|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
615-1203 |
1.76e-46 |
|
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: 182.30 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 615 QKSKLTTEVaelqRQLQLEVKNQQNIKEERERMRANLEELRSQHN-------KKVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:pfam01576 483 QKLNLSTRL----RQLEDERNSLQEQLEEEEEAKRNVERQLSTLQaqlsdmkKKLEEDAGTLEALEEGKKRLQRELEALT 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQhqtEIRDLQDQLSEMHDELDSAKRSEDREKGalIEELLQAKQDLQDLLIAKEEQ------------EDLLRK 755
Cdd:pfam01576 559 QQLEEKAA---AYDKLEKTKNRLQQELDDLLVDLDHQRQ--LVSNLEKKQKKFDQMLAEEKAisaryaeerdraEAEARE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 756 RERELTALKGALkEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAgtEMRVKLLQEENEkLQ 835
Cdd:pfam01576 634 KETRALSLARAL-EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--EMKTQLEELEDE-LQ 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 836 GRSE---ELEQRVAQLQRQIE-DLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRT 911
Cdd:pfam01576 710 ATEDaklRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAA 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 912 TQEQKQLSEKLKEESEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIVEASRTSTLELQNQL---DEYKEKNRRELAE 988
Cdd:pfam01576 790 NKGREEAVKQLKKLQAQMKDLQRELEEARASR----DEILAQSKESEKKLKNLEAELLQLQEDLaasERARRQAQQERDE 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 989 MQRQLKEKTleAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISL 1068
Cdd:pfam01576 866 LADEIASGA--SGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQL 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1069 ERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHL---SLTD 1145
Cdd:pfam01576 944 ERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRhadQYKD 1023
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 1146 QKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDL 1203
Cdd:pfam01576 1024 QAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
608-1186 |
7.65e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 128.52 E-value: 7.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDR---EKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALK 764
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEaeeELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 765 GALKEEVS------SHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRS 838
Cdd:COG1196 393 RAAAELAAqleeleEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQ-LEEALVQARREEKEAVSARRALENELEAA---------QRNL 908
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLAGLRGLAGAVAVLIGVEAAYEAAleaalaaalQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 909 SRTTQEQKQLSEKLKEE---------SEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYK 979
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 980 EKNRRELAEMQRQLKEKTLEAEksRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQ 1059
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGE--GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1060 DLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLqlsnRRLERKVKEL--V-MQV 1136
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL----ERLEREIEALgpVnLLA 786
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1137 DDEHlsltdqkDQLSLRLKAMKRQVEEAEEEIDRLEsskkKLQRELEEQM 1186
Cdd:COG1196 787 IEEY-------EELEERYDFLSEQREDLEEARETLE----EAIEEIDRET 825
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
609-1203 |
3.70e-29 |
|
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: 126.44 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 609 VKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQ 688
Cdd:pfam01576 175 AKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 689 VKMEREQHQTEIRDLQDQLSEMHDELDS---AKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKG 765
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESeraARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 ALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRV 845
Cdd:pfam01576 335 ALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 846 AQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEE 925
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 926 SEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQnQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRL 1005
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLE-ALEEGKKRLQRELEALTQQLEEKAAAYDKLEK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1006 TAMKMQDEdkVSQLEMELEEERNNSDLLsERISRSREQMeqvrneLLQERA--ARQDLECDKISLERQNKDLKS-RIIHL 1082
Cdd:pfam01576 574 TKNRLQQE--LDDLLVDLDHQRQLVSNL-EKKQKKFDQM------LAEEKAisARYAEERDRAEAEAREKETRAlSLARA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1083 EGSYRSSKEGLVVQMEARIAELEDRLESEE---RDRASLQLSNRRLERKVKELVMQV---DDEHLSLTDQKDQLSLRLKA 1156
Cdd:pfam01576 645 LEEALEAKEELERTNKQLRAEMEDLVSSKDdvgKNVHELERSKRALEQQVEEMKTQLeelEDELQATEDAKLRLEVNMQA 724
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 1157 MKRQVEEAEEEIDRLESSKKKL----QRELEEQMDMNEHLQGQLNSMKKDL 1203
Cdd:pfam01576 725 LKAQFERDLQARDEQGEEKRRQlvkqVRELEAELEDERKQRAQAVAAKKKL 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
645-1209 |
3.15e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 645 ERMRANLEelrsqhnkkveenstlqqRLEESEGELRKNLEELfqvkmEREQHQTEI-RDLQDQLsemhdeldsakrsEDR 723
Cdd:COG1196 182 EATEENLE------------------RLEDILGELERQLEPL-----ERQAEKAERyRELKEEL-------------KEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 724 EKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALkgalkeevsshdqemdklkeqyDAELQALRESVEEATKNV 803
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL----------------------EAELEELRLELEELELEL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 804 EVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQA 883
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 884 RREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERwhlgktIEKLQKEMADIVEA 963
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL------EELEEALAELEEEE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 964 SRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSD------------ 1031
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGflegvkaallla 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1032 -----------------------------LLSERISRSREQMEQVRNELLQERAARQD-LECDKISLERQNKDLKSRIIH 1081
Cdd:COG1196 518 glrglagavavligveaayeaaleaalaaALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAI 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1082 LEGsyRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVmQVDDEHLSLTDQKDQLSLRLKAMKRQV 1161
Cdd:COG1196 598 GAA--VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR-EVTLEGEGGSAGGSLTGGSRRELLAAL 674
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1622953339 1162 EEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKKL 1209
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELE 722
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
611-1207 |
4.61e-25 |
|
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: 113.23 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 611 DLLEQKSKLTTEVAELQRQL-----QLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEE 685
Cdd:TIGR02168 203 KSLERQAEKAERYKELKAELrelelALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 686 LFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDReKGALIEELLQAKQDLQDLLIAKEEQEDLLRKrerELTALKG 765
Cdd:TIGR02168 283 IEELQKELYALANEISRLEQQKQILRERLANLERQLEE-LEAQLEELESKLDELAEELAELEEKLEELKE---ELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 ALKEEVSSHdQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQ-----GRSEE 840
Cdd:TIGR02168 359 ELEELEAEL-EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 841 LEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALE---NELEAAQRNLSRTTQEQKQ 917
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 918 -------LSEKLKEESE--------------------------------QKEQLRRL-------------KNEMENERWH 945
Cdd:TIGR02168 518 lsgilgvLSELISVDEGyeaaieaalggrlqavvvenlnaakkaiaflkQNELGRVTflpldsikgteiqGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 946 LG---------KTIEKLQKEMADI-----VEASRTSTLELQNQLDEYK-------------------------------- 979
Cdd:TIGR02168 598 EGflgvakdlvKFDPKLRKALSYLlggvlVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitggsaktnssilerrr 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 980 --EKNRRELAEMQRQLKEKT------------LEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQME 1045
Cdd:TIGR02168 678 eiEELEEKIEELEEKIAELEkalaelrkeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1046 QVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGL------VVQMEARIAELEDRLESEERDRASLQ 1119
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraeLTLLNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1120 LSNRRLERKVKEL---VMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQ---RELEEQMDMNEH-- 1191
Cdd:TIGR02168 838 RRLEDLEEQIEELsedIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSeelRELESKRSELRRel 917
|
730
....*....|....*...
