEKGSD 339
Cdd:PRK04863 365 EE---QNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqQALDVQQTRaiqyqqavqaLERAKqlcglPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 340 GAASSYQlKQLEEQNARLKDALVRMRDlSSSEKQEHVKLQKLMEK----------KNQELEVVRQQRER--LQEELSQAE 407
Cdd:PRK04863 442 DWLEEFQ-AKEQEATEELLSLEQKLSV-AQAAHSQFEQAYQLVRKiagevsrseaWDVARELLRRLREQrhLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 408 STIDELKEQVDAALGAEEMV---EMLTDRNLNLEEKVRELREtvgDLEAMNEMNDELQENARETELELREQLDMAGARVR 484
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLaefCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 485 E----------AQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:PRK04863 597 RlaarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
208-533 |
2.99e-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: 58.43 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEA---KEALEAKERymee 283
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEeVDSLKS----QLADYQQALDVQQTRAiqyQQAVQALEK---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 284 madtADAI-EMATLDKEMAEERAESLQQEVEALKERVDELttdleilkaeiEEKGSDGAASSYQLKQLEEQNARLKDALV 362
Cdd:COG3096 425 ----ARALcGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-----------EQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 363 RmrdlssseKQEHVKLQKLMEKkNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgAEEMVEML---TDRNLNLEE 439
Cdd:COG3096 490 R--------SQAWQTARELLRR-YRSQQALAQRLQQLRAQLAELEQRLRQQQN-------AERLLEEFcqrIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 440 KVRELRETvgdLEAMNEMNDELQENARETELELREQLDMAGARVRE----------AQKRVEAAQETVAdyqQTIKKYRQ 509
Cdd:COG3096 554 ELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlaAQDALERLREQSG---EALADSQE 627
|
330 340
....*....|....*....|....
gi 1039774237 510 LTAHLQDVnreLTNQQEASVERQQ 533
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 ... |
202-499 |
3.00e-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: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE---QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 278
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 279 RYMEEMADTADAI--EMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL 350
Cdd:pfam02463 261 EKEEEKLAQVLKEnkEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 351 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML 430
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDL 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 431 TDRNLN-LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 499
Cdd:pfam02463 421 LKEEKKeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
210-534 |
3.76e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKealeakerymeemadtad 289
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-----KEKLNIQKNIDKIKNKLLKLELL------------------ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 aieMATLDKEmaEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLeeqnarlkdalvrmrdlss 369
Cdd:TIGR04523 203 ---LSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 370 seKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvEMLTDRNLNLEEKVRELRETVG 449
Cdd:TIGR04523 259 --KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--------DWNKELKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 450 DL----EAMNEMNDELQ------ENARETELELREQLdmagarvREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNR 519
Cdd:TIGR04523 329 QIsqnnKIISQLNEQISqlkkelTNSESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKN---LESQINDLES 398
|
330
....*....|....*
gi 1039774237 520 ELTNQQEASVERQQQ 534
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQ 413
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
207-417 |
3.77e-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: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETlRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmad 286
Cdd:COG5185 287 LIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE--- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 tADAIEmATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDG-AASSYQLKQLE----------EQNA 355
Cdd:COG5185 363 -IENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEELQrqieqatssnEEVS 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 356 RLKDALVRMRDLSSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQV 417
Cdd:COG5185 441 KLLNELISELNKVMREADEESQ-SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
205-450 |
3.81e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 205 EGLRAQVRDLEEKLETLRlkrsEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQR---RLKEARKEAKEALEAKERYM 281
Cdd:COG4913 664 ASAEREIAELEAELERLD----ASSDDLAALEE---QLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRL 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEK----------------GSDGAASS 344
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAmrafnrewpaetadldADLESLPE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 345 YQ--LKQLEEQN-----ARLKDALVR-----MRDLSSSEKQEHVKLQKLMEKKNQELE--------------------VV 392
Cdd:COG4913 817 YLalLDRLEEDGlpeyeERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSLKripfgpgrylrlearprpdpEV 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 393 RQQRERLQEELSQAESTIDELKEQVDAALgaEEMVEMLTDRNlnlEEKVRELRETVGD 450
Cdd:COG4913 897 REFRQELRAVTSGASLFDEELSEARFAAL--KRLIERLRSEE---EESDRRWRARVLD 949
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
213-502 |
4.87e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 213 DLEEKLETLRLKRSEDKAKLKELEK----HKIQLEQVQEWKSKMQE--------QQADLQRRLKEARKEAKEALEAKeRY 280
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESqeqqQRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAEEAK-RF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIE--MATLDKEmaEERAESLQQEVEALKErvdelttdleilkaeieekgsdgaassyQLKQLEEQNARLK 358
Cdd:PRK04863 913 VQQHGNALAQLEpiVSVLQSD--PEQFEQLKQDYQQAQQ----------------------------TQRDAKQQAFALT 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 359 DALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAE--------------STIDELKEQVDAAlgA 423
Cdd:PRK04863 963 EVVQRRAHFSYEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslkSSYDAKRQMLQEL--K 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 424 EEMVEMLTDRNLNLEEKVRELREtvgdleamnEMNDELQEN-ARETELELreQLDMAGARVREAQKRVEAAQEtvaDYQQ 502
Cdd:PRK04863 1041 QELQDLGVPADSGAEERARARRD---------ELHARLSANrSRRNQLEK--QLTFCEAEMDNLTKKLRKLER---DYHE 1106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
203-494 |
5.69e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLE-EKLETLRLKRSEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARK--------EAKE 272
Cdd:PTZ00121 1068 QDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEArKAEEAKKKAEDARKAEEARKaedarkaeEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 273 ALEAKERYMEEMADTADAIEMAtldkemaeERAESLQQEVEAlkERVDELTTDLEILKAEiEEKGSDGAASSYQLKQLEE 352
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAEEA--------RKAEDAKKAEAA--RKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 353 qnarlkdalvrMRDLSSSEKQEHVKlqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTD 432
Cdd:PTZ00121 1217 -----------ARKAEDAKKAEAVK--KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 433 RNLNLEEKVRELR--ETVGDLEAMNEMNDELQ--ENARETELELREQLDMAGARVREAQKRVEAAQ 494
Cdd:PTZ00121 1284 KKAEEKKKADEAKkaEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
219-535 |
5.92e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 219 ETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 298
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 299 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHV-- 376
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQELQALSEAEAeq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 377 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNE 456
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 457 MNDELQE-NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQP 535
Cdd:COG4372 264 ELAILVEkDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
259-1026 |
6.88e-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: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 259 LQRRLKEARKEAKEALEAKEryMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgs 338
Cdd:COG1196 198 LERQLEPLERQAEKAERYRE--LKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 339 dgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVD 418
Cdd:COG1196 272 -------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 419 AALGAEEMvemltdrnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 498
Cdd:COG1196 341 ELEEELEE----------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 499 DYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikFAETKAHAKAIEMELRQMEVAQANRHMSLLTAf 578
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----------AAEEEAELEEEEEALLELLAELLEEAALLEAA- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 579 mpdsflrpggdhdcvlvlllmpRLICKAELIRKQAQEKFDLSENCSERPGLRGA-AGEQLSFAAGLVYSLSLLQATLHRY 657
Cdd:COG1196 479 ----------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAY 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 658 EHALSQCSVdvykkvGSLYPEMSAHERSLDFLIELLhKDQLDETVNVEPLTKaikyyqhlysIHLAEQPEDSTMQLADhi 737
Cdd:COG1196 537 EAALEAALA------AALQNIVVEDDEVAAAAIEYL-KAAKAGRATFLPLDK----------IRARAALAAALARGAI-- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 738 kftqsaldcmgvevgrlraflqgGQEATDIALLLRDLEtscsdtrqfckkirrrmpgtdapgiPAALAFGSQVSDTLLDC 817
Cdd:COG1196 598 -----------------------GAAVDLVASDLREAD-------------------------ARYYVLGDTLLGRTLVA 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 818 RKHLTWVVavlqevaaaaaqliaplaenegLPVAALEELAFKASEQIYGSPSSSpyeclrqsctilistmnklataMQEG 897
Cdd:COG1196 630 ARLEAALR----------------------RAVTLAGRLREVTLEGEGGSAGGS----------------------LTGG 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 898 EydaerppskpppVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 977
Cdd:COG1196 666 S------------RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1039774237 978 IEKVQTRLDETQTLLRKKEKDFEETMdalqADIDQLEAEKAELKQRLNS 1026
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEP----PDLEELERELERLEREIEA 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
283-537 |
7.04e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQNARLKDALV 362
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 363 RMRD-----------LSSSEKQEHVK----LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmv 427
Cdd:COG3883 94 ALYRsggsvsyldvlLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 428 emltdrnlNLEEKVRELRETVGDLEAmnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 507
Cdd:COG3883 172 --------ELEAQQAEQEALLAQLSA-----EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|
gi 1039774237 508 RQLTAHLQDVNRELTNQQEASVERQQQPPP 537
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
213-482 |
7.19e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 213 DLEEKLETLRLKRSEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQR---------------RLKEARKEAKEALEAk 277
Cdd:COG3096 833 DPEAELAALRQRRSELER---ELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELDAAQEA- 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 278 ERYMEEMADTADAIE--MATLDKEMAEEraESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQ-----LKQL 350
Cdd:COG3096 909 QAFIQQHGKALAQLEplVAVLQSDPEQF--EQLQADYLQAKEQQRRLKQQIFALSEVVQRR----PHFSYEdavglLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 351 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeEMVEML 430
Cdd:COG3096 983 SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-----EAEERA 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 431 TDRNLNLEEKVRELRETVGDLEAM-----NEMnDELQENARETELE---LREQLDMAGAR 482
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQltrceAEM-DSLQKRLRKAERDykqEREQVVQAKAG 1116
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
201-506 |
8.22e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 56.83 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRA-QVRDLEEKLE-----TLRLkrseDKAKLKELEkhkiQLEQVQEWKSKMQEQQADLQRRLKEArkEAKEAL 274
Cdd:PLN02939 119 SKDGEQLSDfQLEDLVGMIQnaeknILLL----NQARLQALE----DLEKILTEKEALQGKINILEMRLSET--DARIKL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 275 EAKERYMEEMADTadaiEMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQLK 348
Cdd:PLN02939 189 AAQEKIHVEILEE----QLEKLRNELLIRGAteglcvHSLSKELDVLKEENMLLKDDIQFLKAELIEV----AETEERVF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 349 QLEEQNARLKDALvrmRDLSSsekqehvklqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeemve 428
Cdd:PLN02939 261 KLEKERSLLDASL---RELES----------KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAA------- 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 429 MLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETELELREQLDMAGArvrEAQKRVEAAQETVADYQQTIKK 506
Cdd:PLN02939 321 LVLDQNQDLRDKVDKLEASLKEAN-VSKFSSYKVELLQQKLKLLEERLQASDH---EIHSYIQLYQESIKEFQDTLSK 394
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
202-414 |
1.10e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 54.92 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQ-------------------- 260
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELnEKLNELREELDELRKELAelnkaggsidklrkeierle 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 261 --------------------RRLKEARKEAKEALEAKERYMEEMADTADA-IEMATLDKEMAE--ERAESLQQEVEALKE 317
Cdd:COG1340 123 wrqqtevlspeeekelvekiKELEKELEKAKKALEKNEKLKELRAELKELrKEAEEIHKKIKElaEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 318 RVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmeKKNQELEVVRQQRE 397
Cdd:COG1340 203 EADELRKEADELHKEIVEAQ----------EKADELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAE 270
|
250
....*....|....*...
gi 1039774237 398 RLQEELSQAES-TIDELK 414
Cdd:COG1340 271 EIFEKLKKGEKlTTEELK 288
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
201-507 |
1.91e-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: 55.41 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQvqewkskmqeQQADLQRRLKEARKEakeaLEAKERy 280
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----------QLKVLSRSINKIKQN----LEQKQK- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 meEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDElttdLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDA 360
Cdd:TIGR04523 490 --ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----LESEKKEKESK----------ISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 361 LVRMrdlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLNLEEK 440
Cdd:TIGR04523 554 LKKE------------NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK-DLIKE--IEEKEKKISSLEKE 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 441 VRELRETVGDLEAMnEMNDELQENARETELEL-REQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 507
Cdd:TIGR04523 619 LEKAKKENEKLSSI-IKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDW 685
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-509 |
2.08e-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: 55.57 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME 282
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRdlgeELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMADT-ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL---KAEIEEKGSDGAAssyqlkQLEEQNARLK 358
Cdd:pfam01576 349 EMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEG------QLQELQARLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 359 DAlvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaaLGAEEmvemlTDRNLNL 437
Cdd:pfam01576 423 ES-----ERQRAELAEKLsKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE-----LLQEE-----TRQKLNL 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 438 EEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 509
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
206-564 |
2.81e-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: 54.70 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 206 GLRAQVRDLEEklETLRLKRSEDKAKLK--ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA--LEAK-ERY 280
Cdd:pfam05622 63 LLQKQLEQLQE--ENFRLETARDDYRIKceELEKEVLELQHRNEELTSLAEEAQALKDEMDILRESSDKVkkLEATvETY 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADaiematldkemaeeraesLQQEVEALKERvdelTTDLEILKAEIEEKGSDGAASSYQL----KQLEEQNAR 356
Cdd:pfam05622 141 KKKLEDLGD------------------LRRQVKLLEER----NAEYMQRTLQLEEELKKANALRGQLetykRQVQELHGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 357 LkdalvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDR 433
Cdd:pfam05622 199 L-----------SEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELRcaqLQQAELSQADALLSPSSDP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 434 --NLNLEEKVRELRETVGDLEAMNEM---NDELQENARETEL------------ELREQLDMAGARVREAQKRVE----A 492
Cdd:pfam05622 268 gdNLAAEIMPAEIREKLIRLQHENKMlrlGQEGSYRERLTELqqlledanrrknELETQNRLANQRILELQQQVEelqkA 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039774237 493 AQETVADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQqqpPPETFDFKIKFAETKAHAKAIEMELRQME 564
Cdd:pfam05622 348 LQEQGSKAEDSSLLKQKLEEHLEklhEAQSELQKKKEQIEELE---PKQDSNLAQKIDELQEALRKKDEDMKAME 419
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
207-490 |
2.82e-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: 55.12 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeema 285
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 286 DTADAIEMATL-----DKEMAEERAESL------------QQEVEALK------ERVDELTTDLEILKAEIEEKGSDGAA 342
Cdd:pfam15921 407 DTGNSITIDHLrreldDRNMEVQRLEALlkamksecqgqmERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 343 SSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQeelsQAESTIDELKEQVdaaLG 422
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR----NVQTECEALKLQM---AE 559
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 423 AEEMVEMLTDRNLNLEEKVRELRETVGdleAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRV 490
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAG---AMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARV 627
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
346-506 |
3.24e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 346 QLKQLEEQNARLKDALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 425
Cdd:COG1579 18 ELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 426 M------VEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDmagARVREAQKRVEAAQETVAD 499
Cdd:COG1579 91 YealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167
|
....*..
gi 1039774237 500 YQQTIKK 506
Cdd:COG1579 168 LAAKIPP 174
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
203-534 |
3.52e-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: 54.97 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 282
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP-LCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALV 362
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 363 RMRDL----SSSEKQEHVKLQKLMEKKNQELEV--VRQQRERLQEELSQAESTIDEL------KEQVDAALGAEEMVEML 430
Cdd:TIGR00618 595 RLQDLteklSEAEDMLACEQHALLRKLQPEQDLqdVRLHLQQCSQELALKLTALHALqltltqERVREHALSIRVLPKEL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 431 TDRNLNLEEKVRELRETV-GDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ---T 503
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLtYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqarT 754
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1039774237 504 IKKYR---------------QLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:TIGR00618 755 VLKARteahfnnneevtaalQTGAELSHLAAEIQFFNRLREEDTHL 800
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
202-365 |
3.66e-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: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRlkrsedkaklKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErym 281
Cdd:COG1579 24 HRLKELPAELAELEDELAALE----------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 eeMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDAL 361
Cdd:COG1579 91 --YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAEL 158
|
....
