|
Name |
Accession |
Description |
Interval |
E-value |
| Dynactin |
pfam12455 |
Dynein associated protein; This domain family is found in eukaryotes, and is approximately 280 ... |
509-786 |
2.63e-85 |
|
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: 279.11 E-value: 2.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 509 LQEVNRELMSQQEANSEQQQ----QPAEI--FDFKIKFAETKAYAKAIEMELRKMEVIQANRQVSLLISFMPDSFLKHrG 582
Cdd:pfam12455 1 LQSDLEDLRASQQITESESEdlssRSRAMmdLNLKLQSSASKAQAKAIDLELRRLEAQQASEHLEIVQLFLPDSFLRR-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 583 DHDCILALLLIPRLICKSELISKQAQEKFELtescSQKPGMRGAVGERLSFAAGLIYSLTLLQAALHKYEHALSQCSVDV 662
Cdd:pfam12455 80 DRDSVLALLLFKRLAFKADLLASQIREKFPL----SESLILKGHVEEQLFFACELLEKLTWLSALCDRFAAALRSCSVET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 663 YKRVGSLYSELSVHERSLDFLIDLLYKDLLDETVNVEPLTKAIKYYQHLYSIHLAEQPEDCTMQLADHIRFTQSALDCMA 742
Cdd:pfam12455 156 FLKIGGAYPELEPVERALDGWIDLLKRDELDENECAEELQRSIAYFSHLAEVHLADSLEDLADELLMRVLLLQSALDSIA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 688582234 743 VEVGRLRAFIQTGQ------DEEA--FCVLLKDLDTSCSDIRQFCKKIRRRM 786
Cdd:pfam12455 236 AALGRLKTLLQSGLpdpdggDEEAsdLFELLQTLITQARSAKVISKKILRRL 287
|
|
| CAP_GLY |
pfam01302 |
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ... |
31-96 |
2.32e-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: 114.42 E-value: 2.32e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 31 VGSLVEVIGkGHRGTVAYIGNTLFASGKWVGVILDEPKGKNDGTVQGKRYFLCQENHGIFVRQSQI 96
Cdd:pfam01302 1 VGDRVEVPG-GRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
|
|
| CAP_GLY |
smart01052 |
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ... |
31-97 |
1.33e-28 |
|
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: 109.60 E-value: 1.33e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688582234 31 VGSLVEVIGKGHRGTVAYIGNTLFASGKWVGVILDEP-KGKNDGTVQGKRYFLCQENHGIFVRQSQIQ 97
Cdd:smart01052 1 VGDRVEVGGGGRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-535 |
1.13e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.41 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 199 EESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEE 278
Cdd:PRK02224 313 EARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 279 MADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAA-----------SSYHVKQLEE 347
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveGSPHVETIEE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 348 QNARLKEALVRMRDLsasEKQEHGKQQKLMEKKnfELDALRCHKEKLQEEMKMAEKTIDELKEQVDASlgaEEMVEMLTE 427
Cdd:PRK02224 473 DRERVEELEAELEDL---EEEVEEVEERLERAE--DLVEAEDRIERLEERREDLEELIAERRETIEEK---RERAEELRE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 428 RNLDLEEKVRELRETVAD--------LEAINEMNDELQENAREtelelREQLDlgaagvreaekRVEAAQETVADYQQTI 499
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEaeeeaeeaREEVAELNSKLAELKER-----IESLE-----------RIRTLLAAIADAEDEI 608
|
330 340 350
....*....|....*....|....*....|....*.
gi 688582234 500 QKYRELTANLQEVNRELMSQQEANSEQQQQPAEIFD 535
Cdd:PRK02224 609 ERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-516 |
4.31e-17 |
|
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: 87.43 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAK----REAKEALEAK 272
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARLSHSRipeiQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 273 ERYMEEMADTADAIEMA-TLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNAR 351
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 352 LKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEemvemlternlD 431
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-----------D 955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 432 LEEKVRELRETVADLEAINEMNDELQENARETELELREQLDlgaagVREAEKrvEAAQETVADYQQT-----IQKYRELT 506
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA-----KLEEER--KAILERIEEYEKKkrevfMEAFEAIN 1028
|
330
....*....|
gi 688582234 507 ANLQEVNREL 516
Cdd:TIGR02169 1029 ENFNEIFAEL 1038
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-463 |
4.60e-17 |
|
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: 87.42 E-value: 4.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 200 ESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLE----QLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERY 275
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEIL--------------KHEIEEKGSDGAASSYH 341
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerasleealallRSELEELSEELRELESK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 342 VKQLEEQNARLKEALVRMR-DLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDA----SL 416
Cdd:TIGR02168 910 RSELRRELEELREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvNL 989
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 688582234 417 GAEEMVEMLTERNLDLEEKVRELRETVADLE-AINEMNDELQENARET 463
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEeAIEEIDREARERFKDT 1037
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
36-446 |
1.01e-16 |
|
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: 85.51 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 36 EVIGKGHRGTVAYIGNTLFASGKWVGVILDEPKGKNDGTVQGKRYFLCQENHGIFVRQSQIQLvedgadttspetpealt 115
Cdd:COG5244 9 RVLLGDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSL----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 116 skmlkreiiegLKSNKVTTTRRpkqtraGVGVKVGSGSASAGEM--SSSEPSTPAQTPLAAPVIPSPVgALPSPGAPPIP 193
Cdd:COG5244 72 -----------LNGNAAYEKIK------GGLVCESKGMDKDGEIkqENHEDRIHFEESKIRRLEETIE-ALKSTEKEEIV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 194 GPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIqLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKE 273
Cdd:COG5244 134 ELRRENEELDKINLSLRERISSEEPELNKDGSKLSYDELKEF-VEESRVQVYDMVELVSDISETLNRNGSIQRSSVRECE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RymeemadtadaiematldkemaeeraeslqleadalKERVDELTMDLEILKHEIEEKGsdgaassyhvKQLEeqnaRLK 353
Cdd:COG5244 213 R------------------------------------SNIHDVLFLVNGILDGVIDELN----------GELE----RLR 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 354 EALVRMRDLSASEKQEHGKQQKLMEK-KNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDL 432
Cdd:COG5244 243 RQLVSLMSSHGIEVEENSRLKATLEKfQSLELKVNTLQEELYQNKLLKKFYQIYEPFAQAALSSQLQYLAEVIESENFGK 322
|
410
....*....|....*.
gi 688582234 433 EE--KVRELRETVADL 446
Cdd:COG5244 323 LEniEIHIILKVLSSI 338
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-510 |
1.81e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.99 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 206 VKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADA 285
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 286 IEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSAS 365
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 366 EKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEmvemlternlDLEEKVRELRETVAD 445
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE----------EEEEALEEAAEEEAE 453
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688582234 446 LEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQ 510
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
210-529 |
1.68e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 210 EEKLETL-KMKRTED-----KAKLKELEKhkiQLEQLQEwKSKMQEQQNELQKQLKEAKREA-----KEALEAKERYMEE 278
Cdd:COG1196 172 ERKEEAErKLEATEEnlerlEDILGELER---QLEPLER-QAEKAERYRELKEELKELEAELlllklRELEAELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 279 MADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVR 358
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 359 MRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgaeemvemLTERNLDLEEKVRE 438
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE----------LAEELLEALRAAAE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 439 LRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMS 518
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
330
....*....|.
gi 688582234 519 QQEANSEQQQQ 529
Cdd:COG1196 478 ALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-483 |
3.39e-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: 81.26 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 201 SLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMA 280
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 281 DTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMR 360
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 361 dlsaSEKQEHGKQQKLMEKKNFELDA--LRCHKEKLQEEMKMAEKTIDELKEQVDASlgaEEMVEMLTERNLDLEEKVRE 438
Cdd:TIGR02168 393 ----LQIASLNNEIERLEARLERLEDrrERLQQEIEELLKKLEEAELKELQAELEEL---EEELEELQEELERLEEALEE 465
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 688582234 439 LRETVADLE-AINEMNDELQE-NARETELE-LREQLDLGAAGVREAEK 483
Cdd:TIGR02168 466 LREELEEAEqALDAAERELAQlQARLDSLErLQENLEGFSEGVKALLK 513
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-565 |
4.80e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEE--KLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNelQKQLKEAKREAKEALEAKE 273
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKK 1451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 -----RYMEEMADTADAIEMATLDKEMAEE--RAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLE 346
Cdd:PTZ00121 1452 kaeeaKKAEEAKKKAEEAKKADEAKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 347 EqnARLKEALVRMRDLSASEKQEHGKQ-QKLMEKKNFEldalrcHKEKLQEEMKMAEKTIDELKeQVDASLGAEEMVEML 425
Cdd:PTZ00121 1532 E--AKKADEAKKAEEKKKADELKKAEElKKAEEKKKAE------EAKKAEEDKNMALRKAEEAK-KAEEARIEEVMKLYE 1602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TERNLDLEE--KVRELRETVADLEAINEMNDELQENARETELELREqldlgAAGVREAEKRVEAAQETVADYQQTIQKYR 503
Cdd:PTZ00121 1603 EEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK-----AEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688582234 504 ELTANLQEVNRELMSQQEANSEQQQQPAEIfdfKIKFAETKAYAKAI--EMELRKMEVIQANRQ 565
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEEL---KKKEAEEKKKAEELkkAEEENKIKAEEAKKE 1738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
236-558 |
6.48e-15 |
|
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: 80.11 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 236 QLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALeakerymeemadtaDAIEMATLDKEMAEERAESLQLEADALKERVD 315
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELS--------------QELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 316 ELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALvrmRDLSASEKQEhgkqqklmekknfELDALRCHKEKLQ 395
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL---NDLEARLSHS-------------RIPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 396 EEMKMAEKTIDELKEQVDASLG----AEEMVEMLTERNLDLEEKVRELRETVADLEA-INEMNDELqENARETELELREQ 470
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLekeyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkKEELEEEL-EELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 471 LDLGAAGVREAEKRVEAAQETVADYQQTIQKYR----ELTANLQEVNRELMSQQEANSEQQQQPAEIFDFKikfaETKAY 546
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE----DVQAE 959
|
330
....*....|..
gi 688582234 547 AKAIEMELRKME 558
Cdd:TIGR02169 960 LQRVEEEIRALE 971
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-562 |
1.34e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.41 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRA-LVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQnelqKQLKEAKREAKEALEAKERY 275
Cdd:PTZ00121 1273 KAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KKADAAKKKAEEAKKAAEAA 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMdleilKHEIEEKGSDGAASSYHVKQLEEQNARLKEA 355
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMRDLsasEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAE--KTIDELKEQVDASLGAEEmvemLTERNLDLE 433
Cdd:PTZ00121 1424 KKKAEEK---KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEAKKADE----AKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 434 EKVRELRETVADLEAINEMNDelQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVN 513
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKK--AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 688582234 514 RELMSQQEANSEQQQQPAEIFDFkIKFAETKAYAKAIEMELRKMEVIQA 562
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEV-MKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-527 |
1.49e-14 |
|
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: 78.95 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 207 KDLEEKLETLKMKRTEDKAKLKELekhKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAI 286
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 287 EMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASE 366
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 367 K-------QEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgAEEMVEMLTERNLDLEEKVREL 439
Cdd:TIGR02168 837 ErrledleEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL---LRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 440 RetvADLEAINEMNDELQENARETELELREQLD-LGAAGVREAEKRVEAAQETVADYQQTIQKYRELT---ANLQEVNre 515
Cdd:TIGR02168 914 R---RELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkiKELGPVN-- 988
|
330
....*....|..
gi 688582234 516 LMSQQEANSEQQ 527
Cdd:TIGR02168 989 LAAIEEYEELKE 1000
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-1031 |
1.68e-14 |
|
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: 78.95 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEEsLRALvkdLEEKLETLKMKRTEDKAkLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKR--EAKEALEAKE 273
Cdd:TIGR02168 152 AKPEE-RRAI---FEEAAGISKYKERRKET-ERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 rymeemadtadaIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEE-KGSDGAASsyhvKQLEEQNARL 352
Cdd:TIGR02168 227 ------------LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElRLEVSELE----EEIEELQKEL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 353 KEALVRMRDLSaSEKQEHgkqqklmekkNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASlgaEEMVEMLTERNLDL 432
Cdd:TIGR02168 291 YALANEISRLE-QQKQIL----------RERLANLERQLEELEAQLEELESKLDELAEELAEL---EEKLEELKEELESL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 433 EEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIqkyRELTANLQEV 512
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI---EELLKKLEEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 513 NRELMSQQEANSEQqqqpaEIFDFKIKFAETKAYAKAIEMELRKME--VIQANRQVSLL---ISFMPDSFLKHRGDHDCI 587
Cdd:TIGR02168 434 ELKELQAELEELEE-----ELEELQEELERLEEALEELREELEEAEqaLDAAERELAQLqarLDSLERLQENLEGFSEGV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 588 LALLL--------IPRLickSELISkqAQEKFELTESCSQKPGMRGAVGERLSFAAGLIYSLTllQAALHKYeHALSQCS 659
Cdd:TIGR02168 509 KALLKnqsglsgiLGVL---SELIS--VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLK--QNELGRV-TFLPLDS 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 660 VDVYKRVGSLYSELSVHERSLDFLIDLLYKD---------LLDETVNVEPLTKAI---KYYQHLYSIhlaeqpedctMQL 727
Cdd:TIGR02168 581 IKGTEIQGNDREILKNIEGFLGVAKDLVKFDpklrkalsyLLGGVLVVDDLDNALelaKKLRPGYRI----------VTL 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 728 ADHI-----------RFTQSALDCMAVEVGRLRAFI-QTGQDEEAFCVLLKDLDTSCSDIRQFCKKIRRRmpgtdapgip 795
Cdd:TIGR02168 651 DGDLvrpggvitggsAKTNSSILERRREIEELEEKIeELEEKIAELEKALAELRKELEELEEELEQLRKE---------- 720
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 796 aalsfgpqvceaLADSRRQLAWVNAVLQEVAAAAAQLiAPLSEHEGLPAVKLEDMAFKAAEQIYGSQGiNAQECLRQSCS 875
Cdd:TIGR02168 721 ------------LEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 876 VViATMNKMATAMQEGEYDSDrpqtgispvevraaALRAEITDAEG----LGLKLEDRETVIKELKKSLKIKGEELSEAN 951
Cdd:TIGR02168 787 LE-AQIEQLKEELKALREALD--------------ELRAELTLLNEeaanLRERLESLERRIAATERRLEDLEEQIEELS 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 952 VRLSLLEKKLDSASKDADERVEKIQAILDETDSlLKKKEKEFEETMDALQADIDQLESEKVELKHRIS------SQSKMT 1025
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEelreklAQLELR 930
|
....*.
gi 688582234 1026 IESLRG 1031
Cdd:TIGR02168 931 LEGLEV 936
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
207-490 |
3.72e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 207 KDLEEKLETLKMKRTEDKAKLKELEKHKIqleqlqewkskmqeqqnelqkQLKEAKREAKEALEAKERYMEEMADTADAI 286
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQRE---------------------QARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 287 EMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRdLSASE 366
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECR-VAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 367 KQEhgkqqklmekknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgAEEMVEMLTERNLDLEEKVRELRETVADL 446
Cdd:PRK02224 340 HNE-------------EAESLREDADDLEERAEELREEAAELESELEE---AREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 688582234 447 EAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQE 490
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
192-556 |
2.36e-13 |
|
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: 75.10 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 192 IPGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEK---HKIQLEQLQEWKSKMQE--------QQNELQKQLKE 260
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlrrEREKAERYQALLKEKREyegyellkEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 261 AKREAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESL-QLEADALKERVDELTMDLEILKHEIEEKGSDGAASS 339
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 340 YHVKQLEEQNARLKEalvRMRDLSASEKQEHGKQQKLMEkknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgAE 419
Cdd:TIGR02169 322 ERLAKLEAEIDKLLA---EIEELEREIEEERKRRDKLTE----EYAELKEELEDLRAELEEVDKEFAETRDELKD---YR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 420 EMVEMLTERNLDLEEKVRELRETVADL-EAINEMNDELqENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQqt 498
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLsEELADLNAAI-AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE-- 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 499 iQKYRELTANLQEVNRELMSQQE--ANSEQQQQPAEifdfkikfaETKAYAKAIEMELRK 556
Cdd:TIGR02169 469 -QELYDLKEEYDRVEKELSKLQRelAEAEAQARASE---------ERVRGGRAVEEVLKA 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
191-511 |
5.44e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 191 PIPGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQnELQKQLKEAKREAK---- 266
Cdd:PRK03918 439 PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK-ELAEQLKELEEKLKkynl 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 267 EALEAKERYMEEMADTADAI--EMATLDKEMaeERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGaassyhVKQ 344
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLkgEIKSLKKEL--EKLEELKKKLAELEKKLDELEEELAELLKELEELGFES------VEE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 345 LEEQNARLKEALVRMRDLSASEKQEHGKQQKLmEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDaslgaEEMVEM 424
Cdd:PRK03918 590 LEERLKELEPFYNEYLELKDAEKELEREEKEL-KKLEEELDKAFEELAETEKRLEELRKELEELEKKYS-----EEEYEE 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 425 LTERNLDLEEKVRELRetvADLEAINEMNDELQENARETELELREqldlgaagVREAEKRVEAAQETVADYQQTIQKYRE 504
Cdd:PRK03918 664 LREEYLELSRELAGLR---AELEELEKRREEIKKTLEKLKEELEE--------REKAKKELEKLEKALERVEELREKVKK 732
|
....*..