gi 1622953339 1192 --LQGQLNSMKKDLSRLK 1207
Cdd:TIGR02168 918 eeLREKLAQLELRLEGLE 935
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-1185 |
7.55e-25 |
|
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: 112.46 E-value: 7.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 575 KRKVNLVFEKIQTLKSRAAgsaQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNikEERERMRANLEEL 654
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVA---QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 655 RSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKR--------------- 719
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllknqsglsgilgvl 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 720 ----SEDREKGALIEELLQAkqDLQDLLI-----AKEEQEDLLRKRERELT--ALKGALKEEVSSHDQEMDKLKEQYDAE 788
Cdd:TIGR02168 526 seliSVDEGYEAAIEAALGG--RLQAVVVenlnaAKKAIAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGV 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 789 LQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEEN-------------------EKLQGRSEELEQRVAQLQ 849
Cdd:TIGR02168 604 AKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILERRREIEELE 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 850 RQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQK 929
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 930 EQLRRLKNEMENERWHLGKTIEKLQKEMADI---VEASRTSTLELQNQLDEYKE---KNRRELAEMQRQLKEKTLEAEKS 1003
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLkeeLKALREALDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDL 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1004 RLTAMKMQDEdkVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLE 1083
Cdd:TIGR02168 844 EEQIEELSED--IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1084 GSYRSSKEGLVvQMEARIAELEDRLESEERDRASLQLSN--------RRLERKVKELVMQVD---DEHLSLTDQKDQLSL 1152
Cdd:TIGR02168 922 EKLAQLELRLE-GLEVRIDNLQERLSEEYSLTLEEAEALenkieddeEEARRRLKRLENKIKelgPVNLAAIEEYEELKE 1000
|
650 660 670
....*....|....*....|....*....|...
gi 1622953339 1153 RLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQ 1185
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
608-1207 |
8.22e-25 |
|
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: 112.46 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSK--LTTEVAELQRQLQlevkNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEE 685
Cdd:TIGR02168 217 ELKAELRELELalLVLRLEELREELE----ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 686 LfqvkmereqhQTEIRDLQDQLSEMHDELDSAKRSEDrEKGALIEELLQAKQDLQDLLIAKEEQEDLLRKrerELTALKG 765
Cdd:TIGR02168 293 L----------ANEISRLEQQKQILRERLANLERQLE-ELEAQLEELESKLDELAEELAELEEKLEELKE---ELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 ALKEEVSSHdQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQ-----GRSEE 840
Cdd:TIGR02168 359 ELEELEAEL-EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLkkleeAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 841 LEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALE---NELEAAQRNLSRTTQEQKQ 917
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLErlqENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 918 -------LSEKLKEESE--------------------------------QKEQLRRL-------------KNEMENERWH 945
Cdd:TIGR02168 518 lsgilgvLSELISVDEGyeaaieaalggrlqavvvenlnaakkaiaflkQNELGRVTflpldsikgteiqGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 946 LG---------KTIEKLQKEMADI-----VEASRTSTLELQNQLDEYK-------------------------------- 979
Cdd:TIGR02168 598 EGflgvakdlvKFDPKLRKALSYLlggvlVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitggsaktnssilerrr 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 980 --EKNRRELAEMQRQLKEKT------------LEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQME 1045
Cdd:TIGR02168 678 eiEELEEKIEELEEKIAELEkalaelrkeleeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1046 QVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGL------VVQMEARIAELEDRLESEERDRASLQ 1119
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraeLTLLNEEAANLRERLESLERRIAATE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1120 LSNRRLERKVKELVMQV-----------------DDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQREL 1182
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIeslaaeieeleelieelESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740
....*....|....*....|....*
gi 1622953339 1183 EEQMDMNEHLQGQLNSMKKDLSRLK 1207
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
713-1208 |
1.47e-23 |
|
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: 108.23 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 713 ELDSAKRSEDREKgALIEELLQAKQDLQDLLIAKEEQEDLL-RKRERELTALKGALKEevsshdqeMDKLKEQYDAELQA 791
Cdd:TIGR02169 178 ELEEVEENIERLD-LIIDEKRQQLERLRREREKAERYQALLkEKREYEGYELLKEKEA--------LERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 792 LRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLL--------QEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAK 863
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 864 ETLKKYEGEIRQLEEALvQARREEKEAVSAR-RALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENE 942
Cdd:TIGR02169 329 AEIDKLLAEIEELEREI-EEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 943 RWHLGKTIEKLQKEMADIvEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKE-----KTLEAEKSRLTAMKMQDEDKVS 1017
Cdd:TIGR02169 408 LDRLQEELQRLSEELADL-NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlSKYEQELYDLKEEYDRVEKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1018 QLEMELEEERNNSDLLSERISRSREQMEQVRN----------------------------------------------EL 1051
Cdd:TIGR02169 487 KLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakeaiEL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1052 LQERAA--------------RQDLE-----------CDKISLERQ--------------------NKDL--KSRIIHLEG 1084
Cdd:TIGR02169 567 LKRRKAgratflplnkmrdeRRDLSilsedgvigfaVDLVEFDPKyepafkyvfgdtlvvedieaARRLmgKYRMVTLEG 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1085 S-----------YRSSKEGLVV--QMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDqkdqLS 1151
