|
Name |
Accession |
Description |
Interval |
E-value |
| Dynactin |
pfam12455 |
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ... |
510-788 |
2.72e-92 |
|
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 amino acids in length. The family is found in association with pfam01302. There is a single completely conserved residue E that may be functionally important. Dynactin has been associated with Dynein, a kinesin protein which is involved in organelle transport, mitotic spindle assembly and chromosome segregation. Dynactin anchors Dynein to specific subcellular structures.
Pssm-ID: 463591 Cd Length: 287 Bit Score: 298.76 E-value: 2.72e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 510 LQDVNRELTNQQEASVERQQQPPPET-----FDFKIKFAETKAHAKAIEMELRQMEVAQANRHMSLLTAFMPDSFLRPGg 584
Cdd:pfam12455 1 LQSDLEDLRASQQITESESEDLSSRSrammdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRRG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 585 DHDCVLVLLLMPRLICKAELIRKQAQEKFDLSENcserPGLRGAAGEQLSFAAGLVYSLSLLQATLHRYEHALSQCSVDV 664
Cdd:pfam12455 80 DRDSVLALLLFKRLAFKADLLASQIREKFPLSES----LILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 665 YKKVGSLYPEMSAHERSLDFLIELLHKDQLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDSTMQLADHIKFTQSALDCMG 744
Cdd:pfam12455 156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 311893358 745 VEVGRLRAFLQGGQ--------EATDIALLLRDLETSCSDTRQFCKKIRRRM 788
Cdd:pfam12455 236 AALGRLKTLLQSGLpdpdggdeEASDLFELLQTLITQARSAKVISKKILRRL 287
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
12-77 |
1.02e-30 |
|
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.
Pssm-ID: 460154 [Multi-domain] Cd Length: 65 Bit Score: 115.19 E-value: 1.02e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 12 VGSRVEVIGkGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQI 77
Cdd:pfam01302 1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
12-78 |
8.50e-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 311893358 12 VGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEA-KGKNDGTVQGRKYFTCDEGHGIFVRQSQIQ 78
Cdd:smart01052 1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-523 |
1.14e-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: 102.44 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLR--LKRSED-----KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKE 274
Cdd:TIGR02168 170 YKERRKETERKLERTRenLDRLEDilnelERQLKSLERQAEKAERYKELKAELRELELALLvLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 275 RYMEEMADTADAIEMA-----TLDKEMAE--ERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 347
Cdd:TIGR02168 250 EAEEELEELTAELQELeekleELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 348 EQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALG----AEEMV 423
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeierLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 424 EMLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 503
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELE-ELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340
....*....|....*....|
gi 311893358 504 RQLTAHLQDVNRELTNQQEA 523
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
204-498 |
3.22e-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: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 283
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 284 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDL 363
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 364 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnlNLEEKVRELRET 443
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 311893358 444 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ 498
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
204-523 |
6.91e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 99.75 E-value: 6.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 283
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRK---ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 284 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEekgsdgaASSYQLKQLEEQNARLKDALVRMRDL 363
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-------ALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 364 SSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAL----GAEEMVEMLTDRNLNLEEKVRE 439
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLneraSLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 440 LRETVGDLE-AMNEMNDEL-QENARETELELREQ-------------LDMAGARVREAQKRVEAAQETVAD--------- 495
Cdd:TIGR02168 906 LESKRSELRrELEELREKLaQLELRLEGLEVRIDnlqerlseeysltLEEAEALENKIEDDEEEARRRLKRlenkikelg 985
|
330 340 350
....*....|....*....|....*....|....*..
gi 311893358 496 ---------YQQTIKKYRQLTAHLQDVNRELTNQQEA 523
Cdd:TIGR02168 986 pvnlaaieeYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
208-552 |
8.47e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 208 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTADAI 287
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELE------AELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 288 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSE 367
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 368 KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM-LTDRNLNLEEKVRELRETVGD 446
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRaAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 447 LEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNREL-TNQQEASV 525
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELaEAAARLLL 495
|
330 340
....*....|....*....|....*..
gi 311893358 526 ERQQQPPPETFDFKIKFAETKAHAKAI 552
Cdd:COG1196 496 LLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
204-471 |
1.69e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 95.11 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQewksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADT 283
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 284 ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK------AEIEEKGSDGAASSYQLKQLEEQNARLKDAL 357
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDERRERL 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 358 vrmrdlssSEKQEHVKlqKLMEKKNQE-LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEK 436
Cdd:PRK02224 630 --------AEKRERKR--ELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
250 260 270
....*....|....*....|....*....|....*
gi 311893358 437 VRELRETVGDLEAMNEMNDELQENARETELELREQ 471
Cdd:PRK02224 700 REALENRVEALEALYDEAEELESMYGDLRAELRQR 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-530 |
4.23e-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: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 201 EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEAKERYMEEM 280
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 ADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 360
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 361 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNLNLEEKVREL 440
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA--ELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 441 RETVGDLEAMNEMNDELQENARETELELREQLDMAG--ARVREAQKRVEAA--QETVADYQQTIKKYRQ-----LTAHLQ 511
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflEGVKAALLLAGLRglAGAVAVLIGVEAAYEAaleaaLAAALQ 549
|
330
....*....|....*....
gi 311893358 512 DVNRELTNQQEASVERQQQ 530
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKA 568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-487 |
1.25e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 92.44 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEAR----KEAKEALEAK 273
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 274 ERYMEEMADTADAIEMA-TLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 352
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 353 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemltdrnln 432
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED----------- 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 311893358 433 LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 487
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-530 |
1.72e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSE--DKAKLKELEKhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 275
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDllAEAGLDDADA-----EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADaiematlDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 355
Cdd:PRK02224 347 LREDADDLEE-------RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 356 ALVRMRdlsSSEKQEHVKLQKLMEK--KNQEL----------------------EVVRQQRERLQEELSQAESTIDELKE 411
Cdd:PRK02224 420 ERDELR---EREAELEATLRTARERveEAEALleagkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 412 QVDAA---LGAEEMVEMLTDRNLNLEEKVRELRETVGD----LEAMNEMNDELQENARETELELREQLDMAGARV----- 479
Cdd:PRK02224 497 RLERAedlVEAEDRIERLEERREDLEELIAERRETIEEkrerAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevae 576
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 480 -----------REAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:PRK02224 577 lnsklaelkerIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-494 |
1.91e-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: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKE----LEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAK 273
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEaqaeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 274 ERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARL 353
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 354 KDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNL 433
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE------AALLEAALAELLEEL 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 434 EEKVRELRetvGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 494
Cdd:COG1196 487 AEAAARLL---LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
201-491 |
3.59e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.48 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 201 EGLRAQV-----RDLEEKLETLRLKRSEDKAKLKELEKHKIQLeqvqewkskmqeqqadlqrrlKEARKEAKEALEAKER 275
Cdd:PRK02224 190 DQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQA---------------------RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKD 355
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 356 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemltdrnlnLEE 435
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE-----------------LEE 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 436 KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQE 491
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-517 |
4.57e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.50 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQvqewksKMQEQQADLQRrLKEARKEAKEALEAKErym 277
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA------EIEELEAQIEQ-LKEELKALREALDELR--- 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAL 357
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 358 VRMRD-LSSSEKQEHVKLQKLMEKKnQELEVVRQQRERLQEELSQAESTIDELKEQV-----DAALGAEEMVEMLTDRNL 431
Cdd:TIGR02168 890 ALLRSeLEELSEELRELESKRSELR-RELEELREKLAQLELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 432 NLEEKVRELRETVGDLEAMNEMN-DELQE-NARETELEL-REQLDMAGARVREAQKRVEAaqETVADYQQTIKKYRQlta 508
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAiEEYEElKERYDFLTAqKEDLTEAKETLEEAIEEIDR--EARERFKDTFDQVNE--- 1043
|
....*....
gi 311893358 509 HLQDVNREL 517
Cdd:TIGR02168 1044 NFQRVFPKL 1052
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
237-560 |
2.27e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.12 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 237 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALeakerymeemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVD 316
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS--------------QELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 317 ELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALvrmRDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQ 396
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHS--RIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 397 eELSQAESTIDELKEQvdaalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEA-MNEMNDELQE-NARETELE-----LR 469
Cdd:TIGR02169 816 -EIEQKLNRLTLEKEY------LEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEELEElEAALRDLEsrlgdLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 470 EQLDMAGARVREAQKRVEAAQETVADYQQTIKkyrQLTAHLQDVNRELTnQQEASVERQQQPPPETFDFKikfaETKAHA 549
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLS---ELKAKLEALEEELS-EIEDPKGEDEEIPEEELSLE----DVQAEL 960
|
330
....*....|.
gi 311893358 550 KAIEMELRQME 560
Cdd:TIGR02169 961 QRVEEEIRALE 971
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-529 |
2.55e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 2.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLR----LKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 274
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRdrleECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 275 RYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-----------------KGSDGA 337
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 338 AS-----------SYQLKQLEEQNARLKDALVRMRDLSSSEKQehvkLQKLMEKKNQELEVVRQQRERLQEELSQAES-- 404
Cdd:PRK02224 468 ETieedrerveelEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELIAERRETIEEKRERAEElr 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 405 --------------------------------TIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETvgdLEAMNE 452
Cdd:PRK02224 544 eraaeleaeaeekreaaaeaeeeaeeareevaELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREK---REALAE 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 453 MNDELQE---NARETELELREQLDmaGARVREAQ---KRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEASV 525
Cdd:PRK02224 621 LNDERRErlaEKRERKRELEAEFD--EARIEEARedkERAEEYLEQVEEKLDELREERdDLQAEIGAVENELEELEELRE 698
|
....
gi 311893358 526 ERQQ 529
Cdd:PRK02224 699 RREA 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-530 |
6.39e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.58 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRS-EDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEakeaLEAKER 275
Cdd:TIGR02169 197 RQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR----LEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADAI---EMATLDKEMAEERAE--SLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQN 350
Cdd:TIGR02169 273 LLEELNKKIKDLgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE---REIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 351 ARlKDALvrMRDLSSSEKQEHVKLQKLME--KKNQELevvRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTD 428
Cdd:TIGR02169 350 KR-RDKL--TEEYAELKEELEDLRAELEEvdKEFAET---RDELKDYREKLEKLKREINELKRELDR----------LQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 429 RNLNLEEKVRELRETVGDLEamnemndelqenARETELElrEQLDMAGARVREAQKRVEAAQETVADYQQtikKYRQLTA 508
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIE------------AKINELE--EEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE 476
|
330 340
....*....|....*....|....
gi 311893358 509 HLQDVNRELTNQQE--ASVERQQQ 530
Cdd:TIGR02169 477 EYDRVEKELSKLQRelAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
199-440 |
7.56e-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: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKL----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 274
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIeelqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 275 RYMEEMADTADAIEMAtldkemaEERAESLQQEVE-------ALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLE 347
Cdd:TIGR02168 334 ELAEELAELEEKLEEL-------KEELESLEAELEeleaeleELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 348 EQNARLKDALVRM--------RDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA 415
Cdd:TIGR02168 407 ARLERLEDRRERLqqeieellKKLEEAELKELqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
250 260
....*....|....*....|....*
gi 311893358 416 ALGAEEMVEMLTDRNLNLEEKVREL 440
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKAL 511
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
10-408 |
3.03e-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: 77.42 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 10 LRVGSRVEVIGKghRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRqsqiqvfedgadttsp 89
Cdd:COG5244 4 LSVNDRVLLGDK--FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIR---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 90 etPDSSAskVLKREGAdaaakTSKLRGLKPKKAPTARKTTTRRPKPTRpastgvagpssslgpsgsasagELSSSEPStp 169
Cdd:COG5244 66 --PDDDS--LLNGNAA-----YEKIKGGLVCESKGMDKDGEIKQENHE----------------------DRIHFEES-- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 170 aqtpLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIqLEQVQEWKSKMQ 249
Cdd:COG5244 113 ----KIRRLEETIEALKSTEKEEIVELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 250 EQQADLQRRLKEARKEAKEALEAKERymeemadtadaiematldkemaeeraeslqqevealKERVDELTTDLEILKAEI 329
Cdd:COG5244 188 ELVSDISETLNRNGSIQRSSVRECER------------------------------------SNIHDVLFLVNGILDGVI 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 330 EEKGsdgaassyqlKQLEeqnaRLKDALVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAESTIDE 408
Cdd:COG5244 232 DELN----------GELE----RLRRQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYE 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-560 |
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 311893358 198 KEEEGLRA-QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQqadlQRRLKEARKEAKEALEAKERY 276
Cdd:PTZ00121 1273 KAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEI-LKAEIEEKGSDgaassyQLKQLEEQNARLKD 355
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKAD------ELKKAAAAKKKADE 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 356 ALVRMRDLsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEEMVEMLTDRNLNL 433
Cdd:PTZ00121 1423 AKKKAEEK---KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 434 EE--KVRELRETVGDLEAMNEMN--DELQ--ENARETElELREQLDMAGA-RVREAQKRVEAAQETVADYQQTIKKYRQL 506
Cdd:PTZ00121 1500 DEakKAAEAKKKADEAKKAEEAKkaDEAKkaEEAKKAD-EAKKAEEKKKAdELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 311893358 507 TAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 560
Cdd:PTZ00121 1579 ALRKAEEAKKA---EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-502 |
9.02e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRlKRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 276
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAE-EAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnaRLKDA 356
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--KKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 357 LVRMRDLSSSEKQEHVKLQKLMEK-KNQELEVVRQQRERLQEELSQAES----TIDELKEQVDAALGAEEMVEMLTDRNL 431
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEdekkAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 432 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 502
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-563 |
9.49e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.72 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQE----------------------QQADL 255
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkkkadelkkaaaakkkadeakKKAEE 1429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 256 QRRLKEARK---EAKEALEAKE-----RYMEEMADTADAIEMATLDKEMAEE--RAESLQQEVEALKERVDELTTDLEIL 325
Cdd:PTZ00121 1430 KKKADEAKKkaeEAKKADEAKKkaeeaKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 326 KAEIEEKGSDGAASSYQLKQLEEqnARLKDALVRMRDLSSSE---KQEHVK----LQKLMEKKNQELEvvRQQRERLQEE 398
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEE--AKKADEAKKAEEKKKADelkKAEELKkaeeKKKAEEAKKAEED--KNMALRKAEE 1585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 399 LSQAEST---------IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELR 469
Cdd:PTZ00121 1586 AKKAEEArieevmklyEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 470 EQLdmagARVREAQKRveAAQETVADYQQTIKKYRQLTAHLQDVNR--ELTNQQEASVERQQQPPPETFDFKIKFAETKA 547
Cdd:PTZ00121 1664 AEE----AKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEEAKKaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
410
....*....|....*.
gi 311893358 548 HAkaiEMELRQMEVAQ 563
Cdd:PTZ00121 1738 EA---EEDKKKAEEAK 1750
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
120-563 |
4.41e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.41 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 120 KKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIptpalTSPGAAPPLPSPSKE 199
Cdd:PTZ00121 1098 GKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA-----RKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 200 EEGLRAQ-VRDLEEKLETLRLKRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME 278
Cdd:PTZ00121 1173 EDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLK 354
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 355 DALVRMRDlsSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvemLTDRNLNLE 434
Cdd:PTZ00121 1332 DAAKKKAE--EAKKAAEAA-KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE----AKKKAEEDK 1404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 435 EKVRELRETvgdlEAMNEMNDELQENAREtelelREQLDMAGARVREAQKRVEAAQEtvADYQQTIKKYRQLTAHLQDVN 514
Cdd:PTZ00121 1405 KKADELKKA----AAAKKKADEAKKKAEE-----KKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKKAEEAKKAD 1473
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 311893358 515 RELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQ 563
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
183-416 |
5.15e-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: 72.10 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 183 ALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEA 262
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 263 RKEAKEALEAKERYMEEMADTADAIEMATLDKEM-----------AEERAESLQQEVEALKERVDELTTDLEILKAEIEE 331
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 332 KgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 411
Cdd:COG4942 169 L-------EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 311893358 412 QVDAA 416
Cdd:COG4942 242 RTPAA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-487 |
6.37e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRlkrsEDKAKLKELEKHKIQLEqvqEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLK----KELEKLEELKKKLAELE---KKLDELEEELAELLKELEELGFESVEELEERLKE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqlkqleeqnarlkda 356
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK---------------------- 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 357 lvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEK 436
Cdd:PRK03918 655 --------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE----KALER 722
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 311893358 437 VRELRETVGDLEAMNEMN--DELQENARETELELREQlDMAGARVREAQKRVE 487
Cdd:PRK03918 723 VEELREKVKKYKALLKERalSKVGEIASEIFEELTEG-KYSGVRVKAEENKVK 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-564 |
1.36e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKI----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 272
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 273 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 352
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 353 LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-QQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNL 431
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 432 NLEE---------KVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 502
Cdd:COG1196 555 DDEVaaaaieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 503 YRQLTAHLQDVNRELTNQQEASVERQQqpppETFDFKIKFAETKAHAKAIEMELRQMEVAQA 564
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGS----LTGGSRRELLAALLEAEAELEELAERLAEEE 692
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-522 |
1.74e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHK-----------------------IQLEQVQEWKSKMQEQQA 253
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytAELKRIEKELKEIEEKER 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 254 DLQRRLKEARKEAKEalEAKERYMEEMADTADAIE--MATLDKEMAEERAEslqqEVEALKERVDELTTDLEILKAEIEE 331
Cdd:PRK03918 477 KLRKELRELEKVLKK--ESELIKLKELAEQLKELEekLKKYNLEELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEK 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 332 KG---SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE 408
Cdd:PRK03918 551 LEelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 409 LKEQVDAALGAEEMvemltdrnlnLEEKVRELREtvgdleamnEMNDELQENARETELELREQLDMAGARVREAQKRVEA 488
Cdd:PRK03918 631 AFEELAETEKRLEE----------LRKELEELEK---------KYSEEEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
330 340 350
....*....|....*....|....*....|....
gi 311893358 489 AQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 522
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-563 |
2.73e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.63 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSK-------MQEQQADLQRRLKEARKEAKEaL 270
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESlegskrkLEEKIRELEERIEELKKEIEE-L 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 271 EAKERYMEEMADTADaiEMATLDKEMA---------EERAESLQQEVEALKERVDELTTDLEILKaEIEEKGSDGAASSY 341
Cdd:PRK03918 279 EEKVKELKELKEKAE--EYIKLSEFYEeyldelreiEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 342 QLKQLEEQNARLKDALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGA- 419
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGLTPeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAk 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 420 -----------------------------EEMVEMLTDRN-------------LNLEEKVRELRETVGDLEAMNEM---- 453
Cdd:PRK03918 436 gkcpvcgrelteehrkelleeytaelkriEKELKEIEEKErklrkelrelekvLKKESELIKLKELAEQLKELEEKlkky 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 454 -NDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP 532
Cdd:PRK03918 516 nLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERL 594
|
410 420 430
....*....|....*....|....*....|.
gi 311893358 533 PETFDFKIKFAETKAHAKAIEMELRQMEVAQ 563
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
206-487 |
6.96e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKERYMEEMAD 282
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSelpELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 TADAIEMAtldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqlkqLEEQNARLKDAlvrmrd 362
Cdd:PRK03918 236 LKEEIEEL-------EKELESLEGSKRKLEEKIRELEERIEELKKEIEE--------------LEEKVKELKEL------ 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 363 lsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRE 442
Cdd:PRK03918 289 --KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 443 TVGDLEAMNEMNDELQ-----------ENARETELELREQLDMAGARVREAQKRVE 487
Cdd:PRK03918 367 AKAKKEELERLKKRLTgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIK 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
206-523 |
1.04e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEakerymEEMADTAD 285
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 AIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE--IEEKG------------------------------ 333
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerLKEARlllliaaallallglggsllsliltiagvl 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 334 -------SDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKL-MEKKNQELEVVRQQRERLQEELSQAEST 405
Cdd:COG4717 280 flvlgllALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEEL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 406 IDELK----EQVDAALGAEEMVEMLTD--RNLNLEEKVRELRETVGDLEAM--NEMNDELQENARETELELREQLDMAGA 477
Cdd:COG4717 360 EEELQleelEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQleELLGELEELLEALDEEELEEELEELEE 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 311893358 478 RVREAQKRVEAAQETVADYQQTIKK------YRQLTAHLQDVNRELTNQQEA 523
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQleedgeLAELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
293-533 |
3.65e-11 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 67.73 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 293 DKEMAEERAESLQQE--VEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQE 370
Cdd:COG3206 146 DPELAAAVANALAEAylEQNLELRREEARKALEFLEEQLPE----------LRKELEEAEAALEEFRQKNGLVDLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 371 HVklqklmekkNQELEVVRQQRERLQEELSQAESTIDELKEQVD------AALGAEEMVEMLTDRNLNLEEKVRELRETV 444
Cdd:COG3206 216 LL---------LQQLSELESQLAEARAELAEAEARLAALRAQLGsgpdalPELLQSPVIQQLRAQLAELEAELAELSARY 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 445 GD--------LEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLqDVNRE 516
Cdd:COG3206 287 TPnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV-EVARE 365
|
250 260
....*....|....*....|..
gi 311893358 517 -----LTNQQEASVERQQQPPP 533
Cdd:COG3206 366 lyeslLQRLEEARLAEALTVGN 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-473 |
9.79e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 225 KAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARkEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAES 303
Cdd:COG4913 609 RAKLAALEA---ELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAErEIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 304 lqQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvkLQKLMEKKNQ 383
Cdd:COG4913 685 --DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 384 ElEVVRQQRERLQEELSQAESTIDELKEQVDAAL-------------------GAEEMVEMLTD-RNLNLEEKVRELRET 443
Cdd:COG4913 761 D-AVERELRENLEERIDALRARLNRAEEELERAMrafnrewpaetadldadleSLPEYLALLDRlEEDGLPEYEERFKEL 839
|
250 260 270
....*....|....*....|....*....|
gi 311893358 444 VgdLEAMNEMNDELQENARETELELREQLD 473
Cdd:COG4913 840 L--NENSIEFVADLLSKLRRAIREIKERID 867
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
203-528 |
1.12e-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: 66.20 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 282
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRD 362
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS-------EIKDLTNQDSVKELIIKNLDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 363 LSSSEKQ-------EHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeEMVEMLTDRNLNLEE 435
Cdd:TIGR04523 462 TRESLETqlkvlsrSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK---EKIEKLESEKKEKES 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 436 KVRELRETVgdleamNEMNDELQENARETE-LELREQLDmagaRVREAQKRVEAAQETVadyQQTIKKYrqlTAHLQDVN 514
Cdd:TIGR04523 539 KISDLEDEL------NKDDFELKKENLEKEiDEKNKEIE----ELKQTQKSLKKKQEEK---QELIDQK---EKEKKDLI 602
|
330
....*....|....*.