gi 688582234 505 LTANLQE 511
Cdd:PRK03918 733 YKALLKE 739
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
200-470 |
5.77e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 200 ESLRALVKDLEEKLETLKmKRTEDKAKLKELEKhkiQLEQLQEwKSKMQEQQNELQKQLKEAKREAKEAL-EAKERYMEE 278
Cdd:PRK02224 478 EELEAELEDLEEEVEEVE-ERLERAEDLVEAED---RIERLEE-RREDLEELIAERRETIEEKRERAEELrERAAELEAE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 279 MADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTmDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALvr 358
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERL-- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 359 mrdlsaSEKQEhgKQQKLMEKKNFE-LDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVR 437
Cdd:PRK02224 630 ------AEKRE--RKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE 701
|
250 260 270
....*....|....*....|....*....|...
gi 688582234 438 ELRETVADLEAINEMNDELQENARETELELREQ 470
Cdd:PRK02224 702 ALENRVEALEALYDEAEELESMYGDLRAELRQR 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-522 |
1.75e-12 |
|
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: 72.40 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 194 GPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREA-------- 265
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAEVeqleeria 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 266 ------KEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGS------ 333
Cdd:TIGR02168 751 qlskelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErlesle 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 334 -DGAASSYHVKQLEEQNARLKEALVRMRdlsasekQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQV 412
Cdd:TIGR02168 831 rRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 413 DAslgaeemvemLTERNLDLEEKVRELRETVAD----LEAINEMNDELQENARE---TELELREQLDLGAAG-VREAEKR 484
Cdd:TIGR02168 904 RE----------LESKRSELRRELEELREKLAQlelrLEGLEVRIDNLQERLSEeysLTLEEAEALENKIEDdEEEARRR 973
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 688582234 485 VEAAQETVA-----------DYQQTIQKYRELTANLQEVNRELMSQQEA 522
Cdd:TIGR02168 974 LKRLENKIKelgpvnlaaieEYEELKERYDFLTAQKEDLTEAKETLEEA 1022
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
197-532 |
1.88e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDgaassyhVKQLEEQNARLKEAL 356
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED-------ADDLEERAEELREEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 357 VRMRDLSASEKQEHGKQQKLMEKKNFELDALRC--------------HKEKLQEE--------------MKMAEKTIDEL 408
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgnaedFLEELREErdelrereaeleatLRTARERVEEA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 409 KEQVDA--------SLGAEEMVEMLTERnldlEEKVRELRETVADLEAinemndelQENARETELELREQLDLGAAGVRE 480
Cdd:PRK02224 446 EALLEAgkcpecgqPVEGSPHVETIEED----RERVEELEAELEDLEE--------EVEEVEERLERAEDLVEAEDRIER 513
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 688582234 481 AEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAE 532
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-565 |
1.36e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRA--LVKDLEE--KLETLKmKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQ--NELQKQLKEAKREAKEALE 270
Cdd:PTZ00121 1426 KAEEKKKAdeAKKKAEEakKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKK 1504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 271 AKERymEEMADTADAIEMATLDKEM--AEERAESLQLEADALKERVDELTMDLEILKHE----IEEKGSDGAASSYHVKQ 344
Cdd:PTZ00121 1505 AAEA--KKKADEAKKAEEAKKADEAkkAEEAKKADEAKKAEEKKKADELKKAEELKKAEekkkAEEAKKAEEDKNMALRK 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 345 LEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRchkeKLQEEMKMAEKTIDELKEQVDAslgAEEMVEM 424
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK----KAEEEKKKVEQLKKKEAEEKKK---AEELKKA 1655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 425 LTERNLDLEEKVRELREtvaDLEAINEMNDELQENARETELELREQldlgaagvrEAEKRVEAAQETVADYQQTIQKYRE 504
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEA---------EEAKKAEELKKKEAEEKKKAEELKK 1723
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 505 ltanLQEVNRELMSQQEANSEQQQQPAEifDFKIKFAETKAYAKAIEMELRKMEVIQANRQ 565
Cdd:PTZ00121 1724 ----AEEENKIKAEEAKKEAEEDKKKAE--EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
199-558 |
1.36e-11 |
|
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: 69.38 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 199 EESLRALVKDLEEKLETLkMKRTEDKAKlKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEE 278
Cdd:pfam15921 244 EDQLEALKSESQNKIELL-LQQHQDRIE-QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 279 MADTADAIEMATLD-KEMAEERAESLQLE--------ADALKERvDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQN 349
Cdd:pfam15921 322 LESTVSQLRSELREaKRMYEDKIEELEKQlvlanselTEARTER-DQFSQESGNLDDQLQKLLADLHKREKELSLEKEQN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEalvrmRDLSASEKQEHGKQQklMEKKNFE---LDA-LRCHKEKLQEEMKMAEKTIDELKEQVD--ASLGAE---- 419
Cdd:pfam15921 401 KRLWD-----RDTGNSITIDHLRRE--LDDRNMEvqrLEAlLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQlest 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 420 -----EMVEMLTERNLDLEEKVRELRETVADLE----AINEMNDELQENARETELELREQLDLGAAG--VREAEKRVEAA 488
Cdd:pfam15921 474 kemlrKVVEELTAKKMTLESSERTVSDLTASLQekerAIEATNAEITKLRSRVDLKLQELQHLKNEGdhLRNVQTECEAL 553
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 489 QETVADYQQTIQKYRELTANL-QEVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKME 558
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIENMtQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE 624
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
184-534 |
3.38e-11 |
|
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: 68.07 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 184 LPSPGAPPIPGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQL-QEWKSKM-------QEQQNELQ 255
Cdd:TIGR00618 522 NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCdNRSKEDIpnlqnitVRLQDLTE 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 256 KQLKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDE---LTMDLEILKHEIEEKG 332
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREhalSIRVLPKELLASRQLA 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 333 SDGAASSYhvkqleEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALrchKEKLQEEMKMAEKTIDELKEQV 412
Cdd:TIGR00618 682 LQKMQSEK------EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL---GSDLAAREDALNQSLKELMHQA 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 413 DASLGAEEMV-EMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDlgaagvrEAEKRVEAAQET 491
Cdd:TIGR00618 753 RTVLKARTEAhFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP-------SDEDILNLQCET 825
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 688582234 492 VA-DYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIF 534
Cdd:TIGR00618 826 LVqEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
197-563 |
9.86e-11 |
|
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: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDL---EEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKE 273
Cdd:TIGR04523 304 KEQDWNKELKSELknqEKKLEEIQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEM-------ADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLE 346
Cdd:TIGR04523 381 SYKQEIknlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 347 EQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgaeemvemLT 426
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----------LE 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 427 ERNLDLEEKVRELRETvadleaINEMNDELQENARETE-LELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYR-- 503
Cdd:TIGR04523 531 SEKKEKESKISDLEDE------LNKDDFELKKENLEKEiDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIke 604
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688582234 504 --ELTANLQEVNRELmsqQEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKMEVIQAN 563
Cdd:TIGR04523 605 ieEKEKKISSLEKEL---EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-483 |
1.07e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQL-QEWK--SKMQEQQNELQKQLKEAKREAK--EALE 270
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELeKKAEeyEKLKEKLIKLKGEIKSLKKELEklEELK 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 271 AKERYMEEMADTADAiEMATLDKEMAEERAESLqleaDALKERVDEL-------------TMDLEILKHEIEEKGSDGAA 337
Cdd:PRK03918 556 KKLAELEKKLDELEE-ELAELLKELEELGFESV----EELEERLKELepfyneylelkdaEKELEREEKELKKLEEELDK 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 338 SSyhvKQLEEQNARLKEALVRMRDLSAS-EKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASL 416
Cdd:PRK03918 631 AF---EELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688582234 417 GAEEMVEMLtERNLdleEKVRELRETVADLEAINEMN--DELQENARETELELREQLDLGAAGVREAEK 483
Cdd:PRK03918 708 KAKKELEKL-EKAL---ERVEELREKVKKYKALLKERalSKVGEIASEIFEELTEGKYSGVRVKAEENK 772
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-486 |
1.14e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhKIQLEQLqewksKMQEQQNELQKQLKEAKREAKEALEAKERY 275
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK-KMKAEEA-----KKAEEAKIKAEELKKAEEEKKKVEQLKKKE 1642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTAD---AIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKgsdgaASSYHVKQLEEQNARL 352
Cdd:PTZ00121 1643 AEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-----KKAEELKKKEAEEKKK 1717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 353 KEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLgAEEMVEMLTERNLDL 432
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI-EEELDEEDEKRRMEV 1796
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 688582234 433 EEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVE 486
Cdd:PTZ00121 1797 DKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-558 |
1.75e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRAlvkdlEEKLETLKMKRTEDKAKLKELEKHKiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:PTZ00121 1177 KAEAARKA-----EEVRKAEELRKAEDARKAEAARKAE-EERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKEMAEERAESLQlEADALKeRVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEAl 356
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEAR-KADELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA- 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 357 vRMRDLSASEKQEHGKQQKLMEKKnfELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKV 436
Cdd:PTZ00121 1328 -KKKADAAKKKAEEAKKAAEAAKA--EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 437 RELREtVADLEAINEMNDELQENARETELElrEQLDLGAAGVREAEKRVEAAQEtvADYQQTIQKYRELTANLQEVNREl 516
Cdd:PTZ00121 1405 KKADE-LKKAAAAKKKADEAKKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKK- 1478
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 688582234 517 mSQQEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKME 558
Cdd:PTZ00121 1479 -AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-558 |
1.80e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEaLEAKERY 275
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADaiEMATLDKEMAEERAESLQLEadALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEA 355
Cdd:PRK03918 285 LKELKEKAE--EYIKLSEFYEEYLDELREIE--KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMRDLSASEKQEHGKQQKL----MEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEM------L 425
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLtgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpV 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREqldlgaagvreaekrveaaQETVADYQQTIQKYREL 505
Cdd:PRK03918 441 CGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-------------------LEKVLKKESELIKLKEL 501
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 688582234 506 TANLQEVNRELmsqQEANSEQQQQPAEIFD-FKIKFAETKAYAKAIEMELRKME 558
Cdd:PRK03918 502 AEQLKELEEKL---KKYNLEELEKKAEEYEkLKEKLIKLKGEIKSLKKELEKLE 552
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-560 |
3.61e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQ--------------------LQEWKSKMQEQQNELQK 256
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkelLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 257 ---QLKEAKREAK--EALEAKERYMEEMADTADAI-----EMATLDKEMAEERAEslqlEADALKERVDELTMDLEILKH 326
Cdd:PRK03918 471 ieeKERKLRKELRelEKVLKKESELIKLKELAEQLkeleeKLKKYNLEELEKKAE----EYEKLKEKLIKLKGEIKSLKK 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 327 EIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTID 406
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 407 ELKEqvdaslgAEEMVEmlternlDLEEKVRELRETVADLEaiNEMNDELQENARETELELREQLdlgaAGVREAEKRVE 486
Cdd:PRK03918 627 ELDK-------AFEELA-------ETEKRLEELRKELEELE--KKYSEEEYEELREEYLELSREL----AGLRAELEELE 686
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688582234 487 AAQETVAdyqQTIQKYRELTANLQEVNRELMSQQEANSEQQqqpaeifDFKIKFAETKAYAKaiEMELRKMEVI 560
Cdd:PRK03918 687 KRREEIK---KTLEKLKEELEEREKAKKELEKLEKALERVE-------ELREKVKKYKALLK--ERALSKVGEI 748
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-501 |
8.64e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKmKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKqlKEAKREAKEALEAKERY 275
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELKKAEELK 1558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEE-----QNA 350
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekkkvEQL 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 RLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKmaEKTIDELKEQVDASLGAEEMVEMLTERNL 430
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 431 DLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQK 501
Cdd:PTZ00121 1717 KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
196-557 |
1.36e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKM---------KRTEDKAKLKELEKHKIQLE-QLQEWKSKmQEQQNELQKQLKEAKREA 265
Cdd:COG4717 101 EEELEELEAELEELREELEKLEKllqllplyqELEALEAELAELPERLEELEeRLEELREL-EEELEELEAELAELQEEL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 266 KEALEAKERYME-EMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEieekgsdgaassyhvKQ 344
Cdd:COG4717 180 EELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE---------------ER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 345 LEEQNARLKEA----LVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDaslgAEE 420
Cdd:COG4717 245 LKEARLLLLIAaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE----EEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 421 MVEMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQL---DLGAAGVrEAEKRVEAAQETVADYQQ 497
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaaLLAEAGV-EDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 498 TIQKYRELTANLQEVNRELMSQQEANSEQQQqpaeifdfKIKFAETKAYAKAIEMELRKM 557
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEEL--------EEELEELEEELEELEEELEEL 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
208-556 |
1.49e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 208 DLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEakerymEEMADTADAIE 287
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAEELE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 288 MATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHE------------------IEEKGSDGAASSYHV------- 342
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallaLLGLGGSLLSLILTIagvlflv 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 343 --------------KQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLmeKKNFELDALRCHKEKLQEeMKMAEKTIDEL 408
Cdd:COG4717 283 lgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGL--PPDLSPEELLELLDRIEE-LQELLREAEEL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 409 KEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDlgAAGVREAEKRVEAA 488
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE--ALDEEELEEELEEL 437
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 489 QETVADYQQTIQKYRELTANLQEVNRELMSQ---QEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRK 556
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDgelAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
200-483 |
1.59e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 60.69 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 200 ESLRALVKDLEEKLETLKmkrtedkaklKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEM 279
Cdd:COG1340 4 DELSSSLEELEEKIEELR----------EEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 280 ADTADAI-----EMATLDKEMAEERAESLQLEA-----DALKERVDELTMDLEILKHEIEEKgsdgaassyhvKQLEEQN 349
Cdd:COG1340 74 KELKEERdelneKLNELREELDELRKELAELNKaggsiDKLRKEIERLEWRQQTEVLSPEEE-----------KELVEKI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEALVRMrdlsaseKQEHGKQQKLMEKKNfELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAeemVEMLTERN 429
Cdd:COG1340 143 KELEKELEKA-------KKALEKNEKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE---ADELRKEA 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 688582234 430 LDLEEKVRELRETVadlEAINEMNDELQENARETELELREQLDLGAAGVREAEK 483
Cdd:COG1340 212 DELHKEIVEAQEKA---DELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
204-549 |
4.53e-09 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 60.74 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 204 ALVKDLEEKLETLKMKRTEDKakLKELekhkiqLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTA 283
Cdd:COG5185 234 ALKGFQDPESELEDLAQTSDK--LEKL------VEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 284 DaIEMATLDKEMAEERAESLQLEADALKERvdelTMDLEILKHEIEEKgsdgaassyhVKQLEEQNARLKEALVRMRDLS 363
Cdd:COG5185 306 D-IKKATESLEEQLAAAEAEQELEESKRET----ETGIQNLTAEIEQG----------QESLTENLEAIKEEIENIVGEV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 364 ASEKQEhgkqqklmEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGA-----EEMVEMLTERNLDLEEKVRE 438
Cdd:COG5185 371 ELSKSS--------EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAadrqiEELQRQIEQATSSNEEVSKL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 439 LRETVADL-----EAINEMNDELQENARETELELREQLDlgaagvrEAEKRVEAAQETVADYQQTIQKY-----RELTAN 508
Cdd:COG5185 443 LNELISELnkvmrEADEESQSRLEEAYDEINRSVRSKKE-------DLNEELTQIESRVSTLKATLEKLrakleRQLEGV 515
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 688582234 509 LQEVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKA 549
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNA 556
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-472 |
4.60e-09 |
|
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: 61.24 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLEtlKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAK---REAKEALEAKE 273
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEaeiDKLLAEIEELE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEMADTADAI--EMATLDKEMAE--ERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQN 349
Cdd:TIGR02169 343 REIEEERKRRDKLteEYAELKEELEDlrAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEALVRMRDlsasekqehgkqqklmekknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgAEEMVEMLTERN 429
Cdd:TIGR02169 423 ADLNAAIAGIEA---------------------KINELEEEKEDKALEIKKQEWKLEQLAADLSK---YEQELYDLKEEY 478
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 688582234 430 LDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLD 472
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
205-523 |
8.02e-09 |
|
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: 60.45 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 205 LVKDLEEKLETLKMKRTEDKAKLKELEKHKiqlEQLQEWKSKMQEQQNELQKQL---KEAKREAKEALEAKERYMEEMAD 281
Cdd:TIGR01612 749 INKDLNKILEDFKNKEKELSNKINDYAKEK---DELNKYKSKISEIKNHYNDQInidNIKDEDAKQNYDKSKEYIKTISI 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 282 TADAI-----EMATLDKEMAEERAESLQLEADAlKERVDELTMDLEILKHEIEEKGSDGAASSYH-------------VK 343
Cdd:TIGR01612 826 KEDEIfkiinEMKFMKDDFLNKVDKFINFENNC-KEKIDSEHEQFAELTNKIKAEISDDKLNDYEkkfndskslineiNK 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 344 QLEE--QN----ARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRchkeklqeEMKMAEKTideLKEQVDASL- 416
Cdd:TIGR01612 905 SIEEeyQNintlKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIK--------ESNLIEKS---YKDKFDNTLi 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 417 -GAEEMVEMLTERNL-DLEEKVRELretvadLEAINEMNDELQENARETeleLREQLDLGAAGVREAEKRVEAAQETVAD 494
Cdd:TIGR01612 974 dKINELDKAFKDASLnDYEAKNNEL------IKYFNDLKANLGKNKENM---LYHQFDEKEKATNDIEQKIEDANKNIPN 1044
|
330 340 350
....*....|....*....|....*....|....*...