Cdd:TIGR02169 647 ElfeksgamtggSRAPRGGILFsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE----IE 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 1152 LRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
608-1202 |
3.30e-23 |
|
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: 107.46 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQDQLSEMHDELD----SAKRSEDREKG-ALIEELLQAKQDLQDLLIAkeeqeDLLRKRERELTA 762
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAeaeaQARASEERVRGgRAVEEVLKASIQGVHGTVA-----QLGSVGERYATA 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 763 LKGA----------------------LKE------------EVSSHDQEMDKLKEQ----YDAELQALRESVEEATKNV- 803
Cdd:TIGR02169 541 IEVAagnrlnnvvveddavakeaielLKRrkagratflplnKMRDERRDLSILSEDgvigFAVDLVEFDPKYEPAFKYVf 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 804 -EVLASRSNTSEQDQAGTEMRVKLLQEENEK-------------LQGRSEELEQRVAQLQRQIEDLKGDEAKAKEtlkky 869
Cdd:TIGR02169 621 gDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQS----- 695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 870 egEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKT 949
Cdd:TIGR02169 696 --ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 950 IEKLQKEMADIVEASRTSTLElqnQLDEYKEKNRRELAEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEMELEEERNN 1029
Cdd:TIGR02169 774 LHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVSRIEARLRE--IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1030 SDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRsskeglvvQMEARIAELEDRLE 1109
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIE--------ELEAQIEKKRKRLS 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1110 SEERDRASLQLSNRRLERKVKELVmQVDDEHLSLTD---QKDQLSLRLKAMK----RQVEEAEEEIDRLESSKKKLQREL 1182
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDvqaELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLE 999
|
650 660
....*....|....*....|
gi 1622953339 1183 EEQMDMNEHLQgQLNSMKKD 1202
Cdd:TIGR02169 1000 EERKAILERIE-EYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
607-1209 |
5.17e-23 |
|
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: 106.69 E-value: 5.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQL-QLEVKNQQNIKE---------------------ERERMRANLEELRSQHNKKVEE 664
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELeKLTEEISELEKRleeieqlleelnkkikdlgeeEQLRVKEKIGELEAEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 665 NSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAK----------RSEDREKGALIEELLQ 734
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraelEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 735 AKQDLQDLliaKEEQEDLLRKREReLTALKGALKEEVSSHDQEMDKLKE---QYDAELQALRESVEEATKNVEVLASRSN 811
Cdd:TIGR02169 390 YREKLEKL---KREINELKRELDR-LQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 812 TSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAV 891
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 892 SARRA---LENELEAAQ-------RNLSRTT-------QEQKQLSEKLKEES---------EQKEQLRR----------L 935
Cdd:TIGR02169 546 GNRLNnvvVEDDAVAKEaiellkrRKAGRATflplnkmRDERRDLSILSEDGvigfavdlvEFDPKYEPafkyvfgdtlV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 936 KNEMENERWHLGK----TIE-KLQKEMADIVEASRTSTLELQNQLDEYKE--KNRRELAEMQRQLkeKTLEAEKSRLTAM 1008
Cdd:TIGR02169 626 VEDIEAARRLMGKyrmvTLEgELFEKSGAMTGGSRAPRGGILFSRSEPAElqRLRERLEGLKREL--SSLQSELRRIENR 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1009 KMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVR-------NELLQERAARQDLECDKISLERQNKDLKSRIIH 1081
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedlssleQEIENVKSELKELEARIEELEEDLHKLEEALND 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1082 LEGSYRSSK----EGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHL---SLTDQKDQLSLRL 1154
Cdd:TIGR02169 784 LEARLSHSRipeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqikSIEKEIENLNGKK 863
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 1155 KAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKKL 1209
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
635-1213 |
1.49e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 104.76 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 635 KNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLqDQLSEMHDEL 714
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-EELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 715 DSAKRSEDREKGALIEELlqakQDLQDLLIAKEEQEDLLRKRERELTALKG---------ALKEEVSSHDQEMDKLKEQY 785
Cdd:PRK03918 244 EKELESLEGSKRKLEEKI----RELEERIEELKKEIEELEEKVKELKELKEkaeeyiklsEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 786 DAELQALRESVEEATKNVEVLASrsntseqdqagTEMRVKLLQEENEKLQGRSEELEqRVAQLQRQIEDLKgdEAKAKET 865
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE-----------LKKKLKELEKRLEELEERHELYE-EAKAKKEELERLK--KRLTGLT 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 866 LKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQ--LSEKLKEESEQKEQLRRLKNEMENer 943
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKR-- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 944 whlgktIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNR-RELAEMQRQLKEKTleaeksrltamKMQDEDKVSQLEME 1022
Cdd:PRK03918 464 ------IEKELKEIEEKERKLRKELRELEKVLKKESELIKlKELAEQLKELEEKL-----------KKYNLEELEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1023 LEEERNNSDLLSERISRSREQMEQVrNELLQERAA----RQDLECDKISLERQ--------NKDLKSRIIHLEGSYRSSK 1090
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKL-EELKKKLAElekkLDELEEELAELLKEleelgfesVEELEERLKELEPFYNEYL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1091 EglVVQMEARIAELEDRLESEERD----RASLQLSNRRLERKVKEL----VMQVDDEHLSLTDQKDQLSLRLKAMKRQVE 1162
Cdd:PRK03918 606 E--LKDAEKELEREEKELKKLEEEldkaFEELAETEKRLEELRKELeeleKKYSEEEYEELREEYLELSRELAGLRAELE 683