gi 311893358 515 RELTN--QQEASVERQ 528
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 ... |
208-560 |
1.26e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.15 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 208 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEqvqewKSKMQEQQAdlQRRLKEarKEAKEALEAKERYMEEMADTADAI 287
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKA--LEYYQL--KEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 288 EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSE 367
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE----LLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 368 KQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDL 447
Cdd:pfam02463 316 LKES---EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 448 EAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 527
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350
....*....|....*....|....*....|...
gi 311893358 528 QQQpppETFDFKIKFAETKAHAKAIEMELRQME 560
Cdd:pfam02463 473 LLK---ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
206-528 |
2.07e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.39 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADta 284
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELnEELKELAEKRDE----LNAQVKELREEAQELREKRDELNEKVKE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 285 daiematldkemaeeraesLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassYQLKQLEEQNARLKDALVRmRDLS 364
Cdd:COG1340 76 -------------------LKEERDELNEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEWRQQT-EVLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 365 SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQaestIDELKEQVDAalgaeemvemltdrnlnLEEKVRELRetv 444
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAE----LKELRKEAEE-----------------IHKKIKELA--- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 445 gdlEAMNEMNDELQENARETElELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQEA 523
Cdd:COG1340 188 ---EEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRkELKKLRKKQRALKREKEKE 263
|
....*
gi 311893358 524 SVERQ 528
Cdd:COG1340 264 ELEEK 268
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-570 |
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 311893358 198 KEEEGLRAQ-VRDLEE--KLETLRLKR-SEDKAKLKELEKHKI-QLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEA 269
Cdd:PTZ00121 1238 DAEEAKKAEeERNNEEirKFEEARMAHfARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKkaeEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 270 LEAKERyMEEMADTADAI----EMATLDKEMAEERAESLQQEVEALKER--VDELTTDLEILKAEIEEKGSDGAASSYQL 343
Cdd:PTZ00121 1318 DEAKKK-AEEAKKKADAAkkkaEEAKKAAEAAKAEAEAAADEAEAAEEKaeAAEKKKEEAKKKADAAKKKAEEKKKADEA 1396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 344 KQLEEQNARlkdalvrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST--IDELKEQVDAALGAEE 421
Cdd:PTZ00121 1397 KKKAEEDKK---------------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEE 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 422 MVEMLTDRnlnleEKVRELRETVGDLEAMNEMNDELQENARETElELREQLDmAGARVREAQKRVEAAQETVADYQQTIK 501
Cdd:PTZ00121 1462 AKKKAEEA-----KKADEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAE-AKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 502 KYRQL-TAHLQDVNRELTNQQEASVERQQQPPPEtfdfKIKFAETKAHAKAIEMELRQMEVAQANRHMSL 570
Cdd:PTZ00121 1535 KADEAkKAEEKKKADELKKAEELKKAEEKKKAEE----AKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-487 |
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 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARK--EAKEALEAK 273
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaeELKKaeEEKKKVEQL 1638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 274 ERYMEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLE--ILKAEIEEKGSDGAASSYQLKQLEEQNA 351
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---EEENKIKAAEEAKKAEEDKKKAEEAKKAEEdeKKAAEALKKEAEEAKKAEELKKKEAEEK 1715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 352 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgAEEMVEMLTDRNL 431
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI-EEELDEEDEKRRM 1794
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 432 NLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVE 487
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-571 |
3.85e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRR--LKEARKEAKEALEAKER 275
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELeaLEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLK 354
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 355 DALVRMRDLSSSEKQE---------HVKLQKLMEKKNQELEV-------------VRQQRERLQEELSQAESTIDELKEQ 412
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIagvlflvlgllalLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 413 vdAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ-----LDMAGARVREA-QKRV 486
Cdd:COG4717 314 --EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQeiaalLAEAGVEDEEElRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 487 EAAQEtvadyqqtikkYRQLTAHLQDVNRELTNQQEASVERQQQPPPEtfDFKIKFAETKAHAKAIEMELRQM--EVAQA 564
Cdd:COG4717 392 EQAEE-----------YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELreELAEL 458
|
....*..
gi 311893358 565 NRHMSLL 571
Cdd:COG4717 459 EAELEQL 465
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
206-541 |
1.49e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLkRSEDKAKLKELEKHKiQLEQVQEWKSKMQEQQADL---QRRLKEARKEAKE--ALEAKERYMEEM 280
Cdd:pfam17380 288 QQQEKFEKMEQERL-RQEKEEKAREVERRR-KLEEAEKARQAEMDRQAAIyaeQERMAMERERELEriRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 ADTADAIEMATLdKEMaeeraESLQQEVEALKERVdelttdleilKAEIEekgsdgAASSYQLKQlEEQNARLKDALVRM 360
Cdd:pfam17380 366 RQEEIAMEISRM-REL-----ERLQMERQQKNERV----------RQELE------AARKVKILE-EERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 361 RDL-SSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERL-QEELSQAESTIDELKEQVDAALGAEEmvemltdRNL 431
Cdd:pfam17380 423 EQIrAEQEEARQREVRRLEEERAREMERVRleeqerqQQVERLrQQEEERKRKKLELEKEKRDRKRAEEQ-------RRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 432 NLEEKVRELRETVgdleamneMNDELQENARETELELREQLDMAGARVREA--QKRVEAAQETVADYQQTIKKYRQLTAH 509
Cdd:pfam17380 496 ILEKELEERKQAM--------IEEERKRKLLEKEMEERQKAIYEEERRREAeeERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340 350
....*....|....*....|....*....|....
gi 311893358 510 LQ--DVNRELTNQQEASVERQQQPPPETFDFKIK 541
Cdd:pfam17380 568 LEamEREREMMRQIVESEKARAEYEATTPITTIK 601
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
209-466 |
2.58e-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: 61.41 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 209 DLEEKLETLRLKRSEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQ---RRLKEARKEAKEALEAKERYMEEMADTAD 285
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYdllEKEVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 AI--EMATLDK-----EMAEERAESLQQEVEALKERVDELTTDLE-------ILKAEIEEKGSdgaassyQLKQLEEQNA 351
Cdd:pfam06160 309 ELkeELERVQQsytlnENELERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILE-------QLEEIEEEQE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 352 RLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaEEMVEML 426
Cdd:pfam06160 382 EFKESLQSLR------KDELEAREKLDEFKLELREIKRLvEKSNLpglpESYLDYFFDVSDEI----------EDLADEL 445
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 311893358 427 TDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 466
Cdd:pfam06160 446 NEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ 485
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
238-479 |
2.79e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.57 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 238 LEQVQEWKSKMQEQQAD-LQRRLKEARKEAKEALEAKERYMEEMadtadAIEMATLDKEMAEERAESLQQEVEALKERVD 316
Cdd:COG3206 162 LEQNLELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQKN-----GLVDLSEEAKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 317 ELTTDLEILKAEIEEkGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQ-RERL 395
Cdd:COG3206 237 EAEARLAALRAQLGS-GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL----RAQIAALRAQlQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 396 QEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQenARETELELREQLDMA 475
Cdd:COG3206 312 QRILASLEAELEALQAREAS---LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL--QRLEEARLAEALTVG 386
|
....
gi 311893358 476 GARV 479
Cdd:COG3206 387 NVRV 390
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
198-466 |
3.61e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 61.00 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKakLKELEKhKI-----QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 272
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQE-RIdqlydILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 273 KERYMEEMADTADAIEmatldkemaeeRAESLQQEVEALKERVDELTTDLE-------ILKAEIEEkgsdgaaSSYQLKQ 345
Cdd:PRK04778 333 IDRVKQSYTLNESELE-----------SVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEE-------ILKQLEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 346 LEEQNARLKDALVRMRdlssseKQEHVKLQKLMEKKNQELEVVRQ-QRERL----QEELSQAESTIDELkeqvdaalgaE 420
Cdd:PRK04778 395 IEKEQEKLSEMLQGLR------KDELEAREKLERYRNKLHEIKRYlEKSNLpglpEDYLEMFFEVSDEI----------E 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 311893358 421 EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 466
Cdd:PRK04778 459 ALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-527 |
4.10e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 297 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRDLssseKQEHVKLQK 376
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRAL----EQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 377 LMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ--------VDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLE 448
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 449 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVER 527
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
282-526 |
4.18e-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: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 282 DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILkAEIEEKGSDgaasSYQLKQLEEQNARLKDALVRMr 361
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWD----EIDVASAEREIAELEAELERL- 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 362 DLSSSEKQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML--TDRNLNLEEKVRE 439
Cdd:COG4913 681 DASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarLELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 440 LRetvgdleamnemndeLQENARETELELREQLDMAGARVREAQKRVEAAQE---------------TVADYQQTIKKYR 504
Cdd:COG4913 758 AL---------------GDAVERELRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldaDLESLPEYLALLD 822
|
250 260
....*....|....*....|....*..
gi 311893358 505 QLTA-----HLQDVNRELTNQQEASVE 526
Cdd:COG4913 823 RLEEdglpeYEERFKELLNENSIEFVA 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-402 |
4.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLK--EARKEAKEALEAKERY 276
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQ 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAiEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASS---------YQLKQLE 347
Cdd:COG4717 411 LEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEllqeleelkAELRELA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893358 348 EQNARLK---DALVRMRDLSSSEKQEHV--------------KLQKLMEKKNQELEVVRQQRERLQ-EELSQA 402
Cdd:COG4717 490 EEWAALKlalELLEEAREEYREERLPPVleraseyfsrltdgRYRLIRIDEDLSLKVDTEDGRTRPvEELSRG 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-519 |
4.43e-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: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 292 LDKEMAEERAESLQQEVEALkervDELTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSE---- 367
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDL----ERAHEALEDAREQIE-----------LLEPIRELAERYAAARERLAELEYLRaalr 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 368 ----KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEemVEMLTDRnlnLEEKVRELRET 443
Cdd:COG4913 283 lwfaQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR--LEQLERE---IERLERELEER 357
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 444 VGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQEtvaDYQQTIKKYRQLTAHLQDVNRELTN 519
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIAS 430
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
211-522 |
5.17e-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: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 211 EEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADaIEMA 290
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSID-IKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 291 TLDKEMAEERAEsLQQEVEALKErvdELTTDLEILKAEIEEKGSDgaassyQLKQLEEQNARlKDALVRMRDLSSSEKQE 370
Cdd:COG5185 311 TESLEEQLAAAE-AEQELEESKR---ETETGIQNLTAEIEQGQES------LTENLEAIKEE-IENIVGEVELSKSSEEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 371 HVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETVGDL--- 447
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI------EELQRQIEQATSSNEEVSKLLNELISELnkv 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 448 --EAMNEMNDELQENARETELELREQLDmagarvrEAQKRVEAAQETVADYQQTIKKYR-QLTAHLQDVNRELTNQQE 522
Cdd:COG5185 454 mrEADEESQSRLEEAYDEINRSVRSKKE-------DLNEELTQIESRVSTLKATLEKLRaKLERQLEGVRSKLDQVAE 524
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
206-560 |
5.41e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.90 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtad 285
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 aiEMATLDKEMAEERAESLQ--QEVEALKERVDELTTDLEilKAEIEekgsdgaassyqLKQLEEQNARLKDalvrmRDL 363
Cdd:pfam15921 350 --QLVLANSELTEARTERDQfsQESGNLDDQLQKLLADLH--KREKE------------LSLEKEQNKRLWD-----RDT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 364 SSSEKQEHvkLQKLMEKKNQELE----VVRQQRERLQEELSQAESTIDELKEQVD--AALGAE---------EMVEMLTD 428
Cdd:pfam15921 409 GNSITIDH--LRRELDDRNMEVQrleaLLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQlestkemlrKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 429 RNLNLEEKVRELRETVGDLE----AMNEMNDELQENARETELELRE--QLDMAGARVREAQKRVEAAQETVADYQQTIKK 502
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQekerAIEATNAEITKLRSRVDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEI 566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 503 YRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQME 560
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
225-420 |
1.11e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 225 KAKLKELEKHKIQLEQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAE 298
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 299 ERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAAssyqlkQLEEQNArlkDALVRMRDLSSSEKQEHVKLQKLM 378
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAA-----RAPAWLAAQDALA------RLREQSG---EEFEDSQDVTEYMQQLLERERELT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 311893358 379 EKKNQelevVRQQRERLQEE---LSQAESTIDE----LKEQVDAALGAE 420
Cdd:PRK04863 645 VERDE----LAARKQALDEEierLSQPGGSEDPrlnaLAERFGGVLLSE 689
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
287-449 |
1.14e-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: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 287 IEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKdalvrmrdls 364
Cdd:COG1579 10 LDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 365 ssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdaalgaEEMVEMLTDRNLNLEEKVRELRETV 444
Cdd:COG1579 80 --EQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEEL------AELEAELAELEAELEEKKAELDEEL 151
|
....*
gi 311893358 445 GDLEA 449
Cdd:COG1579 152 AELEA 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
307-566 |
1.31e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 307 EVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQnarlKDALVRMRDLSSsEKQEHVKLQKLMEKKN--QE 384
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQ-------QLERLRRE----REKAERYQALLK-EKREYEGYELLKEKEAleRQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 385 LEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNL-EEKVRELRETVGDLEAMnemndelQENARE 463
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLgEEEQLRVKEKIGELEAE-------IASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 464 TELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFA 543
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE---VDKEFAETRD 385
|
250 260
....*....|....*....|...
gi 311893358 544 ETKAHAKAIEMELRQMEVAQANR 566
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKREL 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
198-530 |
2.11e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkIQLEQVQEWKSKMQEQqadlqRRLKEARKEAKEALEAKERYM 277
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLE---QDYQAASDHLNLVQTA-----LRQQEKIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEmadTADAIEMATLDKEMAEERAESLQQEVEALK-------ERVDELTTD----------LEILK-----AEIEEKGSD 335
Cdd:PRK04863 365 EE---QNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqQALDVQQTRaiqyqqavqaLERAKqlcglPDLTADNAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 336 GAASSYQlKQLEEQNARLKDALVRMRDlSSSEKQEHVKLQKLMEK----------KNQELEVVRQQRER--LQEELSQAE 403
Cdd:PRK04863 442 DWLEEFQ-AKEQEATEELLSLEQKLSV-AQAAHSQFEQAYQLVRKiagevsrseaWDVARELLRRLREQrhLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 404 STIDELKEQVDAALGAEEMV---EMLTDRNLNLEEKVRELREtvgDLEAMNEMNDELQENARETELELREQLDMAGARVR 480
Cdd:PRK04863 520 MRLSELEQRLRQQQRAERLLaefCKRLGKNLDDEDELEQLQE---ELEARLESLSESVSEARERRMALRQQLEQLQARIQ 596
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 481 E----------AQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:PRK04863 597 RlaarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
204-529 |
2.26e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEA---KEALEAKERymee 279
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEeVDSLKS----QLADYQQALDVQQTRAiqyQQAVQALEK---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 280 madtADAI-EMATLDKEMAEERAESLQQEVEALKERVDELttdleilkaeiEEKGSDGAASSYQLKQLEEQNARLKDALV 358
Cdd:COG3096 425 ----ARALcGLPDLTPENAEDYLAAFRAKEQQATEEVLEL-----------EQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 359 RmrdlssseKQEHVKLQKLMEKkNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgAEEMVEML---TDRNLNLEE 435
Cdd:COG3096 490 R--------SQAWQTARELLRR-YRSQQALAQRLQQLRAQLAELEQRLRQQQN-------AERLLEEFcqrIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 436 KVRELRETvgdLEAMNEMNDELQENARETELELREQLDMAGARVRE----------AQKRVEAAQETVAdyqQTIKKYRQ 505
Cdd:COG3096 554 ELEELLAE---LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlaAQDALERLREQSG---EALADSQE 627
|
330 340
....*....|....*....|....
gi 311893358 506 LTAHLQDVnreLTNQQEASVERQQ 529
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 ... |
198-495 |
2.62e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE---QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKE 274
Cdd:pfam02463 181 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 275 RYMEEMADTADAI--EMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL 346
Cdd:pfam02463 261 EKEEEKLAQVLKEnkEEEKEKKLQEEELKllakeeEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 347 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEML 426
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDL 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 427 TDRNLN-LEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 495
Cdd:pfam02463 421 LKEEKKeELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
201-446 |
3.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 201 EGLRAQVRDLEEKLETLRlkrsEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQR---RLKEARKEAKEALEAKERYM 277
Cdd:COG4913 664 ASAEREIAELEAELERLD----ASSDDLAALEE---QLEELEAELEELEEELDELKGeigRLEKELEQAEEELDELQDRL 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMATLDKEMAEERAESLQQEV-EALKERVDELTTDLEILKAEIEEK----------------GSDGAASS 340
Cdd:COG4913 737 EAAEDLARLELRALLEERFAAALGDAVERELrENLEERIDALRARLNRAEEELERAmrafnrewpaetadldADLESLPE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 341 YQ--LKQLEEQN-----ARLKDALVR-----MRDLSSSEKQEHVKLQKLMEKKNQELE--------------------VV 388
Cdd:COG4913 817 YLalLDRLEEDGlpeyeERFKELLNEnsiefVADLLSKLRRAIREIKERIDPLNDSLKripfgpgrylrlearprpdpEV 896
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 389 RQQRERLQEELSQAESTIDELKEQVDAALgaEEMVEMLTDRNlnlEEKVRELRETVGD 446
Cdd:COG4913 897 REFRQELRAVTSGASLFDEELSEARFAAL--KRLIERLRSEE---EESDRRWRARVLD 949
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
206-530 |
3.14e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.11 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKealeakerymeemadtad 285
Cdd:TIGR04523 146 EIKKKEKELEKLNNKYNDLKKQKEELENELNLLE-----KEKLNIQKNIDKIKNKLLKLELL------------------ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 aieMATLDKEmaEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLeeqnarlkdalvrmrdlss 365
Cdd:TIGR04523 203 ---LSNLKKK--IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQL------------------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 366 seKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvEMLTDRNLNLEEKVRELRETVG 445
Cdd:TIGR04523 259 --KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ--------DWNKELKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 446 DL----EAMNEMNDELQ------ENARETELELREQLdmagarvREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNR 515
Cdd:TIGR04523 329 QIsqnnKIISQLNEQISqlkkelTNSESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKN---LESQINDLES 398
|
330
....*....|....*
gi 311893358 516 ELTNQQEASVERQQQ 530
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQ 413
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
203-413 |
3.43e-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: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETlRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmad 282
Cdd:COG5185 287 LIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE--- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 tADAIEmATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDG-AASSYQLKQLE----------EQNA 351
Cdd:COG5185 363 -IENIV-GEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTlKAADRQIEELQrqieqatssnEEVS 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 352 RLKDALVRMRDLSSSEKQEHVKlQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQV 413
Cdd:COG5185 441 KLLNELISELNKVMREADEESQ-SRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
209-498 |
3.84e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 209 DLEEKLETLRLKRSEDKAKLKELEK----HKIQLEQVQEWKSKMQE--------QQADLQRRLKEARKEAKEALEAKeRY 276
Cdd:PRK04863 834 DPEAELRQLNRRRVELERALADHESqeqqQRSQLEQAKEGLSALNRllprlnllADETLADRVEEIREQLDEAEEAK-RF 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIE--MATLDKEmaEERAESLQQEVEALKErvdelttdleilkaeieekgsdgaassyQLKQLEEQNARLK 354
Cdd:PRK04863 913 VQQHGNALAQLEpiVSVLQSD--PEQFEQLKQDYQQAQQ----------------------------TQRDAKQQAFALT 962
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 355 DALVRMRDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAE--------------STIDELKEQVDAAlgA 419
Cdd:PRK04863 963 EVVQRRAHFSYEDAAEMLaKNSDLNEKLRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslkSSYDAKRQMLQEL--K 1040
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 420 EEMVEMLTDRNLNLEEKVRELREtvgdleamnEMNDELQEN-ARETELELreQLDMAGARVREAQKRVEAAQEtvaDYQQ 498
Cdd:PRK04863 1041 QELQDLGVPADSGAEERARARRD---------ELHARLSANrSRRNQLEK--QLTFCEAEMDNLTKKLRKLER---DYHE 1106
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
215-531 |
5.02e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 215 ETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 294
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 295 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHV-- 372
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-------EEELKELEEQLESLQEELAALEQELQALSEAEAeq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 373 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNE 452
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 453 MNDELQE-NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQP 531
Cdd:COG4372 264 ELAILVEkDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
199-490 |
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 311893358 199 EEEGLRAQVRDLE-EKLETLRLKRSEDKAKLKELEKHKIQLEQVQEW-KSKMQEQQADLQRRLKEARK--------EAKE 268
Cdd:PTZ00121 1068 QDEGLKPSYKDFDfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEArKAEEAKKKAEDARKAEEARKaedarkaeEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 269 ALEAKERYMEEMADTADAIEMAtldkemaeERAESLQQEVEAlkERVDELTTDLEILKAEiEEKGSDGAASSYQLKQLEE 348
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDARKAEEA--------RKAEDAKKAEAA--RKAEEVRKAEELRKAE-DARKAEAARKAEEERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 349 qnarlkdalvrMRDLSSSEKQEHVKlqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTD 428
Cdd:PTZ00121 1217 -----------ARKAEDAKKAEAVK--KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL 1283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 429 RNLNLEEKVRELR--ETVGDLEAMNEMNDELQ--ENARETELELREQLDMAGARVREAQKRVEAAQ 490
Cdd:PTZ00121 1284 KKAEEKKKADEAKkaEEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAK 1349
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
209-478 |
5.87e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.65 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 209 DLEEKLETLRLKRSEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQR---------------RLKEARKEAKEALEAk 273
Cdd:COG3096 833 DPEAELAALRQRRSELER---ELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELDAAQEA- 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 274 ERYMEEMADTADAIE--MATLDKEMAEEraESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQ-----LKQL 346
Cdd:COG3096 909 QAFIQQHGKALAQLEplVAVLQSDPEQF--EQLQADYLQAKEQQRRLKQQIFALSEVVQRR----PHFSYEdavglLGEN 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 347 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeEMVEML 426
Cdd:COG3096 983 SDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-----EAEERA 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 427 TDRNLNLEEKVRELRETVGDLEAM-----NEMnDELQENARETELE---LREQLDMAGAR 478
Cdd:COG3096 1058 RIRRDELHEELSQNRSRRSQLEKQltrceAEM-DSLQKRLRKAERDykqEREQVVQAKAG 1116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-1022 |
6.16e-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: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 255 LQRRLKEARKEAKEALEAKEryMEEMADTADAIEMAtLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEkgs 334
Cdd:COG1196 198 LERQLEPLERQAEKAERYRE--LKEELKELEAELLL-LKLRELEAELEELEAELEELEAELEELEAELAELEAELEE--- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 335 dgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvRQQRERLQEELSQAESTIDELKEQVD 414
Cdd:COG1196 272 -------LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 415 AALGAEEMvemltdrnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVA 494
Cdd:COG1196 341 ELEEELEE----------AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 495 DYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppetfdfkikFAETKAHAKAIEMELRQMEVAQANRHMSLLTAf 574
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----------AAEEEAELEEEEEALLELLAELLEEAALLEAA- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 575 mpdsflrpggdhdcvlvlllmpRLICKAELIRKQAQEKFDLSENCSERPGLRGA-AGEQLSFAAGLVYSLSLLQATLHRY 653
Cdd:COG1196 479 ----------------------LAELLEELAEAAARLLLLLEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAY 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 654 EHALSQCSVdvykkvGSLYPEMSAHERSLDFLIELLhKDQLDETVNVEPLTKaikyyqhlysIHLAEQPEDSTMQLADhi 733
Cdd:COG1196 537 EAALEAALA------AALQNIVVEDDEVAAAAIEYL-KAAKAGRATFLPLDK----------IRARAALAAALARGAI-- 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 734 kftqsaldcmgvevgrlraflqgGQEATDIALLLRDLEtscsdtrqfckkirrrmpgtdapgiPAALAFGSQVSDTLLDC 813
Cdd:COG1196 598 -----------------------GAAVDLVASDLREAD-------------------------ARYYVLGDTLLGRTLVA 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 814 RKHLTWVVavlqevaaaaaqliaplaenegLPVAALEELAFKASEQIYGSPSSSpyeclrqsctilistmnklataMQEG 893
Cdd:COG1196 630 ARLEAALR----------------------RAVTLAGRLREVTLEGEGGSAGGS----------------------LTGG 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 894 EydaerppskpppVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 973
Cdd:COG1196 666 S------------RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 311893358 974 IEKVQTRLDETQTLLRKKEKDFEETMdalqADIDQLEAEKAELKQRLNS 1022
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEP----PDLEELERELERLEREIEA 778
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
197-502 |
6.22e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 57.22 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRA-QVRDLEEKLE-----TLRLkrseDKAKLKELEkhkiQLEQVQEWKSKMQEQQADLQRRLKEArkEAKEAL 270
Cdd:PLN02939 119 SKDGEQLSDfQLEDLVGMIQnaeknILLL----NQARLQALE----DLEKILTEKEALQGKINILEMRLSET--DARIKL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 271 EAKERYMEEMADTadaiEMATLDKEMAEERA------ESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgAASSYQLK 344
Cdd:PLN02939 189 AAQEKIHVEILEE----QLEKLRNELLIRGAteglcvHSLSKELDVLKEENMLLKDDIQFLKAELIEV----AETEERVF 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 345 QLEEQNARLKDALvrmRDLSSsekqehvklqKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaeemve 424
Cdd:PLN02939 261 KLEKERSLLDASL---RELES----------KFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAA------- 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 425 MLTDRNLNLEEKVRELRETVGDLEaMNEMNDELQENARETELELREQLDMAGArvrEAQKRVEAAQETVADYQQTIKK 502
Cdd:PLN02939 321 LVLDQNQDLRDKVDKLEASLKEAN-VSKFSSYKVELLQQKLKLLEERLQASDH---EIHSYIQLYQESIKEFQDTLSK 394
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
279-533 |
8.62e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSyqlKQLEEQNARLKDALV 358
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 359 RMRD-----------LSSSEKQEHVK----LQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmv 423
Cdd:COG3883 94 ALYRsggsvsyldvlLGSESFSDFLDrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 424 emltdrnlNLEEKVRELRETVGDLEAmnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 503
Cdd:COG3883 172 --------ELEAQQAEQEALLAQLSA-----EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270
....*....|....*....|....*....|
gi 311893358 504 RQLTAHLQDVNRELTNQQEASVERQQQPPP 533
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAA 268
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
198-410 |
8.89e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.30 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQ-------------------- 256
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELnEKLNELREELDELRKELAelnkaggsidklrkeierle 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 257 --------------------RRLKEARKEAKEALEAKERYMEEMADTADA-IEMATLDKEMAE--ERAESLQQEVEALKE 313
Cdd:COG1340 123 wrqqtevlspeeekelvekiKELEKELEKAKKALEKNEKLKELRAELKELrKEAEEIHKKIKElaEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 314 RVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmeKKNQELEVVRQQRE 393
Cdd:COG1340 203 EADELRKEADELHKEIVEAQ----------EKADELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAE 270
|
250
....*....|....*...