gi 688582234 495 YQQTIQKY---------RELTANLQEVNRELMSQQEAN 523
Cdd:TIGR01612 1045 IEIAIHTSiyniideieKEIGKNIELLNKEILEEAEIN 1082
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
190-560 |
8.72e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 190 PPIPGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEAL 269
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 270 EAKERyMEEMADTADAIEMATLDK-----EMAEERAESLQLEADALKERVDELTMDLEILKHEIEE-KGSDGAASSYHVK 343
Cdd:PRK03918 366 EAKAK-KEELERLKKRLTGLTPEKlekelEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElKKAKGKCPVCGRE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 344 QLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKtIDELKEQVDaSLGAEEM-- 421
Cdd:PRK03918 445 LTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-LKELEEKLK-KYNLEELek 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 422 ----VEMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELEL----REQLDLGAAGVREAEKRVEAAQETVa 493
Cdd:PRK03918 523 kaeeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELaellKELEELGFESVEELEERLKELEPFY- 601
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688582234 494 dyqqtiQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIfdfkikfAETKAYAKAIEMELRKMEVI 560
Cdd:PRK03918 602 ------NEYLELKDAEKELEREEKELKKLEEELDKAFEEL-------AETEKRLEELRKELEELEKK 655
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
197-415 |
2.38e-08 |
|
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: 57.85 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKEM-----------AEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQL 345
Cdd:COG4942 104 EELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 346 EEQNARLKEALVRMRDLSASEKQEHGKQQKlmekknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDAS 415
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAA-------ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-532 |
8.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 297 EERAESLQLEADAlKERVDELTMDLEILKHEieekgsdgaASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKL 376
Cdd:COG1196 199 ERQLEPLERQAEK-AERYRELKEELKELEAE---------LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 377 MEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgaeemvemLTERNLDLEEKVRELRETVADLEainemndEL 456
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIAR----------LEERRRELEERLEELEEELAELE-------EE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 457 QENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAE 532
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-566 |
8.71e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLK--MKRTED-KAKLKELEKHKIQLEQlqewkskmqeQQNELQKQLkeakREAKEALEAKE 273
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEkfIKRTENiEELIKEKEKELEEVLR----------EINEISSEL----PELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEMADTADAIematldkEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEkgsdgaassyhvkqLEEQNARLK 353
Cdd:PRK03918 228 KEVKELEELKEEI-------EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE--------------LEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 354 EAlvrmrdlsASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQvdaslgaEEMVEMLTERNLDLE 433
Cdd:PRK03918 287 EL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-------EERLEELKKKLKELE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 434 EKVRELRETVADLEAINEMNDELQE-NARETELELREQldlgAAGVREAEKRVEAAQETVADYQQTI----QKYRELTAN 508
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIgelkKEIKELKKA 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688582234 509 LQEV----------NRELMSQQEAN------SEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKMEVIQANRQV 566
Cdd:PRK03918 428 IEELkkakgkcpvcGRELTEEHRKElleeytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
198-473 |
9.76e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 198 EEESLRalvkDLEEKLETLKMKRTEdKAKLKELEKHKIQ-LEQL-----------QEWKSKMQEQQNELQKQLKEAK--R 263
Cdd:pfam15921 539 EGDHLR----NVQTECEALKLQMAE-KDKVIEILRQQIEnMTQLvgqhgrtagamQVEKAQLEKEINDRRLELQEFKilK 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 264 EAKEA----LEAK--ERYMEEMADTADAIEMATLDKEMAEERAESLQlEADALKERVDELTMDLEILKHEIEEKGSDGAA 337
Cdd:pfam15921 614 DKKDAkireLEARvsDLELEKVKLVNAGSERLRAVKDIKQERDQLLN-EVKTSRNELNSLSEDYEVLKRNFRNKSEEMET 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 338 SSYHVK-QLEEQNARLKEALVRMRDLSASE----KQEHGKQQKLMEKKNfELDALRCHKEKLQEEMKMAEKTIDELKEQv 412
Cdd:pfam15921 693 TTNKLKmQLKSAQSELEQTRNTLKSMEGSDghamKVAMGMQKQITAKRG-QIDALQSKIQFLEEAMTNANKEKHFLKEE- 770
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 413 dASLGAEEMVEMLTERN-----LD-LEEKVRELRETVADLEA--------INEMNDELQENARET-ELELREQLDL 473
Cdd:pfam15921 771 -KNKLSQELSTVATEKNkmageLEvLRSQERRLKEKVANMEValdkaslqFAECQDIIQRQEQESvRLKLQHTLDV 845
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
343-533 |
1.36e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 343 KQLEEQNARLKEALVRMRDLsaseKQEHG-----KQQKLMEKKNFELDALRchkEKLQEEMKMAEKTIDELKEQVD---- 413
Cdd:COG3206 182 EQLPELRKELEEAEAALEEF----RQKNGlvdlsEEAKLLLQQLSELESQL---AEARAELAEAEARLAALRAQLGsgpd 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 414 --ASLGAEEMVEMLTERNLDLEEKVRELRET-------VADLEA-INEMNDELQENARETELELREQLDLGAAGVREAEK 483
Cdd:COG3206 255 alPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAqIAALRAQLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 688582234 484 RVEAAQETVADYQQTIQKYRELTANLqEVNRE-----LMSQQEANSEQQQQPAEI 533
Cdd:COG3206 335 QLAQLEARLAELPELEAELRRLEREV-EVARElyeslLQRLEEARLAEALTVGNV 388
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
210-516 |
1.51e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 210 EEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQkQLKEAKREAKEALEAKERYmeemadtadaiemA 289
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEE---RLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREI-------------A 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 290 TLDKEMAEERAESLQLEadALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQE 369
Cdd:COG4913 672 ELEAELERLDASSDDLA--ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 370 HGKQQklmekknFELDALRCHKEKLQEEMkmaEKTIDELKEQVDASlgAEEMVEMLTERNLDLEEKVRELRETVADLEAI 449
Cdd:COG4913 750 LLEER-------FAAALGDAVERELRENL---EERIDALRARLNRA--EEELERAMRAFNREWPAETADLDADLESLPEY 817
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688582234 450 NEMNDELQENaretELELREQldlgaagvREAEKRVEAAQETVADYQQTI-QKYRELTANLQEVNREL 516
Cdd:COG4913 818 LALLDRLEED----GLPEYEE--------RFKELLNENSIEFVADLLSKLrRAIREIKERIDPLNDSL 873
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
196-502 |
1.87e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLE-QLQEWKSKMQEQQNELQKQLKEAKREAKEaleaker 274
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtQLKVLSRSINKIKQNLEQKQKELKSKEKE------- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 275 ymeemadtadaIEMATLDKEMAEERAESLQLEADALKERVDEltmdLEILKHEIEEKGSDGAassyhvKQLEEQNARLKE 354
Cdd:TIGR04523 498 -----------LKKLNEEKKELEEKVKDLTKKISSLKEKIEK----LESEKKEKESKISDLE------DELNKDDFELKK 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 355 ALVrmrdlsasEKQEHGKQQKLMEKKNfELDALRCHKEKLQEEMKMAEKTIDELKEQvdaslgaeemVEMLTERNLDLEE 434
Cdd:TIGR04523 557 ENL--------EKEIDEKNKEIEELKQ-TQKSLKKKQEEKQELIDQKEKEKKDLIKE----------IEEKEKKISSLEK 617
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688582234 435 KVRELRETVADLEAInEMNDELQENARETELEL-REQLDLGAAGVREAEKRVEAAQETVADYQQTIQKY 502
Cdd:TIGR04523 618 ELEKAKKENEKLSSI-IKNIKSKKNKLKQEVKQiKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDW 685
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
197-516 |
2.13e-07 |
|
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: 55.75 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQL--EQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKER 274
Cdd:pfam02463 194 ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLneERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 275 YMEEMAdtadAIEMATLDKEMAEERAESLQLEADALKER----VDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNA 350
Cdd:pfam02463 274 NKEEEK----EKKLQEEELKLLAKEEEELKSELLKLERRkvddEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 RLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEemvEMLTERNL 430
Cdd:pfam02463 350 KREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE---DLLKEEKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAagvREAEKRVEAAQETVADYQQTIQKYRELTANLQ 510
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE---DLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
....*.
gi 688582234 511 EVNREL 516
Cdd:pfam02463 504 KARSGL 509
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
208-465 |
2.16e-07 |
|
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: 55.25 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 208 DLEEKLETLKMKRTEDKAKLKELEkhkiqLEQLQEWKSKMQEQQNELQKQL---KEAKREAKEALEAKERYMEEMADTAD 284
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLE-----LDEAEEALEEIEERIDQLYDLLekeVDAKKYVEKNLPEIEDYLEHAEEQNK 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 285 AI--EMATLDK-----EMAEERAESLQLEADALKERVDELTMDLE-------ILKHEIEEKGSdgaassyHVKQLEEQNA 350
Cdd:pfam06160 309 ELkeELERVQQsytlnENELERVRGLEKQLEELEKRYDEIVERLEekevaysELQEELEEILE-------QLEEIEEEQE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 RLKEALVRMRdlsaseKQEHGKQQKLmEKKNFELDALRCHKEKLQeeMKMAEKTIDELKEQVDASLgaEEMVEMLTERNL 430
Cdd:pfam06160 382 EFKESLQSLR------KDELEAREKL-DEFKLELREIKRLVEKSN--LPGLPESYLDYFFDVSDEI--EDLADELNEVPL 450
|
250 260 270
....*....|....*....|....*....|....*
gi 688582234 431 DLEEKVRELRETVADLEAINEMNDELQENARETEL 465
Cdd:pfam06160 451 NMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQ 485
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
209-546 |
2.84e-07 |
|
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: 55.34 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 209 LEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTAD-AIE 287
Cdd:pfam15818 9 LLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKGKYQlATE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 288 MATLDKEMAEERAESLQLEADALKERVDELTMDL---------------EILKHEIEEKGSDGAASSYHVKQleEQNarL 352
Cdd:pfam15818 89 IKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLqlhllakedhhkqlnEIEKYYATITGQFGLVKENHGKL--EQN--V 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 353 KEALVRMRDLSA-SEKQEHGKQQKLMEKKNFELDALrchKEKLQEEMKMAEKTID-ELKEQVDASLgaEEMVEMLTERNL 430
Cdd:pfam15818 165 QEAIQLNKRLSAlNKKQESEICSLKKELKKVTSDLI---KSKVTCQYKMGEENINlTIKEQKFQEL--QERLNMELELNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEKVRELRETVADL---------------EAINEMNDELQEnARETELELREQLDLGAAGVREAEKRVEAAQETVADY 495
Cdd:pfam15818 240 KINEEITHIQEEKQDIiisfqhmqqllqqqtQANTEMEAELKA-LKENNQTLERDNELQREKVKENEEKFLNLQNEHEKA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 688582234 496 QQTIQKYRE-LTANLQEVNRELMSQQEANSEQQQQPAEIFDFKiKFAETKAY 546
Cdd:pfam15818 319 LGTWKKHVEeLNGEINEIKNELSSLKETHIKLQEHYNKLCNQK-KFEEDKKF 369
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
198-455 |
3.70e-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: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 198 EEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWK-SKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKEMAEERAESLQLEADAlkERVDELTMDLEILKHEIEEKGSDgaASSYHVKQLEEQN---ARLK 353
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESGKAQAEV--ERLLGILREVENEKNDKDKKIAE--LESLTLRQMKEQNkkvANIK 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 354 EALVRMRDLSASEKQEHGKQQKlmekknfelDALRCHKEKLQEEMKMA-EKTIDELkEQVDASLGAEEmvEMLTERNLDL 432
Cdd:pfam10174 625 HGQQEMKKKGAQLLEEARRRED---------NLADNSQQLQLEELMGAlEKTRQEL-DATKARLSSTQ--QSLAEKDGHL 692
|
250 260
....*....|....*....|...
gi 688582234 433 EEKVRELREtvaDLEAINEMNDE 455
Cdd:pfam10174 693 TNLRAERRK---QLEEILEMKQE 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
219-448 |
4.61e-07 |
|
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: 53.61 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 219 KRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIemATLDKEMAEE 298
Cdd:COG4942 21 AAAEAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL--AELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 299 RAEsLQLEADALKERVDELTM-----DLEILKH--EIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHG 371
Cdd:COG4942 96 RAE-LEAQKEELAELLRALYRlgrqpPLALLLSpeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688582234 372 KQQKLmekknfeLDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgaeemvemLTERNLDLEEKVRELRETVADLEA 448
Cdd:COG4942 175 ELEAL-------LAELEEERAALEALKAERQKLLARLEKELAE----------LAAELAELQQEAEELEALIARLEA 234
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
177-569 |
5.23e-07 |
|
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: 54.21 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 177 IPSPVGALPSPGAPPIPGPSKEEESL--RALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQ--N 252
Cdd:pfam02463 583 LIPKLKLPLKSIAVLEIDPILNLAQLdkATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAekS 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 253 ELQKQLKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEM--AEERAESLQLEADALKERVDELTMDLEILKHEIEE 330
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEqrEKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 331 KGSDgaassyhVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRcHKEKLQEE---MKMAEKTIDE 407
Cdd:pfam02463 743 QKID-------EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKE-EKLKAQEEelrALEEELKEEA 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 408 LKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEA 487
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 488 AQEtvaDYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKmEVIQANRQVS 567
Cdd:pfam02463 895 EKE---EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEE-RNKRLLLAKE 970
|
..
gi 688582234 568 LL 569
Cdd:pfam02463 971 EL 972
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
206-571 |
5.81e-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: 53.87 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 206 VKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQlqEWKSKmQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADA 285
Cdd:TIGR04523 77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKND-KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 286 IEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHE----------IEEKGSDGAASSYHVKQLEEQNARLKEA 355
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKllklelllsnLKKKIQKNKSLESQISELKKQNNQLKDN 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMR-DLSASEKQEHGKQQKLMEKKNFELDALRCHKEKlQEEMKMAEKTIDELKEQVD------ASLGAEEMVEMLTER 428
Cdd:TIGR04523 234 IEKKQqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-QKELEQNNKKIKELEKQLNqlkseiSDLNNQKEQDWNKEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 429 NLDLEEKVRELRETVADL----EAINEMNDELQ------ENARETELELREQLdlgaagvREAEKRVEAAQETVADYQQT 498
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQIsqnnKIISQLNEQISqlkkelTNSESENSEKQREL-------EEKQNEIEKLKKENQSYKQE 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688582234 499 IQKyreLTANLQEVNRELmsqqeansEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKMEVIQANRQVSLLIS 571
Cdd:TIGR04523 386 IKN---LESQINDLESKI--------QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
222-529 |
7.15e-07 |
|
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: 53.82 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 222 EDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAK--------EALEAKERYMEEMADTADAIEMATLDK 293
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEyyqlkeklELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 294 EMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAassyhVKQLEEQNARLKEALVRMRDLSASEKQEHGKQ 373
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK-----LLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 374 QKlmEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMN 453
Cdd:pfam02463 322 EK--KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 454 DELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQ 529
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
197-409 |
7.38e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.61 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQL-EQLQEWKSKMQEQQNELQ-------------------- 255
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELnEKLNELREELDELRKELAelnkaggsidklrkeierle 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 256 --------------------KQLKEAKREAKEALEAKERYMEEMADTADA-IEMATLDKEMAE--ERAESLQLEADALKE 312
Cdd:COG1340 123 wrqqtevlspeeekelvekiKELEKELEKAKKALEKNEKLKELRAELKELrKEAEEIHKKIKElaEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 313 RVDELTMDLEILKHEIEEKGsdgaassyhvKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLmeKKNFELDALRCHKE 392
Cdd:COG1340 203 EADELRKEADELHKEIVEAQ----------EKADELHEEIIELQKELRELRKELKKLRKKQRAL--KREKEKEELEEKAE 270
|
250
....*....|....*...
gi 688582234 393 KLQEEMKMAEK-TIDELK 409
Cdd:COG1340 271 EIFEKLKKGEKlTTEELK 288
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
196-304 |
7.82e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.68 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKiqleqlQEWKSKMQEQQNELQKQLKEAKREAKEAL-EAKE- 273
Cdd:PRK00409 512 GEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLK------EELEEKKEKLQEEEDKLLEEAEKEAQQAIkEAKKe 585
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 688582234 274 --------RYMEEMADTA----DAIEMATLDKEMAEERAESLQ 304
Cdd:PRK00409 586 adeiikelRQLQKGGYASvkahELIEARKRLNKANEKKEKKKK 628
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
198-558 |
1.62e-06 |
|
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: 52.38 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 198 EEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYme 277
Cdd:pfam05622 8 EKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 278 emadtadAIEMATLDKEMAE------------ERAESLQLEADALKERVDELTMdLEILKHEIEEKGSDGAASSYHVKQL 345
Cdd:pfam05622 86 -------RIKCEELEKEVLElqhrneeltslaEEAQALKDEMDILRESSDKVKK-LEATVETYKKKLEDLGDLRRQVKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 346 EEQNA-------RLKEALVR--------------MRDLSASEKQEHGKQQKL-MEKKNFE--LDALRCHKEKLQEEMKMA 401
Cdd:pfam05622 158 EERNAeymqrtlQLEEELKKanalrgqletykrqVQELHGKLSEESKKADKLeFEYKKLEekLEALQKEKERLIIERDTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 402 EKTIDELK---EQVDASLGAEEMVE--MLTERNLDLEEKVRELRETVADLEAINEM---NDELQENARETEL-------- 465
Cdd:pfam05622 238 RETNEELRcaqLQQAELSQADALLSpsSDPGDNLAAEIMPAEIREKLIRLQHENKMlrlGQEGSYRERLTELqqlledan 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 466 ----ELREQLDLGAAGVREAEKRVEAAQETVA-------DYQQTIQKYRELTANLQEVNRELMSQQEANSE----QQQQP 530
Cdd:pfam05622 318 rrknELETQNRLANQRILELQQQVEELQKALQeqgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEElepkQDSNL 397
|
410 420
....*....|....*....|....*...