gi 1039774237 362 VRMR 365
Cdd:COG1579 159 EELE 162
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
288-443 |
3.98e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 288 ADAIEMATLDKEMAEERAESLQQEVEA-LKERVDELTTDLEilkAEIEEKGSDgaassyqLKQLEEQNARLKDALvrmrd 366
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE---KELRERRNE-------LQKLEKRLLQKEENL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 367 lssSEKQEhvklqkLMEKKNQELEVVRQQRERLQEELSQAESTIDEL-KEQVD-----AALGAEEMVEMLTDrnlNLEEK 440
Cdd:PRK12704 99 ---DRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQeleriSGLTAEEAKEILLE---KVEEE 166
|
...
gi 1039774237 441 VRE 443
Cdd:PRK12704 167 ARH 169
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
203-511 |
4.02e-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: 54.13 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---EALEAKER 279
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKtltQRVLERET 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADaiEMATLDKEMAEERaESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKD 359
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT-------QVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 360 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdAALGAEEMVEMLTDRNLNL-E 438
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ---ARLQAAQLTLQLADASLALrE 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 439 EKVRELRETVGDLEAMNEMNDELQENARETeleLREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLT 511
Cdd:pfam07888 298 GRARWAQERETLQQSAEADKDRIEKLSAEL---QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
174-561 |
4.13e-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: 54.67 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 174 AQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKiqleqvQEWKSKMQ 253
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR------DEMLGLAP 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 254 EQQADLQRRLKEArKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALkERVDELTTDLE--ILKA 331
Cdd:TIGR00606 734 GRQSIIDLKEKEI-PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM-ERFQMELKDVErkIAQQ 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 332 EIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERLQEEL- 403
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKlqigtnlQRRQQFEEQLv 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 404 ---SQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----------EEKVRELRETVGDLEA-MNEMNDELQENARET 468
Cdd:TIGR00606 892 elsTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsnkkaQDKVNDIKEKVKNIHGyMKDIENKIQDGKDDY 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 469 ELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQD-VNRELTNQQEASVERQqqppPETFDFKI--- 544
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDnLTLRKRENELKEVEEE----LKQHLKEMgqm 1047
|
410
....*....|....*..
gi 1039774237 545 KFAETKAHAKAIEMELR 561
Cdd:TIGR00606 1048 QVLQMKQEHQKLEENID 1064
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
204-498 |
4.22e-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: 54.34 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 204 EEGLRAQVRDLEEKLETLRLKRSE-----DKAKLK-------------ELEKH-------KIQLEQVQEWKSKMQEQQAD 258
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIEltahcDKLLLEnkeltqeasdmtlELKKHqediincKKQEERMLKQIENLEEKEMN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 259 LQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEmaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKGS 338
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE---KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 339 DGAASSYQLKQLEEQNARLKDALvrmrdlsSSEKQehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE---LKE 415
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELEL-------ASAKQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQK 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 416 QVDAALGAE--EMVEMLtDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL--------ELREQLDMagaRVRE 485
Cdd:pfam05483 693 EIDKRCQHKiaEMVALM-EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELsnikaellSLKKQLEI---EKEE 768
|
330
....*....|...
gi 1039774237 486 AQKRVEAAQETVA 498
Cdd:pfam05483 769 KEKLKMEAKENTA 781
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-509 |
4.31e-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: 54.41 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE-QVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKERYMEEMA 285
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEEKA 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 286 DTADAIEMA------------------------------TLDKEMAEERAESLQQEVE---ALKERVDELTTDLEILKAE 332
Cdd:pfam01576 566 AAYDKLEKTknrlqqelddllvdldhqrqlvsnlekkqkKFDQMLAEEKAISARYAEErdrAEAEAREKETRALSLARAL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 333 IEEKGsdgaassyQLKQLEEQNARLK---DALVRMRDLSSSEKQEHVKLQKLMEkknQELEVVRQQRERLQEELSQAEST 409
Cdd:pfam01576 646 EEALE--------AKEELERTNKQLRaemEDLVSSKDDVGKNVHELERSKRALE---QQVEEMKTQLEELEDELQATEDA 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 410 IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAmnEMNDELQENA------RETELELRE---QLDMAG 480
Cdd:pfam01576 715 KLRLEVNMQALKAQFE--RDLQARDEQGEEKRRQLVKQVRELEA--ELEDERKQRAqavaakKKLELDLKEleaQIDAAN 790
|
330 340
....*....|....*....|....*....
gi 1039774237 481 ARVREAQKRVEAAQETVADYQQTIKKYRQ 509
Cdd:pfam01576 791 KGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
205-534 |
4.34e-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: 54.37 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 205 EGLRAQVRDLEEKL-----ETLRLKRS-EDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 273
Cdd:pfam07111 334 KQLRGQVAELQEQVtsqsqEQAILQRAlQDKAAEVEVERMsakglQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 274 LEAKERYMEEMADTADAI------------EMATLDKEMAEERA-ESLQQEVEALKERVDELTTDLeilkaeieekgsdg 340
Cdd:pfam07111 414 QIWLETTMTRVEQAVARIpslsnrlsyavrKVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADL-------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 341 aasSYQLKQLEEQNARLKDALvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDA 419
Cdd:pfam07111 480 ---SLELEQLREERNRLDAEL----QLSAHLIQQEVgRAREQGEAERQQLSEVAQQ---LEQELQRAQESLASVGQQLEV 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 420 ALGAEEMVemlTDRNLNLEEKVRELRETVGDleamnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 499
Cdd:pfam07111 550 ARQGQQES---TEEAASLRQELTQQQEIYGQ---------ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQ 617
|
330 340 350
....*....|....*....|....*....|....*
gi 1039774237 500 YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:pfam07111 618 IQHRATQEKERNQELRRLQDEARKEEGQRLARRVQ 652
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-335 |
5.08e-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: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKH--KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 279
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 280 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 335
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
203-429 |
5.68e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.06 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWK-SKMQEQQADLQRRLKEARKEAKEALEAKERYM 281
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMATLDKEMAEERAES--LQQEVEALKERVDELTTD-------LEILKAEIEEKGSDGAASSYQLK---Q 349
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESgkAQAEVERLLGILREVENEkndkdkkIAELESLTLRQMKEQNKKVANIKhgqQ 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 350 LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaEEM 426
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADNSQQLQLEELMgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL--EEI 706
|
...
gi 1039774237 427 VEM 429
Cdd:pfam10174 707 LEM 709
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
275-568 |
6.44e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 6.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 275 EAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQN 354
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 355 ARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRN 434
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE---LEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 435 LNLEEKVRELRETVGDlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrQLTAHL 514
Cdd:COG4372 167 AALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA--LLDALE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1039774237 515 QDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQA 568
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
328-533 |
6.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 328 ILKAEIEEKGSD-----GAASSYQLKQLEEQNARLKDAlvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEE 402
Cdd:COG4717 46 MLLERLEKEADElfkpqGRKPELNLKELKELEEELKEA--------EEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 403 LSQAEsTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEamnEMNDELQENARETELELREQLDMAGAR 482
Cdd:COG4717 118 LEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE---ELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 483 VREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 533
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
269-520 |
8.49e-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: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 269 EAKEALEAKERYMEEMADTADAIEM-ATLDKEMAEERAESLQQEVE-ALKERVDELTTDLEILKAEIEEKGS----DGAA 342
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKnKELFEQYKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 343 SSYQLKQLEEQNARLKDalvrmrDLSSSEKQEH--VKLQKLMEKKNQELEVVRQQRERLQEELSQAES--------TID- 411
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIED------DAAKNDKSNKaaIDIQLSLENFENKFLKISDIKKKINDCLKETESiekkissfSIDs 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 412 ---ELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAM-NEMNDE-------LQENARETELELREQLDMAG 480
Cdd:TIGR01612 1641 qdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIeIDVDQHkknyeigIIEKIKEIAIANKEEIESIK 1720
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 481 ARVREAQKRVEAAQET------------------VAD-YQQTIKKYRQLTAHLQDVNRE 520
Cdd:TIGR01612 1721 ELIEPTIENLISSFNTndlegidpnekleeynteIGDiYEEFIELYNIIAGCLETVSKE 1779
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
299-534 |
9.02e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 299 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKG---------SDGAASSYQLKQLEEQnarlKDALVRMRDLSS 369
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlngleSELAELDEEIERYEEQ----REQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 370 SEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgaeemVEMLTDRNLNLEEKVRELRETVG 449
Cdd:PRK02224 241 EVLEEH-------EERREELETLEAEIEDLRETIAETEREREELAEE----------VRDLRERLEELEEERDDLLAEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 450 DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDvnrELTNQQEASV 529
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES---ELEEAREAVE 380
|
....*
gi 1039774237 530 ERQQQ 534
Cdd:PRK02224 381 DRREE 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
249-428 |
9.98e-07 |
|
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: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 249 KSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL------ 322
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 323 ----TTDLEILkaeieeKGSDGAAS----SYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvrQ 394
Cdd:COG3883 98 sggsVSYLDVL------LGSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE---A 168
|
170 180 190
....*....|....*....|....*....|....
gi 1039774237 395 QRERLQEELSQAESTIDELKEQVDAALGAEEMVE 428
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
207-491 |
1.13e-06 |
|
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: 53.19 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLET--LRLKRSEDKAKL--KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---------EAKEA 273
Cdd:pfam05483 354 FEATTCSLEELLRTeqQRLEKNEDQLKIitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkqfeKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 274 LEAKERYM--------EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSY 345
Cdd:pfam05483 434 LKGKEQELifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 346 QLKQLEEqnarlkdalvrmrDLSSSEKQEHVKLQK---LMEKKNQ---ELEVVR----QQRERLQEELSQAESTIDELKE 415
Cdd:pfam05483 514 ELKKHQE-------------DIINCKKQEERMLKQienLEEKEMNlrdELESVReefiQKGDEVKCKLDKSEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 416 QVdaaLGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEM------NDELQENARET-----ELELREQLDMAGARVR 484
Cdd:pfam05483 581 EV---LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsAENKQLNAYEIkvnklELELASAKQKFEEIID 657
|
....*..
gi 1039774237 485 EAQKRVE 491
Cdd:pfam05483 658 NYQKEIE 664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-577 |
1.16e-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: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---------- 271
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvls 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 272 EALEAKERY---MEE----------MADTADAIEMATLDKEMAEERA-------------ESLQQEVEALKERVDELTTD 325
Cdd:TIGR02168 527 ELISVDEGYeaaIEAalggrlqavvVENLNAAKKAIAFLKQNELGRVtflpldsikgteiQGNDREILKNIEGFLGVAKD 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 326 LEILKAEIEEKGS------------DGAASSYQLKQLEEQNARLKDALVRMRDLSS--SEKQEHVKLQKlmekkNQELEV 391
Cdd:TIGR02168 607 LVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSILER-----RREIEE 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 392 VRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELE 471
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 472 LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR----QLTAHLQDVNRELTNQQEASVERQqqpppetfdFKIKFA 547
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLR---------ERLESL 829
|
410 420 430
....*....|....*....|....*....|
gi 1039774237 548 ETKAHAKAIEMELRQMEVAQANRHMSLLTA 577
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
241-421 |
1.90e-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: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 241 QLEQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD 320
Cdd:COG1579 8 ALLDLQELDSELDR----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 321 ELTT--DLEILKAEIEekgsdgaassyqlkQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRE- 397
Cdd:COG1579 84 NVRNnkEYEALQKEIE--------------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDe 149
|
170 180
....*....|....*....|....*..
gi 1039774237 398 ---RLQEELSQAESTIDELKEQVDAAL 421
Cdd:COG1579 150 elaELEAELEELEAEREELAAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-425 |
2.33e-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: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD--- 286
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 -------TADAIEMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgaassyqlkQLEEQNARL 357
Cdd:COG3883 94 alyrsggSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKA---------------------ELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 358 KDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 425
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
201-476 |
2.92e-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: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKM----QEQQADLQRRLKEARKEAKEALEA 276
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 277 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEI--EEKGSDGAASSYQLKQLEEQN 354
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 355 ARLKDALVRMRDLSSSEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRN 434
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSED-------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1039774237 435 LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQL 476
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
208-491 |
3.27e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEAKEALEAKERYmeemaD 286
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEeVDELKS----QLADYQQALDVQQTRAIQYQQAVQAL-----E 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 TADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKA-----------------------------EIEEK 336
Cdd:PRK04863 425 RAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevsrseawdvarELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 337 GSDGAASSYQLKQLE------EQNARLKDALVRMRD---------LSSSE--KQEHVKLQKLMEKKNQELEVVRQQRERL 399
Cdd:PRK04863 505 LREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLAefckrlgknLDDEDelEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 400 QEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQLDMA 479
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALA--------------RLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
330
....*....|..
gi 1039774237 480 GARVREAQKRVE 491
Cdd:PRK04863 651 AARKQALDEEIE 662
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
301-539 |
3.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 301 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDAlvrmrdlssseKQEHVKLQK 380
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----------EEYNELQAELEAL-----------QAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 381 LMEKKNQELEvvrQQRERLQEELSQA------ESTIDELK--EQVDAALGAEEMVEMLTDRNLNLeekVRELRETVGDLE 452
Cdd:COG3883 73 EIAEAEAEIE---ERREELGERARALyrsggsVSYLDVLLgsESFSDFLDRLSALSKIADADADL---LEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 453 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 532
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*..
gi 1039774237 533 QQPPPET 539
Cdd:COG3883 227 AAAAAAA 233
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
198-508 |
3.39e-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: 51.76 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 198 PSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKL-----------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEA 266
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangelekasREETFARTALKNARLDLRRLFDEKQSEKDKKNKA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 267 RKEAKEALEAKERYMEEMADTADAIEMATLDkEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAAssyQ 346
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLE-EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA---E 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 347 LKQLEEQNARLKDAL----VRMRDLSSSEKQEHVKLQKLmEKKNQEL--------EVVRQQRERLQEELSQAESTIDELK 414
Cdd:pfam12128 749 LKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERI-AVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQ 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 415 EQvdaaLGAEEMVEMLTDRNLNLEEKVRE-----LRETVGDLEAMNEMNDELQE--NARETELELREQLDMAGARVREAQ 487
Cdd:pfam12128 828 QQ----LARLIADTKLRRAKLEMERKASEkqqvrLSENLRGLRCEMSKLATLKEdaNSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340
....*....|....*....|.
gi 1039774237 488 KRVEAAQETVADYQQTIKKYR 508
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHS 924
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
304-448 |
3.54e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.62 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 304 RAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME 383
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDE------ASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 384 KKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAE-----------EMVEMLTDRNLNLEEkvrELRETV 448
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEvvsrwtgipvgKLLEGEREKLLNLEE---ELHERV 551
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
196-446 |
3.66e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 196 PLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE 275
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 276 AKERymeemADTadaiematldkemaeERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyQLKQLEEQNA 355
Cdd:COG4913 331 QIRG-----NGG---------------DRLEQLEREIERLERELEERERRRARLEA--------------LLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 356 RLKDALVRMRDlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNL 435
Cdd:COG4913 377 ASAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS----------LERRKS 436
|
250
....*....|.