gi 311893358 394 RLQEELSQAES-TIDELK 410
Cdd:COG1340 271 EIFEKLKKGEKlTTEELK 288
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-505 |
1.47e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.95 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME 278
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRdlgeELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADT-ADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL---KAEIEEKGSDGAAssyqlkQLEEQNARLK 354
Cdd:pfam01576 349 EMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLqqaKQDSEHKRKKLEG------QLQELQARLS 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 355 DAlvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaaLGAEEmvemlTDRNLNL 433
Cdd:pfam01576 423 ES-----ERQRAELAEKLsKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQE-----LLQEE-----TRQKLNL 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 434 EEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 505
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
197-503 |
1.64e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQvqewkskmqeQQADLQRRLKEARKEakeaLEAKERy 276
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET----------QLKVLSRSINKIKQN----LEQKQK- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 meEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDElttdLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDA 356
Cdd:TIGR04523 490 --ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----LESEKKEKESK----------ISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 357 LVRMrdlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLNLEEK 436
Cdd:TIGR04523 554 LKKE------------NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK-DLIKE--IEEKEKKISSLEKE 618
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 437 VRELRETVGDLEAMnEMNDELQENARETELEL-REQLDMAGARVREAQKRVEAAQETVADYQQTIKKY 503
Cdd:TIGR04523 619 LEKAKKENEKLSSI-IKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDW 685
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
199-560 |
1.78e-07 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 55.47 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYme 278
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 emadtadAIEMATLDKEMAE-----ERAESLQQEVEALKERVDEL--TTD-LEILKAEIE---EKGSDGAASSYQLKQLE 347
Cdd:pfam05622 86 -------RIKCEELEKEVLElqhrnEELTSLAEEAQALKDEMDILreSSDkVKKLEATVEtykKKLEDLGDLRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 348 EQNA-------RLKDALVR--------------MRDLS---SSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAE 403
Cdd:pfam05622 159 ERNAeymqrtlQLEEELKKanalrgqletykrqVQELHgklSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 404 STIDELK---EQVDAALGAEEMVEMLTDRNLNLEEKVR--ELRETVGDLEAMNEM---NDELQENARETEL--------- 466
Cdd:pfam05622 239 ETNEELRcaqLQQAELSQADALLSPSSDPGDNLAAEIMpaEIREKLIRLQHENKMlrlGQEGSYRERLTELqqlledanr 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 467 ---ELREQLDMAGARVREAQKRVE----AAQETVADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQqqpPPETF 536
Cdd:pfam05622 319 rknELETQNRLANQRILELQQQVEelqkALQEQGSKAEDSSLLKQKLEEHLEklhEAQSELQKKKEQIEELE---PKQDS 395
|
410 420
....*....|....*....|....
gi 311893358 537 DFKIKFAETKAHAKAIEMELRQME 560
Cdd:pfam05622 396 NLAQKIDELQEALRKKDEDMKAME 419
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-486 |
1.79e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeema 281
Cdd:pfam15921 333 LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 282 DTADAIEMATL-----DKEMAEERAESL------------QQEVEALK------ERVDELTTDLEILKAEIEEKGSDGAA 338
Cdd:pfam15921 407 DTGNSITIDHLrreldDRNMEVQRLEALlkamksecqgqmERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 339 SSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQeelsQAESTIDELKEQVdaaLG 418
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR----NVQTECEALKLQM---AE 559
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 419 AEEMVEMLTDRNLNLEEKVRELRETVGdleAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRV 486
Cdd:pfam15921 560 KDKVIEILRQQIENMTQLVGQHGRTAG---AMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARV 627
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
170-557 |
2.45e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 170 AQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKiqleqvQEWKSKMQ 249
Cdd:TIGR00606 660 GATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR------DEMLGLAP 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 250 EQQADLQRRLKEArKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALkERVDELTTDLE--ILKA 327
Cdd:TIGR00606 734 GRQSIIDLKEKEI-PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM-ERFQMELKDVErkIAQQ 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 328 EIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVR-------QQRERLQEEL- 399
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKlqigtnlQRRQQFEEQLv 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 400 ---SQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----------EEKVRELRETVGDLEA-MNEMNDELQENARET 464
Cdd:TIGR00606 892 elsTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsnkkaQDKVNDIKEKVKNIHGyMKDIENKIQDGKDDY 971
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 465 ELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQD-VNRELTNQQEASVERQqqppPETFDFKI--- 540
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDnLTLRKRENELKEVEEE----LKQHLKEMgqm 1047
|
410
....*....|....*..
gi 311893358 541 KFAETKAHAKAIEMELR 557
Cdd:TIGR00606 1048 QVLQMKQEHQKLEENID 1064
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
201-530 |
2.45e-07 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 55.14 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 201 EGLRAQVRDLEEKL-----ETLRLKRS-EDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 269
Cdd:pfam07111 334 KQLRGQVAELQEQVtsqsqEQAILQRAlQDKAAEVEVERMsakglQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSST 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 270 LEAKERYMEEMADTADAI------------EMATLDKEMAEERA-ESLQQEVEALKERVDELTTDLeilkaeieekgsdg 336
Cdd:pfam07111 414 QIWLETTMTRVEQAVARIpslsnrlsyavrKVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADL-------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 337 aasSYQLKQLEEQNARLKDALvrmrDLSSSEKQEHV-KLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDA 415
Cdd:pfam07111 480 ---SLELEQLREERNRLDAEL----QLSAHLIQQEVgRAREQGEAERQQLSEVAQQ---LEQELQRAQESLASVGQQLEV 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 416 ALGAEEMVemlTDRNLNLEEKVRELRETVGDleamnemndELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 495
Cdd:pfam07111 550 ARQGQQES---TEEAASLRQELTQQQEIYGQ---------ALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQ 617
|
330 340 350
....*....|....*....|....*....|....*
gi 311893358 496 YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:pfam07111 618 IQHRATQEKERNQELRRLQDEARKEEGQRLARRVQ 652
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
200-494 |
2.51e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 200 EEGLRAQVRDLEEKLETLRLKRSE-----DKAKLK-------------ELEKH-------KIQLEQVQEWKSKMQEQQAD 254
Cdd:pfam05483 466 EEHYLKEVEDLKTELEKEKLKNIEltahcDKLLLEnkeltqeasdmtlELKKHqediincKKQEERMLKQIENLEEKEMN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 255 LQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEmaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKGS 334
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE---KQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 335 DGAASSYQLKQLEEQNARLKDALvrmrdlsSSEKQehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDE---LKE 411
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELEL-------ASAKQ---KFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavkLQK 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 412 QVDAALGAE--EMVEMLtDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL--------ELREQLDMagaRVRE 481
Cdd:pfam05483 693 EIDKRCQHKiaEMVALM-EKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELsnikaellSLKKQLEI---EKEE 768
|
330
....*....|...
gi 311893358 482 AQKRVEAAQETVA 494
Cdd:pfam05483 769 KEKLKMEAKENTA 781
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
199-556 |
2.81e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYME 278
Cdd:TIGR00618 436 QQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP-LCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALV 358
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 359 RMRDL----SSSEKQEHVKLQKLMEKKNQELEV--VRQQRERLQEELSQAESTIDEL------KEQVDAALGAEEMVEML 426
Cdd:TIGR00618 595 RLQDLteklSEAEDMLACEQHALLRKLQPEQDLqdVRLHLQQCSQELALKLTALHALqltltqERVREHALSIRVLPKEL 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 427 TDRNLNLEEKVRELRETV-GDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETVADYQQ---T 499
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLtYWKEMLAQCQTLLREletHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqarT 754
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 500 IKKYR---------------QLTAHLQDVNRELTNQQEASVERQQQpppetfdFKIKFAETKAHAKAIEMEL 556
Cdd:TIGR00618 755 VLKARteahfnnneevtaalQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEIGQEIPSDEDIL 819
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-502 |
3.28e-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: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 342 QLKQLEEQNARLKDALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 421
Cdd:COG1579 18 ELDRLEHRLKELPAELAELED-------ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 422 M------VEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDmagARVREAQKRVEAAQETVAD 495
Cdd:COG1579 91 YealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREE 167
|
....*..
gi 311893358 496 YQQTIKK 502
Cdd:COG1579 168 LAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
199-507 |
3.30e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.52 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---EALEAKER 275
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELS---ASSEELSEEKDALLAQRAAHEARIRELEEDIKtltQRVLERET 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADaiEMATLDKEMAEERaESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKD 355
Cdd:pfam07888 151 ELERMKERAK--KAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT-------QVLQLQDTITTLTQ 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 356 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdAALGAEEMVEMLTDRNLNL-E 434
Cdd:pfam07888 221 KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ---ARLQAAQLTLQLADASLALrE 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893358 435 EKVRELRETVGDLEAMNEMNDELQENARETeleLREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLT 507
Cdd:pfam07888 298 GRARWAQERETLQQSAEADKDRIEKLSAEL---QRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQ 367
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-505 |
3.35e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE-QVQEWKSKMQEQQADLQRrLKEARKEAKEALEAKERYMEEMA 281
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaQLSDMKKKLEEDAGTLEA-LEEGKKRLQRELEALTQQLEEKA 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 282 DTADAIEMA------------------------------TLDKEMAEERAESLQQEVE---ALKERVDELTTDLEILKAE 328
Cdd:pfam01576 566 AAYDKLEKTknrlqqelddllvdldhqrqlvsnlekkqkKFDQMLAEEKAISARYAEErdrAEAEAREKETRALSLARAL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 329 IEEKGsdgaassyQLKQLEEQNARLK---DALVRMRDLSSSEKQEHVKLQKLMEkknQELEVVRQQRERLQEELSQAEST 405
Cdd:pfam01576 646 EEALE--------AKEELERTNKQLRaemEDLVSSKDDVGKNVHELERSKRALE---QQVEEMKTQLEELEDELQATEDA 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 406 IDELKEQVDAALGAEEmvEMLTDRNLNLEEKVRELRETVGDLEAmnEMNDELQENA------RETELELRE---QLDMAG 476
Cdd:pfam01576 715 KLRLEVNMQALKAQFE--RDLQARDEQGEEKRRQLVKQVRELEA--ELEDERKQRAqavaakKKLELDLKEleaQIDAAN 790
|
330 340
....*....|....*....|....*....
gi 311893358 477 ARVREAQKRVEAAQETVADYQQTIKKYRQ 505
Cdd:pfam01576 791 KGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
198-361 |
3.63e-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: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRlkrsedkaklKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErym 277
Cdd:COG1579 24 HRLKELPAELAELEDELAALE----------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 eeMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyqLKQLEEQNARLKDAL 357
Cdd:COG1579 91 --YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK----------KAELDEELAELEAEL 158
|
....
gi 311893358 358 VRMR 361
Cdd:COG1579 159 EELE 162
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
199-425 |
3.68e-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: 54.83 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWK-SKMQEQQADLQRRLKEARKEAKEALEAKERYM 277
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMATLDKEMAEERAES--LQQEVEALKERVDELTTD-------LEILKAEIEEKGSDGAASSYQLK---Q 345
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESgkAQAEVERLLGILREVENEkndkdkkIAELESLTLRQMKEQNKKVANIKhgqQ 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 346 LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALgaEEM 422
Cdd:pfam10174 629 EMKKKGAQLLEEARRREDNLADNSQQLQLEELMgalEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL--EEI 706
|
...
gi 311893358 423 VEM 425
Cdd:pfam10174 707 LEM 709
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
284-439 |
4.13e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 284 ADAIEMATLDKEMAEERAESLQQEVEA-LKERVDELTTDLEilkAEIEEKGSDgaassyqLKQLEEQNARLKDALvrmrd 362
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE---KELRERRNE-------LQKLEKRLLQKEENL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 363 lssSEKQEhvklqkLMEKKNQELEVVRQQRERLQEELSQAESTIDEL-KEQVD-----AALGAEEMVEMLTDrnlNLEEK 436
Cdd:PRK12704 99 ---DRKLE------LLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQeleriSGLTAEEAKEILLE---KVEEE 166
|
...
gi 311893358 437 VRE 439
Cdd:PRK12704 167 ARH 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-331 |
4.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKH--KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKER 275
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 276 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 331
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
271-564 |
5.55e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 271 EAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQN 350
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 351 ARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRN 430
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE---LEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 431 LNLEEKVRELRETVGDlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrQLTAHL 510
Cdd:COG4372 167 AALEQELQALSEAEAE-QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA--LLDALE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 311893358 511 QDVNRELTNQQEASVERQQQPPPETFDFKIKFAETKAHAKAIEMELRQMEVAQA 564
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKL 297
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
324-529 |
5.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 324 ILKAEIEEKGSD-----GAASSYQLKQLEEQNARLKDAlvrmrdlsSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEE 398
Cdd:COG4717 46 MLLERLEKEADElfkpqGRKPELNLKELKELEEELKEA--------EEKEEEYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 399 LSQAEsTIDELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEamnEMNDELQENARETELELREQLDMAGAR 478
Cdd:COG4717 118 LEKLE-KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE---ELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 311893358 479 VREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 529
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
203-487 |
6.46e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLET--LRLKRSEDKAKL--KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---------EAKEA 269
Cdd:pfam05483 354 FEATTCSLEELLRTeqQRLEKNEDQLKIitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldekkqfeKIAEE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 270 LEAKERYM--------EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSY 341
Cdd:pfam05483 434 LKGKEQELifllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 342 QLKQLEEqnarlkdalvrmrDLSSSEKQEHVKLQK---LMEKKNQ---ELEVVR----QQRERLQEELSQAESTIDELKE 411
Cdd:pfam05483 514 ELKKHQE-------------DIINCKKQEERMLKQienLEEKEMNlrdELESVReefiQKGDEVKCKLDKSEENARSIEY 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 412 QVdaaLGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEM------NDELQENARET-----ELELREQLDMAGARVR 480
Cdd:pfam05483 581 EV---LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsAENKQLNAYEIkvnklELELASAKQKFEEIID 657
|
....*..
gi 311893358 481 EAQKRVE 487
Cdd:pfam05483 658 NYQKEIE 664
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
295-530 |
7.62e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 295 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKG---------SDGAASSYQLKQLEEQnarlKDALVRMRDLSS 365
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlngleSELAELDEEIERYEEQ----REQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 366 SEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQvdaalgaeemVEMLTDRNLNLEEKVRELRETVG 445
Cdd:PRK02224 241 EVLEEH-------EERREELETLEAEIEDLRETIAETEREREELAEE----------VRDLRERLEELEEERDDLLAEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 446 DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDvnrELTNQQEASV 525
Cdd:PRK02224 304 LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES---ELEEAREAVE 380
|
....*
gi 311893358 526 ERQQQ 530
Cdd:PRK02224 381 DRREE 385
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
265-516 |
8.50e-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: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 265 EAKEALEAKERYMEEMADTADAIEM-ATLDKEMAEERAESLQQEVE-ALKERVDELTTDLEILKAEIEEKGS----DGAA 338
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKnKELFEQYKKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEK 1566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 339 SSYQLKQLEEQNARLKDalvrmrDLSSSEKQEH--VKLQKLMEKKNQELEVVRQQRERLQEELSQAES--------TID- 407
Cdd:TIGR01612 1567 SEQKIKEIKKEKFRIED------DAAKNDKSNKaaIDIQLSLENFENKFLKISDIKKKINDCLKETESiekkissfSIDs 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 408 ---ELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAM-NEMNDE-------LQENARETELELREQLDMAG 476
Cdd:TIGR01612 1641 qdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIeIDVDQHkknyeigIIEKIKEIAIANKEEIESIK 1720
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 477 ARVREAQKRVEAAQET------------------VAD-YQQTIKKYRQLTAHLQDVNRE 516
Cdd:TIGR01612 1721 ELIEPTIENLISSFNTndlegidpnekleeynteIGDiYEEFIELYNIIAGCLETVSKE 1779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-573 |
1.05e-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: 53.52 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAK---------- 267
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvls 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 268 EALEAKERY---MEE----------MADTADAIEMATLDKEMAEERA-------------ESLQQEVEALKERVDELTTD 321
Cdd:TIGR02168 527 ELISVDEGYeaaIEAalggrlqavvVENLNAAKKAIAFLKQNELGRVtflpldsikgteiQGNDREILKNIEGFLGVAKD 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 322 LEILKAEIEEKGS------------DGAASSYQLKQLEEQNARLKDALVRMRDLSS--SEKQEHVKLQKlmekkNQELEV 387
Cdd:TIGR02168 607 LVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITggSAKTNSSILER-----RREIEE 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 388 VRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELE 467
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 468 LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYR----QLTAHLQDVNRELTNQQEASVERQqqpppetfdFKIKFA 543
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkALREALDELRAELTLLNEEAANLR---------ERLESL 829
|
410 420 430
....*....|....*....|....*....|
gi 311893358 544 ETKAHAKAIEMELRQMEVAQANRHMSLLTA 573
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
245-424 |
1.20e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 245 KSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL------ 318
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 319 ----TTDLEILkaeieeKGSDGAAS----SYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEvvrQ 390
Cdd:COG3883 98 sggsVSYLDVL------LGSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE---A 168
|
170 180 190
....*....|....*....|....*....|....
gi 311893358 391 QRERLQEELSQAESTIDELKEQVDAALGAEEMVE 424
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-417 |
1.87e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 237 QLEQVQEWKSKMQEqqadLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD 316
Cdd:COG1579 8 ALLDLQELDSELDR----LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 317 ELTT--DLEILKAEIEekgsdgaassyqlkQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRE- 393
Cdd:COG1579 84 NVRNnkEYEALQKEIE--------------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDe 149
|
170 180
....*....|....*....|....*..
gi 311893358 394 ---RLQEELSQAESTIDELKEQVDAAL 417
Cdd:COG1579 150 elaELEAELEELEAEREELAAKIPPEL 176
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
230-522 |
2.42e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 230 ELEKHKIQLEQVQEWKSKMQEQQadlqrrlKEARKEAKEALEAKERYMEEMADtadaiematldkemaeeRAESLQQEVE 309
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH-------KRARIELEKKASALKRQLDRESD-----------------RNQELQKRIR 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 310 ALKERVDELTtdlEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQEL---- 385
Cdd:pfam05557 59 LLEKREAEAE---EALREQAELNRLKKKYLEALNKKLNEKESQLADA----REVISCLKNELSELRRQIQRAELELqstn 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 386 ---EVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNLNLEEKVRELRETVGDLEAMNEMNDELqenAR 462
Cdd:pfam05557 132 selEELQERLDLLKAKASEAEQLRQNLEKQQSS----------LAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL---AR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 463 ETELE-LREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQE 522
Cdd:pfam05557 199 IPELEkELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQ 259
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
204-487 |
2.60e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ-VQEWKSkmqeQQADLQRRLKEARKEAKEALEAKERYmeemaD 282
Cdd:PRK04863 354 QADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEeVDELKS----QLADYQQALDVQQTRAIQYQQAVQAL-----E 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 TADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKA-----------------------------EIEEK 332
Cdd:PRK04863 425 RAKQLcGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevsrseawdvarELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 333 GSDGAASSYQLKQLE------EQNARLKDALVRMRD---------LSSSE--KQEHVKLQKLMEKKNQELEVVRQQRERL 395
Cdd:PRK04863 505 LREQRHLAEQLQQLRmrlselEQRLRQQQRAERLLAefckrlgknLDDEDelEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 396 QEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQLDMA 475
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALA--------------RLREQSGEEFEDSQDVTEYMQQLLERERELTVERDEL 650
|
330
....*....|..