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 1163 EAEEEIDRLESSKKKLQRELEEQmdmnEHLQGQLNSMKKDLSRLKKLPNKV 1213
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEER----EKAKKELEKLEKALERVEELREKV 730
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
608-1203 |
4.57e-22 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 103.20 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQlevknqqNIKEERERMRANLEELRSqhnkKVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIE-------RYEEQREQARETRDEADE----VLEEHEERREELETLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREkGALIEELLQAKQDLQDlliAKEEQEDLLRKRERELTALKG-- 765
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAEAGLD-DADAEAVEARREELED---RDEELRDRLEECRVAAQAHNEea 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 -ALKEEVSSHDQEMDKLKEQ---YDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEEL 841
Cdd:PRK02224 345 eSLREDADDLEERAEELREEaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 842 EQRVAQLQRQIEDLKGDEAKAKETLKkyEGEIRQLEEALVQArrEEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEK 921
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLE--AGKCPECGQPVEGS--PHVETIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 922 LKEESEQKEQLRRLKNEMENerwhlgktIEKLQKEMADIVEASRTSTLELQNQLDEYKEknrrELAEMQRQLKEKTLEAE 1001
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRED--------LEELIAERRETIEEKRERAEELRERAAELEA----EAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1002 KSRLTAMKMqdEDKVSQLEMELEEERNNSDLLSErISRSREQMEQvRNELLQERAARQDLECDKISlerqnkDLKSRIIH 1081
Cdd:PRK02224 569 EAREEVAEL--NSKLAELKERIESLERIRTLLAA-IADAEDEIER-LREKREALAELNDERRERLA------EKRERKRE 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1082 LEGSYRsskeglvvqmEARIAELEdrlesEERDRAslqlsnrrlerkvKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQV 1161
Cdd:PRK02224 639 LEAEFD----------EARIEEAR-----EDKERA-------------EEYLEQVEEKLDELREERDDLQAEIGAVENEL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1622953339 1162 EEAEEEIDRLESSKKKLQReLEEQMDMNEHLQGQLNSMKKDL 1203
Cdd:PRK02224 691 EELEELRERREALENRVEA-LEALYDEAEELESMYGDLRAEL 731
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
563-1202 |
9.23e-22 |
|
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: 102.45 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 563 LKEGSADNDDATKRKVNLVFEKIQTLKSRAAgSAQGNNQASNStsEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKE 642
Cdd:TIGR02169 274 LEELNKKIKDLGEEEQLRVKEKIGELEAEIA-SLERSIAEKER--ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 643 ERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKrsed 722
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 723 rekgaliEELLQAKQDLQDLLIAKEEQEDLLRKRERELTalkgALKEEVSSHDQEMDKLKEqydaELQALRESVEEATKN 802
Cdd:TIGR02169 427 -------AAIAGIEAKINELEEEKEDKALEIKKQEWKLE----QLAADLSKYEQELYDLKE----EYDRVEKELSKLQRE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 803 VEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIE------------DLKGDEAKAKETLKKYE 870
Cdd:TIGR02169 492 LAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvvEDDAVAKEAIELLKRRK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 871 G---------EIRQLEEA---------------LVQARREEKEAV--------------SARR--------ALENEL--- 901
Cdd:TIGR02169 572 AgratflplnKMRDERRDlsilsedgvigfavdLVEFDPKYEPAFkyvfgdtlvvedieAARRlmgkyrmvTLEGELfek 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 902 ----EAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQnQLDE 977
Cdd:TIGR02169 652 sgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQ 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 978 YKEKNRRELAEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSReqMEQVRNELLQERAA 1057
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSS--LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEE 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1058 RQDLECDKISLERQNKDLKSRIIHLEgsyrSSKEGLVVQMEariaELEDRLESEERDRASLQLSNRRLERKVKEL---VM 1134
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI----DLKEQIKSIEKEIENLNGKKEELEEELEELeaaLR 878
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 1135 QVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKD 1202
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
627-1209 |
2.87e-21 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 100.50 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 627 QRQLQLEVKNQQNIKEERErmranLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQ 706
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 707 LsemhDELDSAKRSEDREKGALIEELLQAKQDLQDLLiakEEQEDLLRKrerelTALKGALKEEVSSHDQEMDKLKEQYD 786
Cdd:PRK02224 260 I----EDLRETIAETEREREELAEEVRDLRERLEELE---EERDDLLAE-----AGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 787 AELQALRESVEEATKNVEVLAsrsntseqdqagtemrvkllqEENEKLQGRSEELEQRVAQLQRQIEDlkgdeakAKETL 866
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLR---------------------EDADDLEERAEELREEAAELESELEE-------AREAV 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 867 KKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEmenerwhl 946
Cdd:PRK02224 380 EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA-------- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 947 GKTIEKLQkemaDIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQD-EDKVSQLEMELEE 1025
Cdd:PRK02224 452 GKCPECGQ----PVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERlEERREDLEELIAE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1026 ERNNSDLLSERISRSREQMEQVRNELLQERAARQDL--ECDKI-----SLERQNKDLKSRIIHLEGsyrsskeglVVQME 1098
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAeeEAEEAreevaELNSKLAELKERIESLER---------IRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1099 ARIAELEDRLESEERDRASLQLSNRrlERKvkelvmqvddEHLS-LTDQKDQLSLRLKAMKrqVEEAEEEIDRLESSKKK 1177
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELND--ERR----------ERLAeKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ 664
|
570 580 590
....*....|....*....|....*....|..