gi 688582234 531 AEifdfkiKFAETKAYAKAIEMELRKME 558
Cdd:pfam05622 398 AQ------KIDELQEALRKKDEDMKAME 419
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
200-535 |
1.70e-06 |
|
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: 52.65 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 200 ESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQ-LQEWKSKMQEQQNELQKQLKEA--KREAKEALEAKERym 276
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEeVDSLKSQLADYQQALDVQQTRAiqYQQAVQALEKARA-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 eemadtadAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEIlkheieekgSDGAASSY-HVKQLEEQNA----- 350
Cdd:COG3096 428 --------LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSV---------ADAARRQFeKAYELVCKIAgever 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 -----RLKEALVRMRDLSASEKQEHGKQQKLMEKknfeldalrchkEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEML 425
Cdd:COG3096 491 sqawqTARELLRRYRSQQALAQRLQQLRAQLAEL------------EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TERnldleekvrelretvadLEAINEMNDELQENARETELELREQLDLGAAGVREAEKR--------------------- 484
Cdd:COG3096 559 LAE-----------------LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdalerlreqsgea 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 688582234 485 VEAAQETVADYQQTIQKYRELTANLQEVnRELMSQQEANSEQQQQPAEIFD 535
Cdd:COG3096 622 LADSQEVTAAMQQLLEREREATVERDEL-AARKQALESQIERLSQPGGAED 671
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
223-504 |
2.16e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 52.21 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 223 DKAKLKELEkhkiQLEQLQEWKSKMQEQQNELQKQLKEAkrEAKEALEAKERYMEEMADTadaiEMATLDKEMAEERA-- 300
Cdd:PLN02939 148 NQARLQALE----DLEKILTEKEALQGKINILEMRLSET--DARIKLAAQEKIHVEILEE----QLEKLRNELLIRGAte 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 301 ----ESLQLEADALKERVDELTMDLEILKHEIEEKgsdgAASSYHVKQLEEQNARLKEALvrmRDLsasEKQEHGKQQKL 376
Cdd:PLN02939 218 glcvHSLSKELDVLKEENMLLKDDIQFLKAELIEV----AETEERVFKLEKERSLLDASL---REL---ESKFIVAQEDV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 377 MEKKNFELDALRCHKEKLQEemkmaekTIDELKEQVDASLgaeemveMLTERNLDLEEKVRELRETVADLEaINEMNDEL 456
Cdd:PLN02939 288 SKLSPLQYDCWWEKVENLQD-------LLDRATNQVEKAA-------LVLDQNQDLRDKVDKLEASLKEAN-VSKFSSYK 352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 688582234 457 QENARETELELREQLDlgaAGVREAEKRVEAAQETVADYQQTIQKYRE 504
Cdd:PLN02939 353 VELLQQKLKLLEERLQ---ASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
384-558 |
2.62e-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: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 384 LDALRCHKEKLQEEMKMAEKTIDELKEQVDA---SLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMNDELQ--- 457
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDAlqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAale 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 458 ---ENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIF 534
Cdd:COG4913 692 eqlEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
170 180
....*....|....*....|....
gi 688582234 535 DFKIKFAETKAYAKAIEMElRKME 558
Cdd:COG4913 772 EERIDALRARLNRAEEELE-RAMR 794
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
207-529 |
3.07e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 207 KDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREakEALEAKERYMEEMADTAdai 286
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAAAITC--- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 287 emaTLDKEMAEERAesLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASE 366
Cdd:TIGR00618 450 ---TAQCEKLEKIH--LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 367 ---------KQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKT-------IDELKEQVDASLGAEEMVEMLTERNL 430
Cdd:TIGR00618 525 pltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltqcDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEKVR--------ELRETVADLEAINEMNDELQENARETELELREQLDL-------GAAGVREAEKRVEAAQETVADY 495
Cdd:TIGR00618 605 EAEDMLAceqhallrKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervreHALSIRVLPKELLASRQLALQK 684
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 688582234 496 QQTiqKYRELTANLQEVN------RELMSQQEANSEQQQQ 529
Cdd:TIGR00618 685 MQS--EKEQLTYWKEMLAqcqtllRELETHIEEYDREFNE 722
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
303-532 |
5.91e-06 |
|
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: 50.15 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 303 LQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNF 382
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 383 ELDALRCHKEKLQEEM--------KMAEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMND 454
Cdd:COG4942 91 EIAELRAELEAQKEELaellralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688582234 455 ELQENARETELELREQLdlgaagvREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAE 532
Cdd:COG4942 171 AERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-356 |
6.13e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 195 PSKEEESLRALVKDLEEKLETL-KMKRTEDKAKLKELEKHKIQLeqLQEWKSKMQEQQNELQKQLKEAkREAKEALEAKE 273
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLrEAEELEEELQLEELEQEIAAL--LAEAGVEDEEELRAALEQAEEY-QELKEELEELE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEMADTADAiEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHvKQLEEQNARLK 353
Cdd:COG4717 409 EQLEELLGELEE-LLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL-QELEELKAELR 486
|
...
gi 688582234 354 EAL 356
Cdd:COG4717 487 ELA 489
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
196-314 |
6.18e-06 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 50.85 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEE-ESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAker 274
Cdd:COG0542 438 SFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE--- 514
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 688582234 275 ymeemADTADAIEMAT---LDKEMAEERAESLQLEaDALKERV 314
Cdd:COG0542 515 -----EDIAEVVSRWTgipVGKLLEGEREKLLNLE-EELHERV 551
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
209-469 |
6.55e-06 |
|
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: 50.51 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 209 LEEKLETLKMKRTEDKA----KLKELEKhkIQLEQlqewkskmqEQQNELQKQLKEAKREAKEALEAKERYMEEmadtaD 284
Cdd:pfam17380 355 QEERKRELERIRQEEIAmeisRMRELER--LQMER---------QQKNERVRQELEAARKVKILEEERQRKIQQ-----Q 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 285 AIEMATLDKEMAEERAESLQ-LEADALKE--RVDELTMD----LEILKHEIEEKGSdgaassyhvKQLEEQNARLKEALV 357
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRrLEEERAREmeRVRLEEQErqqqVERLRQQEEERKR---------KKLELEKEKRDRKRA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 358 RMRDLSASEKQEHGKQQKLMEKKNfeldalrcHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMltERNLDLEEKVR 437
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEER--------KRKLLEKEMEERQKAIYEEERRREAEEERRKQQEM--EERRRIQEQMR 559
|
250 260 270
....*....|....*....|....*....|..
gi 688582234 438 ELRETVADLEAInEMNDELQENARETELELRE 469
Cdd:pfam17380 560 KATEERSRLEAM-EREREMMRQIVESEKARAE 590
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
292-558 |
7.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 292 DKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRdlsaSEKQEHG 371
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLE----KEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 372 KQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDaslgaeemvemlternlDLEEKVR---ELRETVADLEA 448
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-----------------ELEEKVKelkELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 449 INEMNDELQENARETELEL---REQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANS- 524
Cdd:PRK03918 298 LSEFYEEYLDELREIEKRLsrlEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERl 377
|
250 260 270
....*....|....*....|....*....|....
gi 688582234 525 EQQQQPAEIFDFKIKFAETKAYAKAIEMELRKME 558
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
197-531 |
7.17e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNE---LQKQLKEAKREAKEaLEAKE 273
Cdd:TIGR00618 198 LLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEqlkKQQLLKQLRARIEE-LRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEmadTADAIEMATLDKEMAEEraeslqleadalKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLK 353
Cdd:TIGR00618 277 AVLEE---TQERINRARKAAPLAAH------------IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 354 EALVRMRDLSASE---KQEHGKQQKLMEKKNFELdALRCHKEKLQEemkmaEKTIDELKEQVDASLGAEEMVEMLTERNL 430
Cdd:TIGR00618 342 EQRRLLQTLHSQEihiRDAHEVATSIREISCQQH-TLTQHIHTLQQ-----QKTTLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEkvRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQ 510
Cdd:TIGR00618 416 TSAF--RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVL 493
|
330 340
....*....|....*....|.
gi 688582234 511 EVNRELMSQQEANSEQQQQPA 531
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPN 514
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
239-524 |
7.50e-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: 50.12 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 239 QLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKerymeemadtadaiemATLDKEMAEERAESLQLEAD--ALKERVDE 316
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKA----------------SALKRQLDRESDRNQELQKRirLLEKREAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 317 LTmdlEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEAlvrmRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQE 396
Cdd:pfam05557 67 AE---EALREQAELNRLKKKYLEALNKKLNEKESQLADA----REVISCLKNELSELRRQIQRAELELQSTNSELEELQE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 397 EMKMAEKTIDELkEQVDASLGAEEmvEMLTERNLDLEEKVRELRETVADLEAINEMNDELqenARETELE-LREQLDLGA 475
Cdd:pfam05557 140 RLDLLKAKASEA-EQLRQNLEKQQ--SSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL---ARIPELEkELERLREHN 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 688582234 476 AGVREAEKRVEAAQETVADYQQTI---QKYRELTANLQEVNRELmsQQEANS 524
Cdd:pfam05557 214 KHLNENIENKLLLKEEVEDLKRKLereEKYREEAATLELEKEKL--EQELQS 263
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
197-516 |
1.02e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEAL------- 269
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavav 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 270 -----EAKERYMEE----------MADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEK--- 331
Cdd:COG1196 529 ligveAAYEAALEAalaaalqnivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAsdl 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 332 ----------GSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRchkEKLQEEMKMA 401
Cdd:COG1196 609 readaryyvlGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL---EAEAELEELA 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 402 EKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREA 481
Cdd:COG1196 686 ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL 765
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 688582234 482 EKRVEAAQETVA-----------DYQQTIQKYRELTANLQEVNREL 516
Cdd:COG1196 766 ERELERLEREIEalgpvnllaieEYEELEERYDFLSEQREDLEEAR 811
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
199-416 |
1.07e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 199 EESLRALVK--DLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:COG1579 3 PEDLRALLDlqELDSELDRLEHRLKELPAELAELED---ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKEMaeeraESLQLEADALKERVDELTMDLEILKHEIEEKGsdgaassyhvKQLEEQNARLKEAL 356
Cdd:COG1579 80 EQLGNVRNNKEYEALQKEI-----ESLKRRISDLEDEILELMERIEELEEELAELE----------AELAELEAELEEKK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 357 VrmrdlsasekqehgkqqklmekknfELDALrchKEKLQEEMKMAEKTIDELKEQVDASL 416
Cdd:COG1579 145 A-------------------------ELDEE---LAELEAELEELEAEREELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
196-563 |
1.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETlKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKRE--AKEALEAKE 273
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKT-ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVeiARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEMADTADAIEMATLDKEMaeERAESLQLEADALK----ERVDELTMDLEILKHEIEEKGSDgaassyhVKQLEEQN 349
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEV--RKAEELRKAEDARKaeaaRKAEEERKAEEARKAEDAKKAEA-------VKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEAlvrmrdlSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEmVEMLTERN 429
Cdd:PTZ00121 1237 KDAEEA-------KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE-KKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 430 LDLEEKvRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANL 509
Cdd:PTZ00121 1309 KKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 688582234 510 QEVNRELMSQQEAnsEQQQQPAEifDFKIKFAETKayaKAIEMELRKMEVIQAN 563
Cdd:PTZ00121 1388 EEKKKADEAKKKA--EEDKKKAD--ELKKAAAAKK---KADEAKKKAEEKKKAD 1434
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
197-330 |
1.32e-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: 48.00 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEK----HKIQLEQLQEWKSKMQEQQNE---------LQKQLKEAKR 263
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKeikrLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688582234 264 EAKEALEAKERYMEEMADTADAIEmaTLDKEMAEERAESLQLEAdALKERVDELTMDLEILKHEIEE 330
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELA--ELEAELAELEAELEEKKA-ELDEELAELEAELEELEAEREE 167
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
344-493 |
1.35e-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: 48.00 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 344 QLEEQNARLKEALVRMRDLSASEKQEHGKQQKlmekknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEM-- 421
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKT-------ELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 422 ----VEMLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVA 493
Cdd:COG1579 94 lqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
197-465 |
1.64e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.06 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKakLKELEKHKIQL-EQLQ-EWKSK--MQEQQNELQKQLKEAKREAKEALEAK 272
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEELDLDEAEEK--NEEIQERIDQLyDILErEVKARkyVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 273 ERYMEEMADTADAIEmatldkemaeeRAESLQLEADALKERVDELTMDLE-------ILKHEIEEkgsdgaaSSYHVKQL 345
Cdd:PRK04778 334 DRVKQSYTLNESELE-----------SVRQLEKQLESLEKQYDEITERIAeqeiaysELQEELEE-------ILKQLEEI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 346 EEQNARLKEALVRMRD--LSASEKQEHGKQQKLMEKKNFEldalRCHKEKLQEEMKmaektidELKEQVDASLgaEEMVE 423
Cdd:PRK04778 396 EKEQEKLSEMLQGLRKdeLEAREKLERYRNKLHEIKRYLE----KSNLPGLPEDYL-------EMFFEVSDEI--EALAE 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 688582234 424 MLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETEL 465
Cdd:PRK04778 463 ELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQ 504
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
203-493 |
1.99e-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: 48.95 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 203 RALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKErymeemaDT 282
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-------EN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 283 ADAIEMATLDKemaEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALvrmrdl 362
Cdd:pfam05483 575 ARSIEYEVLKK---EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELEL------ 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 363 sASEKQEHGKQQKLMEKknfELDALRCHKEKLQEEMKMAEKTIDE---LKEQVDASLGAE--EMVEMLtERNLDLEEKVR 437
Cdd:pfam05483 646 -ASAKQKFEEIIDNYQK---EIEDKKISEEKLLEEVEKAKAIADEavkLQKEIDKRCQHKiaEMVALM-EKHKHQYDKII 720
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688582234 438 ELRETVADLEAINEMNDELQENARETEL--------ELREQLDLGAagvREAEKRVEAAQETVA 493
Cdd:pfam05483 721 EERDSELGLYKNKEQEQSSAKAALEIELsnikaellSLKKQLEIEK---EEKEKLKMEAKENTA 781
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-529 |
2.04e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQ-LQEWKSKMQEQQNELQKQLKEA--KREAKEALEAKE 273
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEeVDELKSQLADYQQALDVQQTRAiqYQQAVQALERAK 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEEMADTADAiematldkemAEERAESLQLEADALKERVDELTMDLEILK--HEIEEKgsdgAASSyhVKQLEEQNAR 351
Cdd:PRK04863 428 QLCGLPDLTADN----------AEDWLEEFQAKEQEATEELLSLEQKLSVAQaaHSQFEQ----AYQL--VRKIAGEVSR 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 352 ------LKEALVRMRDLSASEKQEHGKQQKLMEKknfeldalrchkEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEML 425
Cdd:PRK04863 492 seawdvARELLRRLREQRHLAEQLQQLRMRLSEL------------EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TErnlDLEEKVRELRETVADL-EAINEMNDELQE-NARETELELREQldlgaaGVREAEKRVEAAQETVADYQQTIQKYR 503
Cdd:PRK04863 560 QE---ELEARLESLSESVSEArERRMALRQQLEQlQARIQRLAARAP------AWLAAQDALARLREQSGEEFEDSQDVT 630
|
330 340
....*....|....*....|....*.
gi 688582234 504 ELTANLQEVNRELmSQQEANSEQQQQ 529
Cdd:PRK04863 631 EYMQQLLEREREL-TVERDELAARKQ 655
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
196-545 |
2.06e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEwkskmqeQQNELQKQLKEAKREAKEALeakery 275
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-------ELEQLEEELEELNEQLQAAQ------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 mEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEA 355
Cdd:COG4372 94 -AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMRDLSASEK----QEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLD 431
Cdd:COG4372 173 LQALSEAEAEQAldelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 432 LEEKVRELRE-TVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQ 510
Cdd:COG4372 253 EEVILKEIEElELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
330 340 350
....*....|....*....|....*....|....*
gi 688582234 511 EVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKA 545
Cdd:COG4372 333 AILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
248-507 |
2.26e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 248 QEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKhe 327
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 328 ieekgsdgaassyhvKQLEEQNARLKEALVRMrdlsasekQEHGKQQKLMEKKNFE--LDALRcHKEKLQEEMKMAEKTI 405
Cdd:COG4942 97 ---------------AELEAQKEELAELLRAL--------YRLGRQPPLALLLSPEdfLDAVR-RLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 406 DELKEQVDAslgaeemvemLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRV 485
Cdd:COG4942 153 EELRADLAE----------LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260
....*....|....*....|..