gi 311893358 476 GARVREAQKRVE 487
Cdd:PRK04863 651 AARKQALDEEIE 662
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
197-472 |
2.66e-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: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKM----QEQQADLQRRLKEARKEAKEALEA 272
Cdd:pfam02463 292 AKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 273 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEI--EEKGSDGAASSYQLKQLEEQN 350
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 351 ARLKDALVRMRDLSSSEKQEHvklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRN 430
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSED-------LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 311893358 431 LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQL 472
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
194-504 |
2.75e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 194 PSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKL-----------KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEA 262
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQSAREKQAAAEEQLvqangelekasREETFARTALKNARLDLRRLFDEKQSEKDKKNKA 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 263 RKEAKEALEAKERYMEEMADTADAIEMATLDkEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAAssyQ 342
Cdd:pfam12128 673 LAERKDSANERLNSLEAQLKQLDKKHQAWLE-EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA---E 748
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 343 LKQLEEQNARLKDAL----VRMRDLSSSEKQEHVKLQKLmEKKNQEL--------EVVRQQRERLQEELSQAESTIDELK 410
Cdd:pfam12128 749 LKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERI-AVRRQEVlryfdwyqETWLQRRPRLATQLSNIERAISELQ 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 411 EQvdaaLGAEEMVEMLTDRNLNLEEKVRE-----LRETVGDLEAMNEMNDELQE--NARETELELREQLDMAGARVREAQ 483
Cdd:pfam12128 828 QQ----LARLIADTKLRRAKLEMERKASEkqqvrLSENLRGLRCEMSKLATLKEdaNSEQAQGSIGERLAQLEDLKLKRD 903
|
330 340
....*....|....*....|.
gi 311893358 484 KRVEAAQETVADYQQTIKKYR 504
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIADHS 924
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
206-421 |
2.80e-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: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD--- 282
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 -------TADAIEMATLDKEMAE--ERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgaassyqlkQLEEQNARL 353
Cdd:COG3883 94 alyrsggSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKA---------------------ELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 354 KDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEE 421
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
192-558 |
3.09e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 192 PLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE 271
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 272 AKERymeemADTadaiematldkemaeERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyQLKQLEEQNA 351
Cdd:COG4913 331 QIRG-----NGG---------------DRLEQLEREIERLERELEERERRRARLEA--------------LLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 352 RLKDALVRMRDlsssekqehvKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgaeemvemLTDRNL 431
Cdd:COG4913 377 ASAEEFAALRA----------EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS----------LERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 432 NLEEKVRELRetvgdleamnemnDELQENARETELELR---EQLDmagarVREAQKRVEAAQETV------------ADY 496
Cdd:COG4913 437 NIPARLLALR-------------DALAEALGLDEAELPfvgELIE-----VRPEEERWRGAIERVlggfaltllvppEHY 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311893358 497 QQTIKKYRQ--LTAHLQdVNRELTNQQEAsveRQQQPPPETFDFKIKFAETKAHAkAIEMELRQ 558
Cdd:COG4913 499 AAALRWVNRlhLRGRLV-YERVRTGLPDP---ERPRLDPDSLAGKLDFKPHPFRA-WLEAELGR 557
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
193-530 |
3.33e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 193 LPSPSKEEE-GLRAQVRDLEEKLETLrlkrsedKAKLKELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALE 271
Cdd:pfam10174 172 LPKKSGEEDwERTRRIAEAEMQLGHL-------EVLLDQKEKENIHLREELHRRNQLQPDPAKT-----KALQTVIEMKD 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 272 AKERYMEEM-ADTADAIEMATLDKEM-AEERAESLQQeVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 349
Cdd:pfam10174 240 TKISSLERNiRDLEDEVQMLKTNGLLhTEDREEEIKQ-MEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 350 NAR-------LKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEM 422
Cdd:pfam10174 319 NSDckqhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV---KERK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 423 VEMLTDRNLNLEEKVR-------ELRETVGDLE--------AMNEMNDELQENARETElELREQldmagaRVREAQKRve 487
Cdd:pfam10174 396 INVLQKKIENLQEQLRdkdkqlaGLKERVKSLQtdssntdtALTTLEEALSEKERIIE-RLKEQ------REREDRER-- 466
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 311893358 488 aaQETVADYQQTIKKYRQLTAHLQdvnRELTNQQEASVERQQQ 530
Cdd:pfam10174 467 --LEELESLKKENKDLKEKVSALQ---PELTEKESSLIDLKEH 504
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
188-475 |
3.75e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 188 GAAPPLPSpskeEEGLRAQVrdleEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMqeqqADLQRRLKEARKEAK 267
Cdd:PRK11281 30 ASNGDLPT----EADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEET----EQLKQQLAQAPAKLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 268 EALEAKERYMEEmADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLe 347
Cdd:PRK11281 98 QAQAELEALKDD-NDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQI- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 348 eqNARLKDALVRMRDLSSSEKQ----EHVKLQKLMEKKNQELEVVRQ-------QRE-------RLQEE----------- 398
Cdd:PRK11281 176 --RNLLKGGKVGGKALRPSQRVllqaEQALLNAQNDLQRKSLEGNTQlqdllqkQRDyltariqRLEHQlqllqeainsk 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 399 -LSQAESTIDELKEQVDAA-LGAEEMVEMLTDRNLNLEEKVrelretvgdLEAMNEMNDELQENareteLELREQLDMA 475
Cdd:PRK11281 254 rLTLSEKTVQEAQSQDEAArIQANPLVAQELEINLQLSQRL---------LKATEKLNTLTQQN-----LRVKNWLDRL 318
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
300-444 |
3.86e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.24 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 300 RAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME 379
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDE------ASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 380 KKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAE-----------EMVEMLTDRNLNLEEkvrELRETV 444
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEvvsrwtgipvgKLLEGEREKLLNLEE---ELHERV 551
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
297-535 |
4.40e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 297 AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGsdgaassyqlKQLEEQNARLKDAlvrmrdlssseKQEHVKLQK 376
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELN----------EEYNELQAELEAL-----------QAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 377 LMEKKNQELEvvrQQRERLQEELSQA------ESTIDELK--EQVDAALGAEEMVEMLTDRNLNLeekVRELRETVGDLE 448
Cdd:COG3883 73 EIAEAEAEIE---ERREELGERARALyrsggsVSYLDVLLgsESFSDFLDRLSALSKIADADADL---LEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 449 AMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQ 528
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
....*..
gi 311893358 529 QQPPPET 535
Cdd:COG3883 227 AAAAAAA 233
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-566 |
5.03e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 5.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETL--RLKRSEDKAKLKELEKHKIQlEQVQEWKSKMQEQQADLQRRLKEarkeaKEALEAKERYMEEm 280
Cdd:pfam01576 66 LAARKQELEEILHELesRLEEEEERSQQLQNEKKKMQ-QHIQDLEEQLDEEEAARQKLQLE-----KVTTEAKIKKLEE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 adtadaiematlDKEMAEERAESLQQEVEALKERVDELTTDLeilkAEIEEKgsdgAASSYQLKQLEEqnARLKDALVRM 360
Cdd:pfam01576 139 ------------DILLLEDQNSKLSKERKLLEERISEFTSNL----AEEEEK----AKSLSKLKNKHE--AMISDLEERL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 361 RdlssSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEmvEMLTDRNlNLEEKVREL 440
Cdd:pfam01576 197 K----KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE--EETAQKN-NALKKIREL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 441 RETVGDLEAMNEMNDELQENARETELELREQLdmagarvrEAQK-RVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTN 519
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEEL--------EALKtELEDTLDTTAAQQELRSKREQEVTELKKALEEETR 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 311893358 520 QQEASVERQQQpppetfdfkikfaetkAHAKAIEMELRQMEVAQANR 566
Cdd:pfam01576 342 SHEAQLQEMRQ----------------KHTQALEELTEQLEQAKRNK 372
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-330 |
5.42e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEdkaKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYM 277
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQ---LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQ 439
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 311893358 278 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE 330
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
201-313 |
5.74e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 201 EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwkSKMQEQQADLQRRLKEARKEAKEALeAKERYMEEM 280
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED--KLLEEAEKEAQQAIKEAKKEADEII-KELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|....*..
gi 311893358 281 ADTA----DAIEMATLDKEMAEERAESLQQEVEALKE 313
Cdd:PRK00409 600 GYASvkahELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
325-560 |
5.84e-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: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 325 LKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRD-------LSSSEKQEHVKLQKLMEKKNQ-------------- 383
Cdd:TIGR02169 644 LEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRErleglkrELSSLQSELRRIENRLDELSQelsdasrkigeiek 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 384 ELEVVRQQRERLQEELSQAESTIDELKEQVDAalgAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN--DELQENA 461
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIEN---VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 462 RETELELREQldmaGARVREAQKRVEAAQETVADYQQTIKkyrqltaHLQDVNRELTNqQEASVERQQQpppetfDFKIK 541
Cdd:TIGR02169 801 SKLEEEVSRI----EARLREIEQKLNRLTLEKEYLEKEIQ-------ELQEQRIDLKE-QIKSIEKEIE------NLNGK 862
|
250
....*....|....*....
gi 311893358 542 FAETKAHAKAIEMELRQME 560
Cdd:TIGR02169 863 KEELEEELEELEAALRDLE 881
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-473 |
6.20e-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: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 246 SKMQEQQADLQRRLKEARKEAKEALEAKERYMEEmadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEIL 325
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADA---RYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 326 KAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST 405
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893358 406 IDELKEQVDAALGAEEMVEMLTDRNLN-LEEKVRELREtvgDLEAMNEMN----DELQEnARETELELREQLD 473
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEeLERELERLER---EIEALGPVNllaiEEYEE-LEERYDFLSEQRE 805
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
193-553 |
7.77e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 193 LPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKE---- 268
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQraml 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 269 --ALEAKERYMEEMAD--------------TADAIEMATLDKE----MAEERAESLQQEVEALKERVDELTTDLEILKAE 328
Cdd:TIGR00606 659 agATAVYSQFITQLTDenqsccpvcqrvfqTEAELQEFISDLQsklrLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSI 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 329 IEEKgsdgaasSYQLKQLEEQNARLKDALVRMR-DLSSSEKQEHVKLQKLMEKKNQELEVVRQQreRLQEELSQAESTID 407
Cdd:TIGR00606 739 IDLK-------EKEIPELRNKLQKVNRDIQRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIME--RFQMELKDVERKIA 809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 408 ELKEQVDAALGAEEMVEMltdrNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE------QLDMAGARVRE 481
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQQV----NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseklQIGTNLQRRQQ 885
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 482 AQKRVEAAQETVADYQQTIKKYR-------QLTAHLQDVNRELTNQQEASVERQQQpppETFDFKIKFAETKAHAKAIE 553
Cdd:TIGR00606 886 FEEQLVELSTEVQSLIREIKDAKeqdspleTFLEKDQQEKEELISSKETSNKKAQD---KVNDIKEKVKNIHGYMKDIE 961
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
209-473 |
9.21e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.85 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 209 DLEEKLETLRLKRSedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYME---------- 278
Cdd:pfam06160 71 EAEELNDKYRFKKA--KKALDEIE------ELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRElrktllanrf 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADTADAIE--MATLDKE---------------------MAEERAESLQQEVEALKERVDELTTD----LEILKAEIEE 331
Cdd:pfam06160 143 SYGPAIDELEkqLAEIEEEfsqfeeltesgdylearevleKLEEETDALEELMEDIPPLYEELKTElpdqLEELKEGYRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 332 KGSDGAASSY-----QLKQLEEQNARLKDALVRMRDLSSSEKQEHVK-----LQKLMEKKNQELEVVRQQRERLQEELSQ 401
Cdd:pfam06160 223 MEEEGYALEHlnvdkEIQQLEEQLEENLALLENLELDEAEEALEEIEeridqLYDLLEKEVDAKKYVEKNLPEIEDYLEH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 402 AESTIDELKEQVD--------------AALGAEEMVEMLTDRNLNLEEKVRE-----------LRETVGDLEAMNEMNDE 456
Cdd:pfam06160 303 AEEQNKELKEELErvqqsytlneneleRVRGLEKQLEELEKRYDEIVERLEEkevayselqeeLEEILEQLEEIEEEQEE 382
|
330 340
....*....|....*....|
gi 311893358 457 LQE---NARETELELREQLD 473
Cdd:pfam06160 383 FKEslqSLRKDELEAREKLD 402
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
198-411 |
1.10e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.97 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKErY 276
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAREDALNQSLKELMHQARTVLKART-E 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEmaeeraESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGaassyqlkqleEQNARLKDA 356
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAEL------SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD-----------EDILNLQCE 824
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 311893358 357 LVrmrdlssseKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 411
Cdd:TIGR00618 825 TL---------VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK 870
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
204-517 |
1.24e-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: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLrLKRS--EDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEaKERYMEEMA 281
Cdd:pfam06160 9 YKEIDELEERKNEL-MNLPvqEELSKVKKLNLTGETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELND-KYRFKKAKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 282 DTADAiematldkemaEERAESLQQEVEALKERVDELTTDLEILKAEIEE---------------KGSDGAAssyqLKQL 346
Cdd:pfam06160 87 ALDEI-----------EELLDDIEEDIKQILEELDELLESEEKNREEVEElkdkyrelrktllanRFSYGPA----IDEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 347 EEQNARLKDALVRMRDLSSSekQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST----IDELKEqvdaalGAEEM 422
Cdd:pfam06160 152 EKQLAEIEEEFSQFEELTES--GDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTElpdqLEELKE------GYREM 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 423 VEM---LTDRNL-----NLEEKVRELRETV--GDLEAMNEMNDELQENAreteLELREQLdmagarvreaQKRVEAAQEt 492
Cdd:pfam06160 224 EEEgyaLEHLNVdkeiqQLEEQLEENLALLenLELDEAEEALEEIEERI----DQLYDLL----------EKEVDAKKY- 288
|
330 340
....*....|....*....|....*
gi 311893358 493 vadYQQTIKKYRQLTAHLQDVNREL 517
Cdd:pfam06160 289 ---VEKNLPEIEDYLEHAEEQNKEL 310
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
251-490 |
1.44e-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: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 251 QQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTtdlEILKAEIE 330
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 331 EKGSDGAASSYQLKQLEEQNarLKDALVRMRDLSSSEKQEhvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 410
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADAD----ADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 411 EQVDAALGAEEMVEMLTDRnlnLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 490
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
199-402 |
1.48e-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: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQ----VQEWKSKMQEQQADLQRRLKEARKEAKEALEake 274
Cdd:pfam00261 37 EVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrkvLENRALKDEEKMEILEAQLKEAKEIAEEADR--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 275 RYMEemadTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEiEEKGSDgAASSYQLkQLEEQNARLK 354
Cdd:pfam00261 114 KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEAS-EEKASE-REDKYEE-QIRFLTEKLK 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 311893358 355 DALVRMRDlsssEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA 402
Cdd:pfam00261 187 EAETRAEF----AERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
206-522 |
1.54e-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: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERymeemadTAD 285
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAEL-------CAA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 AIEMATLDKEMAEERAESLQQeveALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSS 365
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 366 SE---------KQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEST-------IDELKEQVDAALGAEEMVEMLTDR 429
Cdd:TIGR00618 523 PGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcDNRSKEDIPNLQNITVRLQDLTEK 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 430 NLNLEEKVR--------ELRETVGDLEAMNEMNDELQENARE------TELEL-REQLDMAGARVREAQKRVEAAQETVA 494
Cdd:TIGR00618 603 LSEAEDMLAceqhallrKLQPEQDLQDVRLHLQQCSQELALKltalhaLQLTLtQERVREHALSIRVLPKELLASRQLAL 682
|
330 340
....*....|....*....|....*...
gi 311893358 495 DYQQTikKYRQLTAHLQDVNRELTNQQE 522
Cdd:TIGR00618 683 QKMQS--EKEQLTYWKEMLAQCQTLLRE 708
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
198-530 |
1.83e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDK--AKLKELEKHKIQLEQvqewkskmQEQQADLQRRLKEARKEAKEALEA-KE 274
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENRMTLEAIRvtQSDRDLFKHLITEST--------NYVAADYMRHANERRVHLEEALELrRE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 275 RYMEEmadtadaiemATLDKEmaEERAESLQQEVEALKERVDELTTDLEilkaeieekgsdgAASSYQlkQLEEQNARLK 354
Cdd:PRK04863 295 LYTSR----------RQLAAE--QYRLVEMARELAELNEAESDLEQDYQ-------------AASDHL--NLVQTALRQQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 355 DALVRMRDlsssekqEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQ---VDAALgaeemvEMLTDRNL 431
Cdd:PRK04863 348 EKIERYQA-------DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladYQQAL------DVQQTRAI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 432 NLEEKVRELRETvgdlEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHL- 510
Cdd:PRK04863 415 QYQQAVQALERA----KQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVs 490
|
330 340
....*....|....*....|....*..
gi 311893358 511 ----QDVNRELTNQ---QEASVERQQQ 530
Cdd:PRK04863 491 rseaWDVARELLRRlreQRHLAEQLQQ 517
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
203-447 |
1.96e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHkiqleqVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMAD 282
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 tadaiematLDKEMaEERAESLQ---QEVEALKERVDELTTDLEILKaeieekgsDGAASSYQLKQLEEQNARLKDALVR 359
Cdd:PHA02562 246 ---------LVMDI-EDPSAALNklnTAAAKIKSKIEQFQKVIKMYE--------KGGVCPTCTQQISEGPDRITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 360 MRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRErLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTDRNLNLEEKVR 438
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE-LKNKISTNKQSLITLVDKAKKVKAAiEELQAEFVDNAEELAKLQD 386
|
....*....
gi 311893358 439 ELRETVGDL 447
Cdd:PHA02562 387 ELDKIVKTK 395
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
909-1029 |
2.00e-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: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 909 LRAAALRAEIT--DAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA---AKDADERIEKVQTRLDE 983
Cdd:COG1196 213 ERYRELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleLEELELELEEAQAEEYE 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 311893358 984 TQTLLRKKEKDF---EETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1029
Cdd:COG1196 293 LLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-566 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 383 QELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--------EEKVRELRETVGDLEAMNEMN 454
Cdd:COG1196 179 RKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELlllklrelEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 455 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 534
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE---- 334
|
170 180 190
....*....|....*....|....*....|..
gi 311893358 535 tFDFKIKFAETKAHAKAIEMELRQMEVAQANR 566
Cdd:COG1196 335 -LEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
288-524 |
2.08e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 48.03 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 288 EMATLDKEMA--EERAESLQQEVEALKERVDELTT---DLEILKAEIEEkgsdgaassyQLKQLEEQNARLKDALVRMRD 362
Cdd:pfam09728 33 EMKRLQKDLKklKKKQDQLQKEKDQLQSELSKAILaksKLEKLCRELQK----------QNKKLKEESKKLAKEEEEKRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 363 LSSSEKQEHVK-LQKLMEKKNQELEVVRQQRERLQEELsqaESTID--ELKE-QVDAALGAEEMVEMLTDRNLNLEEKVR 438
Cdd:pfam09728 103 ELSEKFQSTLKdIQDKMEEKSEKNNKLREENEELREKL---KSLIEqyELRElHFEKLLKTKELEVQLAEAKLQQATEEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 439 ELRETVGDLEAMNEMNDELQEnARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELT 518
Cdd:pfam09728 180 EKKAQEKEVAKARELKAQVQT-LSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWK 258
|
....*.
gi 311893358 519 NQQEAS 524
Cdd:pfam09728 259 RKWEKS 264
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
210-348 |
2.46e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 210 LEEKLETLRLKRSEDKAK--LKELEK--HKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadtad 285
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKeaEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEE------ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893358 286 aiemaTLDKEMaeERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaaSSYQLKQLEE 348
Cdd:PRK12704 97 -----NLDRKL--ELLEKREEELEKKEKELEQKQQELEKKEEELEEL------IEEQLQELER 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
198-564 |
2.51e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQ-VRDLEEKLETLRLKRSEDkAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKeAKEALEAKERY 276
Cdd:PTZ00121 1123 KAEDARKAEeARKAEDARKAEEARKAED-AKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRK-AEELRKAEDAR 1200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADaiematldkemAEERAESLQQEVEAlkERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEqnARLKDA 356
Cdd:PTZ00121 1201 KAEAARKAE-----------EERKAEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE--ARMAHF 1265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 357 LVRMRDLSSSEKQEHVKLQKLMEKKNqelevvrqqrerlQEELSQAEST--IDELKEQVDAALGAEEmvemLTDRNLNLE 434
Cdd:PTZ00121 1266 ARRQAAIKAEEARKADELKKAEEKKK-------------ADEAKKAEEKkkADEAKKKAEEAKKADE----AKKKAEEAK 1328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 435 EKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ---ETVADYQQTIKKYRQLTAHLQ 511
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEEDKKKAD 1408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 311893358 512 DVNRELTNQQEASVERQQQPPPETFDFKIKFAETKahAKAIEMELRQMEVAQA 564
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKA 1459
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
182-420 |
2.51e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 182 PALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKL-----------ETLRL--------KRSE--DKAK--LKELEKHKIQL 238
Cdd:COG3096 432 PDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsvadaarrqfeKAYELvckiagevERSQawQTARelLRRYRSQQALA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 239 EQVQEWKSKMQE------QQADLQRRLKEARKEAKEALEAKERyMEEMADTADAiEMATLDKEMAE--ERAESLQQEVEA 310
Cdd:COG3096 512 QRLQQLRAQLAEleqrlrQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELEA-QLEELEEQAAEavEQRSELRQQLEQ 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 311 LKERVDELTTdleilKAEIEEKGSDgaassyQLKQLEEQ-NARLKDalvrmrdlsSSEKQEHvkLQKLMEKK---NQELE 386
Cdd:COG3096 590 LRARIKELAA-----RAPAWLAAQD------ALERLREQsGEALAD---------SQEVTAA--MQQLLEREreaTVERD 647
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 311893358 387 VVRQQRERLQ---EELSQAESTID----ELKEQVDAALGAE 420
Cdd:COG3096 648 ELAARKQALEsqiERLSQPGGAEDprllALAERLGGVLLSE 688
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-318 |
2.69e-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: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 193 LPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEwksKMQEQQADLQRRLKEARKEAKEALEA 272
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER---ELAEAEEERLEEELEEEALEEQLEAE 733
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 311893358 273 KERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL 318
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
197-530 |
2.74e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKlkELEKHKIQLEQVQEWKSK--------MQEQQADLQRRLKEARKEAKE 268
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRqlavaeddLQALESELREQLEAGKLEFNE 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 269 ALEAKERYMEEMA---DTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKaeieekgsdgaassyqlKQ 345
Cdd:pfam12128 438 EEYRLKSRLGELKlrlNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR-----------------KR 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 346 LEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEM 425
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELE---LQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGE 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 426 LTDRNLNLEEKVRELRETVGDLEAMNEMNDELQE---NARETELELREQLDMAGARVREAQKRVEAAQETvadYQQTIKK 502
Cdd:pfam12128 578 LNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEalqSAREKQAAAEEQLVQANGELEKASREETFARTA---LKNARLD 654
|
330 340 350
....*....|....*....|....*....|..