gi 1622953339 1178 LQRELEEQMDMNEHLQGQLNSMKKDLSRLKKL 1209
Cdd:PRK02224 665 VEEKLDELREERDDLQAEIGAVENELEELEEL 696
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
595-1208 |
1.71e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 595 SAQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANlEELRSQHNKKVEENSTLQ--QRL 672
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE-DARKAEEARKAEDAKRVEiaRKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 673 EES-EGELRKNLEELFQVKMEREQHQT----EIRDLQD-------QLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQ 740
Cdd:PTZ00121 1161 EDArKAEEARKAEDAKKAEAARKAEEVrkaeELRKAEDarkaeaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 741 DLLIAKEEQEDLLRKRERE-----LTALKGALKEEVSSHDQEMDKLKEQYDAE----------LQALRESVEEATKNVEV 805
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEarmahFARRQAAIKAEEARKADELKKAEEKKKADeakkaeekkkADEAKKKAEEAKKADEA 1320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 806 LASRSNTSEQ-DQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAK-ETLKKYEGEIRQLEEALVQA 883
Cdd:PTZ00121 1321 KKKAEEAKKKaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKA 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 884 RREEKEAVSARRALENELEAAQrnlSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENER--WHLGKTIEKLQK--EMAD 959
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKadEAKK 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 960 IVEASRTSTlELQNQLDEYKEK--NRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERI 1037
Cdd:PTZ00121 1478 KAEEAKKAD-EAKKKAEEAKKKadEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1038 SRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRAS 1117
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1118 LQLSNRRLERKVKELVMQVDDEHLSltdQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMnEHLQGQLN 1197
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKKEA 1712
|
650
....*....|.
gi 1622953339 1198 SMKKDLSRLKK 1208
Cdd:PTZ00121 1713 EEKKKAEELKK 1723
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
670-1038 |
1.74e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.04 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 670 QRLEESEGELRKNLEELfqvkmEREQHQTEI-RDLQDQLSEMhdeldsakrsedrEKGALIEELLQAKQDLQDLLIAKEE 748
Cdd:TIGR02168 189 DRLEDILNELERQLKSL-----ERQAEKAERyKELKAELREL-------------ELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 749 QEDLLRKRERELTALKGALkEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQagtemrvKLLQ 828
Cdd:TIGR02168 251 AEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL-------EELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 829 EENEKLQGRSEELEQRVAQLQRQIEDLKGdeakaketlkkyegEIRQLEEALVQARREEKEAVSARRALENELEAAQRNL 908
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKE--------------ELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 909 SRTTQEQKQLSEKLKEESEQKEQL-RRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLD-----EYKEKN 982
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLeDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELErleeaLEELRE 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 983 RRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDK------VSQLEMELEEERNNSDLLSERIS 1038
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLegfsegVKALLKNQSGLSGILGVLSELIS 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
681-1205 |
1.53e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.82 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 681 KNLEELFQVKM-EREQHQTEIRDLQ---DQLSEMHDELDSAKRSEDrekgaLIEELLQAKQDLQDLLIAKEEQEDLLRKR 756
Cdd:COG4913 207 GDLDDFVREYMlEEPDTFEAADALVehfDDLERAHEALEDAREQIE-----LLEPIRELAERYAAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 757 ERELTALK-GALKEEVSSHDQEMDKLKEQYD---AELQALRESVEEATKnvevlasrsntsEQDQAGTEmRVKLLQEENE 832
Cdd:COG4913 282 RLWFAQRRlELLEAELEELRAELARLEAELErleARLDALREELDELEA------------QIRGNGGD-RLEQLEREIE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 833 KLQGRSEELEQRVAQLQRQIEDLK----GDE-------AKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENEL 901
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGlplpASAeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 902 EAAQRNLSRTTQEQKQLSEKLKEESEQKE----------QLRRlknemENERWH---------LGKTI---EKLQKEMAD 959
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEALGLDEaelpfvgeliEVRP-----EEERWRgaiervlggFALTLlvpPEHYAAALR 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 960 IVEAsrtstLELQNQLDEYKEKNRRELAEMQRqLKEKTLeAEK-----------------SRLTAMKMQDEDKVSQLEM- 1021
Cdd:COG4913 504 WVNR-----LHLRGRLVYERVRTGLPDPERPR-LDPDSL-AGKldfkphpfrawleaelgRRFDYVCVDSPEELRRHPRa 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1022 -----------ELEEERNNSDLLSERI--SRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRS 1088
Cdd:COG4913 577 itragqvkgngTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1089 SKEGL-VVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVmQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEE 1167
Cdd:COG4913 657 SWDEIdVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
570 580 590
....*....|....*....|....*....|....*...