gi 1039774237 436 NLEEKVRELRE 446
Cdd:COG4913 437 NIPARLLALRD 447
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
234-526 |
3.84e-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: 51.28 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 234 ELEKHKIQLEQVQEWKSKMQEQQadlqrrlKEARKEAKEALEAKERYMEEMADtadaiematldkemaeeRAESLQQEVE 313
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH-------KRARIELEKKASALKRQLDRESD-----------------RNQELQKRIR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 314 ALKERVDELTtdlEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQEL---- 389
Cdd:pfam05557 59 LLEKREAEAE---EALREQAELNRLKKKYLEALNKKLNEKESQLADA----REVISCLKNELSELRRQIQRAELELqstn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 390 ---EVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNLNLEEKVRELRETVGDLEAMNEMNDELqenAR 466
Cdd:pfam05557 132 selEELQERLDLLKAKASEAEQLRQNLEKQQSS----------LAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL---AR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 467 ETELE-LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 526
Cdd:pfam05557 199 IPELEkELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
192-479 |
4.71e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.07 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 192 GAAPPLPSpskeEEGLRAQVrdleEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMqeqqADLQRRLKEARKEAK 271
Cdd:PRK11281 30 ASNGDLPT----EADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEET----EQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 272 EALEAKERYMEEmADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLe 351
Cdd:PRK11281 98 QAQAELEALKDD-NDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQI- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 352 eqNARLKDALVRMRDLSSSEKQ----EHVKLQKLMEKKNQELEVVRQ-------QRE-------RLQEE----------- 402
Cdd:PRK11281 176 --RNLLKGGKVGGKALRPSQRVllqaEQALLNAQNDLQRKSLEGNTQlqdllqkQRDyltariqRLEHQlqllqeainsk 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 403 -LSQAESTIDELKEQVDAA-LGAEEMVEMLTDRNLNLEEKVrelretvgdLEAMNEMNDELQENareteLELREQLDMA 479
Cdd:PRK11281 254 rLTLSEKTVQEAQSQDEAArIQANPLVAQELEINLQLSQRL---------LKATEKLNTLTQQN-----LRVKNWLDRL 318
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
197-534 |
4.84e-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: 50.98 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 197 LPSPSKEEE-GLRAQVRDLEEKLETLrlkrsedKAKLKELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALE 275
Cdd:pfam10174 172 LPKKSGEEDwERTRRIAEAEMQLGHL-------EVLLDQKEKENIHLREELHRRNQLQPDPAKT-----KALQTVIEMKD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 276 AKERYMEEM-ADTADAIEMATLDKEM-AEERAESLQQeVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 353
Cdd:pfam10174 240 TKISSLERNiRDLEDEVQMLKTNGLLhTEDREEEIKQ-MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 354 NAR-------LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEM 426
Cdd:pfam10174 319 NSDckqhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 427 VEMLTDRNLNLEEKVR-------ELRETVGDLE--------AMNEMNDELQENARETElELREQldmagaRVREAQKRve 491
Cdd:pfam10174 396 INVLQKKIENLQEQLRdkdkqlaGLKERVKSLQtdssntdtALTTLEEALSEKERIIE-RLKEQ------REREDRER-- 466
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1039774237 492 aaQETVADYQQTIKKYRQLTAHLQdvnRELTNQQEASVERQQQ 534
Cdd:pfam10174 467 --LEELESLKKENKDLKEKVSALQ---PELTEKESSLIDLKEH 504
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
205-317 |
5.54e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 205 EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwkSKMQEQQADLQRRLKEARKEAKEALeAKERYMEEM 284
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED--KLLEEAEKEAQQAIKEAKKEADEII-KELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*..
gi 1039774237 285 ADTA----DAIEMATLDKEMAEERAESLQQEVEALKE 317
Cdd:PRK00409 600 GYASvkahELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-334 |
5.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEdkaKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYM 281
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQ---LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQ 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 282 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE 334
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
250-477 |
6.30e-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: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 250 SKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL 329
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADA---RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 330 KAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST 409
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 410 IDELKEQVDAALGAEEMVEMLTDRNLN-LEEKVRELREtvgDLEAMNEMN----DELQEnARETELELREQLD 477
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEeLERELERLER---EIEALGPVNllaiEEYEE-LEERYDFLSEQRE 805
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
329-564 |
6.74e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 329 LKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRD-------LSSSEKQEHVKLQKLMEKKNQ-------------- 387
Cdd:TIGR02169 644 LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQelsdasrkigeiek 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 388 ELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN--DELQENA 465
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 466 RETELELREQldmaGARVREAQKRVEAAQETVADYQQTIKkyrqltaHLQDVNRELTNqQEASVERQQQpppetfDFKIK 545
Cdd:TIGR02169 801 SKLEEEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQ-------ELQEQRIDLKE-QIKSIEKEIE------NLNGK 862
|
250
....*....|....*....
gi 1039774237 546 FAETKAHAKAIEMELRQME 564
Cdd:TIGR02169 863 KEELEEELEELEAALRDLE 881
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-570 |
7.60e-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: 50.56 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETL--RLKRSEDKAKLKELEKHKIQlEQVQEWKSKMQEQQADLQRRLKEarkeaKEALEAKERYMEEm 284
Cdd:pfam01576 66 LAARKQELEEILHELesRLEEEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQKLQLE-----KVTTEAKIKKLEE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 adtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLeilkAEIEEKgsdgAASSYQLKQLEEqnARLKDALVRM 364
Cdd:pfam01576 139 ------------DILLLEDQNSKLSKERKLLEERISEFTSNL----AEEEEK----AKSLSKLKNKHE--AMISDLEERL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 365 RdlssSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNlNLEEKVREL 444
Cdd:pfam01576 197 K----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKN-NALKKIREL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 445 RETVGDLEAMNEMNDELQENARETELELREQLdmagarvrEAQK-RVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 523
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEEL--------EALKtELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1039774237 524 QQEASVERQQQpppetfdfkikfaetkAHAKAIEMELRQMEVAQANR 570
Cdd:pfam01576 342 SHEAQLQEMRQ----------------KHTQALEELTEQLEQAKRNK 372
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
255-494 |
1.22e-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: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 255 QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTtdlEILKAEIE 334
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 335 EKGSDGAASSYQLKQLEEQNarLKDALVRMRDLSSSEKQEhvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 414
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 415 EQVDAALGAEEMVEMLTDRnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 494
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
213-491 |
1.25e-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: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 213 DLEEKLETLRLKRSedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---------- 282
Cdd:pfam06160 71 EAEELNDKYRFKKA--KKALDEIE------ELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRElrktllanrf 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMADTADAIE--MATLDKE---------------------MAEERAESLQQEVEALKERVDELTTD----LEILKAEIEE 335
Cdd:pfam06160 143 SYGPAIDELEkqLAEIEEEfsqfeeltesgdylearevleKLEEETDALEELMEDIPPLYEELKTElpdqLEELKEGYRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 336 KGSDGAASSY-----QLKQLEEQNARLKDALVRMRDLSSSEKQEHVK-----LQKLMEKKNQELEVVRQQRERLQEELSQ 405
Cdd:pfam06160 223 MEEEGYALEHlnvdkEIQQLEEQLEENLALLENLELDEAEEALEEIEeridqLYDLLEKEVDAKKYVEKNLPEIEDYLEH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 406 AESTIDELKEQVD--------------AALGAEEMVEMLTDRNLNLEEKVRE-----------LRETVGDLEAMNEMNDE 460
Cdd:pfam06160 303 AEEQNKELKEELErvqqsytlneneleRVRGLEKQLEELEKRYDEIVERLEEkevayselqeeLEEILEQLEEIEEEQEE 382
|
330 340 350
....*....|....*....|....*....|....
gi 1039774237 461 LQE---NARETELELREQLDMAGARVREAQKRVE 491
Cdd:pfam06160 383 FKEslqSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
197-557 |
1.27e-05 |
|
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: 49.66 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 197 LPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE---- 272
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQraml 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 273 --ALEAKERYMEEMAD--------------TADAIEMATLDKE----MAEERAESLQQEVEALKERVDELTTDLEILKAE 332
Cdd:TIGR00606 659 agATAVYSQFITQLTDenqsccpvcqrvfqTEAELQEFISDLQsklrLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 333 IEEKgsdgaasSYQLKQLEEQNARLKDALVRMR-DLSSSEKQEHVKLQKLMEKKNQELEVVRQQreRLQEELSQAESTID 411
Cdd:TIGR00606 739 IDLK-------EKEIPELRNKLQKVNRDIQRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIME--RFQMELKDVERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 412 ELKEQVDAALGAEEMVEMltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE------QLDMAGARVRE 485
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseklQIGTNLQRRQQ 885
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 486 AQKRVEAAQETVADYQQTIKKYR-------QLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFAETKAHAKAIE 557
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKeqdspleTFLEKDQQEKEELISSKETSNKKAQD---KVNDIKEKVKNIHGYMKDIE 961
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
202-415 |
1.36e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKErY 280
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAREDALNQSLKELMHQARTVLKART-E 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEmaeeraESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassyqlkqleEQNARLKDA 360
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAEL------SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD-----------EDILNLQCE 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1039774237 361 LVrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 415
Cdd:TIGR00618 825 TL---------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
203-406 |
1.71e-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: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEARKEAKEALEake 278
Cdd:pfam00261 37 EVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrkvLENRALKDEEKMEILEAQLKEAKEIAEEADR--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 279 RYMEemadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEqnaRLK 358
Cdd:pfam00261 114 KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTE---KLK 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1039774237 359 DALVRMRDlsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA 406
Cdd:pfam00261 187 EAETRAEF----AERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
208-521 |
1.89e-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: 48.70 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLrLKRS--EDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEaKERYMEEMA 285
Cdd:pfam06160 9 YKEIDELEERKNEL-MNLPvqEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELND-KYRFKKAKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 286 DTADAiematldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEE---------------KGSDGAAssyqLKQL 350
Cdd:pfam06160 87 ALDEI-----------EELLDDIEEDIKQILEELDELLESEEKNREEVEElkdkyrelrktllanRFSYGPA----IDEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 351 EEQNARLKDALVRMRDLSSSekQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST----IDELKEqvdaalGAEEM 426
Cdd:pfam06160 152 EKQLAEIEEEFSQFEELTES--GDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTElpdqLEELKE------GYREM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 427 VEM---LTDRNL-----NLEEKVRELRETV--GDLEAMNEMNDELQENAreteLELREQLdmagarvreaQKRVEAAQEt 496
Cdd:pfam06160 224 EEEgyaLEHLNVdkeiqQLEEQLEENLALLenLELDEAEEALEEIEERI----DQLYDLL----------EKEVDAKKY- 288
|
330 340
....*....|....*....|....*
gi 1039774237 497 vadYQQTIKKYRQLTAHLQDVNREL 521
Cdd:pfam06160 289 ---VEKNLPEIEDYLEHAEEQNKEL 310
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
913-1033 |
2.03e-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: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 913 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLDE 987
Cdd:COG1196 213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1039774237 988 TQTLLRKKEKDF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1033
Cdd:COG1196 293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
210-526 |
2.14e-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: 49.20 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 210 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeemadTAD 289
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL-------CAA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 AIEMATLDKEMAEERAESLQQeveALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSS 369
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 370 SE---------KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST-------IDELKEQVDAALGAEEMVEMLTDR 433
Cdd:TIGR00618 523 PGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcDNRSKEDIPNLQNITVRLQDLTEK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 434 NLNLEEKVR--------ELRETVGDLEAMNEMNDELQENARE------TELEL-REQLDMAGARVREAQKRVEAAQETVA 498
Cdd:TIGR00618 603 LSEAEDMLAceqhallrKLQPEQDLQDVRLHLQQCSQELALKltalhaLQLTLtQERVREHALSIRVLPKELLASRQLAL 682
|
330 340
....*....|....*....|....*...
gi 1039774237 499 DYQQTikKYRQLTAHLQDVNRELTNQQE 526
Cdd:TIGR00618 683 QKMQS--EKEQLTYWKEMLAQCQTLLRE 708
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
387-570 |
2.15e-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: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 387 QELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--------EEKVRELRETVGDLEAMNEMN 458
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELlllklrelEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 459 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 538
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE---- 334
|
170 180 190
....*....|....*....|....*....|..
gi 1039774237 539 tFDFKIKFAETKAHAKAIEMELRQMEVAQANR 570
Cdd:COG1196 335 -LEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
214-352 |
2.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 214 LEEKLETLRLKRSEDKAK--LKELEK--HKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadtad 289
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKeaEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEE------ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 290 aiemaTLDKEMaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaaSSYQLKQLEE 352
Cdd:PRK12704 97 -----NLDRKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELER 146
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
207-451 |
2.37e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.47 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHkiqleqVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 286
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 tadaiematLDKEMaEERAESLQ---QEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALVR 363
Cdd:PHA02562 246 ---------LVMDI-EDPSAALNklnTAAAKIKSKIEQFQKVIKMYE--------KGGVCPTCTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 364 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTDRNLNLEEKVR 442
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNKISTNKQSLITLVDKAKKVKAAiEELQAEFVDNAEELAKLQD 386
|
....*....
gi 1039774237 443 ELRETVGDL 451
Cdd:PHA02562 387 ELDKIVKTK 395
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
292-528 |
2.37e-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: 47.64 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 292 EMATLDKEMA--EERAESLQQEVEALKERVDELTT---DLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRD 366
Cdd:pfam09728 33 EMKRLQKDLKklKKKQDQLQKEKDQLQSELSKAILaksKLEKLCRELQK----------QNKKLKEESKKLAKEEEEKRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 367 LSSSEKQEHVK-LQKLMEKKNQELEVVRQQRERLQEELsqaESTID--ELKE-QVDAALGAEEMVEMLTDRNLNLEEKVR 442
Cdd:pfam09728 103 ELSEKFQSTLKdIQDKMEEKSEKNNKLREENEELREKL---KSLIEqyELRElHFEKLLKTKELEVQLAEAKLQQATEEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 443 ELRETVGDLEAMNEMNDELQEnARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELT 522
Cdd:pfam09728 180 EKKAQEKEVAKARELKAQVQT-LSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWK 258
|
....*.
gi 1039774237 523 NQQEAS 528
Cdd:pfam09728 259 RKWEKS 264
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
202-534 |
2.44e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDK--AKLKELEKHKIQLEQvqewkskmQEQQADLQRRLKEARKEAKEALEA-KE 278
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENRMTLEAIRvtQSDRDLFKHLITEST--------NYVAADYMRHANERRVHLEEALELrRE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 279 RYMEEmadtadaiemATLDKEmaEERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgAASSYQlkQLEEQNARLK 358
Cdd:PRK04863 295 LYTSR----------RQLAAE--QYRLVEMARELAELNEAESDLEQDYQ-------------AASDHL--NLVQTALRQQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 359 DALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ---VDAALgaeemvEMLTDRNL 435
Cdd:PRK04863 348 EKIERYQA-------DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQAL------DVQQTRAI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 436 NLEEKVRELRETvgdlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHL- 514
Cdd:PRK04863 415 QYQQAVQALERA----KQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVs 490
|
330 340
....*....|....*....|....*..
gi 1039774237 515 ----QDVNRELTNQ---QEASVERQQQ 534
Cdd:PRK04863 491 rseaWDVARELLRRlreQRHLAEQLQQ 517
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
202-568 |
2.50e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQ-VRDLEEKLETLRLKRSEDkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 280
Cdd:PTZ00121 1123 KAEDARKAEeARKAEDARKAEEARKAED-AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-AEELRKAEDAR 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADaiematldkemAEERAESLQQEVEAlkERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEqnARLKDA 360
Cdd:PTZ00121 1201 KAEAARKAE-----------EERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE--ARMAHF 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 361 LVRMRDLSSSEKQEHVKLQKLMEKKNqelevvrqqrerlQEELSQAEST--IDELKEQVDAALGAEEmvemLTDRNLNLE 438
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKK-------------ADEAKKAEEKkkADEAKKKAEEAKKADE----AKKKAEEAK 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 439 EKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ---ETVADYQQTIKKYRQLTAHLQ 515
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 516 DVNRELTNQQEASVERQQQPPPETFDFKIKFAETKahAKAIEMELRQMEVAQA 568
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKA 1459
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-322 |
2.73e-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: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 197 LPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEA 276
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER---ELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1039774237 277 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL 322
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
248-411 |
3.20e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.17 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 248 WKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAiematLDKEMAEERAESLQQEVEALKERVDELTTDLE 327
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-----QQRQEARREREELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 328 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQehvklQKLMEKKNQELEVVRQQRERLQEELSQAE 407
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR-----KLLLKLLDAELEEEKAQRVKKIEEEADLE 173
|
....