gi 688582234 486 EAAQETVADYQQTIQKYRELTA 507
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTP 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
196-459 |
2.60e-05 |
|
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: 48.48 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQL-EQLQEWKSKMQEQQNELQ----------KQLKEAKRE 264
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkDEQNKIKKQLSEKQKELEqnnkkikeleKQLNQLKSE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 265 AKEALEAKE-----RYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDgaass 339
Cdd:TIGR04523 297 ISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE----- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 340 yhVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKM-------AEKTIDELKEQV 412
Cdd:TIGR04523 372 --IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlketiikNNSEIKDLTNQD 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688582234 413 DA------SLGA-----EEMVEMLT----ERNLDLEEKVRELRETVADLEAINEMNDELQEN 459
Cdd:TIGR04523 450 SVkeliikNLDNtreslETQLKVLSrsinKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
208-569 |
2.62e-05 |
|
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: 48.48 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 208 DLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREakeaLEAKErymEEMADTADAIE 287
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE----INEKT---TEISNTQTQLN 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 288 MATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEkgsdgaassyhvkqLEEQnarlkealvrmrdlsasek 367
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--------------LNNQ------------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 368 qehgKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVdaslgaEEMVEMLTERNLDLEEKVRELRETVADLE 447
Cdd:TIGR04523 304 ----KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI------SQLKKELTNSESENSEKQRELEEKQNEIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 448 AINEMND---------ELQENARETELELREQLDlgaagvREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMS 518
Cdd:TIGR04523 374 KLKKENQsykqeiknlESQINDLESKIQNQEKLN------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 519 QQ----------EANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKMEVIQANRQVSLL 569
Cdd:TIGR04523 448 QDsvkeliiknlDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
278-532 |
2.98e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 278 EMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGsdgaassyhvKQLEEQNARLKEALV 357
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----------AEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 358 RMRDLsASEKQEHGKQQKLmekknfeLDALrchkeklqeemkMAEKTIDELKEQVDAslgaeemVEMLTERNLDLeekVR 437
Cdd:COG3883 87 ELGER-ARALYRSGGSVSY-------LDVL------------LGSESFSDFLDRLSA-------LSKIADADADL---LE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 438 ELRETVADLEAINEMNDELQENARETELELREQLDlgaagvrEAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELM 517
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKA-------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
250
....*....|....*
gi 688582234 518 SQQEANSEQQQQPAE 532
Cdd:COG3883 210 AAAAAAAAAAAAAAA 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
196-516 |
3.07e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKmkrtedkAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEakery 275
Cdd:TIGR00606 842 VSKIELNRKLIQDQQEQIQHLK-------SKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE----- 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 meemadtaDAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIeekgsdgaassYHVKQLEeqnarlkea 355
Cdd:TIGR00606 910 --------QDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIH-----------GYMKDIE--------- 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 lvrmrdlsasEKQEHGKQQKLMEKKN------FELDALRCHKEKLQEEMKMAEKTIDELKEQvdaslgaeemvEMLTERN 429
Cdd:TIGR00606 962 ----------NKIQDGKDDYLKQKETelntvnAQLEECEKHQEKINEDMRLMRQDIDTQKIQ-----------ERWLQDN 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 430 LDL---EEKVRELRETVAD-LEAINEMN--------DELQENARETELElrEQLDLGAAGVREAEKRVEAAQETVADYQQ 497
Cdd:TIGR00606 1021 LTLrkrENELKEVEEELKQhLKEMGQMQvlqmkqehQKLEENIDLIKRN--HVLALGRQKGYEKEIKHFKKELREPQFRD 1098
|
330 340
....*....|....*....|..
gi 688582234 498 TIQKYRELTANL---QEVNREL 516
Cdd:TIGR00606 1099 AEEKYREMMIVMrttELVNKDL 1120
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
224-369 |
3.35e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 224 KAKLKELEKHKIQLEQLQEWKSKMQE------QQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEMAE 297
Cdd:PRK04863 499 RELLRRLREQRHLAEQLQQLRMRLSEleqrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEAR 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 298 ERAESLQLEADALKERVDELTMD----------LEILkheiEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEK 367
Cdd:PRK04863 579 ERRMALRQQLEQLQARIQRLAARapawlaaqdaLARL----REQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARK 654
|
..
gi 688582234 368 QE 369
Cdd:PRK04863 655 QA 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
281-508 |
3.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 281 DTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHeIEEKGSDGAASSYHVKQLEEQNARLKEALVRMR 360
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 361 DLSASEKQEHGKQQklmekknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEML--TERNLDLEEKVRE 438
Cdd:COG4913 686 DLAALEEQLEELEA--------ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarLELRALLEERFAA 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688582234 439 L--RETVADL-EAINEMNDELQENARETELELREQLdlgAAGVREAEKRVEAAQETVADYQQTIQKYRELTAN 508
Cdd:COG4913 758 AlgDAVERELrENLEERIDALRARLNRAEEELERAM---RAFNREWPAETADLDADLESLPEYLALLDRLEED 827
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-561 |
4.25e-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: 47.79 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 198 EEESLRALVKDLEEKLETLKMKRTEDK--AKLKELEKHKiqleQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERY 275
Cdd:pfam05483 177 EREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEK 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMAtldKEMAEERAESLQLEADALK---ERVDELTMDLEILKHEIEEKGSDGaassyhvKQLEEQNARL 352
Cdd:pfam05483 253 ENKMKDLTFLLEES---RDKANQLEEKTKLQDENLKeliEKKDHLTKELEDIKMSLQRSMSTQ-------KALEEDLQIA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 353 KEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCH-KEKLQEEMKMAEKTIDELK----EQVDASLGAEEMVEMLTE 427
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSlEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 428 RNLDLEEKVRELRETVADLEAiNEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTA 507
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 688582234 508 NLQEVNRELMSQQEA----NSEQQQQPAE-IFDFKIKFAETKAYAKAIEMELRKMEVIQ 561
Cdd:pfam05483 482 KEKLKNIELTAHCDKllleNKELTQEASDmTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
196-490 |
4.26e-05 |
|
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: 48.04 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERY 275
Cdd:pfam02463 282 KLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMadtadaiemaTLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKgsdgaassyhVKQLEEQNARLKEA 355
Cdd:pfam02463 362 EKLQ----------EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA----------QLLLELARQLEDLL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMRDLSASEKQEHGKQQKLMEKKNF---ELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDL 432
Cdd:pfam02463 422 KEEKKEELEILEEEEESIELKQGKLTEekeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688582234 433 EEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQE 490
Cdd:pfam02463 502 ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
207-312 |
4.32e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 207 KDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKreAKEALEAKERYMEEMADTADAI 286
Cdd:PRK09510 83 KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA--AKAAAAAKAKAEAEAKRAAAAA 160
|
90 100
....*....|....*....|....*.
gi 688582234 287 EMATLDKEMAEERAESLQLEADALKE 312
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKK 186
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
255-502 |
4.86e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 255 QKQLKEAKREAKEALEAKErymeemadtadaiematldKEmAEERAESLQLEAdalKERVDELTMDLEilkHEIEEKGSd 334
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAK-------------------KE-AEAIKKEALLEA---KEEIHKLRNEFE---KELRERRN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 335 gaassyHVKQLEEQNARLKEALvrmrdlsasekqehGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDEL-KEQVD 413
Cdd:PRK12704 83 ------ELQKLEKRLLQKEENL--------------DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 414 -----ASLGAEEMVEMLTERnldLEEKVRElretvadleainemndELQENARETELELREqldlgaagvrEAEKRveaA 488
Cdd:PRK12704 143 eleriSGLTAEEAKEILLEK---VEEEARH----------------EAAVLIKEIEEEAKE----------EADKK---A 190
|
250
....*....|....
gi 688582234 489 QETVAdyqQTIQKY 502
Cdd:PRK12704 191 KEILA---QAIQRC 201
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
198-510 |
4.93e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 198 EEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKER--- 274
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHnhq 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 275 -----YMEEMADTADAIEMATLD-KEMAEERAE------SLQLEADALKERVdeLTMDLEILKHEIE------EKG--SD 334
Cdd:TIGR00606 312 rtvreKERELVDCQRELEKLNKErRLLNQEKTEllveqgRLQLQADRHQEHI--RARDSLIQSLATRleldgfERGpfSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 335 GAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEqvda 414
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ---- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 415 slgaeemvemLTERNLDLEEKVRELRETVADLEAINEMNDELQENARETELElREQLDLGAAGVREAEKRVEAAQETVAD 494
Cdd:TIGR00606 466 ----------LEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQ-NEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
330
....*....|....*.
gi 688582234 495 YQQTIQKYRELTANLQ 510
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQ 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
349-519 |
5.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 349 NARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQE------EMKMAEKTIDELKEQVDASLGAEEMV 422
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 423 EMLTERNLDLEEKVRELRETVADL-----------EAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQET 491
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELkgeigrlekelEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180
....*....|....*....|....*...
gi 688582234 492 VADYQQTIQKYRELTANLQEVNRELMSQ 519
Cdd:COG4913 768 RENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
197-486 |
6.69e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.16 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKA---------------KLKELEKHKI-----------QLEQLQEWKSKMQEQ 250
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAKEssskpselalnemieKLKKEIDLEYteaviamglqeRLENLREEFSKANSQ 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 251 QNELQKQLKEA----KREAKEALEAKERYmEEMADTADAIEMATLDKEMAE--ERAESLQLEADA-LKERVD--ELTMDL 321
Cdd:PLN03229 502 DQLMHPVLMEKieklKDEFNKRLSRAPNY-LSLKYKLDMLNEFSRAKALSEkkSKAEKLKAEINKkFKEVMDrpEIKEKM 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 322 EILKHEIEEKGSDGAAssyhvkqleEQNARLKEALVRMRDLSASEKQEHGKQQKL----MEKKNFEL------DALRCHK 391
Cdd:PLN03229 581 EALKAEVASSGASSGD---------ELDDDLKEKVEKMKKEIELELAGVLKSMGLevigVTKKNKDTaeqtppPNLQEKI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 392 EKLQEEM-KMAEKTID--ELKEQVDasLGAEEMVEMLTERNLDLEEKVRELRETVAD--LEAINEMndELQENARETELE 466
Cdd:PLN03229 652 ESLNEEInKKIERVIRssDLKSKIE--LLKLEVAKASKTPDVTEKEKIEALEQQIKQkiAEALNSS--ELKEKFEELEAE 727
|
330 340 350
....*....|....*....|....*....|...
gi 688582234 467 LREQLDLGAA-------------GVREAEKRVE 486
Cdd:PLN03229 728 LAAARETAAEsngslkndddkeeDSKEDGSRVE 760
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
207-420 |
7.04e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 207 KDLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMAD----- 281
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 282 -----TADAIEMATLDKEMAE--ERAESLQLEADALKERVDELTMDLEILKHEieekgsdgaassyhVKQLEEQNARLKE 354
Cdd:COG3883 96 yrsggSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAK--------------KAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 355 ALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEE 420
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
286-472 |
7.22e-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: 45.69 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 286 IEMATLDKEMA--EERAESLQLEADALKERVDELTMDLEILKHEIEEkgsdgaassyhvkqLEEQNARLKEalvrmrDLS 363
Cdd:COG1579 10 LDLQELDSELDrlEHRLKELPAELAELEDELAALEARLEAAKTELED--------------LEKEIKRLEL------EIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 364 ASEKQEHGKQQKLME-KKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVdaslgaEEMVEMLTERNLDLEEKVRELRET 442
Cdd:COG1579 70 EVEARIKKYEEQLGNvRNNKEYEALQKEIESLKRRISDLEDEILELMERI------EELEEELAELEAELAELEAELEEK 143
|
170 180 190
....*....|....*....|....*....|
gi 688582234 443 VADLEAINEMNDELQENARETELELREQLD 472
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-549 |
1.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 342 VKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEM 421
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 422 VEMLTERnldlEEKVRELRETVADLEAINEMNDELQENARETElELREQLDLGAAGVREAEKRVEAAQEtvADYQQTIQK 501
Cdd:COG4717 128 LPLYQEL----EALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEELEELLEQLSLATE--EELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 688582234 502 YRELTANLQEVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKA 549
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
210-532 |
1.22e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 210 EEKLETLKMKRTEDKAKLKELE----KHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADA 285
Cdd:pfam01576 172 EEKAKSLSKLKNKHEAMISDLEerlkKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALAR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 286 IEMATLDKEMAEERAESLQLEADALKERVD--------------ELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNAR 351
Cdd:pfam01576 252 LEEETAQKNNALKKIRELEAQISELQEDLEseraarnkaekqrrDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 352 LKEAL---VRMRDLSASE-KQEHGKQqklMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQvdaslgaeemVEMLTE 427
Cdd:pfam01576 332 LKKALeeeTRSHEAQLQEmRQKHTQA---LEELTEQLEQAKRNKANLEKAKQALESENAELQAE----------LRTLQQ 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 428 RNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELta 507
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL-- 476
|
330 340 350
....*....|....*....|....*....|...
gi 688582234 508 nLQEVNRELMS--------QQEANSEQQQQPAE 532
Cdd:pfam01576 477 -LQEETRQKLNlstrlrqlEDERNSLQEQLEEE 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
197-523 |
1.26e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRtedkaklkelekhkiqlEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:pfam15921 103 KQKFYLRQSVIDLQTKLQEMQMER-----------------DAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKE--MAEERAESLQLEADALKERVDELTMDLEILKheieekgSDGAASSYHVKQLEEQNARLKE 354
Cdd:pfam15921 166 EDSNTQIEQLRKMMLSHEgvLQEIRSILVDFEEASGKKIYEHDSMSTMHFR-------SLGSAISKILRELDTEISYLKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 355 ALVRMRDLSASEKQEHGKQQKLMekknfeldaLRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERnldLEE 434
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELL---------LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEI---IQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 435 KVRELRET----VADLEA-INEMNDELQENARETE---LELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKyreLT 506
Cdd:pfam15921 307 QARNQNSMymrqLSDLEStVSQLRSELREAKRMYEdkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK---LL 383
|
330
....*....|....*..
gi 688582234 507 ANLQEVNRELMSQQEAN 523
Cdd:pfam15921 384 ADLHKREKELSLEKEQN 400
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
207-528 |
1.31e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 207 KDLEEKLETLKmKR----TEDKAKLKELEKHKIQLEQLQEWKSKMqeqqNELQKQLKEAKREAKEALEakerymeemadt 282
Cdd:PRK11281 39 ADVQAQLDALN-KQklleAEDKLVQQDLEQTLALLDKIDRQKEET----EQLKQQLAQAPAKLRQAQA------------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 283 adaiEMATLDKEMAEERAESLQ-LEADALKERVDELTMDLEILKHEIEEKGSD-----------GAASSYHVKQLEEQNA 350
Cdd:PRK11281 102 ----ELEALKDDNDEETRETLStLSLRQLESRLAQTLDQLQNAQNDLAEYNSQlvslqtqperaQAALYANSQRLQQIRN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 RLKEALVRMRDLSASEKQEHGKQQKLMEKKNfeldalrchkEKLQEEMKMAEKTIDELKEQVDaslgaeemvemlternl 430
Cdd:PRK11281 178 LLKGGKVGGKALRPSQRVLLQAEQALLNAQN----------DLQRKSLEGNTQLQDLLQKQRD----------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEKVRELRETVADL-EAINEMNDELQENAretelelreqldlgaagVREAEKRVEAAQETVADYQQtiqkyRELTANL 509
Cdd:PRK11281 231 YLTARIQRLEHQLQLLqEAINSKRLTLSEKT-----------------VQEAQSQDEAARIQANPLVA-----QELEINL 288
|
330
....*....|....*....
gi 688582234 510 QEVNRELMSQQEANSEQQQ 528
Cdd:PRK11281 289 QLSQRLLKATEKLNTLTQQ 307
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
247-521 |
1.31e-04 |
|
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: 46.58 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 247 MQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIEM-ATLDKEMAEERAESL-QLEADALKERVDELTMDLEIL 324
Cdd:TIGR01612 1470 LKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKnKELFEQYKKDVTELLnKYSALAIKNKFAKTKKDSEII 1549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 325 KHEIEEKGSDgaaSSYHVKQLEEQNARLKEALVRMRDLSA----SEKQEHGKQQKL--MEKKNFELDALR-----CHKEK 393
Cdd:TIGR01612 1550 IKEIKDAHKK---FILEAEKSEQKIKEIKKEKFRIEDDAAkndkSNKAAIDIQLSLenFENKFLKISDIKkkindCLKET 1626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 394 LQEEMKMAEKTID----ELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAI-NEMNDE-------LQENAR 461
Cdd:TIGR01612 1627 ESIEKKISSFSIDsqdtELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIeIDVDQHkknyeigIIEKIK 1706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 462 ETELELREQL---------------------DLgaAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQ 520
Cdd:TIGR01612 1707 EIAIANKEEIesikelieptienlissfntnDL--EGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITYD 1784
|
.
gi 688582234 521 E 521
Cdd:TIGR01612 1785 E 1785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
244-423 |
1.34e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 244 KSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIematldkEMAEERAESLQLEADALKERVDELTMDLEI 323
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 324 LKHEIEEKGSD--------GAAS-------SYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALr 388
Cdd:COG3883 91 RARALYRSGGSvsyldvllGSESfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA- 169
|
170 180 190
....*....|....*....|....*....|....*
gi 688582234 389 chKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVE 423
Cdd:COG3883 170 --KAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
191-502 |
1.48e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 191 PIPGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALE 270
Cdd:PRK01156 456 PVCGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIK 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 271 AKERYMEEMADTADAI--EMATLDKEMAEERAESL--------QLEADALKERVDELTM---DLEILKHEIEEKGSDgaA 337
Cdd:PRK01156 536 IKINELKDKHDKYEEIknRYKSLKLEDLDSKRTSWlnalavisLIDIETNRSRSNEIKKqlnDLESRLQEIEIGFPD--D 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 338 SSY---HVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLmEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDA 414
Cdd:PRK01156 614 KSYidkSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY-KKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDD 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 415 SL----GAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMNDELQenaretelELREQLDlgAAGVrEAEKRVEAAQE 490
Cdd:PRK01156 693 AKanraRLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLK--------RLREAFD--KSGV-PAMIRKSASQA 761
|
330
....*....|..
gi 688582234 491 TVADYQQTIQKY 502
Cdd:PRK01156 762 MTSLTRKYLFEF 773
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
206-451 |
1.52e-04 |
|
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: 46.58 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 206 VKDLEEKLETLKMKRTEDK----------AKLKELEKHKIQLEQLQEWKSKMQEQQNEL-QKQLKEAKREAKEALEAKER 274
Cdd:TIGR01612 1168 PEEIEKKIENIVTKIDKKKniydeikkllNEIAEIEKDKTSLEEVKGINLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEA 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 275 YMEEMadtaDAIematldKEMAEERAESLQLEADALKE-RVDELTMDlEILKHEIEEKGSDGAASSYHVKQLE--EQNAR 351
Cdd:TIGR01612 1248 YIEDL----DEI------KEKSPEIENEMGIEMDIKAEmETFNISHD-DDKDHHIISKKHDENISDIREKSLKiiEDFSE 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 352 ------LKEALvrMRDLSASEKQEHGKQQKLMEKKNFeLDALRCHK-EKLQEEMKMAEKTIDELKEQVDASLGAEEMVEM 424
Cdd:TIGR01612 1317 esdindIKKEL--QKNLLDAQKHNSDINLYLNEIANI-YNILKLNKiKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIK 1393
|
250 260
....*....|....*....|....*..