gi 1622953339 1168 IDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSR 1205
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
599-1208 |
1.01e-16 |
|
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: 85.84 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 599 NNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGE 678
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 679 LRKNLEELFQVKMEREQHQT----------EIRDLQDQLSEMHDE---LDSAKRSEDREKGALIEELLQAKQDLQDLLIA 745
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELllsnlkkkiqKNKSLESQISELKKQnnqLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 746 KEEQEDLLRKRERELTALKGALKE---EVSSHDQEMDKLKEQYDAEL-QALRESVEEATKNVEVLASRSNTSEQDQAGTE 821
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKElekQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 822 MRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEavsarraLENEL 901
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ-------KDEQI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 902 EAAQRNLSRTTQEQKQLSEklkEESEQKEQLRRLKNEMENerwhLGKTIEKLQKemadiveasrtSTLELQNQLDEYK-- 979
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKE---TIIKNNSEIKDLTNQDSV----KELIIKNLDN-----------TRESLETQLKVLSrs 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 980 -EKNRRELAEMQRQLKEKTLEAEKsrLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRsreqmeqvrnellqeraar 1058
Cdd:TIGR04523 477 iNKIKQNLEQKQKELKSKEKELKK--LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE------------------- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1059 qdlecdkisLERQNKDLKSRIIHLEgsYRSSKEGLvvqmEARIAELEDRLESEERDRASLQLSNRRLERKVKELvmqvDD 1138
Cdd:TIGR04523 536 ---------KESKISDLEDELNKDD--FELKKENL----EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK----EK 596
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1139 EHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:TIGR04523 597 EKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
820-1165 |
1.11e-16 |
|
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: 85.88 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 820 TEMRVKLLQEENEKLQGRSEELEQRVAQLQRQiedlkgdeAKAKETLKKYEGEIRQLEEALVQARREEkeavsarraLEN 899
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQ--------AEKAERYKELKAELRELELALLVLRLEE---------LRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 900 ELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIveasrTSTLELQNQLDEYK 979
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL-----EQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 980 EKNRRELAEMQRQLKEK--TLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAA 1057
Cdd:TIGR02168 315 ERQLEELEAQLEELESKldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1058 RQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVvqmEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVD 1137
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE---EAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350
....*....|....*....|....*....|.
gi 1622953339 1138 ---DEHLSLTDQKDQLSLRLKAMKRQVEEAE 1165
Cdd:TIGR02168 472 eaeQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
600-1214 |
1.52e-16 |
|
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: 85.07 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 600 NQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEErermranLEELRSQHNKKVEENSTLQQRLEESEGEL 679
Cdd:TIGR04523 68 EKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE-------IKNDKEQKNKLEVELNKLEKQKKENKKNI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 680 RKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGAL--IEELLQAKQDLQDLLIAKEEQEDLLRKRE 757
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkIKNKLLKLELLLSNLKKKIQKNKSLESQI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 758 RELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDqagtemrvkllqeeNEKLqgr 837
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN--------------NKKI--- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 838 sEELEQRVAQLQRQIEDLKgdEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQ 917
Cdd:TIGR04523 284 -KELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 918 LSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRtstlELQNQLdEYKEKNRRELAEMQRQLKEKT 997
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ----QKDEQI-KKLQQEKELLEKEIERLKETI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 998 LEAEK--SRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDL 1075
Cdd:TIGR04523 436 IKNNSeiKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1076 KSRIihlegsyrSSKEGLVVQMEARIAELEDRLESEERDRASLqlsNRRLERKVKELVMQVDDEHLSltdqkdQLSLRLK 1155
Cdd:TIGR04523 516 TKKI--------SSLKEKIEKLESEKKEKESKISDLEDELNKD---DFELKKENLEKEIDEKNKEIE------ELKQTQK 578
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953339 1156 AMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKKLPNKVL 1214
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
584-1209 |
1.55e-16 |
|
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: 85.41 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 584 KIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQhnkkVE 663
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRAR----IE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 664 ENSTLQQRLEESEGELRknleelFQVKMER-EQHQTEIRDLQDQLSEMHDELDS--AKRSEDREKGALIEELLQAKQDLQ 740
Cdd:TIGR00618 271 ELRAQEAVLEETQERIN------RARKAAPlAAHIKAVTQIEQQAQRIHTELQSkmRSRAKLLMKRAAHVKQQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 741 DLLIAKEEQEDLLRkRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQ------ALRESVEEATKNVEVLASRSNTSE 814
Cdd:TIGR00618 345 RLLQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQklqslcKELDILQREQATIDTRTSAFRDLQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 815 QDQAGTEMRVKLLQEENEKLQGRSEE------LEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEK 888
Cdd:TIGR00618 424 GQLAHAKKQQELQQRYAELCAAAITCtaqcekLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 889 EAV-------SARRALENELEAAQRNLSRTTQEQKQLSEKLK----EESEQKEQLRRLKNEMENERWHLGKTIEKLQkEM 957
Cdd:TIGR00618 504 CPLcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEdvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDN-RS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 958 ADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERI 1037
Cdd:TIGR00618 583 KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1038 S--RSREQ----MEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEgLVVQMEARIAELEDRLESE 1111
Cdd:TIGR00618 663 HalSIRVLpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE-IENASSSLGSDLAAREDAL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1112 ERDRASLQlSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKA-MKRQVEEAEEEIDRLESSKKKLQRELEEQMDM-- 1188
Cdd:TIGR00618 742 NQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAeIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIln 820
|
650 660
....*....|....*....|...
gi 1622953339 1189 --NEHLQGQLNSMKKDLSRLKKL 1209
Cdd:TIGR00618 821 lqCETLVQEEEQFLSRLEEKSAT 843
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
898-1209 |
5.11e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 898 ENELEAAQRNLSR----TTQEQKQLsEKLKEESEQKEQLRRLKNEMEN-ERWHLGKTIEKLQKEMAdiveasrtstlELQ 972
Cdd:COG1196 178 ERKLEATEENLERlediLGELERQL-EPLERQAEKAERYRELKEELKElEAELLLLKLRELEAELE-----------ELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 973 NQLDEykEKNRRELAEMQRQLKEKTLEAEKSRLTamkmqdedkvsQLEMELEEERNNSDLLSERISRSREQMEQVRNELL 1052
Cdd:COG1196 246 AELEE--LEAELEELEAELAELEAELEELRLELE-----------ELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1053 QERAARQDLECDKISLERQNKDLKSRIIHLEGSyRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKEL 1132
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEE-LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 1133 VMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKKL 1209
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
644-1132 |
9.50e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 82.12 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 644 RERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDr 723
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 724 ekgalIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNV 803
Cdd:COG4717 127 -----LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 804 EVLasrsntseqdqagtEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDlkgdeAKAKETLKKYEGEIRQLEEALVQA 883
Cdd:COG4717 202 EEL--------------QQRLAELEEELEEAQEELEELEEELEQLENELEA-----AALEERLKEARLLLLIAAALLALL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 884 rreeKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEmadiVEA 963
Cdd:COG4717 263 ----GLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP----PDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 964 SRTSTLELQNQLDEYKEKnRRELAEMQRQLKEKTLEAEKSRLTAM-KMQDEDKVSQLEMELEEERNnsdlLSERISRSRE 1042
Cdd:COG4717 335 SPEELLELLDRIEELQEL-LREAEELEEELQLEELEQEIAALLAEaGVEDEEELRAALEQAEEYQE----LKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1043 QM----------------EQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEgsyrssKEGLVVQMEARIAELED 1106
Cdd:COG4717 410 QLeellgeleellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLE------EDGELAELLQELEELKA 483
|
490 500
....*....|....*....|....*.