gi 1039774237 408 STID 411
Cdd:PRK12705 174 AERK 177
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
186-424 |
3.20e-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: 48.41 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 186 PALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKL-----------ETLRL--------KRSE--DKAK--LKELEKHKIQL 242
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvadaarrqfeKAYELvckiagevERSQawQTARelLRRYRSQQALA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 243 EQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERyMEEMADTADAiEMATLDKEMAE--ERAESLQQEVEA 314
Cdd:COG3096 512 QRLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEA-QLEELEEQAAEavEQRSELRQQLEQ 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 315 LKERVDELTTdleilKAEIEEKGSDgaassyQLKQLEEQ-NARLKDalvrmrdlsSSEKQEHvkLQKLMEKK---NQELE 390
Cdd:COG3096 590 LRARIKELAA-----RAPAWLAAQD------ALERLREQsGEALAD---------SQEVTAA--MQQLLEREreaTVERD 647
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039774237 391 VVRQQRERLQ---EELSQAESTID----ELKEQVDAALGAE 424
Cdd:COG3096 648 ELAARKQALEsqiERLSQPGGAEDprllALAERLGGVLLSE 688
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
201-534 |
3.50e-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: 48.30 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKlkELEKHKIQLEQVQEWKSK--------MQEQQADLQRRLKEARKEAKE 272
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 273 ALEAKERYMEEMA---DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKaeieekgsdgaassyqlKQ 349
Cdd:pfam12128 438 EEYRLKSRLGELKlrlNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR-----------------KR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 350 LEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM 429
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 430 LTDRNLNLEEKVRELRETVGDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETvadYQQTIKK 506
Cdd:pfam12128 578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEalqSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLD 654
|
330 340 350
....*....|....*....|....*....|..
gi 1039774237 507 YRQLTAHLQD----VNRELTNQQEASVERQQQ 534
Cdd:pfam12128 655 LRRLFDEKQSekdkKNKALAERKDSANERLNS 686
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
204-331 |
3.62e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 204 EEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE-QVQEWkskmqEQQADLQrrLKEARKE-AKEALEAKERYM 281
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEaEAEKW-----EEKARLA--LEKGREDlAREALERKAELE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIematldkEMAEERAESLQQEVEALKERVDELTTDLEILKA 331
Cdd:COG1842 98 AQAEALEAQL-------AQLEEQVEKLKEALRQLESKLEELKAKKDTLKA 140
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
912-1033 |
3.67e-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: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 912 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLDETQTL 991
Cdd:COG1196 252 EAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039774237 992 LRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1033
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
204-380 |
3.73e-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: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 204 EEGLRAQVRDLEEKLETLRLKR-SEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKER 279
Cdd:pfam15905 147 EDGTQKKMSSLSMELMKLRNKLeAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKekiEEKSETEKLLE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADAIEMATLDKEMAEERAE-----------SLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyqLK 348
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDIAQLEELLKekndeieslkqSLEEKEQELSKQIKDLNEKCKLLESEKEEL----------LR 296
|
170 180 190
....*....|....*....|....*....|..
gi 1039774237 349 QLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 380
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
263-418 |
4.34e-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: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 263 LKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEeraesLQQEVEALKERVDElttdleiLKAEIEEKgsdgaa 342
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR-----LEEQVERLEAEVEE-------LEAELEEK------ 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 343 ssyqlkqlEEQNARLKDALVRMRdlsSSEKQEHvklqklmeKKNQELEVVRQQRERLQEELSQAESTIDELKEQVD 418
Cdd:COG2433 440 --------DERIERLERELSEAR---SEERREI--------RKDREISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
222-505 |
4.40e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 222 RLKRSEDKAKL---KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 298
Cdd:COG4372 3 RLGEKVGKARLslfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 299 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKL 378
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 379 QKLMEKKNQELEVVRQQRERLQEELSQAestidELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN 458
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039774237 459 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIK 505
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-416 |
4.60e-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: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRlkrsedkaklKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERY 280
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIE----------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-LEAQLRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqLKQLEEQNARLKDA 360
Cdd:TIGR02169 901 LE------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--------LEDVQAELQRVEEE 966
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 361 LVRMRDLSSSEKQEHvklqKLMEKKNQELEvvrQQRERLQEELSQAESTIDELKEQ 416
Cdd:TIGR02169 967 IRALEPVNMLAIQEY----EEVLKRLDELK---EKRAKLEEERKAILERIEEYEKK 1015
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
257-532 |
4.62e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 257 ADLQRRLKEArKEAKEALEAKERYMEEMADTadaieMATLDK-EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 335
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQT-----LALLDKiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 336 KgSDGAASSYQLKQLEEQNARLKDALvrmrdlsssekQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 415
Cdd:PRK11281 113 E-TRETLSTLSLRQLESRLAQTLDQL-----------QN---AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 416 QVDAALGAEEmvemltdrNLNLEEKVRELRETVGdLEAMNEMN-DELQENARETELeLREQLDMAGARVREAQKRVEAAQ 494
Cdd:PRK11281 178 LLKGGKVGGK--------ALRPSQRVLLQAEQAL-LNAQNDLQrKSLEGNTQLQDL-LQKQRDYLTARIQRLEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039774237 495 ETV-----ADYQQTIKKYRQltahLQDVNRELTN---QQEASVERQ 532
Cdd:PRK11281 248 EAInskrlTLSEKTVQEAQS----QDEAARIQANplvAQELEINLQ 289
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
914-1023 |
5.07e-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: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 914 RAAALRAEITDAE----GLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA------------------- 970
Cdd:COG1579 25 RLKELPAELAELEdelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeieslkrr 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 971 -------AKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQR 1023
Cdd:COG1579 105 isdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
214-538 |
5.92e-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: 47.63 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 214 LEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTAD-AIE 292
Cdd:pfam15818 9 LLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQlATE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 293 MATLDKEMAEERAESLQQEVEALKERVDELTTDLEI--LKAEIEEKGSDGAASSY-----QLKQLEEQNARL----KDAL 361
Cdd:pfam15818 89 IKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLhlLAKEDHHKQLNEIEKYYatitgQFGLVKENHGKLeqnvQEAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 362 VRMRDLSS-SEKQE--------------------HVKLQKLMEKKNQELEVVRQQRERLQEELS---------QAEST-I 410
Cdd:pfam15818 169 QLNKRLSAlNKKQEseicslkkelkkvtsdliksKVTCQYKMGEENINLTIKEQKFQELQERLNmelelnkkiNEEIThI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 411 DELKEQVDAALG-AEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAgarVREAQKR 489
Cdd:pfam15818 249 QEEKQDIIISFQhMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA---LGTWKKH 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039774237 490 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPE 538
Cdd:pfam15818 326 VEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPE 374
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-416 |
5.99e-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: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKH--KIQLEQVqewksKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARvsDLELEKV-----KLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDG-------------AASSYQ 346
Cdd:pfam15921 666 RNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmEGSDGhamkvamgmqkqiTAKRGQ 742
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039774237 347 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME----KKNQ---ELEVVRQQRERLQEELSQAESTIDELKEQ 416
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvatEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
202-475 |
6.08e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLR---------LKRSEDKAKLKeLEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEake 272
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRdelesvreeFIQKGDEVKCK-LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 273 aLEAKERYMEEMADTADAIEmatldkemAEERAESLQQEVEALKerVDELTTDLEILKAEIEEKgSDGAASSYQLKQLEE 352
Cdd:pfam05483 603 -IENKNKNIEELHQENKALK--------KKGSAENKQLNAYEIK--VNKLELELASAKQKFEEI-IDNYQKEIEDKKISE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 353 QNarlkdaLVRMRDLSSSEKQEHVKLQKLMEKKNQE--------LEVVRQQRERLQEElSQAESTIDELKEQVDAALGAE 424
Cdd:pfam05483 671 EK------LLEEVEKAKAIADEAVKLQKEIDKRCQHkiaemvalMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKAA 743
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 425 EMVEMLTDRNlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQ 475
Cdd:pfam05483 744 LEIELSNIKA--------ELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
202-499 |
6.14e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLK-RSEDKAKLKELEKHKIQLEQVQEWKSKMqEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEMLRKVVEELTAKKMTLESSERT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMAT-------------LDKEMAE--------ERAESLQQEVEALKERVDELTTDLEILKAEIE----- 334
Cdd:pfam15921 498 VSDLTASLQEKERAIeatnaeitklrsrVDLKLQElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtql 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 335 --EKGSDGAASSYQLKQLEEQ--NARL-----------KDALVRMRDLSSSEKQ-EHVKLQKLMEKKNQELEVVRQQRER 398
Cdd:pfam15921 578 vgQHGRTAGAMQVEKAQLEKEinDRRLelqefkilkdkKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 399 LQEELSQAESTIDELKEQVDAAL-----GAEEMvEMLTDR-NLNLEEKVRELRETVGDLEAMNEMNDelqeNARETELEL 472
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEM-ETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDG----HAMKVAMGM 732
|
330 340
....*....|....*....|....*..
gi 1039774237 473 REQLDMAGARVREAQKRVEAAQETVAD 499
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTN 759
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-455 |
6.26e-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: 47.48 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMAD 286
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEK---KLKNLEAELLQLQEDLAASERARRQAQQERDEL--ADEIASGASGK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 TADAIEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 364
Cdd:pfam01576 878 SALQDEKRRLEARIAqlEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 365 RDLSSSEKQEHV-----KLQKLMEKKNQEL-------EVVRQQRERLQEELSQAES---TIDELKEQVDAALGA------ 423
Cdd:pfam01576 958 EGTVKSKFKSSIaaleaKIAQLEEQLEQESrerqaanKLVRRTEKKLKEVLLQVEDerrHADQYKDQAEKGNSRmkqlkr 1037
|
250 260 270
....*....|....*....|....*....|....
gi 1039774237 424 --EEMVEMLTDRNLNLEEKVRELRETVGDLEAMN 455
Cdd:pfam01576 1038 qlEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
215-523 |
7.76e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.25 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 215 EEKLETLRLKRSE----------DKAKLKELEKHKIQL--EQVQEW--------KSKMQEQQADLQRRLKEARKEAKEAL 274
Cdd:COG3096 784 EKRLEELRAERDElaeqyakasfDVQKLQRLHQAFSQFvgGHLAVAfapdpeaeLAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 275 EAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELT------TDLEILKAEIEEKGSDGAASSYQL 347
Cdd:COG3096 864 QQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQAFIQqhgkalAQLEPLVAVLQSDPEQFEQLQADY 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 348 KQLEEQNARLKDALVRMRDLssSEKQEHVKLQKL--MEKKNQELEvvrqqrERLQEELSQAESTIDELKEQVDAALG-AE 424
Cdd:COG3096 944 LQAKEQQRRLKQQIFALSEV--VQRRPHFSYEDAvgLLGENSDLN------EKLRARLEQAEEARREAREQLRQAQAqYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 425 EMVEMLTDRNLNLEEKVRELRETVGDLEAMN-EMNDELQENARETELELREQLDMAGARVREAQK---RVEAAQETVAdy 500
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEELGvQADAEAEERARIRRDELHEELSQNRSRRSQLEKqltRCEAEMDSLQ-- 1093
|
330 340
....*....|....*....|...
gi 1039774237 501 qqtiKKYRQLTAHLQDVNRELTN 523
Cdd:COG3096 1094 ----KRLRKAERDYKQEREQVVQ 1112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-407 |
7.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRlkrsedkaklkelEKHKIqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFR-------------QKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAE--SLQQEVEALKER-------VDELTTDLEILKAEIEEKGSDGAASSY-QLKQL 350
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1039774237 351 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQRERLQEELSQAE 407
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRL----EREVEVARELYESLLQRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
207-524 |
7.91e-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: 47.04 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKA---KLKELEKHKIQLEQVQEWKSKMQEQQA---DLQRRLKEAR------------- 267
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKNSKSELAripELEKELERLRehnkhlnenienk 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 268 ---KEAKEALEAKERYMEEMADTADAIEM--------------------ATLDKEMA-EERAESLQQEVEALKERVDELT 323
Cdd:pfam05557 224 lllKEEVEDLKRKLEREEKYREEAATLELekekleqelqswvklaqdtgLNLRSPEDlSRRIEQLQQREIVLKEENSSLT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 324 TDLEILKAEIEEKGSDGAAssyQLKQLEEQNARLK--DALVRM-----------RDL----------------SSSEKQE 374
Cdd:pfam05557 304 SSARQLEKARRELEQELAQ---YLKKIEDLNKKLKrhKALVRRlqrrvllltkeRDGyrailesydkeltmsnYSPQLLE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 375 HVK-LQKLMEKKNQELEVVRQQRERLQEEL-------SQAESTIDELKEQVDAA--LGAEEMVEMLTDRNLNLEEKVREL 444
Cdd:pfam05557 381 RIEeAEDMTQKMQAHNEEMEAQLSVAEEELggykqqaQTLERELQALRQQESLAdpSYSKEEVDSLRRKLETLELERQRL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 445 RETVGDLEA---------MNEMND----ELQEN----ARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTI--- 504
Cdd:pfam05557 461 REQKNELEMelerrclqgDYDPKKtkvlHLSMNpaaeAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTstm 540
|
410 420
....*....|....*....|..
gi 1039774237 505 --KKYRQLTAHLQDvnRELTNQ 524
Cdd:pfam05557 541 nfKEVLDLRKELES--AELKNQ 560
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
202-472 |
7.95e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.16 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKA---------------KLKELEKHKI-----------QLEQVQEWKSKMQEQ 255
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKEssskpselalnemieKLKKEIDLEYteaviamglqeRLENLREEFSKANSQ 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 256 QADLQRRLKEA----RKEAKEALEAKERYmEEMADTADAIEMATLDKEMAE--ERAESLQQEV-EALKERVD--ELTTDL 326
Cdd:PLN03229 502 DQLMHPVLMEKieklKDEFNKRLSRAPNY-LSLKYKLDMLNEFSRAKALSEkkSKAEKLKAEInKKFKEVMDrpEIKEKM 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 327 EILKAEIEEKGS------DGAASSYQLKQLEEQNARLKDAL---------VRMRDLSSSEKQE----HVKLQKLMEKKNQ 387
Cdd:PLN03229 581 EALKAEVASSGAssgdelDDDLKEKVEKMKKEIELELAGVLksmglevigVTKKNKDTAEQTPppnlQEKIESLNEEINK 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 388 ELEVV------RQQRERLQEELSQAESTID------------ELKEQVDAALGAEEMVEmltdRNLNLEEKVRELRETVG 449
Cdd:PLN03229 661 KIERVirssdlKSKIELLKLEVAKASKTPDvtekekiealeqQIKQKIAEALNSSELKE----KFEELEAELAAARETAA 736
|
330 340
....*....|....*....|...
gi 1039774237 450 DLEAMNEMNDELQENARETELEL 472
Cdd:PLN03229 737 ESNGSLKNDDDKEEDSKEDGSRV 759
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
213-541 |
8.37e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 213 DLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEW---KSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadTAD 289
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltqKREAQEEQLKKQQLLKQLRARIEE-LRAQEAVLEE---TQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 AIEMATLDKEMAEEraeslQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlkdalvrmRDLSS 369
Cdd:TIGR00618 285 RINRARKAAPLAAH-----IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----------RRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 370 SEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAES-TIDELKEQVDAALGAEEMVEMLTDRNLNLEEkvRELRETV 448
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 449 GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEAS 528
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330
....*....|...