gi 688582234 425 LTERNLDLEEKVRELRETVADLEaINE 451
Cdd:TIGR01612 1394 KIKDDINLEECKSKIESTLDDKD-IDE 1419
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
208-516 |
1.72e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 208 DLEEKLETLKMKRTedKAKLKELEkhkiqlEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYME---------- 277
Cdd:PRK04778 90 EAEELNDKFRFRKA--KHEINEIE------SLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRElrksllanrf 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 278 EMADTADAIE--MATLD---KEMAEERAESLQLEA----DALKERVDELTMDLEILK---HEIE-------EKGSDGA-- 336
Cdd:PRK04778 162 SFGPALDELEkqLENLEeefSQFVELTESGDYVEAreilDQLEEELAALEQIMEEIPellKELQtelpdqlQELKAGYre 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 337 --ASSYH---------VKQLEEQNARLKEALVRMRDLSASEKQEHGKQQ-----KLMEKknfELDAlrchKEKLQEEMKM 400
Cdd:PRK04778 242 lvEEGYHldhldiekeIQDLKEQIDENLALLEELDLDEAEEKNEEIQERidqlyDILER---EVKA----RKYVEKNSDT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 401 AEKTIDELKEQVDAsLGAEemVEMLTER---NLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDlgaag 477
Cdd:PRK04778 315 LPDFLEHAKEQNKE-LKEE--IDRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELE----- 386
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 688582234 478 vrEAEKRVEAAQETVADYQQTIQKYR--ELTA--NLQEVNREL 516
Cdd:PRK04778 387 --EILKQLEEIEKEQEKLSEMLQGLRkdELEAreKLERYRNKL 427
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
197-551 |
1.99e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLetlkMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYM 276
Cdd:TIGR00606 612 NELESKEEQLSSYEDKL----FDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVF 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 277 EEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDgaassyhVKQLEEQNARLKEAL 356
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE-------IPELRNKLQKVNRDI 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 357 VRMR-DLSASEKQEHGKQQKLMEKKNFELDALRChkEKLQEEMKMAEKTIDELKEQVDASlgaeEMVEMLTERNLDLEEK 435
Cdd:TIGR00606 761 QRLKnDIEEQETLLGTIMPEEESAKVCLTDVTIM--ERFQMELKDVERKIAQQAAKLQGS----DLDRTVQQVNQEKQEK 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 436 VRELRETVADLEAINEMNDELQENARETELELRE----QLDLGAAGVRE---AEKRVEAAQETVADYQQTIQKYRELT-- 506
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkseKLQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEQDSpl 914
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 688582234 507 ----ANLQEVNRELMSQQEANSEQQQQpaEIFDFKIKFAETKAYAKAIE 551
Cdd:TIGR00606 915 etflEKDQQEKEELISSKETSNKKAQD--KVNDIKEKVKNIHGYMKDIE 961
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
273-555 |
2.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 273 ERYMEEMADTADAIEMATLDKEMAEE--RAESLQLEADALKERVDELTMDLEILKHEIEEkgsdgaassyhvkqLEEQna 350
Cdd:PRK02224 165 EEYRERASDARLGVERVLSDQRGSLDqlKAQIEEKEEKDLHERLNGLESELAELDEEIER--------------YEEQ-- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 rlKEALVRMRDLSASEKQEHgkqqklmEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVdaslgaeemvEMLTERNL 430
Cdd:PRK02224 229 --REQARETRDEADEVLEEH-------EERREELETLEAEIEDLRETIAETEREREELAEEV----------RDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEKVRELRETV----ADLEAINEMNDELQENARETELELREQ-LDLGAA-----GVRE--------AEKRVEAAQETV 492
Cdd:PRK02224 290 ELEEERDDLLAEAglddADAEAVEARREELEDRDEELRDRLEECrVAAQAHneeaeSLREdaddleerAEELREEAAELE 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688582234 493 ADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELR 555
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE 432
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
201-470 |
2.21e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 201 SLRALVKDLEEKLETLK----MKRTEDKAKLKELEKHKIQLEQLqewKSKMQEQQNELQKQLKEAkreakEALEAK-ERY 275
Cdd:pfam10174 244 SLERNIRDLEDEVQMLKtnglLHTEDREEEIKQMEVYKSHSKFM---KNKIDQLKQELSKKESEL-----LALQTKlETL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDEltmdleilKHEIEEKGSDgaassyHVKQLEEQNARLKEA 355
Cdd:pfam10174 316 TNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEE--------KESFLNKKTK------QLQDLTEEKSTLAGE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMRD-LSASEKQEHGKQQKLmekknfeldalrchkEKLQEEMKMAEKTIDELKEQV----------DASLGAEEmvEM 424
Cdd:pfam10174 382 IRDLKDmLDVKERKINVLQKKI---------------ENLQEQLRDKDKQLAGLKERVkslqtdssntDTALTTLE--EA 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 688582234 425 LTERNLDLE----EKVRELRETVADLEAINEMNDELQE--NARETELELREQ 470
Cdd:pfam10174 445 LSEKERIIErlkeQREREDRERLEELESLKKENKDLKEkvSALQPELTEKES 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
297-527 |
2.34e-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: 45.71 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 297 EERAESLQLEADALKERVDELTMDLEILkHEIEEKGSDGAASSYHV-------KQLEEQNARLKEALvrmRDLSASEKQE 369
Cdd:COG3096 784 EKRLEELRAERDELAEQYAKASFDVQKL-QRLHQAFSQFVGGHLAVafapdpeAELAALRQRRSELE---RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 370 HGKQQKLMEKK---------------------NFELDALRCHKEKLQE---EMKMAEKTIDELKEQVDASLGAEEMVEML 425
Cdd:COG3096 860 QQLRQQLDQLKeqlqllnkllpqanlladetlADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQSDPEQFEQL 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TERNLDLEEKVRELR-------------------ETVADLEAINEMNDELQENARETELELREqldlgaagvreAEKRVE 486
Cdd:COG3096 940 QADYLQAKEQQRRLKqqifalsevvqrrphfsyeDAVGLLGENSDLNEKLRARLEQAEEARRE-----------AREQLR 1008
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 688582234 487 AAQETVADYQQTIQ--------KYRELTANLQEVNrELMSQQEANSEQQ 527
Cdd:COG3096 1009 QAQAQYSQYNQVLAslkssrdaKQQTLQELEQELE-ELGVQADAEAEER 1056
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
204-387 |
2.43e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 204 ALVKDLEEKLETLKMKrteDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYmeemADTA 283
Cdd:pfam13851 26 ELIKSLKEEIAELKKK---EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARL----KVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 284 DAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLE--------ILKHEIEEKGsdgaassyhvKQLEEQNARLKEA 355
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQqktglknlLLEKKLQALG----------ETLEKKEAQLNEV 168
|
170 180 190
....*....|....*....|....*....|...
gi 688582234 356 LVRMR-DLSASEKQEHgKQQKLMEKKNFELDAL 387
Cdd:pfam13851 169 LAAANlDPDALQAVTE-KLEDVLESKNQLIKDL 200
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
196-503 |
2.52e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKI----QLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEA 271
Cdd:pfam01576 460 SKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslqeQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 272 KERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEI---------------EEKgsdgA 336
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVsnlekkqkkfdqmlaEEK----A 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 337 ASSYHVKQLE--EQNARLKE----ALVRMRDLSASEKQEHGKQQKL----ME----------KKNFELDALRCHKEKLQE 396
Cdd:pfam01576 616 ISARYAEERDraEAEAREKEtralSLARALEEALEAKEELERTNKQlraeMEdlvsskddvgKNVHELERSKRALEQQVE 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 397 EMK-MAEKTIDELKEQVDASLGAE-EMVEMLTERNLDL-------EEKVRELRETVADLEAinEMNDELQENA------R 461
Cdd:pfam01576 696 EMKtQLEELEDELQATEDAKLRLEvNMQALKAQFERDLqardeqgEEKRRQLVKQVRELEA--ELEDERKQRAqavaakK 773
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 688582234 462 ETELELRE---QLDLGAAGVREAEKRVEAAQETVADYQQTIQKYR 503
Cdd:pfam01576 774 KLELDLKEleaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEAR 818
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
303-443 |
2.55e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.46 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 303 LQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSY-HVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKN 381
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688582234 382 FELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAE-----------EMVEMLTERNLDLEEkvrELRETV 443
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEvvsrwtgipvgKLLEGEREKLLNLEE---ELHERV 551
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
209-529 |
2.81e-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: 44.52 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 209 LEEKLETLKMKRTEDKAKLKELEKH-----KIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMadta 283
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEEreralEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 284 daieMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKgsdgaassyhvKQLEEQNARLKEAlvrMRDLS 363
Cdd:pfam13868 104 ----DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEK-----------EEEREEDERILEY---LKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 364 ASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMkmaektidELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETV 443
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEK--------AERDELRAKLYQEEQERKERQKEREEAEKKARQRQEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 444 AD--LEAINEMNDELQENARETELELREQLDLGAAGVR----EAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELM 517
Cdd:pfam13868 238 QQarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEieqeEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEG 317
|
330
....*....|..
gi 688582234 518 SQQEANSEQQQQ 529
Cdd:pfam13868 318 ERLREEEAERRE 329
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
197-529 |
2.98e-04 |
|
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: 44.89 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQL----EQLQEWKSKMQEQQNELQKQLKEAKREAK---EAL 269
Cdd:pfam07888 66 RDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELsassEELSEEKDALLAQRAAHEARIRELEEDIKtltQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 270 EAKERYMEEMADTADaiEMATLDKEMAEERaESLQLEADALKERVDELTMDLEILKHEIEEKGSdgaassyHVKQLEEQN 349
Cdd:pfam07888 146 LERETELERMKERAK--KAGAQRKEEEAER-KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT-------QVLQLQDTI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEqvdASLGAEEMVEMLTERN 429
Cdd:pfam07888 216 TTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ---ARLQAAQLTLQLADAS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 430 LDLEE------KVRE--LRETVADLEAINEMNDELQ--ENARETELELREQLdlgaagvreaekRVEAAQETVADYQQTI 499
Cdd:pfam07888 293 LALREgrarwaQEREtlQQSAEADKDRIEKLSAELQrlEERLQEERMEREKL------------EVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|
gi 688582234 500 QKYRELTaNLQEVNRELMSQQEANSEQQQQ 529
Cdd:pfam07888 361 ESRRELQ-ELKASLRVAQKEKEQLQAEKQE 389
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
198-398 |
3.15e-04 |
|
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: 43.86 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 198 EEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQ----LQEWKSKMQEQQNELQKQLKEAKREAKEALeakE 273
Cdd:pfam00261 37 EVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERgrkvLENRALKDEEKMEILEAQLKEAKEIAEEAD---R 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEemadTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILkhEI-EEKGSDGAASSYHvkQLEEQNARL 352
Cdd:pfam00261 114 KYEE----VARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL--EAsEEKASEREDKYEE--QIRFLTEKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688582234 353 KEALVRMRDlsasEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEM 398
Cdd:pfam00261 186 KEAETRAEF----AERSVQKLEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
204-471 |
3.34e-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: 45.33 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 204 ALVKDLEEKLETLKMKRTEDKAklkELEKHKIQLEQLQEWKSKMQEQQNELQK---------------QLKEAKREAKEA 268
Cdd:COG3096 829 AFAPDPEAELAALRQRRSELER---ELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladRLEELREELDAA 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 269 LEAkERYMEEMADTADAIE--MATLDKEMAEEraESLQLEADALKERVDELTMDLEILKHEIEEKgsdgAASSYH--VKQ 344
Cdd:COG3096 906 QEA-QAFIQQHGKALAQLEplVAVLQSDPEQF--EQLQADYLQAKEQQRRLKQQIFALSEVVQRR----PHFSYEdaVGL 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 345 LEEQ---NARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgaeEM 421
Cdd:COG3096 979 LGENsdlNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA-----EA 1053
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 688582234 422 VEMLTERNLDLEEKVRELRETVADLEAI-----NEMnDELQENARETELE---LREQL 471
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQltrceAEM-DSLQKRLRKAERDykqEREQV 1110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-317 |
3.83e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 193 PGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEwksKMQEQQNELQKQLKEAKREAKEALEAK 272
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER---ELAEAEEERLEEELEEEALEEQLEAER 734
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 688582234 273 ERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDEL 317
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
202-313 |
4.05e-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: 44.37 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 202 LRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEwksKMQEQQNELQKQLKEAKR---EAKEALEAKERYMEE 278
Cdd:COG4942 141 LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA---ELEEERAALEALKAERQKllaRLEKELAELAAELAE 217
|
90 100 110
....*....|....*....|....*....|....*..
gi 688582234 279 MADTADAIE--MATLDKEMAEERAESLQLEADALKER 313
Cdd:COG4942 218 LQQEAEELEalIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
202-544 |
4.72e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 202 LRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREaKEALEAKERYMEEMAD 281
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDD-YNNLKSALNELSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 282 TADAIEM--ATLDKEMAEERAESLQLEadALKERVDELTMDLEILKHE-----IEEKGSDGAASSYhVKQLEEQNARLKE 354
Cdd:PRK01156 250 MKNRYESeiKTAESDLSMELEKNNYYK--ELEERHMKIINDPVYKNRNyindyFKYKNDIENKKQI-LSNIDAEINKYHA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 355 ALVRMRDLSaSEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAE----KTIDELKEQVDASlgaEEMVEMLTERNL 430
Cdd:PRK01156 327 IIKKLSVLQ-KDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIEslkkKIEEYSKNIERMS---AFISEILKIQEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 431 DLEEKVRELRETVADLEAINEMNDELQENA---RETELELREQL--------------DLGAAGVR--------EAEKRV 485
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIralRENLDELSRNMemlngqsvcpvcgtTLGEEKSNhiinhyneKKSRLE 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 486 EAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQ-QQQPAEIFDFKIKFAETK 544
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKiESARADLEDIKIKINELK 542
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
284-559 |
5.10e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 284 DAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDgaassyhVKQLEEQNARLKEalvrMRDLS 363
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQ-------VKELREEAQELRE----KRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 364 ASEKQEHgKQQKLMEKKnfELDALRCHKEKLQEEMKM---AEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRELR 440
Cdd:COG1340 70 NEKVKEL-KEERDELNE--KLNELREELDELRKELAElnkAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 441 ETVADLEAINEMNDELQENARETElELREQLDlgaAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQ 520
Cdd:COG1340 147 KELEKAKKALEKNEKLKELRAELK-ELRKEAE---EIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQ 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 688582234 521 EANSEQQQQ----PAEIFDFKIKFAETKAYAKAIEMELRKMEV 559
Cdd:COG1340 223 EKADELHEEiielQKELRELRKELKKLRKKQRALKREKEKEEL 265
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
196-308 |
5.17e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEalEAKERY 275
Cdd:PRK12704 85 QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ---KQQELEKKEEELEELIEEQLQELERISGLTAE--EAKEIL 159
|
90 100 110
....*....|....*....|....*....|...
gi 688582234 276 MEEMADTADAiEMATLDKEMaEERAEslqLEAD 308
Cdd:PRK12704 160 LEKVEEEARH-EAAVLIKEI-EEEAK---EEAD 187
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
401-533 |
5.30e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 401 AEKTIDELKEQVdaslgaEEMVEMLTERNLDLEEKVRELRETVADLEAI-NEMNDELQENaRETELELREQLDlgaagvR 479
Cdd:PRK00409 507 AKKLIGEDKEKL------NELIASLEELERELEQKAEEAEALLKEAEKLkEELEEKKEKL-QEEEDKLLEEAE------K 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688582234 480 EAEKRVEAAQETVADY----------QQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEI 533
Cdd:PRK00409 574 EAQQAIKEAKKEADEIikelrqlqkgGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
197-326 |
5.70e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKH--KIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKER 274
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688582234 275 YMEEMADTADAIEMATLDKEMAEERAESLQLEAD-------ALKERVDELTMDLEILKH 326
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAeaeaalrDLRRELRELEAEIASLER 433
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
297-602 |
6.67e-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: 44.06 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 297 EERAESLQLEADAlkERVDELTMDLEILKHEIEEkgsDGAASSYHVKQLEEQNARLKEALVRMRD----LSASEKQEHGK 372
Cdd:pfam12128 238 KIRPEFTKLQQEF--NTLESAELRLSHLHFGYKS---DETLIASRQEERQETSAELNQLLRTLDDqwkeKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 373 QQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGA-EEMVEMLTERNLDLEEKVRELRETVA-DLEAIN 450
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENlEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 451 EMNDELQENARET---------------ELELREQLDLGAAGVREAEKRVEAAQET----VADYQQTIQKYRELTANLQE 511
Cdd:pfam12128 393 AGIKDKLAKIREArdrqlavaeddlqalESELREQLEAGKLEFNEEEYRLKSRLGElklrLNQATATPELLLQLENFDER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 512 VNRELMSQQEANSEQQQQPAEIFDFKIKFaeTKAYAKAIEMELRKMEVIQANRQVSLLISFMPDSFL----KHRGDHDCI 587
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRR--DQASEALRQASRRLEERQSALDELELQLFPQAGTLLhflrKEAPDWEQS 550
|
330
....*....|....*
gi 688582234 588 LALLLIPRLICKSEL 602
Cdd:pfam12128 551 IGKVISPELLHRTDL 565
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
197-441 |
7.27e-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: 43.37 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEwkskMQEQQNELQKQLKEAKREAKEALEAK-ERY 275
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLRE----EIDEFNEEQAEWKELEKEEEREEDERiLEY 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMATLDKEMAEE----RAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNAR 351
Cdd:pfam13868 161 LKEKAEREEEREAEREEIEEEKEreiaRLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 352 LKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRchKEKLQEEMKMAEKTIDELKEQVDAslgAEEMVEMLTERNLD 431
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE--QEEAEKRRMKRLEHRRELEKQIEE---REEQRAAEREEELE 315
|
250
....*....|
gi 688582234 432 LEEKVRELRE 441
Cdd:pfam13868 316 EGERLREEEA 325
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
296-552 |
8.28e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 296 AEERAESLQLEADALKERVDELTMDLEilkhEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKqqk 375
Cdd:PLN02939 154 ALEDLEKILTEKEALQGKINILEMRLS----ETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSK--- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 376 lmekknfELDALRCHKEKLQEEMKMAEKTIDELKEqvdaslgAEEMVEMLTERNLDLEEKVRELRETVADLEAINEMNDE 455
Cdd:PLN02939 227 -------ELDVLKEENMLLKDDIQFLKAELIEVAE-------TEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 456 LQENARETELE-LREQLDlgaagvrEAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQqqpaeif 534
Cdd:PLN02939 293 LQYDCWWEKVEnLQDLLD-------RATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQ------- 358
|
250
....*....|....*...