gi 1622953339 1107 RLESEERDRASLQLSNRRLERKVKEL 1132
Cdd:COG4717 484 ELRELAEEWAALKLALELLEEAREEY 509
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
633-1201 |
1.19e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 633 EVKNQQNIKEERERMRANlEELRSQHNKKVEEnstlQQRLEESEG--ELRKNLEElfQVKMEREQHQTEIRDLQDQLSEM 710
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAE-EERKAEEARKAED----AKKAEAVKKaeEAKKDAEE--AKKAEEERNNEEIRKFEEARMAH 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 711 HDELDSAKRSEDREKGaliEELLQAKQdlqdlliakEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQ 790
Cdd:PTZ00121 1265 FARRQAAIKAEEARKA---DELKKAEE---------KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 791 ALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRvAQLQRQIEDLK---------GDEAK 861
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-AEEKKKADEAKkkaeedkkkADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 862 AKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQR----NLSRTTQEQKQlSEKLKEESEQKEQLRRLKN 937
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeEAKKKAEEAKK-ADEAKKKAEEAKKADEAKK 1490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 938 EMENERwhlgKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVS 1017
Cdd:PTZ00121 1491 KAEEAK----KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA 1566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1018 QLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLER-----------QNKDLKSRIIHLEGSY 1086
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelkkaeeEKKKVEQLKKKEAEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1087 RSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEE 1166
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1622953339 1167 EID--------RLESSKKKLQRELEEQMDMNEHLQGQLNSMKK 1201
Cdd:PTZ00121 1727 ENKikaeeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
577-1077 |
1.34e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 577 KVNLVFEKIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRS 656
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 657 QHNKKVEE-------NSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSaKRSEDREKGALI 729
Cdd:PRK02224 294 ERDDLLAEaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE-LREEAAELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 730 EELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQ---YDAELQALRESVEEATKNVEvl 806
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREReaeLEATLRTARERVEEAEALLE-- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 807 ASRSNTSEQDQAGTEmRVKLLQEENEKLqgrsEELEQRVAQLQRQIEDLKGDEAKAKEtLKKYEGEIRQLEE--ALVQAR 884
Cdd:PRK02224 451 AGKCPECGQPVEGSP-HVETIEEDRERV----EELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEErrEDLEEL 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 885 REEKEAVSARRALE-NELEAAQRNLSRTTQEQKQLSEKLKEESEqkEQLRRLKnEMENERWHLGKTIEKLQKemadiVEA 963
Cdd:PRK02224 525 IAERRETIEEKRERaEELRERAAELEAEAEEKREAAAEAEEEAE--EAREEVA-ELNSKLAELKERIESLER-----IRT 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 964 SRTSTLELQNQLDEYKEKnRRELAEMQRQLKEKTleAEKSrltamkmqdeDKVSQLEMELEEERnnSDLLSERISRSREQ 1043
Cdd:PRK02224 597 LLAAIADAEDEIERLREK-REALAELNDERRERL--AEKR----------ERKRELEAEFDEAR--IEEAREDKERAEEY 661
|
490 500 510
....*....|....*....|....*....|....
gi 1622953339 1044 MEQVRNELLQERAARQDLECDKISLERQNKDLKS 1077
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
604-1207 |
3.61e-15 |
|
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: 80.93 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 604 NSTSEVKDllEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNL 683
Cdd:pfam15921 95 NESNELHE--KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 684 EELFQVKMEREQHQTEIR----DLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQD----LQDLLIAKEEQEDLLRK 755
Cdd:pfam15921 173 EQLRKMMLSHEGVLQEIRsilvDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTeisyLKGRIFPVEDQLEALKS 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 756 RERELTALKgalkeeVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSeQDQAgtemrvkllQEENEKLQ 835
Cdd:pfam15921 253 ESQNKIELL------LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII-QEQA---------RNQNSMYM 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 836 GRSEELEQRVAQLQRQIEDLKgdeakaketlKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEq 915
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAK----------RMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAD- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 916 kqLSEKLKEESEQKEQLRRL-KNEMENErwhlgKTIEKLQKEMADI-VEASRTSTL------ELQNQLDEY------KEK 981
Cdd:pfam15921 386 --LHKREKELSLEKEQNKRLwDRDTGNS-----ITIDHLRRELDDRnMEVQRLEALlkamksECQGQMERQmaaiqgKNE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 982 NRRELAEMQRQLK--EKTLEAEKSRLTAMKM---QDEDKVSQLEMELEE-----ERNNSDL--LSERISRSREQMEQVRN 1049
Cdd:pfam15921 459 SLEKVSSLTAQLEstKEMLRKVVEELTAKKMtleSSERTVSDLTASLQEkeraiEATNAEItkLRSRVDLKLQELQHLKN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1050 EllQERAARQDLECDKISLERQNKDlksRIIHLEGSYRSSKEGLVVQ-------MEARIAELEDRLESEERDRASLQLSN 1122
Cdd:pfam15921 539 E--GDHLRNVQTECEALKLQMAEKD---KVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLELQEFKILK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1123 RRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKD 1202
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETT 693
|
....*
gi 1622953339 1203 LSRLK 1207
Cdd:pfam15921 694 TNKLK 698
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
829-1181 |
9.47e-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: 79.73 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 829 EENEKLQGRSEELEQRVAQLQRQIEDLKGDeakaKETLKKYEGEIRQLEEalvqarREEKEAVSARRALENELEAAQRNL 908