gi 311893358 503 YRQLTAHLQD----VNRELTNQQEASVERQQQ 530
Cdd:pfam12128 655 LRRLFDEKQSekdkKNKALAERKDSANERLNS 686
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
200-376 |
2.92e-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: 47.88 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 200 EEGLRAQVRDLEEKLETLRLKR-SEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARK---EAKEALEAKER 275
Cdd:pfam15905 147 EDGTQKKMSSLSMELMKLRNKLeAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKekiEEKSETEKLLE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADAIEMATLD----KEMAEERA---ESLQQEVEA----LKERVDELTTDLEILKAEIEEKgsdgaassyqLK 344
Cdd:pfam15905 227 YITELSCVSEQVEKYKLDiaqlEELLKEKNdeiESLKQSLEEkeqeLSKQIKDLNEKCKLLESEKEEL----------LR 296
|
170 180 190
....*....|....*....|....*....|..
gi 311893358 345 QLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 376
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
244-407 |
2.99e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.17 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 244 WKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAiematLDKEMAEERAESLQQEVEALKERVDELTTDLE 323
Cdd:PRK12705 24 LLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERN-----QQRQEARREREELQREEERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 324 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQehvklQKLMEKKNQELEVVRQQRERLQEELSQAE 403
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEQAR-----KLLLKLLDAELEEEKAQRVKKIEEEADLE 173
|
....
gi 311893358 404 STID 407
Cdd:PRK12705 174 AERK 177
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
200-327 |
3.36e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 200 EEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLE-QVQEWkskmqEQQADLQrrLKEARKE-AKEALEAKERYM 277
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEaEAEKW-----EEKARLA--LEKGREDlAREALERKAELE 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIematldkEMAEERAESLQQEVEALKERVDELTTDLEILKA 327
Cdd:COG1842 98 AQAEALEAQL-------AQLEEQVEKLKEALRQLESKLEELKAKKDTLKA 140
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
210-534 |
3.57e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 48.40 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 210 LEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTAD-AIE 288
Cdd:pfam15818 9 LLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQlATE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 289 MATLDKEMAEERAESLQQEVEALKERVDELTTDLEI--LKAEIEEKGSDGAASSY-----QLKQLEEQNARL----KDAL 357
Cdd:pfam15818 89 IKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLhlLAKEDHHKQLNEIEKYYatitgQFGLVKENHGKLeqnvQEAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 358 VRMRDLSS-SEKQE--------------------HVKLQKLMEKKNQELEVVRQQRERLQEELS---------QAEST-I 406
Cdd:pfam15818 169 QLNKRLSAlNKKQEseicslkkelkkvtsdliksKVTCQYKMGEENINLTIKEQKFQELQERLNmelelnkkiNEEIThI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 407 DELKEQVDAALG-AEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAgarVREAQKR 485
Cdd:pfam15818 249 QEEKQDIIISFQhMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA---LGTWKKH 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 311893358 486 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPE 534
Cdd:pfam15818 326 VEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPE 374
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
908-1029 |
3.58e-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: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 908 ELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDAdERIEKVQTRLDETQTL 987
Cdd:COG1196 252 EAELEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAE 327
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 311893358 988 LRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1029
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-495 |
3.61e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLK-RSEDKAKLKELEKHKIQLEQVQEWKSKMqEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:pfam15921 419 RELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTAQL-ESTKEMLRKVVEELTAKKMTLESSERT 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMAT-------------LDKEMAE--------ERAESLQQEVEALKERVDELTTDLEILKAEIE----- 330
Cdd:pfam15921 498 VSDLTASLQEKERAIeatnaeitklrsrVDLKLQElqhlknegDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtql 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 331 --EKGSDGAASSYQLKQLEEQ--NARL-----------KDALVRMRDLSSSEKQ-EHVKLQKLMEKKNQELEVVRQQRER 394
Cdd:pfam15921 578 vgQHGRTAGAMQVEKAQLEKEinDRRLelqefkilkdkKDAKIRELEARVSDLElEKVKLVNAGSERLRAVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 395 LQEELSQAESTIDELKEQVDAAL-----GAEEMvEMLTDR-NLNLEEKVRELRETVGDLEAMNEMNDelqeNARETELEL 468
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKrnfrnKSEEM-ETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDG----HAMKVAMGM 732
|
330 340
....*....|....*....|....*..
gi 311893358 469 REQLDMAGARVREAQKRVEAAQETVAD 495
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTN 759
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
203-520 |
3.61e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.20 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKA---KLKELEKHKIQLEQVQEWKSKMQEQQA---DLQRRLKEAR------------- 263
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKNSKSELAripELEKELERLRehnkhlnenienk 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 264 ---KEAKEALEAKERYMEEMADTADAIEM--------------------ATLDKEMA-EERAESLQQEVEALKERVDELT 319
Cdd:pfam05557 224 lllKEEVEDLKRKLEREEKYREEAATLELekekleqelqswvklaqdtgLNLRSPEDlSRRIEQLQQREIVLKEENSSLT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 320 TDLEILKAEIEEKGSDGAAssyQLKQLEEQNARLK--DALVRM-----------RDL----------------SSSEKQE 370
Cdd:pfam05557 304 SSARQLEKARRELEQELAQ---YLKKIEDLNKKLKrhKALVRRlqrrvllltkeRDGyrailesydkeltmsnYSPQLLE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 371 HVK-LQKLMEKKNQELEVVRQQRERLQEEL-------SQAESTIDELKEQVDAA--LGAEEMVEMLTDRNLNLEEKVREL 440
Cdd:pfam05557 381 RIEeAEDMTQKMQAHNEEMEAQLSVAEEELggykqqaQTLERELQALRQQESLAdpSYSKEEVDSLRRKLETLELERQRL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 441 RETVGDLEA---------MNEMND----ELQEN----ARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTI--- 500
Cdd:pfam05557 461 REQKNELEMelerrclqgDYDPKKtkvlHLSMNpaaeAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTstm 540
|
410 420
....*....|....*....|..
gi 311893358 501 --KKYRQLTAHLQDvnRELTNQ 520
Cdd:pfam05557 541 nfKEVLDLRKELES--AELKNQ 560
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
253-528 |
3.78e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 253 ADLQRRLKEArKEAKEALEAKERYMEEMADTadaieMATLDK-EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE 331
Cdd:PRK11281 39 ADVQAQLDAL-NKQKLLEAEDKLVQQDLEQT-----LALLDKiDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 332 KgSDGAASSYQLKQLEEQNARLKDALvrmrdlsssekQEhvkLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 411
Cdd:PRK11281 113 E-TRETLSTLSLRQLESRLAQTLDQL-----------QN---AQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 412 QVDAALGAEEmvemltdrNLNLEEKVRELRETVGdLEAMNEMN-DELQENARETELeLREQLDMAGARVREAQKRVEAAQ 490
Cdd:PRK11281 178 LLKGGKVGGK--------ALRPSQRVLLQAEQAL-LNAQNDLQrKSLEGNTQLQDL-LQKQRDYLTARIQRLEHQLQLLQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 311893358 491 ETV-----ADYQQTIKKYRQltahLQDVNRELTN---QQEASVERQ 528
Cdd:PRK11281 248 EAInskrlTLSEKTVQEAQS----QDEAARIQANplvAQELEINLQ 289
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-471 |
3.85e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLR---------LKRSEDKAKLKeLEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEake 268
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRdelesvreeFIQKGDEVKCK-LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ--- 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 269 aLEAKERYMEEMADTADAIEmatldkemAEERAESLQQEVEALKerVDELTTDLEILKAEIEEKgSDGAASSYQLKQLEE 348
Cdd:pfam05483 603 -IENKNKNIEELHQENKALK--------KKGSAENKQLNAYEIK--VNKLELELASAKQKFEEI-IDNYQKEIEDKKISE 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 349 QNarlkdaLVRMRDLSSSEKQEHVKLQKLMEKKNQE--------LEVVRQQRERLQEElSQAESTIDELKEQVDAALGAE 420
Cdd:pfam05483 671 EK------LLEEVEKAKAIADEAVKLQKEIDKRCQHkiaemvalMEKHKHQYDKIIEE-RDSELGLYKNKEQEQSSAKAA 743
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 311893358 421 EMVEMLTDRNlnleekvrELRETVGDLEAMNEMNDELQENARETELELREQ 471
Cdd:pfam05483 744 LEIELSNIKA--------ELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
218-501 |
3.90e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 218 RLKRSEDKAKL---KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDK 294
Cdd:COG4372 3 RLGEKVGKARLslfGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 295 EMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKL 374
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK-------ERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 375 QKLMEKKNQELEVVRQQRERLQEELSQAestidELKEQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMN 454
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQ-----ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 311893358 455 DELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIK 501
Cdd:COG4372 231 LGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
199-412 |
4.09e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKH--KIQLEQVqewksKMQEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARvsDLELEKV-----KLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMAtldKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDG-------------AASSYQ 342
Cdd:pfam15921 666 RNELNSLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmEGSDGhamkvamgmqkqiTAKRGQ 742
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 311893358 343 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLME----KKNQ---ELEVVRQQRERLQEELSQAESTIDELKEQ 412
Cdd:pfam15921 743 IDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELStvatEKNKmagELEVLRSQERRLKEKVANMEVALDKASLQ 819
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-412 |
4.23e-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: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRlkrsedkaklKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEaLEAKERY 276
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIE----------KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-LEAQLRE 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEemadtaDAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyqLKQLEEQNARLKDA 356
Cdd:TIGR02169 901 LE------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS--------LEDVQAELQRVEEE 966
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 357 LVRMRDLSSSEKQEHvklqKLMEKKNQELEvvrQQRERLQEELSQAESTIDELKEQ 412
Cdd:TIGR02169 967 IRALEPVNMLAIQEY----EEVLKRLDELK---EKRAKLEEERKAILERIEEYEKK 1015
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
259-414 |
4.31e-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: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 259 LKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEeraesLQQEVEALKERVDElttdleiLKAEIEEKgsdgaa 338
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR-----LEEQVERLEAEVEE-------LEAELEEK------ 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 339 ssyqlkqlEEQNARLKDALVRMRdlsSSEKQEHvklqklmeKKNQELEVVRQQRERLQEELSQAESTIDELKEQVD 414
Cdd:COG2433 440 --------DERIERLERELSEAR---SEERREI--------RKDREISRLDREIERLERELEEERERIEELKRKLE 496
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
910-1019 |
4.98e-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: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 910 RAAALRAEITDAE----GLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSA------------------- 966
Cdd:COG1579 25 RLKELPAELAELEdelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealqkeieslkrr 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 967 -------AKDADERIEKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQR 1019
Cdd:COG1579 105 isdledeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-451 |
5.71e-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: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMAD 282
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEK---KLKNLEAELLQLQEDLAASERARRQAQQERDEL--ADEIASGASGK 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 TADAIEMATLDKEMA--EERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRM 360
Cdd:pfam01576 878 SALQDEKRRLEARIAqlEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEM 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 361 RDLSSSEKQEHV-----KLQKLMEKKNQEL-------EVVRQQRERLQEELSQAES---TIDELKEQVDAALGA------ 419
Cdd:pfam01576 958 EGTVKSKFKSSIaaleaKIAQLEEQLEQESrerqaanKLVRRTEKKLKEVLLQVEDerrHADQYKDQAEKGNSRmkqlkr 1037
|
250 260 270
....*....|....*....|....*....|....
gi 311893358 420 --EEMVEMLTDRNLNLEEKVRELRETVGDLEAMN 451
Cdd:pfam01576 1038 qlEEAEEEASRANAARRKLQRELDDATESNESMN 1071
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
198-522 |
5.96e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 46.95 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRlkRSEDKAKLKELEKHKIQLEQVQE-WKSKMQEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELR--RRDQKRQETLERERRLLLQQSQEqWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAESLQQEvEALKERVDELTTDLEILKAEIEEKGSDgAASSYQLKQLEEQNarlkda 356
Cdd:pfam15558 96 WREQAEDQENQRQEKLERARQEAEQRKQCQE-QRLKEKEEELQALREQNSLQLQERLEE-ACHKRQLKEREEQK------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 357 lvRMRDLSSSEKQEHVKLQKLMEKKNQElevvrqqrERLQEELSQaestidELKEQVdaalgAEEMVEMLtdrnlnLEEK 436
Cdd:pfam15558 168 --KVQENNLSELLNHQARKVLVDCQAKA--------EELLRRLSL------EQSLQR-----SQENYEQL------VEER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 437 VRELREtvgdlEAMNEmNDELQENARETELELREQLDMAGARVREAQKRVE----AAQETVADYQQTIKKYRQLTAHLQD 512
Cdd:pfam15558 221 HRELRE-----KAQKE-EEQFQRAKWRAEEKEEERQEHKEALAELADRKIQqarqVAHKTVQDKAQRARELNLEREKNHH 294
|
330
....*....|
gi 311893358 513 VNRELTNQQE 522
Cdd:pfam15558 295 ILKLKVEKEE 304
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
209-537 |
6.29e-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: 47.66 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 209 DLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEW---KSKMQEQQADLQRRLKEARKEAKEaLEAKERYMEEmadTAD 285
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltqKREAQEEQLKKQQLLKQLRARIEE-LRAQEAVLEE---TQE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 AIEMATLDKEMAEEraeslQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlkdalvrmRDLSS 365
Cdd:TIGR00618 285 RINRARKAAPLAAH-----IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-----------RRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 366 SEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAES-TIDELKEQVDAALGAEEMVEMLTDRNLNLEEkvRELRETV 444
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQkTTLTQKLQSLCKELDILQREQATIDTRTSAF--RDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 445 GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEAS 524
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330
....*....|...
gi 311893358 525 VERQQQPPPETFD 537
Cdd:TIGR00618 507 CGSCIHPNPARQD 519
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
197-403 |
6.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRlkrsedkaklkelEKHKIqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFR-------------QKNGL--VDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAE--SLQQEVEALKER-------VDELTTDLEILKAEIEEKGSDGAASSY-QLKQL 346
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILASLEaELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 311893358 347 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLmekkNQELEVVRQQRERLQEELSQAE 403
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRL----EREVEVARELYESLLQRLEEAR 378
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
211-519 |
6.56e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 211 EEKLETLRLKRSE----------DKAKLKELEKHKIQL--EQVQEW--------KSKMQEQQADLQRRLKEARKEAKEAL 270
Cdd:COG3096 784 EKRLEELRAERDElaeqyakasfDVQKLQRLHQAFSQFvgGHLAVAfapdpeaeLAALRQRRSELERELAQHRAQEQQLR 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 271 EAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELT------TDLEILKAEIEEKGSDGAASSYQL 343
Cdd:COG3096 864 QQLDQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQAFIQqhgkalAQLEPLVAVLQSDPEQFEQLQADY 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 344 KQLEEQNARLKDALVRMRDLssSEKQEHVKLQKL--MEKKNQELEvvrqqrERLQEELSQAESTIDELKEQVDAALG-AE 420
Cdd:COG3096 944 LQAKEQQRRLKQQIFALSEV--VQRRPHFSYEDAvgLLGENSDLN------EKLRARLEQAEEARREAREQLRQAQAqYS 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 421 EMVEMLTDRNLNLEEKVRELRETVGDLEAMN-EMNDELQENARETELELREQLDMAGARVREAQK---RVEAAQETVAdy 496
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQELEQELEELGvQADAEAEERARIRRDELHEELSQNRSRRSQLEKqltRCEAEMDSLQ-- 1093
|
330 340
....*....|....*....|...
gi 311893358 497 qqtiKKYRQLTAHLQDVNRELTN 519
Cdd:COG3096 1094 ----KRLRKAERDYKQEREQVVQ 1112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-561 |
7.47e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRsedkaklkelekhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 277
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMER-----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEieekgSDGAASSYQLKQLEEQNARLKDAL 357
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR-----SLGSAISKILRELDTEISYLKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 358 VRMRDlsssekqehvKLQKLMEKKNQELEVVRQQ-RERLQEELSQAESTIDELKEQVDAALGA--------EEMVEMLTD 428
Cdd:pfam15921 241 FPVED----------QLEALKSESQNKIELLLQQhQDRIEQLISEHEVEITGLTEKASSARSQansiqsqlEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 429 RNLNLEEKVRELRETVGDLEAmnemndELQENARETE---LELREQLDMAGARVREAqkRVEAAQETvadyQQTIKKYRQ 505
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRS------ELREAKRMYEdkiEELEKQLVLANSELTEA--RTERDQFS----QESGNLDDQ 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 506 LTAHLQDVNREltnQQEASVERQQQppPETFDFKIKFAETKAHAKAiEMELRQMEV 561
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 ... |
199-530 |
7.73e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDK--AKLKELEKHKiqleQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE----------IEEKGSDGAASSYQLK-- 344
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlqrsmstqkaLEEDLQIATKTICQLTee 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 345 ---QLEEQN-ARLKDALVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK---------- 410
Cdd:pfam05483 333 keaQMEELNkAKAAHSFV-----VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkevel 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 411 EQVDAALGAEemvEMLTDRNLNLEEKVRELR----ETVGDLEAM-NEMND-ELQENARETELE--LREQLDMAGARVREA 482
Cdd:pfam05483 408 EELKKILAED---EKLLDEKKQFEKIAEELKgkeqELIFLLQAReKEIHDlEIQLTAIKTSEEhyLKEVEDLKTELEKEK 484
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 311893358 483 QKRVeaaqETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:pfam05483 485 LKNI----ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
198-468 |
8.81e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 46.77 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKA---------------KLKELEKHKI-----------QLEQVQEWKSKMQEQ 251
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKEssskpselalnemieKLKKEIDLEYteaviamglqeRLENLREEFSKANSQ 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 252 QADLQRRLKEA----RKEAKEALEAKERYmEEMADTADAIEMATLDKEMAE--ERAESLQQEV-EALKERVD--ELTTDL 322
Cdd:PLN03229 502 DQLMHPVLMEKieklKDEFNKRLSRAPNY-LSLKYKLDMLNEFSRAKALSEkkSKAEKLKAEInKKFKEVMDrpEIKEKM 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 323 EILKAEIEEKGS------DGAASSYQLKQLEEQNARLKDAL---------VRMRDLSSSEKQE----HVKLQKLMEKKNQ 383
Cdd:PLN03229 581 EALKAEVASSGAssgdelDDDLKEKVEKMKKEIELELAGVLksmglevigVTKKNKDTAEQTPppnlQEKIESLNEEINK 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 384 ELEVV------RQQRERLQEELSQAESTID------------ELKEQVDAALGAEEMVEmltdRNLNLEEKVRELRETVG 445
Cdd:PLN03229 661 KIERVirssdlKSKIELLKLEVAKASKTPDvtekekiealeqQIKQKIAEALNSSELKE----KFEELEAELAAARETAA 736
|
330 340
....*....|....*....|...
gi 311893358 446 DLEAMNEMNDELQENARETELEL 468
Cdd:PLN03229 737 ESNGSLKNDDDKEEDSKEDGSRV 759
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
266-419 |
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 311893358 266 AKEALEAKERYMEEMADTADAIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaas 339
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATDDEELEEakktikALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEK-------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 340 syQLKQLEEQNARLKDALvrMRDLSSSEKQEHVKLQKLMEKKNQEL------------------EVVRQQRERLQEELSQ 401
Cdd:cd22656 154 --DQTALETLEKALKDLL--TDEGGAIARKEIKDLQKELEKLNEEYaaklkakidelkaliaddEAKLAAALRLIADLTA 229
|
170
....*....|....*...
gi 311893358 402 AESTIDELKEQVDAALGA 419
Cdd:cd22656 230 ADTDLDNLLALIGPAIPA 247
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
203-472 |
9.97e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 46.07 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKL-----KELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 277
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRLyslyeKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMATLDKEMAEERAESLQQEVEALK----ERVDELTTDLeilkaeieekgsdgaasSYQLKQLEEQNARL 353
Cdd:pfam00038 103 NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheEEVRELQAQV-----------------SDTQVNVEMDAARK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 354 KDALVRMRDLSSS-EKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDaALGAEemVEMLTDRNLN 432
Cdd:pfam00038 166 LDLTSALAEIRAQyEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQ-SLEIE--LQSLKKQKAS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 311893358 433 LEEKVRELRET-VGDLEAMNEMNDELQENARETELELREQL 472
Cdd:pfam00038 243 LERQLAETEERyELQLADYQELISELEAELQETRQEMARQL 283
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
206-575 |
1.04e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 206 QVRDLEEKLETLRLKRSedKAKLKELEkhkiqlEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYmEEM----- 280
Cdd:PRK04778 87 QLFEAEELNDKFRFRKA--KHEINEIE------SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLY-RELrksll 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 ------ADTADAIE--MATLDKEMAEerAESLQQE---------VEALKERVDELTTDLEILKAEIEEKGSDGAAssyQL 343
Cdd:PRK04778 158 anrfsfGPALDELEkqLENLEEEFSQ--FVELTESgdyveareiLDQLEEELAALEQIMEEIPELLKELQTELPD---QL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 344 KQLEEQNARLKDA---------LVRMRDLssseKQEHVKLQKLMEkkNQELEVVRQQRERLQEELSQ------------- 401
Cdd:PRK04778 233 QELKAGYRELVEEgyhldhldiEKEIQDL----KEQIDENLALLE--ELDLDEAEEKNEEIQERIDQlydilerevkark 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 402 -AESTIDELKEQVDAAlgaEEMVEML---TDR-------NLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE 470
Cdd:PRK04778 307 yVEKNSDTLPDFLEHA---KEQNKELkeeIDRvkqsytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 471 QLDMAGARVREAQKRVEAAQETVADY-------QQTIKKYRQLtahLQDVNREltnqqeasVERQQQPP-PEtfDFKIKF 542
Cdd:PRK04778 384 ELEEILKQLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNK---LHEIKRY--------LEKSNLPGlPE--DYLEMF 450
|
410 420 430
....*....|....*....|....*....|....*
gi 311893358 543 AETKAHAKAIEMEL--RQMEVAQANRHMSLLTAFM 575
Cdd:PRK04778 451 FEVSDEIEALAEELeeKPINMEAVNRLLEEATEDV 485
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
199-530 |
1.30e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERYME 278
Cdd:PRK04863 559 LQEELEARLESLSESVSEARERRMALRQQLEQLQ------ARIQRLAARAPAWLA-AQDALARLREQSGEEFEDSQDVTE 631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADTADAIEMATLDKEMAEERAESLQQEVE--------------ALKER-----VDELTTDLEILKAEIEEKGSDGAAS 339
Cdd:PRK04863 632 YMQQLLERERELTVERDELAARKQALDEEIErlsqpggsedprlnALAERfggvlLSEIYDDVSLEDAPYFSALYGPARH 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 340 -------SYQLKQLEEQNARLKDALV------RMRD-LSSSEKQEHVKLQKLMEK-----------------KNQELEVV 388
Cdd:PRK04863 712 aivvpdlSDAAEQLAGLEDCPEDLYLiegdpdSFDDsVFSVEELEKAVVVKIADRqwrysrfpevplfgraaREKRIEQL 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 389 RQQRERLQEELSQAESTIDELK---EQVDAALGAEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQ---ENAR 462
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQrlhQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRsqlEQAK 871
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 463 ETELELREQLDMA--------GARVREAQKRVEAAQET---VADYQQTIKKYRQLTAHLQ---DVNRELTNQQEASVERQ 528
Cdd:PRK04863 872 EGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQAQQTQ 951
|
..