gi 688582234 535 dfKIKFAETKAYAKAIEM 552
Cdd:PLN02939 359 --KLKLLEERLQASDHEI 374
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
209-331 |
8.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 209 LEEKLETLKMKRTEDKAK--LKELEK--HKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEaLEAKERYMEEMADTad 284
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKriLEEAKKeaEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQK-LEKRLLQKEENLDR-- 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 688582234 285 aiEMATLDKEmaEERAESLQLEADALKERVDELTMDLEILKHEIEEK 331
Cdd:PRK12704 101 --KLELLEKR--EEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
205-567 |
8.58e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 205 LVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMaDTAD 284
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKE 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 285 AIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHE-------IEEKGSDGAASSYHVKQLEEQNARLKEALV 357
Cdd:TIGR00606 619 EQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAELQEFIS 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 358 RMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQV-DASLGAEEMVEMLTERNLDLEEKV 436
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNRDIQRLKNDIEEQETLLGTIM 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 437 REL---RETVADLEAINEMNDELQENARETELELRE-QLDLGAAGVREAEKRVEAAQEtvadyqqtiqKYRELTANLQEV 512
Cdd:TIGR00606 779 PEEesaKVCLTDVTIMERFQMELKDVERKIAQQAAKlQGSDLDRTVQQVNQEKQEKQH----------ELDTVVSKIELN 848
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 688582234 513 NRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKAIEMELRKM--EVIQANRQVS 567
Cdd:TIGR00606 849 RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELstEVQSLIREIK 905
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
206-316 |
8.65e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 206 VKDLEEKLETLKMKRteDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMAdtada 285
Cdd:COG0542 413 LDELERRLEQLEIEK--EALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG----- 485
|
90 100 110
....*....|....*....|....*....|.
gi 688582234 286 iEMATLDKEMAEERAEsLQLEADALKERVDE 316
Cdd:COG0542 486 -KIPELEKELAELEEE-LAELAPLLREEVTE 514
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
236-331 |
9.15e-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: 40.93 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 236 QLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTA--DAIEMATLDKEMAEERAESLQLEA-DALKE 312
Cdd:COG0711 39 GLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAkaEAEAEAERIIAQAEAEIEQERAKAlAELRA 118
|
90 100
....*....|....*....|.
gi 688582234 313 RVDELTMDL--EILKHEIEEK 331
Cdd:COG0711 119 EVADLAVAIaeKILGKELDAA 139
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-375 |
9.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhkiQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEA-------- 268
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyld 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 269 --LEAKEryMEEMADTADAIE-MATLDKEM------AEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASs 339
Cdd:COG3883 107 vlLGSES--FSDFLDRLSALSkIADADADLleelkaDKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL- 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 688582234 340 yhVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQK 375
Cdd:COG3883 184 --LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
256-469 |
1.05e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 256 KQLKEAKREAKEALEAKERYMEEMADTADaiEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEkgsdg 335
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTDLKERES--QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 336 aassyhvKQLEEQN----ARLKEALVRMRdLSASEKQEHGKQQKLMEKKNFELDALRCH-----KEKLQEEMKMAE-KTI 405
Cdd:pfam05262 253 -------KQQEAKNlpkpADTSSPKEDKQ-VAENQKREIEKAQIEIKKNDEEALKAKDHkafdlKQESKASEKEAEdKEL 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 406 DELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEAINE--MNDELQENARETELELRE 469
Cdd:pfam05262 325 EAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSNPVYGLKVVDPitNLSELVLIDLKTEVRLRE 390
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
202-531 |
1.22e-03 |
|
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: 43.20 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 202 LRALVKDLEEKL------ETLKMKRTEDKAKLKELEKH-----KIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALE 270
Cdd:pfam07111 336 LRGQVAELQEQVtsqsqeQAILQRALQDKAAEVEVERMsakglQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 271 AKERYMEEMADTADAI------------EMATLDKEMAEERA-ESLQLEADALKERVDELTMDLeilkheieekgsdgaa 337
Cdd:pfam07111 416 WLETTMTRVEQAVARIpslsnrlsyavrKVHTIKGLMARKVAlAQLRQESCPPPPPAPPVDADL---------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 338 sSYHVKQLEEQNARLKEALvrmrDLSASE-KQEHGKQQKLMEKKNFELDALrchKEKLQEEMKMAEKTIDELKEQVDASL 416
Cdd:pfam07111 480 -SLELEQLREERNRLDAEL----QLSAHLiQQEVGRAREQGEAERQQLSEV---AQQLEQELQRAQESLASVGQQLEVAR 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 417 GAEEmvemlternlDLEEKVRELRETVADLEAIneMNDELQENARETELELREQLDlgaagvrEAEKRVEAAQETVADYQ 496
Cdd:pfam07111 552 QGQQ----------ESTEEAASLRQELTQQQEI--YGQALQEKVAEVETRLREQLS-------DTKRRLNEARREQAKAV 612
|
330 340 350
....*....|....*....|....*....|....*.
gi 688582234 497 QTIQKYRELTANLQEVNRELMS-QQEANSEQQQQPA 531
Cdd:pfam07111 613 VSLRQIQHRATQEKERNQELRRlQDEARKEEGQRLA 648
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
179-402 |
1.28e-03 |
|
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: 43.02 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 179 SPVGALPSPGAPPIPGPSKEEESLRALVKDLEE--------KLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQ 250
Cdd:pfam15709 298 SPTQTFVVTGNMESEEERSEEDPSKALLEKREQekasrdrlRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREE 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 251 QNELQKQLKEAKREAKEALEAKERYMEEmadtadaiematldkemaEERAESLQLEADALKERVDELTMD---LEILKHE 327
Cdd:pfam15709 378 LELEQQRRFEEIRLRKQRLEEERQRQEE------------------EERKQRLQLQAAQERARQQQEEFRrklQELQRKK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 328 IEEKGSDGAASSYHVKQLEEQnarLKEALVRMRDLSASEKQEHGKQ-QKLMEKKNFELDALRCHKEK-----LQEEMKMA 401
Cdd:pfam15709 440 QQEEAERAEAEKQRQKELEMQ---LAEEQKRLMEMAEEERLEYQRQkQEAEEKARLEAEERRQKEEEaarlaLEEAMKQA 516
|
.
gi 688582234 402 E 402
Cdd:pfam15709 517 Q 517
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
196-529 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 196 SKEEESLRALvkdlEEKLETLKMKRTEDKAKLKELEKHKIQLEqlqewkskmqEQQNELQKQLK---EAKREAKEA---L 269
Cdd:pfam01576 1 TRQEEEMQAK----EEELQKVKERQQKAESELKELEKKHQQLC----------EEKNALQEQLQaetELCAEAEEMrarL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 270 EAKERYMEEMADTADaiemATLDKEmaEERAESLQLEADALKERVDELTMDLEilkheieekgsdgaassyhvkqlEEQN 349
Cdd:pfam01576 67 AARKQELEEILHELE----SRLEEE--EERSQQLQNEKKKMQQHIQDLEEQLD-----------------------EEEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEALvrmrdlsasEKQEHGKQQKLMEKknfELDALRCHKEKLQEEMKMAEKTIDELKEQVDASlgaEEMVEMLTERN 429
Cdd:pfam01576 118 ARQKLQL---------EKVTTEAKIKKLEE---DILLLEDQNSKLSKERKLLEERISEFTSNLAEE---EEKAKSLSKLK 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 430 L-------DLEEKVRELRETVADLEAINEMNDELQENARETELELREQLDLGAAGVREAEKRVEAAQ----ETVADYQQT 498
Cdd:pfam01576 183 NkheamisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALarleEETAQKNNA 262
|
330 340 350
....*....|....*....|....*....|.
gi 688582234 499 IQKYRELTANLQEVNRELMSQQEANSEQQQQ 529
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESERAARNKAEKQ 293
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
361-564 |
1.57e-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: 42.44 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 361 DLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDAslgAEEMVEMLTERNLDLEEKVRELR 440
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA---LEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 441 ETVADL-EAINEMNDELQENARETELELReqldLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQ 519
Cdd:COG4942 97 AELEAQkEELAELLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688582234 520 QE------------------ANSEQQQQ----PAEIFDFKIKFAETKAYAKAIEMELRKMEVIQANR 564
Cdd:COG4942 173 RAeleallaeleeeraaleaLKAERQKLlarlEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
248-558 |
1.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 248 QEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIEMATlDKEMAEE--RAESLQLEADALK---------ERVDE 316
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEarKAEDARKAEEARKaedakrveiARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 317 LTMDLEILKHEIEEKGSDGAASSYHVKQLEE----QNARLKEALVR---MRDLSASEKQEHGKQ----QKLMEKKNFELD 385
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAARKaeeERKAEEARKAEDAKKaeavKKAEEAKKDAEE 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 386 ALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETvADLEAINEMNDELQENARETEL 465
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA-EEKKKADEAKKKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 466 -----ELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIFDFKIKF 540
Cdd:PTZ00121 1321 kkkaeEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
330
....*....|....*...
gi 688582234 541 AETKAYAKaiemELRKME 558
Cdd:PTZ00121 1401 EEDKKKAD----ELKKAA 1414
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
197-518 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEKhkiqleqlqewKSK-MQEQQNELQKQLKEAKREAKEALEAKERY 275
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEILAQSKESEK-----------KLKnLEAELLQLQEDLAASERARRQAQQERDEL 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 276 MEEMADTADAIEMATLDKEMAEERaeslqleadalkervdeltmdLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEA 355
Cdd:pfam01576 867 ADEIASGASGKSALQDEKRRLEAR---------------------IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTE 925
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 356 LVRMRdlSASEKQEHGKQQklMEKKNFELdalrchKEKLQEEmkmaEKTIdelKEQVDASLGAEEMVEMLTERNLDLEEK 435
Cdd:pfam01576 926 LAAER--STSQKSESARQQ--LERQNKEL------KAKLQEM----EGTV---KSKFKSSIAALEAKIAQLEEQLEQESR 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 436 VRE-----LRETVADL-EAINEMNDElqenaRETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKY-REL--- 505
Cdd:pfam01576 989 ERQaanklVRRTEKKLkEVLLQVEDE-----RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLqRELdda 1063
|
330
....*....|...
gi 688582234 506 TANLQEVNRELMS 518
Cdd:pfam01576 1064 TESNESMNREVST 1076
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
236-473 |
1.76e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.26 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 236 QLEQLQEWKSKMQEQQNELQKQLKEA-KREAKealeakerYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERV 314
Cdd:pfam17078 11 QIDALTKTNLQLTVQSQNLLSKLEIAqQKESK--------FLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 315 DELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNfeldalRCHKEKL 394
Cdd:pfam17078 83 EELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKLEN------EKQLENY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688582234 395 QEEMKMAEKTIDELKEQVDASLgaEEMVEMLTERNLDLEEKVRELReTVADLEAINEMNDELQENAreteLELREQLDL 473
Cdd:pfam17078 157 QQRISSNDKDIDTKLDSYNNKF--KNLDNIYVNKNNKLLTKLDSLA-QLLDLPSWLNLYPESRNKI----LEYAEKMEL 228
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
392-505 |
1.78e-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: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 392 EKLQEEMKMAEKTIDELKEQVDASlgaEEMVEMLTERNLDLEEKVRELRETVADLEA-INEMNDELQENARET-ELELRE 469
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRL---EEQVERLEAEVEELEAELEEKDERIERLEReLSEARSEERREIRKDrEISRLD 471
|
90 100 110
....*....|....*....|....*....|....*.
gi 688582234 470 qldlgaAGVREAEKRVEAAQETVADYQQTIQKYREL 505
Cdd:COG2433 472 ------REIERLERELEEERERIEELKRKLERLKEL 501
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
258-410 |
1.81e-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: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 258 LKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEMAEeraesLQLEADALKERVDEltmdleiLKHEIEEKgsdgaa 337
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRR-----LEEQVERLEAEVEE-------LEAELEEK------ 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688582234 338 ssyhvkqlEEQNARLKEALVRMRDlsaSEKQEHGKQQKLmEKKNFELDALRCHKEKLQEEMKMAEKTIDELKE 410
Cdd:COG2433 440 --------DERIERLERELSEARS---EERREIRKDREI-SRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
217-424 |
1.89e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 41.54 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 217 KMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKErymeemadTADAIEMATLDKEMA 296
Cdd:PRK06669 4 VIFKRSNVINKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEI--------IEEAEEDAFEIVEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 297 EERAESLQLEAdalkerVDELTMDLEILKHEIEekgsdgaassyhvKQLEEQNARLKEALVRMRDLSASEKQEHGKQqkl 376
Cdd:PRK06669 76 EEEAKEELLKK------TDEASSIIEKLQMQIE-------------REQEEWEEELERLIEEAKAEGYEEGYEKGRE--- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 688582234 377 mekknfelDALRCHKEKLQEEMKMAEKTIDELKEQVDASlgAEEMVEM 424
Cdd:PRK06669 134 --------EGLEEVRELIEQLNKIIEKLIKKREEILESS--EEEIVEL 171
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
191-388 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 191 PIPGPSKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEkhkiqLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALE 270
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 271 AKerymeeMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAAssyHVKQLEEQNA 350
Cdd:COG4913 331 QI------RGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAA---LLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|....*....
gi 688582234 351 RLKEALVR-MRDLSASEKQEHGKQQklmekknfELDALR 388
Cdd:COG4913 402 ALEEALAEaEAALRDLRRELRELEA--------EIASLE 432
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
197-532 |
2.15e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDK--AKLKELEKHKIQLEQLQEWKSKMQeQQNELQKQLKEA------KREAKEA 268
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENRMTLEAIRvtQSDRDLFKHLITESTNYVAADYMR-HANERRVHLEEAlelrreLYTSRRQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 269 LEAKERYMEEMADTADAIEMATLDKEMAEERA-ESLQL--EADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQL 345
Cdd:PRK04863 302 LAAEQYRLVEMARELAELNEAESDLEQDYQAAsDHLNLvqTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEEN 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 346 EEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALrchkEKLQEEMKMAEKTIDELKEQVdASLGAEEmvEML 425
Cdd:PRK04863 382 EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL----ERAKQLCGLPDLTADNAEDWL-EEFQAKE--QEA 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TERNLDLEEKVRelretVAD---------LEAINEMNDEL-----QENARETELELREQLDLGA------AGVREAEKRV 485
Cdd:PRK04863 455 TEELLSLEQKLS-----VAQaahsqfeqaYQLVRKIAGEVsrseaWDVARELLRRLREQRHLAEqlqqlrMRLSELEQRL 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 688582234 486 E---AAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAE 532
Cdd:PRK04863 530 RqqqRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
202-321 |
2.53e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.98 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 202 LRALVKDLEEKLETLKmKR--TEDKAKLKEL-EKHKIQLEQLQEwkskMQEQQNELQKQLKEAKREAKEALEAKErymee 278
Cdd:PRK05431 4 IKLIRENPEAVKEALA-KRgfPLDVDELLELdEERRELQTELEE----LQAERNALSKEIGQAKRKGEDAEALIA----- 73
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 688582234 279 madtadaiEMATLDKEMAEeraesLQLEADALKERVDELTMDL 321
Cdd:PRK05431 74 --------EVKELKEEIKA-----LEAELDELEAELEELLLRI 103
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
237-440 |
2.54e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 237 LEQLQEWKSKMQ----EQQN-ELQKQLKE-AKREA-----KEALEAKERYMEEMADTADA----IEMATLDKEMA--EER 299
Cdd:pfam15294 69 FSQAEKWHLKLQadisELENrELLEQIAEfEEREFtssnkKPNFELNKPKLEPLNEGGGSallhMEIERLKEENEklKER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 300 AESLQLEADALKERVDELTMDLEILKHEIEEKGsDGAASSYHVKQLEEQNARLKEalvrmrDLSASeKQEHGKQQKLMEK 379
Cdd:pfam15294 149 LKTLESQATQALDEKSKLEKALKDLQKEQGAKK-DVKSNLKEISDLEEKMAALKS------DLEKT-LNASTALQKSLEE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 380 knfELDALRCHKEKLQEEMKMAEKtidELKEQVDASLGAEEMVEMLTERNldleEKVRELR 440
Cdd:pfam15294 221 ---DLASTKHELLKVQEQLEMAEK---ELEKKFQQTAAYRNMKEMLTKKN----EQIKELR 271
|
|
| PCRF |
pfam03462 |
PCRF domain; This domain is found in peptide chain release factors. |
224-331 |
3.39e-03 |
|
PCRF domain; This domain is found in peptide chain release factors.