gi 1039774237 529 VERQQQPPPETFD 541
Cdd:TIGR00618 507 CGSCIHPNPARQD 519
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
202-526 |
8.44e-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: 46.57 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRlkRSEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELR--RRDQKRQETLERERRLLLQQSQEqWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEKGSDgAASSYQLKQLEEQNarlkda 360
Cdd:pfam15558 96 WREQAEDQENQRQEKLERARQEAEQRKQCQE-QRLKEKEEELQALREQNSLQLQERLEE-ACHKRQLKEREEQK------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 361 lvRMRDLSSSEKQEHVKLQKLMEKKNQElevvrqqrERLQEELSQaestidELKEQVdaalgAEEMVEMLtdrnlnLEEK 440
Cdd:pfam15558 168 --KVQENNLSELLNHQARKVLVDCQAKA--------EELLRRLSL------EQSLQR-----SQENYEQL------VEER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 441 VRELREtvgdlEAMNEmNDELQENARETELELREQLDMAGARVREAQKRVE----AAQETVADYQQTIKKYRQLTAHLQD 516
Cdd:pfam15558 221 HRELRE-----KAQKE-EEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqarqVAHKTVQDKAQRARELNLEREKNHH 294
|
330
....*....|
gi 1039774237 517 VNRELTNQQE 526
Cdd:pfam15558 295 ILKLKVEKEE 304
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
270-423 |
9.79e-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: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 270 AKEALEAKERYMEEMADTADAIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaas 343
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEELEEakktikALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK-------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 344 syQLKQLEEQNARLKDALvrMRDLSSSEKQEHVKLQKLMEKKNQEL------------------EVVRQQRERLQEELSQ 405
Cdd:cd22656 154 --DQTALETLEKALKDLL--TDEGGAIARKEIKDLQKELEKLNEEYaaklkakidelkaliaddEAKLAAALRLIADLTA 229
|
170
....*....|....*...
gi 1039774237 406 AESTIDELKEQVDAALGA 423
Cdd:cd22656 230 ADTDLDNLLALIGPAIPA 247
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
202-565 |
1.22e-04 |
|
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: 46.65 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRsedkaklkelekhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 281
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMER-----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEieekgSDGAASSYQLKQLEEQNARLKDAL 361
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 362 VRMRDlsssekqehvKLQKLMEKKNQELEVVRQQ-RERLQEELSQAESTIDELKEQVDAALGA--------EEMVEMLTD 432
Cdd:pfam15921 241 FPVED----------QLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGLTEKASSARSQansiqsqlEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 433 RNLNLEEKVRELRETVGDLEAmnemndELQENARETE---LELREQLDMAGARVREAqkRVEAAQETvadyQQTIKKYRQ 509
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRS------ELREAKRMYEdkiEELEKQLVLANSELTEA--RTERDQFS----QESGNLDDQ 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 510 LTAHLQDVNREltnQQEASVERQQQppPETFDFKIKFAETKAHAKAiEMELRQMEV 565
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 ... |
203-534 |
1.23e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDK--AKLKELEKHKiqleQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE----------IEEKGSDGAASSYQLK-- 348
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlqrsmstqkaLEEDLQIATKTICQLTee 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 349 ---QLEEQN-ARLKDALVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---------- 414
Cdd:pfam05483 333 keaQMEELNkAKAAHSFV-----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkevel 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 415 EQVDAALGAEemvEMLTDRNLNLEEKVRELR----ETVGDLEAM-NEMND-ELQENARETELE--LREQLDMAGARVREA 486
Cdd:pfam05483 408 EELKKILAED---EKLLDEKKQFEKIAEELKgkeqELIFLLQAReKEIHDlEIQLTAIKTSEEhyLKEVEDLKTELEKEK 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1039774237 487 QKRVeaaqETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:pfam05483 485 LKNI----ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
241-336 |
1.26e-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: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 241 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTA--DAIEMATLDKEMAEERAESLQQE-VEALKE 317
Cdd:COG0711 39 GLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAkaEAEAEAERIIAQAEAEIEQERAKaLAELRA 118
|
90 100
....*....|....*....|.
gi 1039774237 318 RVDELTTDL--EILKAEIEEK 336
Cdd:COG0711 119 EVADLAVAIaeKILGKELDAA 139
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
207-476 |
1.31e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKL-----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 281
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLeilkaeieekgsdgaasSYQLKQLEEQNARL 357
Cdd:pfam00038 103 NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheEEVRELQAQV-----------------SDTQVNVEMDAARK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 358 KDALVRMRDLSSS-EKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLN 436
Cdd:pfam00038 166 LDLTSALAEIRAQyEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQ-SLEIE--LQSLKKQKAS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039774237 437 LEEKVRELRET-VGDLEAMNEMNDELQENARETELELREQL 476
Cdd:pfam00038 243 LERQLAETEERyELQLADYQELISELEAELQETRQEMARQL 283
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
379-570 |
1.40e-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: 45.91 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 379 QKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEmn 458
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 459 dELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 538
Cdd:COG4942 94 -ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---- 168
|
170 180 190
....*....|....*....|....*....|..
gi 1039774237 539 tfdFKIKFAETKAHAKAIEMELRQMEVAQANR 570
Cdd:COG4942 169 ---LEAERAELEALLAELEEERAALEALKAER 197
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
213-579 |
1.47e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.98 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 213 DLEEKLETLRLKRSedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYmEEM-------- 284
Cdd:PRK04778 90 EAEELNDKFRFRKA--KHEINEIE------SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLY-RELrksllanr 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 ---ADTADAIE--MATLDKEMAEerAESLQQE---------VEALKERVDELTTDLEILKAEIEEKGSDGAAssyQLKQL 350
Cdd:PRK04778 161 fsfGPALDELEkqLENLEEEFSQ--FVELTESgdyveareiLDQLEEELAALEQIMEEIPELLKELQTELPD---QLQEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 351 EEQNARLKDA---------LVRMRDLssseKQEHVKLQKLMEkkNQELEVVRQQRERLQEELSQ--------------AE 407
Cdd:PRK04778 236 KAGYRELVEEgyhldhldiEKEIQDL----KEQIDENLALLE--ELDLDEAEEKNEEIQERIDQlydilerevkarkyVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 408 STIDELKEQVDAAlgaEEMVEML---TDR-------NLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLD 477
Cdd:PRK04778 310 KNSDTLPDFLEHA---KEQNKELkeeIDRvkqsytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 478 MAGARVREAQKRVEAAQETVADY-------QQTIKKYRQLtahLQDVNREltnqqeasVERQQQPP-PEtfDFKIKFAET 549
Cdd:PRK04778 387 EILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNK---LHEIKRY--------LEKSNLPGlPE--DYLEMFFEV 453
|
410 420 430
....*....|....*....|....*....|..
gi 1039774237 550 KAHAKAIEMEL--RQMEVAQANRHMSLLTAFM 579
Cdd:PRK04778 454 SDEIEALAEELeeKPINMEAVNRLLEEATEDV 485
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
393-553 |
1.79e-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: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 393 RQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnLNL-------EEKVRELREtvgDLEAMNEMNDElQENA 465
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrqQEKIERYQE---DLEELTERLEE-QEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 466 REtelELREQLDMAGARVREAQKRVEAAQETVADYQQTIK-------KYRQLTAHLQDVNR-----ELT-----NQQEAS 528
Cdd:COG3096 370 VE---EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARAlcglpDLTpenaeDYLAAF 446
|
170 180
....*....|....*....|....*
gi 1039774237 529 VERQQQPPPETFDFKIKFAETKAHA 553
Cdd:COG3096 447 RAKEQQATEEVLELEQKLSVADAAR 471
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
203-534 |
1.82e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERYME 282
Cdd:PRK04863 559 LQEELEARLESLSESVSEARERRMALRQQLEQLQ------ARIQRLAARAPAWLA-AQDALARLREQSGEEFEDSQDVTE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMADTADAIEMATLDKEMAEERAESLQQEVE--------------ALKER-----VDELTTDLEILKAEIEEKGSDGAAS 343
Cdd:PRK04863 632 YMQQLLERERELTVERDELAARKQALDEEIErlsqpggsedprlnALAERfggvlLSEIYDDVSLEDAPYFSALYGPARH 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 344 -------SYQLKQLEEQNARLKDALV------RMRD-LSSSEKQEHVKLQKLMEK-----------------KNQELEVV 392
Cdd:PRK04863 712 aivvpdlSDAAEQLAGLEDCPEDLYLiegdpdSFDDsVFSVEELEKAVVVKIADRqwrysrfpevplfgraaREKRIEQL 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 393 RQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQ---ENAR 466
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRsqlEQAK 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 467 ETELELREQLDMA--------GARVREAQKRVEAAQET---VADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQ 532
Cdd:PRK04863 872 EGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQ 951
|
..
gi 1039774237 533 QQ 534
Cdd:PRK04863 952 RD 953
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
201-319 |
1.91e-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: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEE-EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAker 279
Cdd:COG0542 438 SFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--- 514
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039774237 280 ymeemADTADAIEMAT---LDKeMAEERAESLQQEVEALKERV 319
Cdd:COG0542 515 -----EDIAEVVSRWTgipVGK-LLEGEREKLLNLEEELHERV 551
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
290-519 |
1.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 290 AIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqLKQLEEQNARLKDALVR 363
Cdd:COG4717 45 AMLLERLEKEADElfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEE-----------LEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 364 MRdlsssekQEHVKLQKLmekknQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnlnLEEKVRE 443
Cdd:COG4717 114 LR-------EELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 444 LRETVgdleamnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNR 519
Cdd:COG4717 179 LEELL----------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
236-533 |
2.25e-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: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 236 EKHKIQLEQVQEWkskMQEQQAdLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMATLDKE-MAEERAESLQQEveA 314
Cdd:pfam12128 214 PKSRLNRQQVEHW---IRDIQA-IAGIMKIRPEFTKLQQEFNTLESAEL-------RLSHLHFGyKSDETLIASRQE--E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 315 LKERVDELTTDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDAlvrmrDLSSSEKQEHVKLqkLMEKKNQELEVVRQ 394
Cdd:pfam12128 281 RQETSAELNQLLRTLDDQWKEK-------------RDELNGELSAA-----DAAVAKDRSELEA--LEDQHGAFLDADIE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 395 QRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--EEKVRELRETVGDLEAMNEMNDELQENARET---- 468
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqal 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 469 ELELREQLDMAGARVREAQKRVEAAQET----VADYQQTIKKYRQLTAHLQDVN--RELTNQQEASVERQQ 533
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGElklrLNQATATPELLLQLENFDERIEraREEQEAANAEVERLQ 491
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
214-329 |
2.26e-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: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 214 LEEKLETLrlkrsedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 281
Cdd:COG0216 2 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKKLLEDIEEA-------- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039774237 282 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 329
Cdd:COG0216 63 KELLEEESDPEM----REMAKE-------ELEELEARLEELEEELKIL 99
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
243-481 |
2.33e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 243 EQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERY---MEEMaDTAD--AIEMATLDKEM-----AEERAESLQQEV 312
Cdd:COG0497 155 ELLEEYREAYRAWRA-LKKELEELRADEAERARELDLLrfqLEEL-EAAAlqPGEEEELEEERrrlsnAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 313 EALKERVDELTTDLEILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMRDLSSS------------EKQEHV---- 376
Cdd:COG0497 233 EALSGGEGGALDLLGQALRALER------LAEYD-PSLAELAERLESALIELEEAASElrryldslefdpERLEEVeerl 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 377 -KLQKLMEKKNQELEVVRQQRERLQEELSQ---AESTIDELKEQVDAALGAeemvemltdrnlnLEEKVREL----RETV 448
Cdd:COG0497 306 aLLRRLARKYGVTVEELLAYAEELRAELAElenSDERLEELEAELAEAEAE-------------LLEAAEKLsaarKKAA 372
|
250 260 270
....*....|....*....|....*....|....*...