gi 311893358 529 QQ 530
Cdd:PRK04863 952 RD 953
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
237-332 |
1.48e-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: 43.24 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 237 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTA--DAIEMATLDKEMAEERAESLQQE-VEALKE 313
Cdd:COG0711 39 GLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAkaEAEAEAERIIAQAEAEIEQERAKaLAELRA 118
|
90 100
....*....|....*....|.
gi 311893358 314 RVDELTTDL--EILKAEIEEK 332
Cdd:COG0711 119 EVADLAVAIaeKILGKELDAA 139
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
375-566 |
1.50e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 375 QKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAAlgaEEMVEMLTDRNLNLEEKVRELRETVGDLEAMNEmn 454
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKEIA-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 455 dELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQpppe 534
Cdd:COG4942 94 -ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE---- 168
|
170 180 190
....*....|....*....|....*....|..
gi 311893358 535 tfdFKIKFAETKAHAKAIEMELRQMEVAQANR 566
Cdd:COG4942 169 ---LEAERAELEALLAELEEERAALEALKAER 197
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-529 |
1.56e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 232 EKHKIQLEQVQEWkskMQEQQAdLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMATLDKE-MAEERAESLQQEveA 310
Cdd:pfam12128 214 PKSRLNRQQVEHW---IRDIQA-IAGIMKIRPEFTKLQQEFNTLESAEL-------RLSHLHFGyKSDETLIASRQE--E 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 311 LKERVDELTTDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDAlvrmrDLSSSEKQEHVKLqkLMEKKNQELEVVRQ 390
Cdd:pfam12128 281 RQETSAELNQLLRTLDDQWKEK-------------RDELNGELSAA-----DAAVAKDRSELEA--LEDQHGAFLDADIE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 391 QRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL--EEKVRELRETVGDLEAMNEMNDELQENARET---- 464
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDlqal 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 465 ELELREQLDMAGARVREAQKRVEAAQET----VADYQQTIKKYRQLTAHLQDVN--RELTNQQEASVERQQ 529
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGElklrLNQATATPELLLQLENFDERIEraREEQEAANAEVERLQ 491
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
389-549 |
1.57e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 389 RQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnLNL-------EEKVRELREtvgDLEAMNEMNDElQENA 461
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDH-LNLvqtalrqQEKIERYQE---DLEELTERLEE-QEEV 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 462 REtelELREQLDMAGARVREAQKRVEAAQETVADYQQTIK-------KYRQLTAHLQDVNR-----ELT-----NQQEAS 524
Cdd:COG3096 370 VE---EAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDvqqtraiQYQQAVQALEKARAlcglpDLTpenaeDYLAAF 446
|
170 180
....*....|....*....|....*
gi 311893358 525 VERQQQPPPETFDFKIKFAETKAHA 549
Cdd:COG3096 447 RAKEQQATEEVLELEQKLSVADAAR 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
286-515 |
1.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 286 AIEMATLDKEMAE------ERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaassyqLKQLEEQNARLKDALVR 359
Cdd:COG4717 45 AMLLERLEKEADElfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQEE-----------LEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 360 MRdlsssekQEHVKLQKLmekknQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRnlnLEEKVRE 439
Cdd:COG4717 114 LR-------EELEKLEKL-----LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE---LAELQEE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 440 LRETVgdleamnemnDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNR 515
Cdd:COG4717 179 LEELL----------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
226-354 |
1.95e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.63 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 226 AKLKELEKHKIQLEQVQEwkskmqEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLdkemAEERAESLQ 305
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAA------DAEAQLQKLQEDLEKQAEIAREAQQNYERELVLHAEDIKALQA----LREELNELK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 311893358 306 QEVEALKERVDELTTDLEILKAEIEEkgsdgaassyQLKQLEEQNARLK 354
Cdd:pfam07926 71 AEIAELKAEAESAKAELEESEESWEE----------QKKELEKELSELE 109
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
197-315 |
2.03e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEE-EGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAker 275
Cdd:COG0542 438 SFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--- 514
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 311893358 276 ymeemADTADAIEMAT---LDKeMAEERAESLQQEVEALKERV 315
Cdd:COG0542 515 -----EDIAEVVSRWTgipVGK-LLEGEREKLLNLEEELHERV 551
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
210-325 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 210 LEEKLETLrlkrsedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 277
Cdd:COG0216 2 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKKLLEDIEEA-------- 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 311893358 278 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 325
Cdd:COG0216 63 KELLEEESDPEM----REMAKE-------ELEELEARLEELEEELKIL 99
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
239-477 |
2.11e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 239 EQVQEWKSKMQEQQAdLQRRLKEARKEAKEALEAKERY---MEEMaDTAD--AIEMATLDKEM-----AEERAESLQQEV 308
Cdd:COG0497 155 ELLEEYREAYRAWRA-LKKELEELRADEAERARELDLLrfqLEEL-EAAAlqPGEEEELEEERrrlsnAEKLREALQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 309 EALKERVDELTTDLEILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMRDLSSS------------EKQEHV---- 372
Cdd:COG0497 233 EALSGGEGGALDLLGQALRALER------LAEYD-PSLAELAERLESALIELEEAASElrryldslefdpERLEEVeerl 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 373 -KLQKLMEKKNQELEVVRQQRERLQEELSQ---AESTIDELKEQVDAALGAeemvemltdrnlnLEEKVREL----RETV 444
Cdd:COG0497 306 aLLRRLARKYGVTVEELLAYAEELRAELAElenSDERLEELEAELAEAEAE-------------LLEAAEKLsaarKKAA 372
|
250 260 270
....*....|....*....|....*....|....*...
gi 311893358 445 GDLEAmnEMNDELQ----ENAR-ETELELREQLDMAGA 477
Cdd:COG0497 373 KKLEK--AVTAELAdlgmPNARfEVEVTPLEEPGPNGA 408
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
210-460 |
2.17e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 210 LEEKLETLRLKRSEDKAKLKELekhKIQLEQVQEWKSKMQEQQADLQRRLKEarkeaKEA-LEAKERYMEEMAD--TADA 286
Cdd:pfam10174 308 LQTKLETLTNQNSDCKQHIEVL---KESLTAKEQRAAILQTEVDALRLRLEE-----KESfLNKKTKQLQDLTEekSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 287 IEMATLdKEM---AEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA---RLKDALVRM 360
Cdd:pfam10174 380 GEIRDL-KDMldvKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSekeRIIERLKEQ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 361 RDLSSSEKQEHVklqklmEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA-ALGAEEMVEMLTDRNLNLEEKVRE 439
Cdd:pfam10174 459 REREDRERLEEL------ESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlASSGLKKDSKLKSLEIAVEQKKEE 532
|
250 260
....*....|....*....|.
gi 311893358 440 LRETVGDLEAMNEMNDELQEN 460
Cdd:pfam10174 533 CSKLENQLKKAHNAEEAVRTN 553
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
203-421 |
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 311893358 203 LRAQVRDLEEKLETL--RLKRSEDKaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlkEARKEAKEALEAKERYMEEM 280
Cdd:pfam12128 313 ADAAVAKDRSELEALedQHGAFLDA----DIETAAADQEQLPSWQSELENLEERL-----KALTGKHQDVTAKYNRRRSK 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 ADTADAIEMATLDKEMA---EERAESLQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLK-QLEEQNARLKDA 356
Cdd:pfam12128 384 IKEQNNRDIAGIKDKLAkirEARDRQLAVAEDDLQALESELREQLEAGKLEFNE-------EEYRLKsRLGELKLRLNQA 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311893358 357 LVrmrdlSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAestiDELKEQVDAALGAEE 421
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 ... |
302-412 |
2.46e-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: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 302 ESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGAASSYQlKQLEEQNARLKdALVRMRDLSSSEKQEHVKLQKLME 379
Cdd:pfam07926 4 SSLQSEIKRLKEEAADAEAQLQKLQEDLEKqaEIAREAQQNYE-RELVLHAEDIK-ALQALREELNELKAEIAELKAEAE 81
|
90 100 110
....*....|....*....|....*....|....*..
gi 311893358 380 KKNQELEVVR----QQRERLQEELSQAESTIDELKEQ 412
Cdd:pfam07926 82 SAKAELEESEesweEQKKELEKELSELEKRIEDLNEQ 118
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
211-482 |
2.49e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 211 EEKLETLRLKRSEDKAKLKElEKHKIQLEqvqewKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadtadaiEMA 290
Cdd:PRK01156 464 EEKSNHIINHYNEKKSRLEE-KIREIEIE-----VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-------RAD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 291 TLDKEMAEERAESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSY-----QLKQLEEQNARLKDALVRMRDL-- 363
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRYKSL--KLEDLDSKRTSWLNALAVISLidietNRSRSNEIKKQLNDLESRLQEIei 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 364 ---------SSSEKQEHVKLQKLMEKKNqELEVVRQQRERLQEelsqaesTIDELKEQVDAALGAEEMVEMLTDRNLNLE 434
Cdd:PRK01156 609 gfpddksyiDKSIREIENEANNLNNKYN-EIQENKILIEKLRG-------KIDNYKKQIAEIDSIIPDLKEITSRINDIE 680
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 435 EKVRELRETVGDLEA---------------MNEMNDELQEnaRETELELREQLDMAGA---RVREA 482
Cdd:PRK01156 681 DNLKKSRKALDDAKAnrarlestieilrtrINELSDRIND--INETLESMKKIKKAIGdlkRLREA 744
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
373-530 |
2.53e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 373 KLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEmltdrnlNLEEKVRELRETVGDLEAMNE 452
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-------ELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 453 MNDELQENAretelELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:COG4717 127 LLPLYQELE-----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
197-523 |
2.62e-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: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEE-EGLRAQVRDLEEKLETLRLKRSEDKAKLK--------ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKE--ARKE 265
Cdd:pfam05701 192 TKESlESAHAAHLEAEEHRIGAALAREQDKLNWEkelkqaeeELQRLNQQLLSAKDLKSKLETASALLLDLKAElaAYME 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 266 AKEALEAKERYMEEMADTADAIEMATLDKEMAEERA--ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQL 343
Cdd:pfam05701 272 SKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKAniEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 344 KQLEEQNARLKD--ALVRMRDLSSSEKQehVKLQKLMEKKNQELE----VVRQQRERL---QEELSQA-------ESTID 407
Cdd:pfam05701 352 SSLEAELNRTKSeiALVQAKEKEAREKM--VELPKQLQQAAQEAEeaksLAQAAREELrkaKEEAEQAkaaastvESRLE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 408 ELKEQVDAALGAEEMVemLTDRNLNLEEKVRELRETVGDLEAM----NEMNDELQENARETElelreqlDMAGARVREAQ 483
Cdd:pfam05701 430 AVLKEIEAAKASEKLA--LAAIKALQESESSAESTNQEDSPRGvtlsLEEYYELSKRAHEAE-------ELANKRVAEAV 500
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 311893358 484 KRVEAAQETvadyqqtikKYRQLtAHLQDVNRELTNQQEA 523
Cdd:pfam05701 501 SQIEEAKES---------ELRSL-EKLEEVNREMEERKEA 530
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
324-519 |
3.00e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 324 ILKAEIEEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHvklQKLMEKKNQELEVVRQQRERLQEELSQAE 403
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARK---QNKYDELVEEAKTIKAEIEELTDELLNLV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 404 STIDE--------------LKEQVDAALG--------------------AEEMVEMLTDRNLNLEEKVRELRETVGDLEA 449
Cdd:PHA02562 248 MDIEDpsaalnklntaaakIKSKIEQFQKvikmyekggvcptctqqiseGPDRITKIKDKLKELQHSLEKLDTAIDELEE 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311893358 450 -MNEMND---ELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKKyrqLTAHLQDVNRELTN 519
Cdd:PHA02562 328 iMDEFNEqskKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK---LQDELDKIVKTKSE 397
|
|
| CASP_C |
pfam08172 |
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ... |
297-438 |
3.21e-04 |
|
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.
Pssm-ID: 462392 [Multi-domain] Cd Length: 247 Bit Score: 43.81 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 297 AEERAESLQQEVEALKERVDELTTDLEILKAEIEE--KGSDGA-ASSYQLKQLEEQNARLKDALVrmrdLSSSEKQEHVK 373
Cdd:pfam08172 2 LQEELSSLNAELEEQQELNAKLENDLLKVQDEASNafSFNDASsAGSGVSRYPPSGGRRSPTSSI----ISGFEPSESSS 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 374 LQKlmekkNQELEVVRQQRER-------LQEELSQAESTIDELKEQVDAalgaeemveMLTDrNLNLEEKVR 438
Cdd:pfam08172 78 SSD-----SSILPIVTSQRDRfrqrnaeLEEELRKQFETISSLRQEIAS---------LQKD-NLKLYEKTR 134
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
385-560 |
3.69e-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: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 385 LEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNLNL-----EEKVRELRETVGDLEAMNEMNDELQE 459
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALlvlrlEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 460 NARETELELrEQLDmagARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPP------- 532
Cdd:TIGR02168 261 ELQELEEKL-EELR---LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELEskldela 336
|
170 180 190
....*....|....*....|....*....|....*
gi 311893358 533 -------PETFDFKIKFAETKAHAKAIEMELRQME 560
Cdd:TIGR02168 337 eelaeleEKLEELKEELESLEAELEELEAELEELE 371
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
199-477 |
3.96e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETlRLKRSEDkaklkELEKHKIQLEQVQEWKSKMQEQQADLqrrlKEARKEAKEALEAKERYME 278
Cdd:COG3096 974 DAVGLLGENSDLNEKLRA-RLEQAEE-----ARREAREQLRQAQAQYSQYNQVLASL----KSSRDAKQQTLQELEQELE 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMADTADAIematldkemAEERAES----LQQEVEALKERVDELTTDLEILKAEIEEkgsdgaaSSYQLKQLEEQNARLK 354
Cdd:COG3096 1044 ELGVQADAE---------AEERARIrrdeLHEELSQNRSRRSQLEKQLTRCEAEMDS-------LQKRLRKAERDYKQER 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 355 DALVrmrdlssSEKQEHVKLQKLMEKKNQELEVVRQqrerlqeELSQAEStiDELKEQVDAALGAEEMV----EMLTDrN 430
Cdd:COG3096 1108 EQVV-------QAKAGWCAVLRLARDNDVERRLHRR-------ELAYLSA--DELRSMSDKALGALRLAvadnEHLRD-A 1170
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 431 LNLEE-------KV-------RELRE--------TVGDLEAMNEMNDELqenARET-ELELREQlDMAGA 477
Cdd:COG3096 1171 LRLSEdprrperKVqfyiavyQHLRErirqdiirTDDPVEAIEQMEIEL---ARLTeELTSREQ-KLAIS 1236
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
194-530 |
4.08e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 194 PSPSKEeegLRAQVRDLEEKLETLRLKRSEDkaklkELEKHKIQL-EQVQEWKSKMQEQQ------ADLQRRLKEARKEA 266
Cdd:PRK10929 78 PKLSAE---LRQQLNNERDEPRSVPPNMSTD-----ALEQEILQVsSQLLEKSRQAQQEQdrareiSDSLSQLPQQQTEA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 267 KEALEAKERYMEEMADTADAIEMATLdkemaeeraESLQQEVEALKERVDELttDLEILKAEIEEKGSDGAASSYQlKQL 346
Cdd:PRK10929 150 RRQLNEIERRLQTLGTPNTPLAQAQL---------TALQAESAALKALVDEL--ELAQLSANNRQELARLRSELAK-KRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 347 EEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-----EVVRQQRErLQEELSQAESTIDELKEQVDAAlgaee 421
Cdd:PRK10929 218 QQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGDLpksivAQFKINRE-LSQALNQQAQRMDLIASQQRQA----- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 422 mvemlTDRNLNLEEKVRELRETVGDLEAMNEMNDELQEN-ARETELELREQLD--MAGARVreaqKRVEaaqetvadYQQ 498
Cdd:PRK10929 292 -----ASQTLQVRQALNTLREQSQWLGVSNALGEALRAQvARLPEMPKPQQLDteMAQLRV----QRLR--------YED 354
|
330 340 350
....*....|....*....|....*....|..
gi 311893358 499 TIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:PRK10929 355 LLNKQPQLRQIRQADGQPLTAEQNRILDAQLR 386
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
211-351 |
4.63e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 211 EEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEAleAKERYMEEMADTADAIEMA 290
Cdd:PRK09510 86 QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA--AKAKAEAEAKRAAAAAKKA 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 291 TLDKEMAEERAESLQQEVEALKERVDELTTdleilKAEIEEKGSDGAASSYQLKQLEEQNA 351
Cdd:PRK09510 164 AAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-----KAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
240-559 |
5.01e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 240 QVQEWKSKMQEQQADLQRRLKEARKEAKEaleaKERYMEEMADTAD--AIEMATLDKEMAE--ERAESLQQEVEALKERV 315
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKK----KEKRRDEMLGLAPgrQSIIDLKEKEIPElrNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 316 DELTTDLEILKAEiEEKGSDGAASSYQLKQLEEQnarLKDALVRMRDL-----SSSEKQEHVKLQKLMEKKNQELEVVRQ 390
Cdd:TIGR00606 768 EEQETLLGTIMPE-EESAKVCLTDVTIMERFQME---LKDVERKIAQQaaklqGSDLDRTVQQVNQEKQEKQHELDTVVS 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 391 QRERLQEELSQAESTIDELKEQVDaALGAEEM-VEMLTDRNLNLEEKVRELRETVgdleamNEMNDELQEnARETELELR 469
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTN-ELKSEKLqIGTNLQRRQQFEEQLVELSTEV------QSLIREIKD-AKEQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 470 EQLDMAGARVREAQKRVEAAQETVADYQQTIK-KYRQLTAHLQDVNRELtnqQEASVERQQQPPPETFDFKIKFAETKAH 548
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKeKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKH 992
|
330
....*....|.
gi 311893358 549 AKAIEMELRQM 559
Cdd:TIGR00606 993 QEKINEDMRLM 1003
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
197-302 |
5.75e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEalEAKERY 276
Cdd:PRK12704 85 QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ---KQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEIL 159
|
90 100
....*....|....*....|....*.
gi 311893358 277 MEEMADTADAiEMATLDKEMaEERAE 302
Cdd:PRK12704 160 LEKVEEEARH-EAAVLIKEI-EEEAK 183
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
197-315 |
6.18e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKlkelekhkiqlEQVQEWKSKMQEQQADLQrrlkeaRKEAKEALEAKERY 276
Cdd:COG1842 111 EEQVEKLKEALRQLESKLEELKAKKDTLKAR-----------AKAAKAQEKVNEALSGID------SDDATSALERMEEK 173
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 311893358 277 MEEMADTADAIEM----ATLDKEMAE-ERAESLQQEVEALKERV 315
Cdd:COG1842 174 IEEMEARAEAAAElaagDSLDDELAElEADSEVEDELAALKAKM 217
|
|
| PCRF |
pfam03462 |
PCRF domain; This domain is found in peptide chain release factors. |
225-318 |
6.84e-04 |
|
PCRF domain; This domain is found in peptide chain release factors.