Pssm-ID: 460929 [Multi-domain] Cd Length: 192 Bit Score: 40.06 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 224 KAKLKELEKhkiQLEQLQEWKSkmqeqQNELQKQLKEAKrEAKEALEAKERYMEEMADTADAIEMATLD--KEMAEERAE 301
Cdd:pfam03462 2 EERYEELEA---LLSDPDVWDD-----QKRAQKLSKEYS-ELEPIVEAYREYKQALEDLEEAKELLEDPelAELAEEELE 72
|
90 100 110
....*....|....*....|....*....|...
gi 688582234 302 slqleadALKERVDELTMDLEIL---KHEIEEK 331
Cdd:pfam03462 73 -------ELEKRLEELEEELKLLllpKDPNDDK 98
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
326-499 |
3.82e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.58 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 326 HEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRdlsasekqehgkqqklMEKKNFELDALRCH------KEKLQEemk 399
Cdd:pfam05911 660 SSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLK----------------SEKENLEVELASCTenlestKSQLQE--- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 400 mAEKTIDELKEQVDA-----SLGAE------EMVEMLTERNLDLEEKVRELRETVADLEaiNEMNDELQ--ENARETELE 466
Cdd:pfam05911 721 -SEQLIAELRSELASlkesnSLAETqlkcmaESYEDLETRLTELEAELNELRQKFEALE--VELEEEKNchEELEAKCLE 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 688582234 467 LREQLD------LGAAGVREAEKR------VEAAQETVADYQQTI 499
Cdd:pfam05911 798 LQEQLErnekkeSSNCDADQEDKKlqqekeITAASEKLAECQETI 842
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
232-565 |
4.26e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 232 KHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALK 311
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 312 ERVDELTMDLEILKHEIEEKGSDgaassyhVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRchK 391
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKE-------RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE--Q 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 392 EKLQEEMKMAEKTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRElretvADLEAINEMNDELQENARETELELREQL 471
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE-----ELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 472 DLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIFDFKIKFAETKAYAKAIE 551
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|....
gi 688582234 552 MELRKMEVIQANRQ 565
Cdd:COG4372 327 KLELALAILLAELA 340
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
121-566 |
4.29e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 121 REIIEGLKSNKVTTTRRPKQTRagvGVKVGSGSASAGEMSSSEPSTPAQTPLAAPVIPSPVGALPspgappipgpsKEEE 200
Cdd:pfam09731 44 EEVVLYALGEDPPLAPKPKTFR---PLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEE-----------KEAT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 201 SLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLeqlqewksKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMA 280
Cdd:pfam09731 110 KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATA--------VAKEAKDDAIQAVKAHTDSLKEASDTAEISREKAT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 281 DTADAIEMAtLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEI------EEKGSDGAASSYHVKQLEEQNAR-LK 353
Cdd:pfam09731 182 DSALQKAEA-LAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLdnveekVEKAQSLAKLVDQYKELVASERIvFQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 354 EALVRMRD-----LSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQ-EEMKMAEKTIDELKEQVDAsLGAEEMVEMLTE 427
Cdd:pfam09731 261 QELVSIFPdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKkREEKHIERALEKQKEELDK-LAEELSARLEEV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 428 RNLDLEEKVRELREtvadleainemndELQENARETELELREQLDlgaagvREAEKRVEAAQETVAdyQQTIQKYRELTA 507
Cdd:pfam09731 340 RAADEAQLRLEFER-------------EREEIRESYEEKLRTELE------RQAEAHEEHLKDVLV--EQEIELQREFLQ 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 508 NLqevnRELMSQQEANseqqqqpaeifdFKIKFAETKAYAKAIEMELR-KMEVIQANRQV 566
Cdd:pfam09731 399 DI----KEKVEEERAG------------RLLKLNELLANLKGLEKATSsHSEVEDENRKA 442
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
199-474 |
4.55e-03 |
|
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: 41.36 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 199 EESLRALVKDLEEKLETLKMKRTEDKAK----LKELEKHKIQLE-QLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKE 273
Cdd:pfam12128 652 RLDLRRLFDEKQSEKDKKNKALAERKDSanerLNSLEAQLKQLDkKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 274 RYMEE---MADTADAIEMATLDKEMAEERAeslQLEADalKERVDELTMDLEILKHEIEEKGSDG-AASSYHVKQLEE-- 347
Cdd:pfam12128 732 ALLKAaiaARRSGAKAELKALETWYKRDLA---SLGVD--PDVIAKLKREIRTLERKIERIAVRRqEVLRYFDWYQETwl 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 348 -QNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEM------------KMAEKTIDELKEQVDA 414
Cdd:pfam12128 807 qRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLsenlrglrcemsKLATLKEDANSEQAQG 886
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688582234 415 SLG-----AEEMVEMLTERNLDLEEKVRELRETVADLeaineMNDELQENARETELELREQLDLG 474
Cdd:pfam12128 887 SIGerlaqLEDLKLKRDYLSESVKKYVEHFKNVIADH-----SGSGLAETWESLREEDHYQNDKG 946
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
206-484 |
4.72e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 206 VKDLEEKLETLKMKRTEDKAKLK----ELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKReAKEALEAKerymeeMAD 281
Cdd:pfam15905 75 QKELEKEIRALVQERGEQDKRLQaleeELEKVEAKLNAAVREKTSLSASVASLEKQLLELTR-VNELLKAK------FSE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 282 TADAIEMATLDKEMAEERA--ESLQLEADALKErvdELTMDLEILKHEIEEKgsdgaassyhvkqlEEQNARLKEALVRM 359
Cdd:pfam15905 148 DGTQKKMSSLSMELMKLRNklEAKMKEVMAKQE---GMEGKLQVTQKNLEHS--------------KGKVAQLEEKLVST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 360 RDLSASEKQEHGKQQKLMEKKNFELDALRCHKE---KLQEEMKMAEKTIDELKEQVDASlgaeemVEMLTERNLDLEEKV 436
Cdd:pfam15905 211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYKLdiaQLEELLKEKNDEIESLKQSLEEK------EQELSKQIKDLNEKC 284
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 688582234 437 RELRETVADLEAinemNDELQENARETELE-LREQLDLGAAGVREAEKR 484
Cdd:pfam15905 285 KLLESEKEELLR----EYEEKEQTLNAELEeLKEKLTLEEQEHQKLQQK 329
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
203-528 |
5.02e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 203 RALVKDLEEKLETLKMKRTEDK-AKLKELEKHKIQLEQLQEWKSKMQEQQN----ELQKQLKEAkreakEALEAKERYME 277
Cdd:PRK04778 28 YKRIDELEERKQELENLPVNDElEKVKKLNLTGQSEEKFEEWRQKWDEIVTnslpDIEEQLFEA-----EELNDKFRFRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 278 EMADTADAIEMATLdkemAEERAESLQLEADALKE-------RVDELTMDLEILKHEIEEK-GSDGAAssyhVKQLEEQN 349
Cdd:PRK04778 103 AKHEINEIESLLDL----IEEDIEQILEELQELLEseeknreEVEQLKDLYRELRKSLLANrFSFGPA----LDELEKQL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 350 ARLKEALVRMRDLSasEKQEHGKQQKLMEKKNFELDALRchkEKLQEEMKMAEKTIDELKEQV-DASLGAEEMVE---ML 425
Cdd:PRK04778 175 ENLEEEFSQFVELT--ESGDYVEAREILDQLEEELAALE---QIMEEIPELLKELQTELPDQLqELKAGYRELVEegyHL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 426 TERNLD-----LEEKVRELRETVADLEaINEMNDELQENARETElELREQLDlgaagvRE--AEKRVEAAQETVADY--- 495
Cdd:PRK04778 250 DHLDIEkeiqdLKEQIDENLALLEELD-LDEAEEKNEEIQERID-QLYDILE------REvkARKYVEKNSDTLPDFleh 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 688582234 496 ---------------QQT-------IQKYRELTANLQEVNRELMSQQEANSEQQQ 528
Cdd:PRK04778 322 akeqnkelkeeidrvKQSytlneseLESVRQLEKQLESLEKQYDEITERIAEQEI 376
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
226-324 |
5.79e-03 |
|
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: 40.37 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 226 KLKELEKHKIQLEQL----------QEWKSKMQEQqNELQKqLKEAKREAKEALEAKErYMEEMADTADAIEMatldKEM 295
Cdd:COG0216 5 KLEALEERYEELEALlsdpevisdqKRFRKLSKEY-AELEP-IVEAYREYKKLLEDIE-EAKELLEEESDPEM----REM 77
|
90 100
....*....|....*....|....*....
gi 688582234 296 AEEraeslqlEADALKERVDELTMDLEIL 324
Cdd:COG0216 78 AKE-------ELEELEARLEELEEELKIL 99
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
301-441 |
6.34e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.44 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 301 ESLQLEADALKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNARLKEALVRMRDLsASEKQEHGKQQKLMEKK 380
Cdd:pfam12718 3 NSLKLEAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVEKLEEQLKEAKEK-AEESEKLKTNNENLTRK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688582234 381 NfeldalrchkEKLQEEMKMAEKTIDELKEQV-DASLGAEEM---VEMLTERNLDLEEKVRELRE 441
Cdd:pfam12718 82 I----------QLLEEELEESDKRLKETTEKLrETDVKAEHLerkVQALEQERDEWEKKYEELEE 136
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
202-446 |
6.43e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 202 LRALVKDLEEKLETLKMKRTEDKAKLKELEKHkiqleqLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMAD 281
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYNKN------IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 282 tadaiematLDKEMaEERAESLQleadALKERVDELTMDLEILKHEIE--EKGSDGAASSyhvKQLEEQNARLKEALVRM 359
Cdd:PHA02562 246 ---------LVMDI-EDPSAALN----KLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCT---QQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 360 RDLSASEKQEHGKQQKLMEKKNFELDA----------LRCHKEKLQ---EEMKMAEKTIDELKEQ-VDASLGAEEMVEML 425
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQskkllelknkISTNKQSLItlvDKAKKVKAAIEELQAEfVDNAEELAKLQDEL 388
|
250 260
....*....|....*....|...
gi 688582234 426 TERNLDLEEKVREL--RETVADL 446
Cdd:PHA02562 389 DKIVKTKSELVKEKyhRGIVTDL 411
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
204-369 |
6.63e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 204 ALVKDLEEKLETLKMKRTEDKAKL--KELEKHKIQL-EQLQEWKSKMQEQQNELQK------QLKEAKREAKEALEAKER 274
Cdd:PRK10929 79 KLSAELRQQLNNERDEPRSVPPNMstDALEQEILQVsSQLLEKSRQAQQEQDRAREisdslsQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 275 YMEEMADTADAIEMATLdkemaeeraESLQLEADALKERVDELTM----------------------------DLEILKH 326
Cdd:PRK10929 159 RLQTLGTPNTPLAQAQL---------TALQAESAALKALVDELELaqlsannrqelarlrselakkrsqqldaYLQALRN 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 688582234 327 EIEEKGSDGAASS-YHVKQLEEQNARLKEALVRM----RDLSASEKQE 369
Cdd:PRK10929 230 QLNSQRQREAERAlESTELLAEQSGDLPKSIVAQfkinRELSQALNQQ 277
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
199-482 |
6.76e-03 |
|
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: 40.86 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 199 EESLRALVKDLEEKLETLKMK----RTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKER 274
Cdd:pfam05483 438 EQELIFLLQAREKEIHDLEIQltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 275 YMEEMADTADAIEMATLDKEMAEERAESLQLEADA----LKERVDELTMDLEILKHEIEEKGSDGAASSYHVKQLEEQNA 350
Cdd:pfam05483 518 HQEDIINCKKQEERMLKQIENLEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 351 RLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRCHKEKLQEEMKMAEKTIDEL-----KEQVDASLGAEEMVEML 425
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIidnyqKEIEDKKISEEKLLEEV 677
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688582234 426 TERNLDLEEKVR-----------ELRETVADLEAINEMNDELQENaRETELEL---REQLDLGAAGVREAE 482
Cdd:pfam05483 678 EKAKAIADEAVKlqkeidkrcqhKIAEMVALMEKHKHQYDKIIEE-RDSELGLyknKEQEQSSAKAALEIE 747
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
379-558 |
7.21e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 40.70 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 379 KKNFELDALRCHKEKLQEEMKMAEKTIDELKEQVDASLGAEEMVE----MLTERNLDLEEKVRELRETVADLEAINEMND 454
Cdd:PRK05035 452 KARFEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKakkaAATQPIVIKAGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 455 ELQENARETELELREQLDLGAAGVREAEKRVEAAQETVADYQQTIQKYRELTANLQEVNRELMSQQEANSEQQQQPAEIF 534
Cdd:PRK05035 532 ARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVD 611
|
170 180
....*....|....*....|....
gi 688582234 535 DFKIKFAETKAYAKAIEMELRKME 558
Cdd:PRK05035 612 PKKAAVAAAIARAKAKKAEQQANA 635
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
213-448 |
8.24e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 213 LETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEMADTADAIEMATLD 292
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 293 KEMAEERAESLQLEADALKER-VDELTMDLEILKHEIEEKGSDgaassyhvKQLEEQNARLKEAlvrMRDLSASEKQEHG 371
Cdd:pfam06008 98 IKEINEKVATLGENDFALPSSdLSRMLAEAQRMLGEIRSRDFG--------TQLQNAEAELKAA---QDLLSRIQTWFQS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688582234 372 KQQKLMEKKNFELDALRCHKEKLQEemkmaekTIDELKEQVDASLGAEEMVEMLTERNLDLEEKVRELRETVADLEA 448
Cdd:pfam06008 167 PQEENKALANALRDSLAEYEAKLSD-------LRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
403-558 |
8.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 403 KTIDELKEQVDAslgAEEMVEMLT-----ERNLDLEEKVRELRETVADLEAINEMNDELQENARETELELREQL-DLGAA 476
Cdd:COG4913 262 ERYAAARERLAE---LEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 477 GVREAEKRVEAAQETVADYQQTIQKYRELTANL-----------QEVNRELMSQQEA-NSEQQQQPAEIFDFKIKFAETK 544
Cdd:COG4913 339 RLEQLEREIERLERELEERERRRARLEALLAALglplpasaeefAALRAEAAALLEAlEEELEALEEALAEAEAALRDLR 418
|
170
....*....|....
gi 688582234 545 AYAKAIEMELRKME 558
Cdd:COG4913 419 RELRELEAEIASLE 432
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
200-300 |
8.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 200 ESLRALVKDLEEKLETLKMKRTEDKAKLKELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKERYMEEM 279
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
90 100
....*....|....*....|.
gi 688582234 280 ADTADAIEMATLDKEMAEERA 300
Cdd:COG3883 216 AAAAAAAAAAAAAAAAAAAAA 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
257-455 |
8.49e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 257 QLKEAKREAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSDGA 336
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 337 ASSYHVKQLEEQNARLKEALVRMRDLSASEKQEHGKQQKLMEKKNFELDALRchkEKLQEEMKMAEKTIDELkEQVDasL 416
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL---EELERELERLEREIEAL-GPVN--L 784
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 688582234 417 GA-EEMVEM------LTERNLDLEEKVRELRetvadlEAINEMNDE 455
Cdd:COG1196 785 LAiEEYEELeerydfLSEQREDLEEARETLE------EAIEEIDRE 824
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
196-270 |
8.81e-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: 39.14 E-value: 8.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688582234 196 SKEEESLRALVKDLEEKLETLKMKRTEDKAKLKELE-KHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALE 270
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEaELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
200-334 |
8.83e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 200 ESLRALVKDLEEKLETLKMKRTEDKAKL---------KELEKHKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAK---- 266
Cdd:COG1842 61 EELEAEAEKWEEKARLALEKGREDLAREalerkaeleAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDtlka 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 267 --EALEAKERYMEEMADTADAIEMATLDKemAEERAESLQLEADALKERVDELTMDLEILKHEIEEKGSD 334
Cdd:COG1842 141 raKAAKAQEKVNEALSGIDSDDATSALER--MEEKIEEMEARAEAAAELAAGDSLDDELAELEADSEVED 208
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
206-526 |
8.86e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.59 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 206 VKDLEEKLETLKMKRTEDKAKLKELekhkiqleqlqewKSKMQEQQNELQKQlkeaKREAKEALEAKERYMEEMADtada 285
Cdd:PTZ00440 1079 IKLLEEKVEALLKKIDENKNKLIEI-------------KNKSHEHVVNADKE----KNKQTEHYNKKKKSLEKIYK---- 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 286 iEMATLDKEMaeeraESLQLEADALKErVDELTMDLE-ILKHEIEEKGSDGAASSYHVKqlEEQNARLKEALVRMRDLSA 364
Cdd:PTZ00440 1138 -QMEKTLKEL-----ENMNLEDITLNE-VNEIEIEYErILIDHIVEQINNEAKKSKTIM--EEIESYKKDIDQVKKNMSK 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 365 SEKQEH------GKQQKLMEKKNfELDALRCHKEKLQEEMKMAEKT--IDELKEQVDASLGaeemvEMLTERNlDLEEKV 436
Cdd:PTZ00440 1209 ERNDHLttfeynAYYDKATASYE-NIEELTTEAKGLKGEANRSTNVdeLKEIKLQVFSYLQ-----QVIKENN-KMENAL 1281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 437 RELRETVADLEAI--NEMNDELQENARETE---LELREQLDLGAAGVREAEKRVEAAQE------------TVADYQQTI 499
Cdd:PTZ00440 1282 HEIKNMYEFLISIdsEKILKEILNSTKKAEefsNDAKKELEKTDNLIKQVEAKIEQAKEhknkiygsledkQIDDEIKKI 1361
|
330 340
....*....|....*....|....*...
gi 688582234 500 -QKYRELTANLQEVNrELMSQQEANSEQ 526
Cdd:PTZ00440 1362 eQIKEEISNKRKEIN-KYLSNIKSNKEK 1388
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
197-339 |
9.55e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688582234 197 KEEESLRALVKDLEEKLETLKMKRTEDKAKLKELEK--HKIQLEQLQEWKSKMQEQQNELQKQLKEAKREAKEALEAKER 274
Cdd:pfam05262 224 KKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNlpKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDH 303
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688582234 275 YMEEMAdtadaiematldKEMAEERAESLQLEADALKERvDELTMDLEILKHEIEEKGSDGAASS 339
Cdd:pfam05262 304 KAFDLK------------QESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQVEAQPTSLNEDA 355
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