gi 1039774237 449 GDLEAmnEMNDELQ----ENAR-ETELELREQLDMAGA 481
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 ... |
230-358 |
2.51e-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: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 230 AKLKELEKHKIQLEQVQEwkskmqEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLdkemAEERAESLQ 309
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAA------DAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQA----LREELNELK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1039774237 310 QEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLK 358
Cdd:pfam07926 71 AEIAELKAEAESAKAELEESEESWEE----------QKKELEKELSELE 109
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
214-464 |
2.61e-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: 45.20 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 214 LEEKLETLRLKRSEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEarkeaKEA-LEAKERYMEEMAD--TADA 290
Cdd:pfam10174 308 LQTKLETLTNQNSDCKQHIEVL---KESLTAKEQRAAILQTEVDALRLRLEE-----KESfLNKKTKQLQDLTEekSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 291 IEMATLDK--EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA---RLKDALVRMR 365
Cdd:pfam10174 380 GEIRDLKDmlDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 366 DLSSSEKQEHVklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA-ALGAEEMVEMLTDRNLNLEEKVREL 444
Cdd:pfam10174 460 EREDRERLEEL------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKSLEIAVEQKKEEC 533
|
250 260
....*....|....*....|
gi 1039774237 445 RETVGDLEAMNEMNDELQEN 464
Cdd:pfam10174 534 SKLENQLKKAHNAEEAVRTN 553
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
377-534 |
2.90e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 377 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlNLEEKVRELRETVGDLEAMNE 456
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 457 MNDELQENAretelELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:COG4717 127 LLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
201-527 |
2.92e-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: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEE-EGLRAQVRDLEEKLETLRLKRSEDKAKLK--------ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE--ARKE 269
Cdd:pfam05701 192 TKESlESAHAAHLEAEEHRIGAALAREQDKLNWEkelkqaeeELQRLNQQLLSAKDLKSKLETASALLLDLKAElaAYME 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 270 AKEALEAKERYMEEMADTADAIEMATLDKEMAEERA--ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQL 347
Cdd:pfam05701 272 SKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKAniEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 348 KQLEEQNARLKD--ALVRMRDLSSSEKQehVKLQKLMEKKNQELE----VVRQQRERL---QEELSQA-------ESTID 411
Cdd:pfam05701 352 SSLEAELNRTKSeiALVQAKEKEAREKM--VELPKQLQQAAQEAEeaksLAQAAREELrkaKEEAEQAkaaastvESRLE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 412 ELKEQVDAALGAEEMVemLTDRNLNLEEKVRELRETVGDLEAM----NEMNDELQENARETElelreqlDMAGARVREAQ 487
Cdd:pfam05701 430 AVLKEIEAAKASEKLA--LAAIKALQESESSAESTNQEDSPRGvtlsLEEYYELSKRAHEAE-------ELANKRVAEAV 500
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1039774237 488 KRVEAAQETvadyqqtikKYRQLtAHLQDVNRELTNQQEA 527
Cdd:pfam05701 501 SQIEEAKES---------ELRSL-EKLEEVNREMEERKEA 530
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
215-355 |
2.97e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 215 EEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMADTADAIEMA 294
Cdd:PRK09510 86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA--AKAKAEAEAKRAAAAAKKA 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 295 TLDKEMAEERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAASSYQLKQLEEQNA 355
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-----KAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
207-425 |
3.07e-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: 45.21 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETL--RLKRSEDKaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALEAKERYMEEM 284
Cdd:pfam12128 313 ADAAVAKDRSELEALedQHGAFLDA----DIETAAADQEQLPSWQSELENLEERL-----KALTGKHQDVTAKYNRRRSK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 ADTADAIEMATLDKEMA---EERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLK-QLEEQNARLKDA 360
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLAkirEARDRQLAVAEDDLQALESELREQLEAGKLEFNE-------EEYRLKsRLGELKLRLNQA 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039774237 361 LVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAestiDELKEQVDAALGAEE 425
Cdd:pfam12128 457 TA-----TPELLLQLENFDERIERAREEQEAANAEVERLQSELRQA----RKRRDQASEALRQAS 512
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
306-416 |
3.41e-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: 41.86 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 306 ESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGAASSYQlKQLEEQNARLKdALVRMRDLSSSEKQEHVKLQKLME 383
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNYE-RELVLHAEDIK-ALQALREELNELKAEIAELKAEAE 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 1039774237 384 KKNQELEVVR----QQRERLQEELSQAESTIDELKEQ 416
Cdd:pfam07926 82 SAKAELEESEesweEQKKELEKELSELEKRIEDLNEQ 118
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
215-486 |
3.61e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 215 EEKLETLRLKRSEDKAKLKElEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMA 294
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEE-KIREIEIE-----VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-------RAD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 295 TLDKEMAEERAESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSY-----QLKQLEEQNARLKDALVRMRDL-- 367
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRYKSL--KLEDLDSKRTSWLNALAVISLidietNRSRSNEIKKQLNDLESRLQEIei 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 368 ---------SSSEKQEHVKLQKLMEKKNqELEVVRQQRERLQEelsqaesTIDELKEQVDAALGAEEMVEMLTDRNLNLE 438
Cdd:PRK01156 609 gfpddksyiDKSIREIENEANNLNNKYN-EIQENKILIEKLRG-------KIDNYKKQIAEIDSIIPDLKEITSRINDIE 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 439 EKVRELRETVGDLEA---------------MNEMNDELQEnaRETELELREQLDMAGA---RVREA 486
Cdd:PRK01156 681 DNLKKSRKALDDAKAnrarlestieilrtrINELSDRIND--INETLESMKKIKKAIGdlkRLREA 744
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
98-302 |
3.78e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 98 EDGADTTSPETPDSSASKVLKREGADAAAKTSKLTTTRRPKPTRPASTGVAGpssslgpsgsasagELSSSEP--STPAQ 175
Cdd:NF033875 49 QPGTTTVQPDNPDPQSGSETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGA--------------EQSSATPndTTNAQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 176 TPLAA--------PIIPTPALTSPGAAPPLPSPSKEEEGlraQVRDLEEKLETLRLKRSEDKAK----LKELEKHKIQLE 243
Cdd:NF033875 115 QPTVGaeksaqeqPVVSPETTNEPLGQPTEVAPAENEAN---KSTSIPKEFETPDVDKAVDEAKkdpnITVVEKPAEDLG 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039774237 244 QVQEWKSKMQEQQADlQRRLKEARKEAKEALEAK---ERYMEEMADTA--DAIEMATLDKEMAE 302
Cdd:NF033875 192 NVSSKDLAAKEKEVD-QLQKEQAKKIAQQAAELKaknEKIAKENAEIAakNKAEKERYEKEVAE 254
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
328-523 |
3.81e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 328 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAE 407
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 408 STIDE--------------LKEQVDAALG--------------------AEEMVEMLTDRNLNLEEKVRELRETVGDLEA 453
Cdd:PHA02562 248 MDIEDpsaalnklntaaakIKSKIEQFQKvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039774237 454 -MNEMND---ELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNRELTN 523
Cdd:PHA02562 328 iMDEFNEqskKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSE 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
389-564 |
3.98e-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: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 389 LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----EEKVRELRETVGDLEAMNEMNDELQE 463
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 464 NARETELELrEQLDmagARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP------- 536
Cdd:TIGR02168 261 ELQELEEKL-EELR---LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldela 336
|
170 180 190
....*....|....*....|....*....|....*
gi 1039774237 537 -------PETFDFKIKFAETKAHAKAIEMELRQME 564
Cdd:TIGR02168 337 eelaeleEKLEELKEELESLEAELEELEAELEELE 371
|
|
| CASP_C |
pfam08172 |
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ... |
301-442 |
4.40e-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: 43.43 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 301 AEERAESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGA-ASSYQLKQLEEQNARLKDALVrmrdLSSSEKQEHVK 377
Cdd:pfam08172 2 LQEELSSLNAELEEQQELNAKLENDLLKVQDEASNafSFNDASsAGSGVSRYPPSGGRRSPTSSI----ISGFEPSESSS 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 378 LQKlmekkNQELEVVRQQRER-------LQEELSQAESTIDELKEQVDAalgaeemveMLTDrNLNLEEKVR 442
Cdd:pfam08172 78 SSD-----SSILPIVTSQRDRfrqrnaeLEEELRKQFETISSLRQEIAS---------LQKD-NLKLYEKTR 134
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
203-481 |
4.98e-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: 44.56 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETlRLKRSEDkaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlKEARKEAKEALEAKERYME 282
Cdd:COG3096 974 DAVGLLGENSDLNEKLRA-RLEQAEE-----ARREAREQLRQAQAQYSQYNQVLASL----KSSRDAKQQTLQELEQELE 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMADTADAIematldkemAEERAES----LQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLKQLEEQNARLK 358
Cdd:COG3096 1044 ELGVQADAE---------AEERARIrrdeLHEELSQNRSRRSQLEKQLTRCEAEMDS-------LQKRLRKAERDYKQER 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 359 DALVrmrdlssSEKQEHVKLQKLMEKKNQELEVVRQqrerlqeELSQAEStiDELKEQVDAALGAEEMV----EMLTDrN 434
Cdd:COG3096 1108 EQVV-------QAKAGWCAVLRLARDNDVERRLHRR-------ELAYLSA--DELRSMSDKALGALRLAvadnEHLRD-A 1170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 435 LNLEE-------KV-------RELRE--------TVGDLEAMNEMNDELqenARET-ELELREQlDMAGA 481
Cdd:COG3096 1171 LRLSEdprrperKVqfyiavyQHLRErirqdiirTDDPVEAIEQMEIEL---ARLTeELTSREQ-KLAIS 1236
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
201-306 |
5.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEalEAKERY 280
Cdd:PRK12704 85 QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ---KQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEIL 159
|
90 100
....*....|....*....|....*.
gi 1039774237 281 MEEMADTADAiEMATLDKEMaEERAE 306
Cdd:PRK12704 160 LEKVEEEARH-EAAVLIKEI-EEEAK 183
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
198-534 |
5.53e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 198 PSPSKEeegLRAQVRDLEEKLETLRLKRSEDkaklkELEKHKIQL-EQVQEWKSKMQEQQ------ADLQRRLKEARKEA 270
Cdd:PRK10929 78 PKLSAE---LRQQLNNERDEPRSVPPNMSTD-----ALEQEILQVsSQLLEKSRQAQQEQdrareiSDSLSQLPQQQTEA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 271 KEALEAKERYMEEMADTADAIEMATLdkemaeeraESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSYQlKQL 350
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQAQL---------TALQAESAALKALVDEL--ELAQLSANNRQELARLRSELAK-KRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 351 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-----EVVRQQRErLQEELSQAESTIDELKEQVDAAlgaee 425
Cdd:PRK10929 218 QQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLpksivAQFKINRE-LSQALNQQAQRMDLIASQQRQA----- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 426 mvemlTDRNLNLEEKVRELRETVGDLEAMNEMNDELQEN-ARETELELREQLD--MAGARVreaqKRVEaaqetvadYQQ 502
Cdd:PRK10929 292 -----ASQTLQVRQALNTLREQSQWLGVSNALGEALRAQvARLPEMPKPQQLDteMAQLRV----QRLR--------YED 354
|
330 340 350
....*....|....*....|....*....|..
gi 1039774237 503 TIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:PRK10929 355 LLNKQPQLRQIRQADGQPLTAEQNRILDAQLR 386
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
201-319 |
6.70e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKlkelekhkiqlEQVQEWKSKMQEQQADLQrrlkeaRKEAKEALEAKERY 280
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKAR-----------AKAAKAQEKVNEALSGID------SDDATSALERMEEK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039774237 281 MEEMADTADAIEM----ATLDKEMAE-ERAESLQQEVEALKERV 319
Cdd:COG1842 174 IEEMEARAEAAAElaagDSLDDELAElEADSEVEDELAALKAKM 217
|
|
| PCRF |
pfam03462 |
PCRF domain; This domain is found in peptide chain release factors. |
229-322 |
7.09e-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: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 229 KAKLKELEKhkiQLEQVQEWKSkmqeqQADLQRRLKEaRKEAKEALEAKERYMEEMADTADAIEMATLD--KEMAEERAE 306
Cdd:pfam03462 2 EERYEELEA---LLSDPDVWDD-----QKRAQKLSKE-YSELEPIVEAYREYKQALEDLEEAKELLEDPelAELAEEELE 72
|
90
....*....|....*.
gi 1039774237 307 SLQQEVEALKERVDEL 322
Cdd:pfam03462 73 ELEKRLEELEEELKLL 88
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
244-563 |
7.38e-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: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 244 QVQEWKSKMQEQQADLQRRLKEARKEAKEaleaKERYMEEMADTAD--AIEMATLDKEMAE--ERAESLQQEVEALKERV 319
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKK----KEKRRDEMLGLAPgrQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 320 DELTTDLEILKAEiEEKGSDGAASSYQLKQLEEQnarLKDALVRMRDL-----SSSEKQEHVKLQKLMEKKNQELEVVRQ 394
Cdd:TIGR00606 768 EEQETLLGTIMPE-EESAKVCLTDVTIMERFQME---LKDVERKIAQQaaklqGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 395 QRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVgdleamNEMNDELQEnARETELELRE 474
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV------QSLIREIKD-AKEQDSPLET 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 475 QLDMAGARVREAQKRVEAAQETVADYQQTIK-KYRQLTAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAHA 553
Cdd:TIGR00606 917 FLEKDQQEKEELISSKETSNKKAQDKVNDIKeKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKHQ 993
|
330
....*....|
gi 1039774237 554 KAIEMELRQM 563
Cdd:TIGR00606 994 EKINEDMRLM 1003
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
81-214 |
7.75e-04 |
|
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: 43.75 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 81 CDEGHGIFVRQSQIQVFEDGADTtSPETpdssasKVLKREGADAAAKTSKLTTTRRPKPTRPA----STGVAGPSSSLGP 156
Cdd:pfam05109 376 CENISGAFASNRTFDITVSGLGT-APKT------LIITRTATNATTTTHKVIFSKAPESTTTSptlnTTGFAAPNTTTGL 448
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 157 SGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDL 214
Cdd:pfam05109 449 PSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPRDNGTESKAPDM 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
893-1034 |
8.36e-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: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 893 AMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKgeeLSEANVRLSLLEKKLDSAAK 972
Cdd:TIGR02169 654 AMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 973 DAD---ERIEKVQTRLDETQ---TLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEG 1034
Cdd:TIGR02169 731 EEEklkERLEELEEDLSSLEqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
232-470 |
9.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 232 LKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAieMATLDKEMAEERAESLQQE 311
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL--LREAEELEEELQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 312 VEALKERVDelTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKlmEKKNQELEV 391
Cdd:COG4717 372 IAALLAEAG--VEDEEELRAALE-----------QAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 392 VRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNlNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 470
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
200-409 |
9.52e-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: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 200 PSKEEEGLRAQVRDLEEKLETLR--LKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAK 277
Cdd:pfam15709 320 PSKALLEKREQEKASRDRLRAERaeMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 278 ERYMEEMAdtadaiEMATLDKEMAEERAESLQQEVEalkervdelTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARL 357
Cdd:pfam15709 400 RQRQEEEE------RKQRLQLQAAQERARQQQEEFR---------RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 358 KDALVRMRDLSSSEKQEhvKLQKLMEKKNQELEvVRQQRERLQEELSQAEST 409
Cdd:pfam15709 465 QKRLMEMAEEERLEYQR--QKQEAEEKARLEAE-ERRQKEEEAARLALEEAM 513
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
214-489 |
1.02e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 214 LEEKLETLRLKRSEDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadta 288
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEEreralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 289 daieMATLDKEMAEERAESLQQ--EVEALKERVDELTTDLEILKAE--IEEKGSDGAASSYQLKQLEEQNARLKdalvRM 364
Cdd:pfam13868 104 ----DEIVERIQEEDQAEAEEKleKQRQLREEIDEFNEEQAEWKELekEEEREEDERILEYLKEKAEREEEREA----ER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 365 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEstiDELKEQVDAALGAEEMVEMLTDRNLNLEEKVREL 444
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK---ERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039774237 445 RETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKR 489
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
211-448 |
1.07e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 211 VRDLEEKLETLRLKRSEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArKEAKEALEAKerymeeMAD 286
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQaleeELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAK------FSE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 TADAIEMATLDKEMAEERA--ESLQQEVEALKE----RVDELTTDLEILKAEI---EEKGSD----GAASSYQLKQLEEQ 353
Cdd:pfam15905 148 DGTQKKMSSLSMELMKLRNklEAKMKEVMAKQEgmegKLQVTQKNLEHSKGKVaqlEEKLVStekeKIEEKSETEKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 354 NARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTD 432
Cdd:pfam15905 228 ITELSCV----SEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQELSKQIKDLNEKCKLLESEkEELLREYEE 300
|
250
....*....|....*.
gi 1039774237 433 RNLNLEEKVRELRETV 448
Cdd:pfam15905 301 KEQTLNAELEELKEKL 316
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
912-1030 |
1.09e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 912 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSaakdADERIEKVQTRLDETQTL 991
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANE 296
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039774237 992 LRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1030
Cdd:TIGR02168 297 ISRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEE 338
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
212-577 |
1.16e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 212 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArkeAKEALEAKERYMEEMADTADAi 291
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---LTETLKKEVKSLQNEKADLDR- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 292 EMATLDKEMAE-ERAESLQQEVEALKErvDELTTDLEILKaeIEEKGSDGAASSY----QLKQLEEQNARLKDALVRMRD 366
Cdd:TIGR00606 516 KLRKLDQEMEQlNHHTTTRTQMEMLTK--DKMDKDEQIRK--IKSRHSDELTSLLgyfpNKKQLEDWLHSKSKEINQTRD 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 367 LSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA------ESTIDELKEQVD------AALGA-----EEMVEM 429
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEksskqrAMLAGatavySQFITQ 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 430 LTDRNLNLEEKVRELRETVGDLeamNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 509
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 510 LTAHLQDVNRELtnQQEASVERQQQPPPETFDFKIKFAETKAHAKAIeMELRQMEVAQANRHMSLLTA 577
Cdd:TIGR00606 749 LRNKLQKVNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAA 813
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
214-329 |
1.22e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 42.76 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 214 LEEKLETLrlkrsedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 281
Cdd:PRK00591 4 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKQAQEDLEEA-------- 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1039774237 282 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 329
Cdd:PRK00591 65 KEMLEEESDPEM----REMAKE-------ELKELEERLEELEEELKIL 101
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
229-498 |
1.33e-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: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 229 KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEER---- 304
Cdd:pfam05701 134 AAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHriga 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 305 AESLQQEVEALKERVDELTTDLEILKAEI----EEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 380
Cdd:pfam05701 214 ALAREQDKLNWEKELKQAEEELQRLNQQLlsakDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 381 LMEKKNQELEVVRQQRER--------------LQEELSQAESTIDELKEQVDAALGAEemvemltdrnLNLEEkvrELRE 446
Cdd:pfam05701 294 ALASAKKELEEVKANIEKakdevnclrvaaasLRSELEKEKAELASLRQREGMASIAV----------SSLEA---ELNR 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 447 TVGDLEAMNEMNDElqenARETELELREQLDMAGARVREAQKRVEAAQETVA 498
Cdd:pfam05701 361 TKSEIALVQAKEKE----AREKMVELPKQLQQAAQEAEEAKSLAQAAREELR 408
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
201-516 |
1.38e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 280
Cdd:PRK01156 203 KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADA-----IEMATLDKEMAEERA--ESLQQEVEALKERVDELtTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 353
Cdd:PRK01156 283 MKIINDPVYKnrnyiNDYFKYKNDIENKKQilSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 354 NARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-------EVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 426
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 427 V----EMLTDRNL------NL-EEKVRELRETVG-DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 494
Cdd:PRK01156 442 LsrnmEMLNGQSVcpvcgtTLgEEKSNHIINHYNeKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521
|
330 340
....*....|....*....|..