Pssm-ID: 460929 [Multi-domain] Cd Length: 192 Bit Score: 41.99 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 225 KAKLKELEKhkiQLEQVQEWKSkmqeqQADLQRRLKEaRKEAKEALEAKERYMEEMADTADAIEMATLD--KEMAEERAE 302
Cdd:pfam03462 2 EERYEELEA---LLSDPDVWDD-----QKRAQKLSKE-YSELEPIVEAYREYKQALEDLEEAKELLEDPelAELAEEELE 72
|
90
....*....|....*.
gi 311893358 303 SLQQEVEALKERVDEL 318
Cdd:pfam03462 73 ELEKRLEELEEELKLL 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
889-1030 |
7.37e-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: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 889 AMQEGEYDAERPPSKPPPVELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKgeeLSEANVRLSLLEKKLDSAAK 968
Cdd:TIGR02169 654 AMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKIGEIEKEIEQLEQ 730
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 969 DAD---ERIEKVQTRLDETQ---TLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEG 1030
Cdd:TIGR02169 731 EEEklkERLEELEEDLSSLEqeiENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
228-466 |
7.54e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 228 LKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAieMATLDKEMAEERAESLQQE 307
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL--LREAEELEEELQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 308 VEALKERVDelTTDLEILKAEIEekgsdgaassyQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKlmEKKNQELEV 387
Cdd:COG4717 372 IAALLAEAG--VEDEEELRAALE-----------QAEEYQELKEELEELEEQLEELLGELEELLEALDE--EELEEELEE 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 388 VRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDRNlNLEEKVRELRETVGDLEAMNEMNDELQENARETEL 466
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
208-573 |
7.71e-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: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 208 RDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArkeAKEALEAKERYMEEMADTADAi 287
Cdd:TIGR00606 440 RTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNS---LTETLKKEVKSLQNEKADLDR- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 288 EMATLDKEMAE-ERAESLQQEVEALKErvDELTTDLEILKaeIEEKGSDGAASSY----QLKQLEEQNARLKDALVRMRD 362
Cdd:TIGR00606 516 KLRKLDQEMEQlNHHTTTRTQMEMLTK--DKMDKDEQIRK--IKSRHSDELTSLLgyfpNKKQLEDWLHSKSKEINQTRD 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 363 LSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQA------ESTIDELKEQVD------AALGA-----EEMVEM 425
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEksskqrAMLAGatavySQFITQ 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 426 LTDRNLNLEEKVRELRETVGDLeamNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQ 505
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAEL---QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPE 748
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 506 LTAHLQDVNRELtnQQEASVERQQQPPPETFDFKIKFAETKAHAKAIeMELRQMEVAQANRHMSLLTA 573
Cdd:TIGR00606 749 LRNKLQKVNRDI--QRLKNDIEEQETLLGTIMPEEESAKVCLTDVTI-MERFQMELKDVERKIAQQAA 813
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
210-485 |
8.54e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 210 LEEKLETLRLKRSEDKAKLKELEKH-----KIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMadta 284
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEEreralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 285 daieMATLDKEMAEERAESLQQ--EVEALKERVDELTTDLEILKAE--IEEKGSDGAASSYQLKQLEEQNARLKdalvRM 360
Cdd:pfam13868 104 ----DEIVERIQEEDQAEAEEKleKQRQLREEIDEFNEEQAEWKELekEEEREEDERILEYLKEKAEREEEREA----ER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 361 RDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAEstiDELKEQVDAALGAEEMVEMLTDRNLNLEEKVREL 440
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERK---ERQKEREEAEKKARQRQELQQAREEQIELKERRL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 311893358 441 RETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKR 485
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
207-444 |
9.00e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 207 VRDLEEKLETLRLKRSEDKAKLK----ELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEArKEAKEALEAKerymeeMAD 282
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQaleeELEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNELLKAK------FSE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 TADAIEMATLDKEMAEERA--ESLQQEVEALKE----RVDELTTDLEILKAEI---EEKGSD----GAASSYQLKQLEEQ 349
Cdd:pfam15905 148 DGTQKKMSSLSMELMKLRNklEAKMKEVMAKQEgmegKLQVTQKNLEHSKGKVaqlEEKLVStekeKIEEKSETEKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 350 NARLKDAlvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQrerLQEELSQAESTIDELKEQVDAALGA-EEMVEMLTD 428
Cdd:pfam15905 228 ITELSCV----SEQVEKYKLDIAQLEELLKEKNDEIESLKQS---LEEKEQELSKQIKDLNEKCKLLESEkEELLREYEE 300
|
250
....*....|....*.
gi 311893358 429 RNLNLEEKVRELRETV 444
Cdd:pfam15905 301 KEQTLNAELEELKEKL 316
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
196-405 |
9.45e-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: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 196 PSKEEEGLRAQVRDLEEKLETLR--LKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAK 273
Cdd:pfam15709 320 PSKALLEKREQEKASRDRLRAERaeMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 274 ERYMEEMAdtadaiEMATLDKEMAEERAESLQQEVEalkervdelTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARL 353
Cdd:pfam15709 400 RQRQEEEE------RKQRLQLQAAQERARQQQEEFR---------RKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEE 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 311893358 354 KDALVRMRDLSSSEKQEhvKLQKLMEKKNQELEvVRQQRERLQEELSQAEST 405
Cdd:pfam15709 465 QKRLMEMAEEERLEYQR--QKQEAEEKARLEAE-ERRQKEEEAARLALEEAM 513
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
197-512 |
9.83e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERY 276
Cdd:PRK01156 203 KKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADA-----IEMATLDKEMAEERA--ESLQQEVEALKERVDELtTDLEILKAEIEEKGSDGAASSYQLKQLEEQ 349
Cdd:PRK01156 283 MKIINDPVYKnrnyiNDYFKYKNDIENKKQilSNIDAEINKYHAIIKKL-SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 350 NARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQEL-------EVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEM 422
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILkiqeidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 423 V----EMLTDRNL------NL-EEKVRELRETVG-DLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQ 490
Cdd:PRK01156 442 LsrnmEMLNGQSVcpvcgtTLgEEKSNHIINHYNeKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEY 521
|
330 340
....*....|....*....|..
gi 311893358 491 ETVADYQQTIKKYRQLTAHLQD 512
Cdd:PRK01156 522 NKIESARADLEDIKIKINELKD 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
908-1026 |
1.02e-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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 908 ELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSaakdADERIEKVQTRLDETQTL 987
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----LEEEIEELQKELYALANE 296
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 311893358 988 LRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1026
Cdd:TIGR02168 297 ISRLEQQKQILrerLANLERQLEELEAQLEELESKLDELAEE 338
|
|
| prfA |
PRK00591 |
peptide chain release factor 1; Validated |
210-325 |
1.14e-03 |
|
peptide chain release factor 1; Validated
Pssm-ID: 234801 [Multi-domain] Cd Length: 359 Bit Score: 42.76 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 210 LEEKLETLrlkrsedKAKLKELEKhkiQLEQ------VQEWKSKMQEQqADLQ------RRLKEARKEAKEAleakerym 277
Cdd:PRK00591 4 MLDKLEAL-------EERYEELEA---LLSDpevisdQKRFRKLSKEY-AELEpiveayREYKQAQEDLEEA-------- 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 311893358 278 EEMADTADAIEMatldKEMAEEraeslqqEVEALKERVDELTTDLEIL 325
Cdd:PRK00591 65 KEMLEEESDPEM----REMAKE-------ELKELEERLEELEEELKIL 101
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
214-513 |
1.20e-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: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 214 LETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKealeAKERYMEEMADTADAIEmATLD 293
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK----SYENELDPLKNRLKEIE-HNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 294 KEMaeeraeSLQQEVEALKERVDELTTDLEILKAEIEE--KGSDgaassYQLKQLEEQNARLkdalvrmrdlSSSEKQEH 371
Cdd:TIGR00606 263 KIM------KLDNEIKALKSRKKQMEKDNSELELKMEKvfQGTD-----EQLNDLYHNHQRT----------VREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 372 VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDA--ALGAEEMVEMLTD---RNLNLEEKVRELRETV-- 444
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdSLIQSLATRLELDgfeRGPFSERQIKNFHTLVie 401
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 445 ---GDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDV 513
Cdd:TIGR00606 402 rqeDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRI 473
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
907-1032 |
1.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 907 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLK-IKGE--------ELSEANVRLSLLEKK---LDSAAKDADERI 974
Cdd:COG1579 50 AKTELEDLEKEIKRLE---LEIEEVEARIKKYEEQLGnVRNNkeyealqkEIESLKRRISDLEDEileLMERIEELEEEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 975 EKVQTRLDETQTLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIEGLR 1032
Cdd:COG1579 127 AELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYERIR 184
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
225-494 |
1.28e-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: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 225 KAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEER---- 300
Cdd:pfam05701 134 AAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHriga 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 301 AESLQQEVEALKERVDELTTDLEILKAEI----EEKGSDGAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQK 376
Cdd:pfam05701 214 ALAREQDKLNWEKELKQAEEELQRLNQQLlsakDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 377 LMEKKNQELEVVRQQRER--------------LQEELSQAESTIDELKEQVDAALGAEemvemltdrnLNLEEkvrELRE 442
Cdd:pfam05701 294 ALASAKKELEEVKANIEKakdevnclrvaaasLRSELEKEKAELASLRQREGMASIAV----------SSLEA---ELNR 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 311893358 443 TVGDLEAMNEMNDElqenARETELELREQLDMAGARVREAQKRVEAAQETVA 494
Cdd:pfam05701 361 TKSEIALVQAKEKE----AREKMVELPKQLQQAAQEAEEAKSLAQAAREELR 408
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
197-361 |
1.30e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 42.63 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLR----LKRSEdKAKLKELEKHkiqLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALE- 271
Cdd:pfam10498 183 SKPREIIESNVDAAEWKLELERvlpqLKVTI-KADAKDWRAH---LEQMKQHKKSIEESLPDTKSQLDKLHTDISKTLEk 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 272 --AKERY----MEEMADtadaiEMATLDKEMAEERaESLQQEVEALKERVDEL---TTDLEILKAEIEEKG---SDGAas 339
Cdd:pfam10498 259 ieSREKYinsqLEPLIQ-----EYREAQDELSEVQ-EKYKQLSEGVTERTRELaeiTEELEKVKQEMEERGssmTDGS-- 330
|
170 180
....*....|....*....|..
gi 311893358 340 syqlkqleeQNARLKDALVRMR 361
Cdd:pfam10498 331 ---------PLVKIKQALTKLK 343
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
200-557 |
1.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 200 EEGLRAQVRDLEEKLETLrlkrSEDKAKLKELEKHKIQLEqvQEWKSKMQEQQadlqrRLKEARKEAKEALEAKERYMEE 279
Cdd:PRK01156 189 EEKLKSSNLELENIKKQI----ADDEKSHSITLKEIERLS--IEYNNAMDDYN-----NLKSALNELSSLEDMKNRYESE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 280 MADTADAIEMATLD----KEMAEERAESLQQEVEALKERVDE---LTTDLEILKAEIEekGSDGAASSYQ--LKQLEEQN 350
Cdd:PRK01156 258 IKTAESDLSMELEKnnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIENKKQILS--NIDAEINKYHaiIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 351 ARLKDALV---RMRDLS---SSEKQEHVKLQKLM---EKKNQELEVVRQQRERLQEELSQAESTidelkeqvdAALGAEE 421
Cdd:PRK01156 336 KDYNDYIKkksRYDDLNnqiLELEGYEMDYNSYLksiESLKKKIEEYSKNIERMSAFISEILKI---------QEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 422 MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENAR-----------ETELELREQLDMAGARVREAQKRVEAAQ 490
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 491 ETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQPPPETFDFKIKFAETK-AHAKAIEMELR 557
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKdKHDKYEEIKNR 554
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
927-1026 |
1.38e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.31 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 927 KLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADERI-EKVQTRLDETQtLLRKKEKDFEETMDALQAD 1005
Cdd:smart00787 162 LLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAkEKLKKLLQEIM-IKVKKLEELEEELQELESK 240
|
90 100
....*....|....*....|.
gi 311893358 1006 IDQLEAEKAELKQRLNSQSKR 1026
Cdd:smart00787 241 IEDLTNKKSELNTEIAEAEKK 261
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
254-328 |
1.45e-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: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 254 DLQRRLKEARK-----EAKEALEAKERYMEEMADTADAIEMATLD-------------------KEMAEERAESLQQEVE 309
Cdd:cd23165 1 DQQKINKFSRLnarlhELKEELKAKKKELENLEDASDELELADDDepvpykigevfvhlsleeaQERLEKAKEELEEEIE 80
|
90
....*....|....*....
gi 311893358 310 ALKERVDELTTDLEILKAE 328
Cdd:cd23165 81 KLEEEIDEIEEEMKELKVQ 99
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
203-286 |
1.54e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 41.07 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL--------EQVQEWKSKMQEQQADLQ----------RRLKEARK 264
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLeeklkdreEELREKRKLNQDLQDELValqlqlnmaeEKLRKLEK 155
|
90 100
....*....|....*....|..
gi 311893358 265 EAKEALEakeRYMEEMADTADA 286
Cdd:pfam08614 156 ENRELVE---RWMKRKGQEAEA 174
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
198-484 |
1.56e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEdkaklkELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 277
Cdd:pfam05667 310 NEAPAATSSPPTKVETEEELQQQREE------ELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMAtldkEMAEERAESLQQEVEALKERVDELTT-----------DLEILKAEIEEKGSDgaaSSYQLKQL 346
Cdd:pfam05667 384 KQYKVKKKTLDLL----PDAEENIAKLQALVDASAQRLVELAGqwekhrvplieEYRALKEAKSNKEDE---SQRKLEEI 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 347 EEQNARLKD--ALVRMRDlsssekQEHVKLQKLMEKKNQE----------LEVV---RQQRERLQEELSQaestIDELKE 411
Cdd:pfam05667 457 KELREKIKEvaEEAKQKE------ELYKQLVAEYERLPKDvsrsaytrriLEIVkniKKQKEEITKILSD----TKSLQK 526
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 311893358 412 QVDAALGAEEMVEMLTDRNLNLEEKVRE-LRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQK 484
Cdd:pfam05667 527 EINSLTGKLDRTFTVTDELVFKDAKKDEsVRKAYKYLAALHENCEQLIQTVEETGTIMREIRDLEEQIETESGK 600
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
197-397 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVqewKSKMQEQQADLQRRLKEARkeaKEALEAKERY 276
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE---LEELREKLAQLELRLEGLE---VRIDNLQERL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERVDELTtdlEILKAEIEEkgsdgaassyqlkqLEEQNARLKDA 356
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDEEEAR---RRLKRLENKIKELG---PVNLAAIEE--------------YEELKERYDFL 1005
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 311893358 357 LVRMRDLSSSEKQehvkLQKLMEKKNQELevvrqqRERLQE 397
Cdd:TIGR02168 1006 TAQKEDLTEAKET----LEEAIEEIDREA------RERFKD 1036
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
894-1020 |
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 311893358 894 EYDAERPPSKPPPVELRAAALRAEITDAEGlglKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKDADER 973
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERRE 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 311893358 974 IEKVQ--TRLDETQTLLRKKEKDFEETMDALQADIDQL-EAEKAELKQRL 1020
Cdd:COG2433 461 IRKDReiSRLDREIERLERELEEERERIEELKRKLERLkELWKLEHSGEL 510
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
198-491 |
1.70e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETlrlKRSEDKAKLKELEKHKIQLEQ-VQEWKSKMQEQQadlQRRLKEARKEAKEaleakerY 276
Cdd:pfam02029 23 KEEEEPSGQVTESVEPNEH---NSYEEDSELKPSGQGGLDEEEaFLDRTAKREERR---QKRLQEALERQKE-------F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 277 MEEMADTADAIemATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEE-KGSDGAASSYQlkQLEEQNARLKD 355
Cdd:pfam02029 90 DPTIADEKESV--AERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnKWSTEVRQAEE--EGEEEEDKSEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 356 ALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMV---EMLTDRNLN 432
Cdd:pfam02029 166 AEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSqerEEEAEVFLE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 433 LEEKVRELRETVGDLEamNEMNDELQENARETELELREQLdmagaRVREAQKRVEAAQE 491
Cdd:pfam02029 246 AEQKLEELRRRRQEKE--SEEFEKLRQKQQEAELELEELK-----KKREERRKLLEEEE 297
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-513 |
1.73e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 203 LRAQVRDLEEK---LETLRLKR----SEDKAKLKELEKHKIQLEQvqeWKSKMQEQQADLQRRLKEARKEAKEALEAKER 275
Cdd:pfam01576 164 FTSNLAEEEEKaksLSKLKNKHeamiSDLEERLKKEEKGRQELEK---AKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 YMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVD--------------ELTTDLEILKAEIEEKGSDGAASSY 341
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrDLGEELEALKTELEDTLDTTAAQQE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 342 QLKQLEEQNARLKDALvrmrdlsSSEKQEH-VKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVdAALGAE 420
Cdd:pfam01576 321 LRSKREQEVTELKKAL-------EEETRSHeAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEN-AELQAE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 421 emVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAdyqqti 500
Cdd:pfam01576 393 --LRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVS------ 464
|
330
....*....|...
gi 311893358 501 kkyrQLTAHLQDV 513
Cdd:pfam01576 465 ----SLESQLQDT 473
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
200-474 |
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 311893358 200 EEGLrAQVRDLEEKLETLRLkrSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQ-RRLKEARKEAKEALEAKErymE 278
Cdd:PRK05771 27 ELGV-VHIEDLKEELSNERL--RKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIE---K 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 279 EMadtadaiematldKEMAEERAEsLQQEVEALKERVDELT--TDLEI-LKAEIEEKGSDGAASSYQLKQLEEQNARLKD 355
Cdd:PRK05771 101 EI-------------KELEEEISE-LENEIKELEQEIERLEpwGNFDLdLSLLLGFKYVSVFVGTVPEDKLEELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 356 ALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERLQEELSQAEsTIDELKEQvdaalgaeemvemltdrnl 431
Cdd:PRK05771 167 ENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELEEEGTPSE-LIREIKEE------------------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 311893358 432 nLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQLDM 474
Cdd:PRK05771 224 -LEEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEA 265
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
908-1043 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 908 ELRAAALRAEITDAEGLGLKLEDRETVIKELKkslkikgEELSEANVRLSLLEKKLDsaakDADERIEKVQTRLDETQTL 987
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLE-------AELEELRAELARLEAELE----RLEARLDALREELDELEAQ 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 988 LRKKEKDfeeTMDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRGPPPSGIATLV 1043
Cdd:COG4913 332 IRGNGGD---RLEQLEREIERLERELEERERRRARLEAL-LAALGLPLPASAEEFA 383
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
198-530 |
1.76e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLR--LKRSEDkAKLK---ELEKHKIQL--------EQVQEWKSKMQEQQADLQRRLKEARK 264
Cdd:pfam01576 685 RSKRALEQQVEEMKTQLEELEdeLQATED-AKLRlevNMQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERK 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 265 EAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDELTT---DLEILKAEIEEKGSDGAASSY 341
Cdd:pfam01576 764 QRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARAsrdEILAQSKESEKKLKNLEAELL 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 342 QLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV-VRQQRERLQEELSQAESTIDELK------EQVD 414
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRkstlqvEQLT 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 415 AALGAEE-MVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETEL-ELREQLD-------MAGARVREAQKR 485
Cdd:pfam01576 924 TELAAERsTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIaQLEEQLEqesrerqAANKLVRRTEKK 1003
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 311893358 486 VEAAQETVADYQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQQ 530
Cdd:pfam01576 1004 LKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASR 1048
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
198-470 |
1.79e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLE----EKLETLRLKRSEDKAKLK-ELE---KHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEA 269
Cdd:pfam17380 360 RELERIRQEEIAMEisrmRELERLQMERQQKNERVRqELEaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 270 LEakerymeemadtadaiematldkemaEERAeslqQEVEALKERVDELTTDLEILKAEIEEKgsdgaassyQLKQLEEQ 349
Cdd:pfam17380 440 LE--------------------------EERA----REMERVRLEEQERQQQVERLRQQEEER---------KRKKLELE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 350 NARlkdalvrmRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTDR 429
Cdd:pfam17380 481 KEK--------RDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 311893358 430 nlNLEEKVRELRETVGDLEAMnEMNDELQENARETELELRE 470
Cdd:pfam17380 553 --RIQEQMRKATEERSRLEAM-EREREMMRQIVESEKARAE 590
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
168-314 |
1.89e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.69 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 168 TPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQvrdLEEKLETLRLKRSEDKAKLKELEkhkiqlEQVQEWKSK 247
Cdd:pfam08614 23 NAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQ---LREELAELYRSRGELAQRLVDLN------EELQELEKK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 311893358 248 MQEQQ---ADLQRR---LKEARKEAKEALEAKERYMEEMADtadaiEMATLDKE--MAEERAESLQQEVEALKER 314
Cdd:pfam08614 94 LREDErrlAALEAEraqLEEKLKDREEELREKRKLNQDLQD-----ELVALQLQlnMAEEKLRKLEKENRELVER 163
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
374-564 |
1.97e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 374 LQKLMEKKNQELEVVRQQRERLQEELSQaesTIDELKEQVDAALgaeemvemltdrnLNLEEKVRELREtvgdleamnem 453
Cdd:PRK00409 528 LERELEQKAEEAEALLKEAEKLKEELEE---KKEKLQEEEDKLL-------------EEAEKEAQQAIK----------- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 454 ndELQENARETELELREQLDMAGARVR-----EAQKRVEAAQETVADYQQTIK------------KYRQL--TAHLQDV- 513
Cdd:PRK00409 581 --EAKKEADEIIKELRQLQKGGYASVKaheliEARKRLNKANEKKEKKKKKQKekqeelkvgdevKYLSLgqKGEVLSIp 658
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 514 -NRELTNQ--------QEASVERQQQPPPETFDfKIKFAETKAHAKAIEMELRQMEVAQA 564
Cdd:PRK00409 659 dDKEAIVQagimkmkvPLSDLEKIQKPKKKKKK-KPKTVKPKPRTVSLELDLRGMRYEEA 717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1026 |
2.02e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 907 VELRAAALRAEITD----AEGLGLKLEDRETVIKELKKSLKIKGEE--------LSEANVRLSLLEKKLDSAA---KDAD 971
Cdd:TIGR02169 242 IERQLASLEEELEKlteeISELEKRLEEIEQLLEELNKKIKDLGEEeqlrvkekIGELEAEIASLERSIAEKErelEDAE 321
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 972 ERIEKVQTRLDETQTLLRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKR 1026
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEErkrRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
198-312 |
2.03e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLetLRLKRSEDKAKLKELEKHkiQLEQVQEWKSKMQEqqadlqrRLKEARKEAKEALEAKERym 277
Cdd:cd16269 200 IEAERAKAEAAEQERKL--LEEQQRELEQKLEDQERS--YEEHLRQLKEKMEE-------ERENLLKEQERALESKLK-- 266
|
90 100 110
....*....|....*....|....*....|....*
gi 311893358 278 eemadtadaiEMATLDKEMAEERAESLQQEVEALK 312
Cdd:cd16269 267 ----------EQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
947-1032 |
2.24e-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: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 947 EELSEANVRLSLLEKKLDSAAKDADE---RIEKVQTRLDETQTLLRKKEKDfeetMDALQADIDQLEAEKAELKQRLNSQ 1023
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQE----LAALEAELAELEKEIAELRAELEAQ 102
|
....*....
gi 311893358 1024 SKRTIEGLR 1032
Cdd:COG4942 103 KEELAELLR 111
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
180-333 |
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 311893358 180 PTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRlkrsedkAKLKELEkhkiqleqvqewkskmqEQQADLQRRL 259
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKD-----------------ERIERLEREL 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 260 KEARKEAKEALEaKERYMEEMadtadaiematldkemaEERAESLQQEVEALKERVDELTTDLEILKA--EIEEKG 333
Cdd:COG2433 451 SEARSEERREIR-KDREISRL-----------------DREIERLERELEEERERIEELKRKLERLKElwKLEHSG 508
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
257-529 |
2.48e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 41.56 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 257 RRLKEARKEAKEALEAKERYMEE--MADTADA-IEMATLDKEM--AEERAESLQQEVEALKERVDE-LTTDLEILKAEIE 330
Cdd:COG1538 50 RARIEAAKAQAEAAEADLRAARLdlAAEVAQAyFDLLAAQEQLalAEENLALAEELLELARARYEAgLASRLDVLQAEAQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 331 EkgsdgAASSYQLKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELK 410
Cdd:COG1538 130 L-----AQARAQLAQAEAQLAQARNALALLLGLPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 411 EQVDAA-------------LGAEEMVEMLTDRN------LNLEEKVRELRETVGDLEAMNEMNDELQENARETELELREQ 471
Cdd:COG1538 205 AEIGVAraaflpslslsasYGYSSSDDLFSGGSdtwsvgLSLSLPLFDGGRNRARVRAAKAQLEQAEAQYEQTVLQALQE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 311893358 472 LDMAGARVREAQKRVEAAQETVAD----YQQTIKKYRQLTAHLQDVNRELTNQQEASVERQQ 529
Cdd:COG1538 285 VEDALAALRAAREQLEALEEALEAaeeaLELARARYRAGLASLLDVLDAQRELLQAQLNLIQ 346
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
84-197 |
2.63e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.21 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 84 ADTTSPeTPdssaskvlkregadaAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSS 163
Cdd:pfam05109 471 ADVTSP-TP---------------AGTTSGASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTTPTPNA 534
|
90 100 110
....*....|....*....|....*....|....