gi 1039774237 495 ETVADYQQTIKKYRQLTAHLQD 516
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKD 543
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
201-365 |
1.46e-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: 42.25 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLR----LKRSEdKAKLKELEKHkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE- 275
Cdd:pfam10498 183 SKPREIIESNVDAAEWKLELERvlpqLKVTI-KADAKDWRAH---LEQMKQHKKSIEESLPDTKSQLDKLHTDISKTLEk 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 276 --AKERY----MEEMADtadaiEMATLDKEMAEERaESLQQEVEALKERVDEL---TTDLEILKAEIEEKG---SDGAas 343
Cdd:pfam10498 259 ieSREKYinsqLEPLIQ-----EYREAQDELSEVQ-EKYKQLSEGVTERTRELaeiTEELEKVKQEMEERGssmTDGS-- 330
|
170 180
....*....|....*....|..
gi 1039774237 344 syqlkqleeQNARLKDALVRMR 365
Cdd:pfam10498 331 ---------PLVKIKQALTKLK 343
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
258-332 |
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 1039774237 258 DLQRRLKEARK-----EAKEALEAKERYMEEMADTADAIEMATLD-------------------KEMAEERAESLQQEVE 313
Cdd:cd23165 1 DQQKINKFSRLnarlhELKEELKAKKKELENLEDASDELELADDDepvpykigevfvhlsleeaQERLEKAKEELEEEIE 80
|
90
....*....|....*....
gi 1039774237 314 ALKERVDELTTDLEILKAE 332
Cdd:cd23165 81 KLEEEIDEIEEEMKELKVQ 99
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
931-1030 |
1.63e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.93 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 931 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERI-EKVQTRLDETQtLLRKKEKDFEETMDALQAD 1009
Cdd:smart00787 162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIM-IKVKKLEELEEELQELESK 240
|
90 100
....*....|....*....|.
gi 1039774237 1010 IDQLEAEKAELKQRLNSQSKR 1030
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKK 261
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
218-517 |
1.66e-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: 42.73 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 218 LETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKealeAKERYMEEMADTADAIEmATLD 297
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK----SYENELDPLKNRLKEIE-HNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 298 KEMaeeraeSLQQEVEALKERVDELTTDLEILKAEIEE--KGSDgaassYQLKQLEEQNARLkdalvrmrdlSSSEKQEH 375
Cdd:TIGR00606 263 KIM------KLDNEIKALKSRKKQMEKDNSELELKMEKvfQGTD-----EQLNDLYHNHQRT----------VREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 376 VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA--ALGAEEMVEMLTD---RNLNLEEKVRELRETV-- 448
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDgfeRGPFSERQIKNFHTLVie 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 449 ---GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDV 517
Cdd:TIGR00606 402 rqeDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
898-1024 |
1.67e-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: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 898 EYDAERPPSKPPPVELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 977
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1039774237 978 IEKVQ--TRLDETQTLLRKKEKDFEETMDALQADIDQL-EAEKAELKQRL 1024
Cdd:COG2433 461 IRKDReiSRLDREIERLERELEEERERIEELKRKLERLkELWKLEHSGEL 510
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
202-495 |
1.72e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETlrlKRSEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQadlQRRLKEARKEAKEaleakerY 280
Cdd:pfam02029 23 KEEEEPSGQVTESVEPNEH---NSYEEDSELKPSGQGGLDEEEaFLDRTAKREERR---QKRLQEALERQKE-------F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIemATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDGAASSYQlkQLEEQNARLKD 359
Cdd:pfam02029 90 DPTIADEKESV--AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnKWSTEVRQAEE--EGEEEEDKSEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 360 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMV---EMLTDRNLN 436
Cdd:pfam02029 166 AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 437 LEEKVRELRETVGDLEamNEMNDELQENARETELELREQLdmagaRVREAQKRVEAAQE 495
Cdd:pfam02029 246 AEQKLEELRRRRQEKE--SEEFEKLRQKQQEAELELEELK-----KKREERRKLLEEEE 297
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
204-478 |
1.75e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 204 EEGLrAQVRDLEEKLETLRLkrSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKErymE 282
Cdd:PRK05771 27 ELGV-VHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIE---K 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 283 EMadtadaiematldKEMAEERAEsLQQEVEALKERVDELT--TDLEI-LKAEIEEKGSDGAASSYQLKQLEEQNARLKD 359
Cdd:PRK05771 101 EI-------------KELEEEISE-LENEIKELEQEIERLEpwGNFDLdLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 360 ALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAEsTIDELKEQvdaalgaeemvemltdrnl 435
Cdd:PRK05771 167 ENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEE------------------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1039774237 436 nLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDM 478
Cdd:PRK05771 224 -LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEA 265
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
202-488 |
1.83e-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: 42.32 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEdkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 281
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREE------ELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMAtldkEMAEERAESLQQEVEALKERVDELTT-----------DLEILKAEIEEKGSDgaaSSYQLKQL 350
Cdd:pfam05667 384 KQYKVKKKTLDLL----PDAEENIAKLQALVDASAQRLVELAGqwekhrvplieEYRALKEAKSNKEDE---SQRKLEEI 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 351 EEQNARLKD--ALVRMRDlsssekQEHVKLQKLMEKKNQE----------LEVV---RQQRERLQEELSQaestIDELKE 415
Cdd:pfam05667 457 KELREKIKEvaEEAKQKE------ELYKQLVAEYERLPKDvsrsaytrriLEIVkniKKQKEEITKILSD----TKSLQK 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039774237 416 QVDAALGAEEMVEMLTDRNLNLEEKVRE-LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQK 488
Cdd:pfam05667 527 EINSLTGKLDRTFTVTDELVFKDAKKDEsVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-401 |
1.88e-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: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVqewKSKMQEQQADLQRRLKEARkeaKEALEAKERY 280
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 281 MEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERVDELTtdlEILKAEIEEkgsdgaassyqlkqLEEQNARLKDA 360
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKIKELG---PVNLAAIEE--------------YEELKERYDFL 1005
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1039774237 361 LVRMRDLSSSEKQehvkLQKLMEKKNQELevvrqqRERLQE 401
Cdd:TIGR02168 1006 TAQKEDLTEAKET----LEEAIEEIDREA------RERFKD 1036
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
912-1047 |
1.90e-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: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 912 ELRAAALRAEITDAEGLGLKLEDRETVIKELKkslkikgEELSEANVRLSLLEKKLDsaakDADERIEKVQTRLDETQTL 991
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLE-------AELEELRAELARLEAELE----RLEARLDALREELDELEAQ 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 992 LRKKEKDfeeTMDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRGPPPSGIATLV 1047
Cdd:COG4913 332 IRGNGGD---RLEQLEREIERLERELEERERRRARLEAL-LAALGLPLPASAEEFA 383
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
378-568 |
1.95e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 378 LQKLMEKKNQELEVVRQQRERLQEELSQaesTIDELKEQVDAALgaeemvemltdrnLNLEEKVRELREtvgdleamnem 457
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEE---KKEKLQEEEDKLL-------------EEAEKEAQQAIK----------- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 458 ndELQENARETELELREQLDMAGARVR-----EAQKRVEAAQETVADYQQTIK------------KYRQL--TAHLQDV- 517
Cdd:PRK00409 581 --EAKKEADEIIKELRQLQKGGYASVKaheliEARKRLNKANEKKEKKKKKQKekqeelkvgdevKYLSLgqKGEVLSIp 658
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 518 -NRELTNQ--------QEASVERQQQPPPETFDfKIKFAETKAHAKAIEMELRQMEVAQA 568
Cdd:PRK00409 659 dDKEAIVQagimkmkvPLSDLEKIQKPKKKKKK-KPKTVKPKPRTVSLELDLRGMRYEEA 717
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
207-290 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQ----------RRLKEARK 268
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLeeklkdreEELREKRKLNQDLQDELValqlqlnmaeEKLRKLEK 155
|
90 100
....*....|....*....|..
gi 1039774237 269 EAKEALEakeRYMEEMADTADA 290
Cdd:pfam08614 156 ENRELVE---RWMKRKGQEAEA 174
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
204-561 |
2.12e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 204 EEGLRAQVRDLEEKLETLrlkrSEDKAKLKELEKHKIQLEqvQEWKSKMQEQQadlqrRLKEARKEAKEALEAKERYMEE 283
Cdd:PRK01156 189 EEKLKSSNLELENIKKQI----ADDEKSHSITLKEIERLS--IEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 284 MADTADAIEMATLD----KEMAEERAESLQQEVEALKERVDE---LTTDLEILKAEIEekGSDGAASSYQ--LKQLEEQN 354
Cdd:PRK01156 258 IKTAESDLSMELEKnnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILS--NIDAEINKYHaiIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 355 ARLKDALV---RMRDLS---SSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTidelkeqvdAALGAEE 425
Cdd:PRK01156 336 KDYNDYIKkksRYDDLNnqiLELEGYEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKI---------QEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 426 MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENAR-----------ETELELREQLDMAGARVREAQKRVEAAQ 494
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 495 ETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETK-AHAKAIEMELR 561
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdKHDKYEEIKNR 554
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-534 |
2.13e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLR--LKRSEDkAKLK---ELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARK 268
Cdd:pfam01576 685 RSKRALEQQVEEMKTQLEELEdeLQATED-AKLRlevNMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 269 EAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTT---DLEILKAEIEEKGSDGAASSY 345
Cdd:pfam01576 764 QRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAsrdEILAQSKESEKKLKNLEAELL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 346 QLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV-VRQQRERLQEELSQAESTIDELK------EQVD 418
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRkstlqvEQLT 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 419 AALGAEE-MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL-ELREQLD-------MAGARVREAQKR 489
Cdd:pfam01576 924 TELAAERsTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIaQLEEQLEqesrerqAANKLVRRTEKK 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1039774237 490 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 534
Cdd:pfam01576 1004 LKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR 1048
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
202-474 |
2.15e-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: 42.42 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLE----EKLETLRLKRSEDKAKLK-ELE---KHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 273
Cdd:pfam17380 360 RELERIRQEEIAMEisrmRELERLQMERQQKNERVRqELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 274 LEakerymeemadtadaiematldkemaEERAeslqQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyQLKQLEEQ 353
Cdd:pfam17380 440 LE--------------------------EERA----REMERVRLEEQERQQQVERLRQQEEER---------KRKKLELE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 354 NARlkdalvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDR 433
Cdd:pfam17380 481 KEK--------RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039774237 434 nlNLEEKVRELRETVGDLEAMnEMNDELQENARETELELRE 474
Cdd:pfam17380 553 --RIQEQMRKATEERSRLEAM-EREREMMRQIVESEKARAE 590
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
911-1030 |
2.19e-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: 42.36 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 911 VELRAAALRAEITD----AEGLGLKLEDRETVIKELKKSLKIKGEE--------LSEANVRLSLLEKKLDSAA---KDAD 975
Cdd:TIGR02169 242 IERQLASLEEELEKlteeISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekIGELEAEIASLERSIAEKErelEDAE 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 976 ERIEKVQTRLDETQTLLRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1030
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
951-1036 |
2.20e-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: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 951 EELSEANVRLSLLEKKLDSAAKDADE---RIEKVQTRLDETQTLLRKKEKDfeetMDALQADIDQLEAEKAELKQRLNSQ 1027
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQE----LAALEAELAELEKEIAELRAELEAQ 102
|
....*....
gi 1039774237 1028 SKRTIEGLR 1036
Cdd:COG4942 103 KEELAELLR 111
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
202-316 |
2.24e-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: 41.41 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLetLRLKRSEDKAKLKELEKHkiQLEQVQEWKSKMQEqqadlqrRLKEARKEAKEALEAKERym 281
Cdd:cd16269 200 IEAERAKAEAAEQERKL--LEEQQRELEQKLEDQERS--YEEHLRQLKEKMEE-------ERENLLKEQERALESKLK-- 266
|
90 100 110
....*....|....*....|....*....|....*
gi 1039774237 282 eemadtadaiEMATLDKEMAEERAESLQQEVEALK 316
Cdd:cd16269 267 ----------EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
207-517 |
2.24e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 207 LRAQVRDLEEK---LETLRLKR----SEDKAKLKELEKHKIQLEQvqeWKSKMQEQQADLQRRLKEARKEAKEALEAKER 279
Cdd:pfam01576 164 FTSNLAEEEEKaksLSKLKNKHeamiSDLEERLKKEEKGRQELEK---AKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD--------------ELTTDLEILKAEIEEKGSDGAASSY 345
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrDLGEELEALKTELEDTLDTTAAQQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 346 QLKQLEEQNARLKDALvrmrdlsSSEKQEH-VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGAE 424
Cdd:pfam01576 321 LRSKREQEVTELKKAL-------EEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN-AELQAE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 425 emVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAdyqqti 504
Cdd:pfam01576 393 --LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------ 464
|
330
....*....|...
gi 1039774237 505 kkyrQLTAHLQDV 517
Cdd:pfam01576 465 ----SLESQLQDT 473
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
184-337 |
2.32e-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: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 184 PTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRlkrsedkAKLKELEkhkiqleqvqewkskmqEQQADLQRRL 263
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKD-----------------ERIERLEREL 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 264 KEARKEAKEALEaKERYMEEMadtadaiematldkemaEERAESLQQEVEALKERVDELTTDLEILKA--EIEEKG 337
Cdd:COG2433 451 SEARSEERREIR-KDREISRL-----------------DREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
172-318 |
2.50e-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: 40.30 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 172 TPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQvrdLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSK 251
Cdd:pfam08614 23 NAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQ---LREELAELYRSRGELAQRLVDLN------EELQELEKK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039774237 252 MQEQQ---ADLQRR---LKEARKEAKEALEAKERYMEEMADtadaiEMATLDKE--MAEERAESLQQEVEALKER 318
Cdd:pfam08614 94 LREDErrlAALEAEraqLEEKLKDREEELREKRKLNQDLQD-----ELVALQLQlnMAEEKLRKLEKENRELVER 163
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
261-533 |
2.59e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 41.56 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 261 RRLKEARKEAKEALEAKERYMEE--MADTADA-IEMATLDKEM--AEERAESLQQEVEALKERVDE-LTTDLEILKAEIE 334
Cdd:COG1538 50 RARIEAAKAQAEAAEADLRAARLdlAAEVAQAyFDLLAAQEQLalAEENLALAEELLELARARYEAgLASRLDVLQAEAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 335 EkgsdgAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 414
Cdd:COG1538 130 L-----AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 415 EQVDAA-------------LGAEEMVEMLTDRN------LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ 475
Cdd:COG1538 205 AEIGVAraaflpslslsasYGYSSSDDLFSGGSdtwsvgLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 476 LDMAGARVREAQKRVEAAQETVAD----YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 533
Cdd:COG1538 285 VEDALAALRAAREQLEALEEALEAaeeaLELARARYRAGLASLLDVLDAQRELLQAQLNLIQ 346
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
224-353 |
2.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 224 KRSEDKAKLKELE------KHKIQLEQ-VQEWKSKMQEQQADLQRRlKEARKEAKEALEAKERYMEEMADTADAiEMATL 296
Cdd:PRK12704 49 KEAEAIKKEALLEakeeihKLRNEFEKeLRERRNELQKLEKRLLQK-EENLDRKLELLEKREEELEKKEKELEQ-KQQEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1039774237 297 DKEmaEERAESLQQEVEALKERVDELTTD--LEILKAEIEEKGSDGAASsyQLKQLEEQ 353
Cdd:PRK12704 127 EKK--EEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAV--LIKEIEEE 181
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
384-534 |
2.79e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 384 KKNQELevVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEKVRELRETVGDLEAMNEMNDELQE 463
Cdd:COG1566 68 KKGQVL--ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIA----AAEAQLAAAQAQLDLAQRELERYQALYK 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039774237 464 NaretELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVnreltNQQEASVERQQQ 534
Cdd:COG1566 142 K----GAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQV-----AQAEAALAQAEL 203
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
275-502 |
3.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 275 EAKERYMEEMADTADAIE-MATLDKEMAEER--AESLQQEVEALKERVDELTTDLEilkaEIEEKGSDGAASSYQ--LKQ 349
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIAsLEELERELEQKAeeAEALLKEAEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQqaIKE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 350 LEEQNARLKDALVRMRDlsssEKQEHVKLQKLMEKKNQelevVRQQRERLQEELSQAESTIDELKEqvdaalGAE----- 424
Cdd:PRK00409 582 AKKEADEIIKELRQLQK----GGYASVKAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKV------GDEvkyls 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 425 -----EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRVEAA--Q 494
Cdd:PRK00409 648 lgqkgEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvslELDLRGMRYEEALERLDKYldD 727
|
....*...
gi 1039774237 495 ETVADYQQ 502
Cdd:PRK00409 728 ALLAGYGE 735
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
254-499 |
3.19e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 42.00 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 254 EQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE 332
Cdd:COG5644 331 EPRTESERKMHQALLDAGLENESALKKQEELALNKLSVeEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 333 IEEKGSDGAASSyqlkQLEEQNARLKDALVRMrdlssseKQEHVKLQKLMEKknqelevvrqqrerLQEELSQAESTIDE 412
Cdd:COG5644 411 KEKEMALIPKSE----DLENEKSEEARALERM-------TQRHKNTSSWTRK--------------MLERASHGEGTREA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 413 LKEQVDAalgAEEMVEMLTDRNLNLEEKVRElrETVGDLEamNEMNDELQENARETELELREQLDMAGARVREAQKRvEA 492
Cdd:COG5644 466 VNEQIRK---GDELMQRIHGKEIMDGEDVSE--FSDSDYD--TNEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQM-AA 537
|
....*..
gi 1039774237 493 AQETVAD 499
Cdd:COG5644 538 SKISVAD 544
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
209-415 |
3.70e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 209 AQVRDLEEKLETLRLKRSEDKaklKELEKHKIQLEQVQEWKSKMQEQQADLQRrlKEARKEAKEALEAKERYMEEMADTA 288
Cdd:COG5022 817 ACIIKLQKTIKREKKLRETEE---VEFSLKAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 289 DAIEMA-----TLDKEMAE---ERAESLQQEVEALKERVDELTTDLEilKAEIEEKGSDGAASSYQLKQLEEQNARLKDA 360
Cdd:COG5022 892 KSISSLklvnlELESEIIElkkSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHEVESKLKET 969
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039774237 361 LVRMRDLSSSEKQEHVKLQK---LMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 415
Cdd:COG5022 970 SEEYEDLLKKSTILVREGNKansELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
203-499 |
3.78e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.39 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLEtLRLKRSEDKAKLKELEKHKIQL------EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 276
Cdd:pfam02029 60 EEEAFLDRTAKREERRQ-KRLQEALERQKEFDPTIADEKEsvaerkENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 277 KER---YMEEMADTADAIEMATLDKEMAEERAESL----QQEVEALKERVDELTTDLEILKAE---IEEKGSDGAASSYQ 346
Cdd:pfam02029 139 EYQenkWSTEVRQAEEEGEEEEDKSEEAEEVPTENfakeEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 347 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmEKKNQELEvvRQQRERLQEELSQAESTIDELKeqvdaalgaeem 426
Cdd:pfam02029 219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEEL-RRRRQEKE--SEEFEKLRQKQQEAELELEELK------------ 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039774237 427 vemltdrnlnleeKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 499
Cdd:pfam02029 284 -------------KKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSSE 343
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
300-485 |
3.91e-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: 39.55 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 300 MAEERAESLQQEVEALKERVDElttDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDALVRMRDLSSSEkqehvkLQ 379
Cdd:pfam01442 23 VAQELVDRLEKETEALRERLQK---DLEEVRAKLEPY-------------LEELQAKLGQNVEELRQRLEPY------TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 380 KLMEKKNQELEVVRQQRERLQEEL-SQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELRETVGdleamnEMN 458
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELrERLEQNVDALRARLAPY--AEELRQ-------KLAERLEELKESLA------PYA 145
|
170 180
....*....|....*....|....*..
gi 1039774237 459 DELQENARETELELREQLDMAGARVRE 485
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
244-467 |
4.16e-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: 41.17 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 244 QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL- 322
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 323 -----------TTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV 391
Cdd:pfam05701 112 qgiadeasvaaKAQLEVAKARHAAAVAELKSVKEELESLRKE----YASLVSERDIAIKRAEEAVSASKEIEKTVEELTI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 392 vrqQRERLQEELSQAESTIDELKEQ-VDAALGAEEmvEMLT-DRNLN-LEEKVRELRETV---GDLEAMNEMNDELQENA 465
Cdd:pfam05701 188 ---ELIATKESLESAHAAHLEAEEHrIGAALAREQ--DKLNwEKELKqAEEELQRLNQQLlsaKDLKSKLETASALLLDL 262
|
..
gi 1039774237 466 RE 467
Cdd:pfam05701 263 KA 264
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
911-1024 |
4.53e-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: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 911 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLE----------KKLDSAAKDADERIEK 980
Cdd:TIGR02169 376 VDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieakiNELEEEKEDKALEIKK 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039774237 981 VQTRLDETQTLLRKKEKDFEetmdALQADIDQLEAEKAELKQRL 1024
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELY----DLKEEYDRVEKELSKLQREL 492
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
203-357 |
4.62e-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: 40.51 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 203 EEEGLRAQVRDLEEKLETLR--LKRSEDKAkLKELEKHKIQL----EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 276
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRteLQELEAQQ-QEEAESSREQLqeleEQLATERSARREAEAELERLQEELRYLEEELRRS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 277 KERYMEEMADTADAIEMATlDKEMAEERAESLQQEVEAlkeRVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 356
Cdd:pfam09787 134 KATLQSRIKDREAEIEKLR-NQLTSKSQSSSSQSELEN---RLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKE 209
|
.
gi 1039774237 357 L 357
Cdd:pfam09787 210 L 210
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
216-446 |
4.77e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 216 EKLETLRLKRSEDK--AKLKELE-------KHKIQLEQVQEWKSKMQEQQADLqRRLKEARKEAKEALEAKERYmeEMAD 286
Cdd:PRK05771 7 KKVLIVTLKSYKDEvlEALHELGvvhiedlKEELSNERLRKLRSLLTKLSEAL-DKLRSYLPKLNPLREEKKKV--SVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 287 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK----------AEIEEKGSDGAASSYQLKQLEEQNAR 356
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlsLLLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 357 LKDALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERL------QEELSQAESTIDELKEQVDAALG-AEE 425
Cdd:PRK05771 164 SDVENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLLEeLKE 240
|
250 260
....*....|....*....|.
gi 1039774237 426 MVEMLTDRNLNLEEKVRELRE 446
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELE 261
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
209-335 |
4.88e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 40.98 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 209 AQVRDLEEKLETLRlkrSEDKAKLKELEKHKI-------QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 281
Cdd:COG4477 347 EKVRNLEKQIEELE---KRYDEIDERIEEEKVayselqeELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAIEMATL---------DKEMAEERAESLQQE-------VEALKERVDELTTDLEILKAEIEE 335
Cdd:COG4477 424 KKLREIKRRLEKSNLpglpeeyleMFEEASDEIEELSEElnevplnMDEVNRLLEEAEEDIETLEEKTEE 493
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
235-417 |
5.14e-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: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 235 LEKHKIQLEQVQE----WKSKMQEQQADLQRrLKEARKEAKEALEAK-ERYmeemadtadaiematldkEMAEERAESLQ 309
Cdd:pfam10168 549 LKKHDLAREEIQKrvklLKLQKEQQLQELQS-LEEERKSLSERAEKLaEKY------------------EEIKDKQEKLM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 310 QEVEALKERVDELTTDL-EILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMrdlssSEKQEHVKLQKLMEKKNqE 388
Cdd:pfam10168 610 RRCKKVLQRLNSQLPVLsDAEREMKKE------LETIN-EQLKHLANAIKQAKKKM-----NYQRYQIAKSQSIRKKS-S 676
|
170 180
....*....|....*....|....*....
gi 1039774237 389 LEVVRQQRERLQEELSQAESTIDELKEQV 417
Cdd:pfam10168 677 LSLSEKQRKTIKEILKQLGSEIDELIKQV 705
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
208-352 |
5.18e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 208 RAQVRDLEEKLETLRLKRSEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQ---------RRLKEARKEAKEALEAKE 278
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEA---ELAKKKAEERREAETARAEAEAAYEIAeanaerevqRQLEIAEREREIELQEKE 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 279 RYMEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERvdeLTTDLEILKAEIEEKGSDGAASSYQ--LKQLEE 352
Cdd:COG2268 299 AEREEAELEADVRKPAEAEKQAAEAEAE---AEAEAIRAK---GLAEAEGKRALAEAWNKLGDAAILLmlIEKLPE 368
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
205-381 |
5.62e-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: 40.39 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 205 EGLRaqvRDLEEKLETLRlkrsEDKAKLKElekhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErymeem 284
Cdd:smart00787 143 EGLK---EGLDENLEGLK----EDYKLLMK------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP------ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 adtadaiemATLDKemAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRM 364
Cdd:smart00787 204 ---------TELDR--AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKKLEQC 265
|
170 180
....*....|....*....|.
gi 1039774237 365 RDLSSSE----KQEHVKLQKL 381
Cdd:smart00787 266 RGFTFKEieklKEQLKLLQSL 286
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
911-1033 |
5.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 911 VELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKkldsaAKDADERIEKVQTRL-DETQ 989
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLtGLTP 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1039774237 990 TLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1033
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| Not3 |
pfam04065 |
Not1 N-terminal domain, CCR4-Not complex component; |
216-358 |
5.97e-03 |
|
Not1 N-terminal domain, CCR4-Not complex component;
Pssm-ID: 461155 [Multi-domain] Cd Length: 228 Bit Score: 39.84 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 216 EKLETLrLKRSedkakLKELEKHKiqlEQVQEW--------KSKMQEQqadlqRRLKEARKEAKEALEakeRYMEEMADT 287
Cdd:pfam04065 40 EKLEAD-LKKE-----IKKLQRLR---DQIKTWlssndikdKKKLLEN-----RKLIEEAMERFKAVE---KESKTKAFS 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 288 ADAIEMATLDKEMAEERAEslQQEVEALKERVDELTTDLEILKAEIE-----EKGSDGAASSYQLKQLEEQNARLK 358
Cdd:pfam04065 103 KEGLSLAAASKLDPKEKEK--AEARDWLSDSIDELNRQIEALEAEIEslqaqKKKKKKDSEKARLEELEKLIERHK 176
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
912-1037 |
6.00e-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: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 912 ELRAAALRAEITDAEGLGLKLEDRE--TVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKD---ADERIEKVQTRLD 986
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESKLD 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1039774237 987 ETQTLLRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRG 1037
Cdd:TIGR02168 334 ELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQ-LETLRS 386
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
919-1030 |
6.05e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 919 RAEITDAEglglklEDRETVIKELKKSLK-IKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTR-------LDETQT 990
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRllqkeenLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039774237 991 LLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKR 1030
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
306-411 |
6.14e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 306 ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLkdalvrmrdlssseKQEHVKLQKlmekk 385
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL--------------EAQLEQLQE----- 205
|
90 100
....*....|....*....|....*.
gi 1039774237 386 nQELEVVRQQRERLQEELSQAESTID 411
Cdd:PRK11448 206 -KAAETSQERKQKRKEITDQAAKRLE 230
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
202-360 |
6.84e-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: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 202 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQ--ADLQRRLKEARKE----AKEALE 275
Cdd:cd22656 128 KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK---ALKDLLTDEGGAIARKeiKDLQKELEKLNEEyaakLKAKID 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 276 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERV-------DELTTDLEILKAEIEEKGSDGAA---SSY 345
Cdd:cd22656 205 ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeklqgawQAIATDLDSLKDLLEDDISKIPAailAKL 284
|
170
....*....|....*
gi 1039774237 346 QLKQLEEQNARLKDA 360
Cdd:cd22656 285 ELEKAIEKWNELAEK 299
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
241-332 |
7.03e-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: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 241 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtaDAIEMATLDKEMAEERA-ESLQQEVEALKERV 319
Cdd:cd06503 38 SLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE--EILAEAKEEAERILEQAkAEIEQEKEKALAEL 115
|
90
....*....|...
gi 1039774237 320 DELTTDLEILKAE 332
Cdd:cd06503 116 RKEVADLAVEAAE 128
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
201-515 |
8.48e-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: 40.42 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 201 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKER 279
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 280 ymeEMADTADAI-----EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE---EKGSDGAASSYQLKQ-- 349
Cdd:TIGR00606 320 ---ELVDCQRELeklnkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRlelDGFERGPFSERQIKNfh 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 350 ---LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgaeem 426
Cdd:TIGR00606 397 tlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ----------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 427 VEMLTDRNLNLEEkvrELRETVGDLEAMNEMNDELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 506
Cdd:TIGR00606 466 LEGSSDRILELDQ---ELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
....*....
gi 1039774237 507 YRQLTAHLQ 515
Cdd:TIGR00606 542 KDKMDKDEQ 550
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
209-403 |
8.50e-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: 39.35 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 209 AQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQRR---LKEARKEAKEALEAKERYMEEM 284
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEELNQRweeLRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 285 ADTADaiematLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDalvRM 364
Cdd:cd00176 113 RDADD------LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-------EPRLKSLNELAEELLE---EG 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1039774237 365 RDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEEL 403
Cdd:cd00176 177 HPDADEEIEE--KLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
197-407 |
8.95e-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: 40.49 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 197 LPSPSKEEEGLRAQVRDLEEKLETLRLK-RSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAkEALE 275
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQ 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 276 AKERYMEEmadtadAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyqlkqleeQNA 355
Cdd:pfam15921 748 SKIQFLEE------AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS---------------------QER 800
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1039774237 356 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvrQQRERLQEELSQAE 407
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQE-----SVRLKLQHTLDVKE 847
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
939-1029 |
9.84e-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: 39.75 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 939 IKELKKSLKIKGEELSEANVRLSLLEKKLDSAA---KDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEA 1015
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLkqlAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90
....*....|....
gi 1039774237 1016 EKAELKQRLNSQSK 1029
Cdd:COG4942 102 QKEELAELLRALYR 115
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
215-416 |
9.93e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.09 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 215 EEKLETLRLKRSEDKAKLKELEK-----------HKIQLEQVQ--EWKSKMQEQQADLQRRLKEARKEakEALEAKERYM 281
Cdd:pfam03528 92 QEAIDEVKSQWQEEVASLQAIMKetvreyevqfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQEE--ENLEDEMKKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039774237 282 EEMADTADAI------EMATLDKEMAEerAESLQQEVEALKerVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA 355
Cdd:pfam03528 170 QEDAEKLRSVvmpmekEIAALKAKLTE--AEDKIKELEASK--MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAE 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039774237 356 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKN-QELEVVR---QQRERLQEELSQAE-STIDELKEQ 416
Cdd:pfam03528 246 KLRKELHEVCHLLEQERQQHNQLKHTWQKANdQFLESQRllmRDMQRMESVLTSEQlRQVEEIKKK 311
|
|
| |