gi 311893358 164 SEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPS 197
Cdd:pfam05109 535 TSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPN 568
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
220-349 |
2.83e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 220 KRSEDKAKLKELE------KHKIQLEQ-VQEWKSKMQEQQADLQRRlKEARKEAKEALEAKERYMEEMADTADAiEMATL 292
Cdd:PRK12704 49 KEAEAIKKEALLEakeeihKLRNEFEKeLRERRNELQKLEKRLLQK-EENLDRKLELLEKREEELEKKEKELEQ-KQQEL 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 311893358 293 DKEmaEERAESLQQEVEALKERVDELTTD--LEILKAEIEEKGSDGAASsyQLKQLEEQ 349
Cdd:PRK12704 127 EKK--EEELEELIEEQLQELERISGLTAEeaKEILLEKVEEEARHEAAV--LIKEIEEE 181
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
380-530 |
2.89e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 41.57 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 380 KKNQELevVRQQRERLQEELSQAESTIDELKEQVDAALGAEEMVEMLTdrnlNLEEKVRELRETVGDLEAMNEMNDELQE 459
Cdd:COG1566 68 KKGQVL--ARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIA----AAEAQLAAAQAQLDLAQRELERYQALYK 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 311893358 460 NaretELELREQLDMAGARVREAQKRVEAAQETVADYQQTIKKYRQLTAHLQDVnreltNQQEASVERQQQ 530
Cdd:COG1566 142 K----GAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQV-----AQAEAALAQAEL 203
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
205-411 |
2.92e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.99 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 205 AQVRDLEEKLETLRLKRSEDKaklKELEKHKIQLEQVQEWKSKMQEQQADLQRrlKEARKEAKEALEAKERYMEEMADTA 284
Cdd:COG5022 817 ACIIKLQKTIKREKKLRETEE---VEFSLKAEVLIQKFGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 285 DAIEMA-----TLDKEMAE---ERAESLQQEVEALKERVDELTTDLEilKAEIEEKGSDGAASSYQLKQLEEQNARLKDA 356
Cdd:COG5022 892 KSISSLklvnlELESEIIElkkSLSSDLIENLEFKTELIARLKKLLN--NIDLEEGPSIEYVKLPELNKLHEVESKLKET 969
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 357 LVRMRDLSSSEKQEHVKLQK---LMEKKNQELEVVRQQRERLQEELSQAESTIDELKE 411
Cdd:COG5022 970 SEEYEDLLKKSTILVREGNKansELKNFKKELAELSKQYGALQESTKQLKELPVEVAE 1027
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
296-481 |
3.01e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.94 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 296 MAEERAESLQQEVEALKERVDElttDLEILKAEIEEKgsdgaassyqlkqLEEQNARLKDALVRMRDLSSSEkqehvkLQ 375
Cdd:pfam01442 23 VAQELVDRLEKETEALRERLQK---DLEEVRAKLEPY-------------LEELQAKLGQNVEELRQRLEPY------TE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 376 KLMEKKNQELEVVRQQRERLQEEL-SQAESTIDELKEQVDAAlgAEEMVEmltdrnlNLEEKVRELRETVGdleamnEMN 454
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELrERLEQNVDALRARLAPY--AEELRQ-------KLAERLEELKESLA------PYA 145
|
170 180
....*....|....*....|....*..
gi 311893358 455 DELQENARETELELREQLDMAGARVRE 481
Cdd:pfam01442 146 EEVQAQLSQRLQELREKLEPQAEDLRE 172
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
250-495 |
3.11e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 42.00 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 250 EQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAI-EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAE 328
Cdd:COG5644 331 EPRTESERKMHQALLDAGLENESALKKQEELALNKLSVeEVAERTRQLRFMRELMFREERKAKRVAKIKSKTYRKIRKNR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 329 IEEKGSDGAASSyqlkQLEEQNARLKDALVRMrdlssseKQEHVKLQKLMEKknqelevvrqqrerLQEELSQAESTIDE 408
Cdd:COG5644 411 KEKEMALIPKSE----DLENEKSEEARALERM-------TQRHKNTSSWTRK--------------MLERASHGEGTREA 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 409 LKEQVDAalgAEEMVEMLTDRNLNLEEKVRElrETVGDLEamNEMNDELQENARETELELREQLDMAGARVREAQKRvEA 488
Cdd:COG5644 466 VNEQIRK---GDELMQRIHGKEIMDGEDVSE--FSDSDYD--TNEQVSTAFEKIRNEEELKGVLGMKFMRDASNRQM-AA 537
|
....*..
gi 311893358 489 AQETVAD 495
Cdd:COG5644 538 SKISVAD 544
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
271-498 |
3.14e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 271 EAKERYMEEMADTADAIE-MATLDKEMAEER--AESLQQEVEALKERVDELTTDLEilkaEIEEKGSDGAASSYQ--LKQ 345
Cdd:PRK00409 506 EAKKLIGEDKEKLNELIAsLEELERELEQKAeeAEALLKEAEKLKEELEEKKEKLQ----EEEDKLLEEAEKEAQqaIKE 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 346 LEEQNARLKDALVRMRDlsssEKQEHVKLQKLMEKKNQelevVRQQRERLQEELSQAESTIDELKEqvdaalGAE----- 420
Cdd:PRK00409 582 AKKEADEIIKELRQLQK----GGYASVKAHELIEARKR----LNKANEKKEKKKKKQKEKQEELKV------GDEvkyls 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 421 -----EMVEMLTDRNLNLEEKVRELRETVGDLEAMNEMNDELQENARETELELRE---QLDMAGARVREAQKRVEAA--Q 490
Cdd:PRK00409 648 lgqkgEVLSIPDDKEAIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTvslELDLRGMRYEEALERLDKYldD 727
|
....*...
gi 311893358 491 ETVADYQQ 498
Cdd:PRK00409 728 ALLAGYGE 735
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
199-353 |
3.28e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 199 EEEGLRAQVRDLEEKLETLR--LKRSEDKAkLKELEKHKIQL----EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 272
Cdd:pfam09787 55 ERDLLREEIQKLRGQIQQLRteLQELEAQQ-QEEAESSREQLqeleEQLATERSARREAEAELERLQEELRYLEEELRRS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 273 KERYMEEMADTADAIEMATlDKEMAEERAESLQQEVEAlkeRVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNAR 352
Cdd:pfam09787 134 KATLQSRIKDREAEIEKLR-NQLTSKSQSSSSQSELEN---RLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKE 209
|
.
gi 311893358 353 L 353
Cdd:pfam09787 210 L 210
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
201-377 |
3.76e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 201 EGLRaqvRDLEEKLETLRlkrsEDKAKLKElekhkiQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKErymeem 280
Cdd:smart00787 143 EGLK---EGLDENLEGLK----EDYKLLMK------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDP------ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 adtadaiemATLDKemAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKGSdgaassyQLKQLEEQNARLKDALVRM 360
Cdd:smart00787 204 ---------TELDR--AKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTN-------KKSELNTEIAEAEKKLEQC 265
|
170 180
....*....|....*....|.
gi 311893358 361 RDLSSSE----KQEHVKLQKL 377
Cdd:smart00787 266 RGFTFKEieklKEQLKLLQSL 286
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
199-495 |
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 311893358 199 EEEGLRAQVRDLEEKLEtLRLKRSEDKAKLKELEKHKIQL------EQVQEWKSKMQEQQADLQRRLKEARKEAKEALEA 272
Cdd:pfam02029 60 EEEAFLDRTAKREERRQ-KRLQEALERQKEFDPTIADEKEsvaerkENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 273 KER---YMEEMADTADAIEMATLDKEMAEERAESL----QQEVEALKERVDELTTDLEILKAE---IEEKGSDGAASSYQ 342
Cdd:pfam02029 139 EYQenkWSTEVRQAEEEGEEEEDKSEEAEEVPTENfakeEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 343 LKQLEEQNARLKDALVRMRDLSSSEKQEHVKLQKLmEKKNQELEvvRQQRERLQEELSQAESTIDELKeqvdaalgaeem 422
Cdd:pfam02029 219 LKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEEL-RRRRQEKE--SEEFEKLRQKQQEAELELEELK------------ 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 311893358 423 vemltdrnlnleeKVRELRETVGDLEAMNEMNDELQENARETELELREQLDMAGARVREAQKRVEAAQETVAD 495
Cdd:pfam02029 284 -------------KKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSSE 343
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
240-463 |
3.96e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 240 QVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERVDEL- 318
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 319 -----------TTDLEILKAEIEEKGSDGAASSYQLKQLEEQnarlKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEV 387
Cdd:pfam05701 112 qgiadeasvaaKAQLEVAKARHAAAVAELKSVKEELESLRKE----YASLVSERDIAIKRAEEAVSASKEIEKTVEELTI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 388 vrqQRERLQEELSQAESTIDELKEQ-VDAALGAEEmvEMLT-DRNLN-LEEKVRELRETV---GDLEAMNEMNDELQENA 461
Cdd:pfam05701 188 ---ELIATKESLESAHAAHLEAEEHrIGAALAREQ--DKLNwEKELKqAEEELQRLNQQLlsaKDLKSKLETASALLLDL 262
|
..
gi 311893358 462 RE 463
Cdd:pfam05701 263 KA 264
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
205-331 |
4.22e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 41.37 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 205 AQVRDLEEKLETLRlkrSEDKAKLKELEKHKI-------QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYM 277
Cdd:COG4477 347 EKVRNLEKQIEELE---KRYDEIDERIEEEKVayselqeELEEIEEQLEEIEEEQEEFSEKLKSLRKDELEAREKLDELK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAIEMATL---------DKEMAEERAESLQQE-------VEALKERVDELTTDLEILKAEIEE 331
Cdd:COG4477 424 KKLREIKRRLEKSNLpglpeeyleMFEEASDEIEELSEElnevplnMDEVNRLLEEAEEDIETLEEKTEE 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
907-1020 |
4.39e-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: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 907 VELRAAALRAEITDAEglgLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLE----------KKLDSAAKDADERIEK 976
Cdd:TIGR02169 376 VDKEFAETRDELKDYR---EKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiagieakiNELEEEKEDKALEIKK 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 311893358 977 VQTRLDETQTLLRKKEKDFEetmdALQADIDQLEAEKAELKQRL 1020
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELY----DLKEEYDRVEKELSKLQREL 492
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
231-413 |
4.49e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 231 LEKHKIQLEQVQE----WKSKMQEQQADLQRrLKEARKEAKEALEAK-ERYmeemadtadaiematldkEMAEERAESLQ 305
Cdd:pfam10168 549 LKKHDLAREEIQKrvklLKLQKEQQLQELQS-LEEERKSLSERAEKLaEKY------------------EEIKDKQEKLM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 306 QEVEALKERVDELTTDL-EILKAEIEEkgsdgaASSYQlKQLEEQNARLKDALVRMrdlssSEKQEHVKLQKLMEKKNqE 384
Cdd:pfam10168 610 RRCKKVLQRLNSQLPVLsDAEREMKKE------LETIN-EQLKHLANAIKQAKKKM-----NYQRYQIAKSQSIRKKS-S 676
|
170 180
....*....|....*....|....*....
gi 311893358 385 LEVVRQQRERLQEELSQAESTIDELKEQV 413
Cdd:pfam10168 677 LSLSEKQRKTIKEILKQLGSEIDELIKQV 705
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
212-442 |
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 311893358 212 EKLETLRLKRSEDK--AKLKELE-------KHKIQLEQVQEWKSKMQEQQADLqRRLKEARKEAKEALEAKERYmeEMAD 282
Cdd:PRK05771 7 KKVLIVTLKSYKDEvlEALHELGvvhiedlKEELSNERLRKLRSLLTKLSEAL-DKLRSYLPKLNPLREEKKKV--SVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 283 TADAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILK----------AEIEEKGSDGAASSYQLKQLEEQNAR 352
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlsLLLGFKYVSVFVGTVPEDKLEELKLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 353 LKDALVrmrDLSSSEKQEH----VKLQKLMEKKNQELEVVRQQRERL------QEELSQAESTIDELKEQVDAALG-AEE 421
Cdd:PRK05771 164 SDVENV---EYISTDKGYVyvvvVVLKELSDEVEEELKKLGFERLELeeegtpSELIREIKEELEEIEKERESLLEeLKE 240
|
250 260
....*....|....*....|.
gi 311893358 422 MVEMLTDRNLNLEEKVRELRE 442
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELE 261
|
|
| Not3 |
pfam04065 |
Not1 N-terminal domain, CCR4-Not complex component; |
212-354 |
5.08e-03 |
|
Not1 N-terminal domain, CCR4-Not complex component;
Pssm-ID: 461155 [Multi-domain] Cd Length: 228 Bit Score: 39.84 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 212 EKLETLrLKRSedkakLKELEKHKiqlEQVQEW--------KSKMQEQqadlqRRLKEARKEAKEALEakeRYMEEMADT 283
Cdd:pfam04065 40 EKLEAD-LKKE-----IKKLQRLR---DQIKTWlssndikdKKKLLEN-----RKLIEEAMERFKAVE---KESKTKAFS 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 284 ADAIEMATLDKEMAEERAEslQQEVEALKERVDELTTDLEILKAEIE-----EKGSDGAASSYQLKQLEEQNARLK 354
Cdd:pfam04065 103 KEGLSLAAASKLDPKEKEK--AEARDWLSDSIDELNRQIEALEAEIEslqaqKKKKKKDSEKARLEELEKLIERHK 176
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
908-1033 |
5.61e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 908 ELRAAALRAEITDAEGLGLKLEDRE--TVIKELKKSLKIKGEELSEANVRLSLLEKKLDSAAKD---ADERIEKVQTRLD 982
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSEleEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESKLD 333
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 311893358 983 ETQTLLRKKEKDFEET---MDALQADIDQLEAEKAELKQRLNSQSKRtIEGLRG 1033
Cdd:TIGR02168 334 ELAEELAELEEKLEELkeeLESLEAELEELEAELEELESRLEELEEQ-LETLRS 386
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
907-1029 |
5.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 907 VELRAAALRAEITDAEGLGLKLEDRETVIKELKKSLKIKGEELSEANVRLSLLEKkldsaAKDADERIEKVQTRL-DETQ 985
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLtGLTP 386
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 311893358 986 TLLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKRTIE 1029
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
205-399 |
5.80e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 39.74 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 205 AQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQL-EQVQEWKSKMQEQQADLQRR---LKEARKEAKEALEAKERYMEEM 280
Cdd:cd00176 33 ESVEALLKKHEALEAELAAHEERVEALNELGEQLiEEGHPDAEEIQERLEELNQRweeLRELAEERRQRLEEALDLQQFF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 281 ADTADaiematLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIEEKgsdgaasSYQLKQLEEQNARLKDalvRM 360
Cdd:cd00176 113 RDADD------LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH-------EPRLKSLNELAEELLE---EG 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 311893358 361 RDLSSSEKQEhvKLQKLMEKKNQELEVVRQQRERLQEEL 399
Cdd:cd00176 177 HPDADEEIEE--KLEELNERWEELLELAEERQKKLEEAL 213
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
197-511 |
5.86e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 197 SKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQ-EWKSKMQEQQADLQRRLKEARKEAKEALEAKER 275
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKER 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 276 ymeEMADTADAI-----EMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAEIE---EKGSDGAASSYQLKQ-- 345
Cdd:TIGR00606 320 ---ELVDCQRELeklnkERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRlelDGFERGPFSERQIKNfh 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 346 ---LEEQNARLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQELEVVRQQRERLQEELSQAESTIDELKEqvdaalgaeem 422
Cdd:TIGR00606 397 tlvIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ----------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 423 VEMLTDRNLNLEEkvrELRETVGDLEAMNEMNDELQENARETELElREQLDMAGARVREAQKRVEAAQETVADYQQTIKK 502
Cdd:TIGR00606 466 LEGSSDRILELDQ---ELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
....*....
gi 311893358 503 YRQLTAHLQ 511
Cdd:TIGR00606 542 KDKMDKDEQ 550
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
193-403 |
6.07e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 193 LPSPSKEEEGLRAQVRDLEEKLETLRLK-RSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAkEALE 271
Cdd:pfam15921 669 LNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQI-DALQ 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 272 AKERYMEEmadtadAIEMATLDKEMAEERAESLQQEVEALKERVDELTTDLEILKAeieekgsdgaassyqlkqleeQNA 351
Cdd:pfam15921 748 SKIQFLEE------AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS---------------------QER 800
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 311893358 352 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKNQElevvrQQRERLQEELSQAE 403
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQE-----SVRLKLQHTLDVKE 847
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
302-407 |
6.25e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 302 ESLQQEVEALKERVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNARLkdalvrmrdlssseKQEHVKLQKlmekk 381
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQEL--------------EAQLEQLQE----- 205
|
90 100
....*....|....*....|....*.
gi 311893358 382 nQELEVVRQQRERLQEELSQAESTID 407
Cdd:PRK11448 206 -KAAETSQERKQKRKEITDQAAKRLE 230
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
204-348 |
6.26e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 204 RAQVRDLEEKLETLRLKRSEDKAklkELEKHKIQLEQVQEWKSKMQEQQADLQ---------RRLKEARKEAKEALEAKE 274
Cdd:COG2268 222 EAEEAELEQEREIETARIAEAEA---ELAKKKAEERREAETARAEAEAAYEIAeanaerevqRQLEIAEREREIELQEKE 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 275 RYMEEMADTADAIEMATLDKEMAEERAEslqQEVEALKERvdeLTTDLEILKAEIEEKGSDGAASSYQ--LKQLEE 348
Cdd:COG2268 299 AEREEAELEADVRKPAEAEKQAAEAEAE---AEAEAIRAK---GLAEAEGKRALAEAWNKLGDAAILLmlIEKLPE 368
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
239-529 |
6.28e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 239 EQVQEWKSKMQEQQADLQRRLkearKEAKEALEAKERYMEEmadtaDAIEMATLDKEMAEERAESL------QQEVEALK 312
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRL----NESNELHEKQKFYLRQ-----SVIDLQTKLQEMQMERDAMAdirrreSQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 313 ERVDELTTDLEILKAEIEEKGSDGAASSYQLKQL----EEQNARLKDALVRMRDLSSSEKQEHVKLQKlMEKKNQELEVV 388
Cdd:pfam15921 145 NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEASGKKIYEHDSMST-MHFRSLGSAIS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 389 RQQRErLQEELSQAESTIDELKEQVDaALGAEEM--VEMLTDRNLN---------------LEEKVRELRETVGDLEAMN 451
Cdd:pfam15921 224 KILRE-LDTEISYLKGRIFPVEDQLE-ALKSESQnkIELLLQQHQDrieqliseheveitgLTEKASSARSQANSIQSQL 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311893358 452 EMndeLQENARETELELREQLDMAGARVREAQKRVEAAQETVADyqqtikKYRQLTAHLQDVNRELTnqqEASVERQQ 529
Cdd:pfam15921 302 EI---IQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYED------KIEELEKQLVLANSELT---EARTERDQ 367
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
74-194 |
6.29e-03 |
|
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.
Pssm-ID: 435117 [Multi-domain] Cd Length: 288 Bit Score: 40.13 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 74 QSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPaSTGVAGPSSSLGPS 153
Cdd:pfam16072 135 EDKIIIINNGPPGSVTTTSAGSGTTVINAGGQQPAAPAAPAYPVAPAAYPAQAPAAAPAPAPGAP-QTPLAPLNPVAAAP 213
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 311893358 154 GSAsAGELSSSEPSTPAQTPlAAPIIPTPALTSPGAAPPLP 194
Cdd:pfam16072 214 AAA-AGAAAAPVVAAAAPAA-AAPPPPAPAAPPADAAPPAP 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
915-1026 |
6.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 915 RAEITDAEglglklEDRETVIKELKKSLK-IKGEELSEANVRLSLLEKKLDSAAKDADERIEKVQTR-------LDETQT 986
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRllqkeenLDRKLE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 311893358 987 LLRKKEKDFEETMDALQADIDQLEAEKAELKQRLNSQSKR 1026
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
198-356 |
6.49e-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: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 198 KEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKhkiQLEQVQEWKSKMQEQQ--ADLQRRLKEARKE----AKEALE 271
Cdd:cd22656 128 KEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEK---ALKDLLTDEGGAIARKeiKDLQKELEKLNEEyaakLKAKID 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 272 AKERYMEEMADTADAIEMATLDKEMAEERAESLQQEVEALKERV-------DELTTDLEILKAEIEEKGSDGAA---SSY 341
Cdd:cd22656 205 ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALeklqgawQAIATDLDSLKDLLEDDISKIPAailAKL 284
|
170
....*....|....*
gi 311893358 342 QLKQLEEQNARLKDA 356
Cdd:cd22656 285 ELEKAIEKWNELAEK 299
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
84-200 |
7.33e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 84 ADTTSPETPDSSASKVLkrEGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSS 163
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPAT--PGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAV 2811
|
90 100 110
....*....|....*....|....*....|....*...
gi 311893358 164 SEPsTPAQTPLAAPIIPTPALTSPG-AAPPLPSPSKEE 200
Cdd:PHA03247 2812 LAP-AAALPPAASPAGPLPPPTSAQpTAPPPPPGPPPP 2848
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
211-412 |
7.36e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 40.47 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 211 EEKLETLRLKRSEDKAKLKELEK-----------HKIQLEQVQ--EWKSKMQEQQADLQRRLKEARKEakEALEAKERYM 277
Cdd:pfam03528 92 QEAIDEVKSQWQEEVASLQAIMKetvreyevqfhRRLEQERAQwnQYRESAEREIADLRRRLSEGQEE--ENLEDEMKKA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 278 EEMADTADAI------EMATLDKEMAEerAESLQQEVEALKerVDELTTDLEILKAEIEEKGSDGAASSYQLKQLEEQNA 351
Cdd:pfam03528 170 QEDAEKLRSVvmpmekEIAALKAKLTE--AEDKIKELEASK--MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEDAE 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 311893358 352 RLKDALVRMRDLSSSEKQEHVKLQKLMEKKN-QELEVVR---QQRERLQEELSQAE-STIDELKEQ 412
Cdd:pfam03528 246 KLRKELHEVCHLLEQERQQHNQLKHTWQKANdQFLESQRllmRDMQRMESVLTSEQlRQVEEIKKK 311
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
237-328 |
7.52e-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: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311893358 237 QLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADtaDAIEMATLDKEMAEERA-ESLQQEVEALKERV 315
Cdd:cd06503 38 SLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKIKE--EILAEAKEEAERILEQAkAEIEQEKEKALAEL 115
|
90
....*....|...
gi 311893358 316 DELTTDLEILKAE 328
Cdd:cd06503 116 RKEVADLAVEAAE 128
|
|
| |