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKRE------YEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 909 SRTTQEQKQLSEKLKE---ESEQKEQL-----RRLKNEMENERWHLGKTIEKLQKEMAdiveasrtstlELQNQLDEYKe 980
Cdd:TIGR02169 247 ASLEEELEKLTEEISElekRLEEIEQLleelnKKIKDLGEEEQLRVKEKIGELEAEIA-----------SLERSIAEKE- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 981 knrRELAEMQRQLKEktLEAEKSRLTAmkmqdedKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQD 1060
Cdd:TIGR02169 315 ---RELEDAEERLAK--LEAEIDKLLA-------EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1061 LECDKISLERQNKDLKSRIIHLEGSYRSSKEGL------VVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVM 1134
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELqrlseeLADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622953339 1135 QVDDEHlsltDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRE 1181
Cdd:TIGR02169 463 DLSKYE----QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
607-1201 |
1.03e-14 |
|
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: 79.45 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQLEvknqQNIKEERERMRANLEelrsqhNKKVEenstLQQRLEESEGELRKNLEEL 686
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQAE----TELCAEAEEMRARLA------ARKQE----LEEILHELESRLEEEEERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 687 FQVKMEREQHQTEIRDLQDQLSEMHDeldsakrsedrekgalieellqAKQDLQdllIAKEEQEDLLRKRERELTALkga 766
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLDEEEA----------------------ARQKLQ---LEKVTTEAKIKKLEEDILLL--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 767 lkEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNvevLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVA 846
Cdd:pfam01576 144 --EDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS---LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 QLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEES 926
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 927 EQKEQLR--------------RLKNEMENERWHLGKTIEKLQK----EMADIVEASRTSTLELQNQLDEYKeKNRRELAE 988
Cdd:pfam01576 299 EELEALKteledtldttaaqqELRSKREQEVTELKKALEEETRsheaQLQEMRQKHTQALEELTEQLEQAK-RNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 989 MQRQLKEKTLE--AEKSRLTAMKMQDEDKVSQLEMELEE--------ERNNSDLLsERISRSREQMEQVRNELLQERAAR 1058
Cdd:pfam01576 378 AKQALESENAElqAELRTLQQAKQDSEHKRKKLEGQLQElqarlsesERQRAELA-EKLSKLQSELESVSSLLNEAEGKN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1059 QDLECDKISLERQNKDLKSrIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDD 1138
Cdd:pfam01576 457 IKLSKDVSSLESQLQDTQE-LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1139 EHLS---LTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKK 1201
Cdd:pfam01576 536 DAGTleaLEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
622-1171 |
2.20e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.42 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 622 EVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEElfqvkmEREQHQTEIR 701
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER------EIERLERELE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 702 DLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLliakEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKL 781
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL----EEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 782 KEQ---YDAELQALRESVEEATKNVEvlasrsntSEQDQAGTEMRVKLLQE----------------------------- 829
Cdd:COG4913 432 ERRksnIPARLLALRDALAEALGLDE--------AELPFVGELIEVRPEEErwrgaiervlggfaltllvppehyaaalr 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 830 --ENEKLQGR--SEELEQRVAQLQRQIED-------LKGDEAKAKETLKKY------------EGEIRQLEEALVQA--- 883
Cdd:COG4913 504 wvNRLHLRGRlvYERVRTGLPDPERPRLDpdslagkLDFKPHPFRAWLEAElgrrfdyvcvdsPEELRRHPRAITRAgqv 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 884 ----RREEK--------------EAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKN--EMENER 943
Cdd:COG4913 584 kgngTRHEKddrrrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEysWDEIDV 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 944 WHLGKTIEKLQKEMADIVEASrtSTLElqnQLDEYKEKNRRELAEMQRQLKEktLEAEKSRLtamkmqdEDKVSQLEMEL 1023
Cdd:COG4913 664 ASAEREIAELEAELERLDASS--DDLA---ALEEQLEELEAELEELEEELDE--LKGEIGRL-------EKELEQAEEEL 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1024 EEERNNSDLLSERIS-RSREQMEQVRNELLQERAARQDLEcdkiSLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIA 1102
Cdd:COG4913 730 DELQDRLEAAEDLARlELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERAMRAFNREWPAETA 805
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1103 ELEDRLESEERDRASL-QLSNRRLERKVKELvmqvddEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRL 1171
Cdd:COG4913 806 DLDADLESLPEYLALLdRLEEDGLPEYEERF------KELLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
583-999 |
2.60e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 583 EKIQTLKSRAAGSaqgNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKV 662
Cdd:PRK02224 349 EDADDLEERAEEL---REEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 663 EENSTLQQRLEESEGELRKNLEELFQVK-------MEREQHQTEIRDLQDQLSEMHDELDSAKrsedrekgALIEELLQA 735
Cdd:PRK02224 426 EREAELEATLRTARERVEEAEALLEAGKcpecgqpVEGSPHVETIEEDRERVEELEAELEDLE--------EEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 736 KQDLQDLLIAKEEQEDLLRKRER--ELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTS 813
Cdd:PRK02224 498 LERAEDLVEAEDRIERLEERREDleELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 814 EQDQAGTEMRVKLLqEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARreekeavsa 893
Cdd:PRK02224 578 NSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR--------- 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 894 rraleneLEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIveASRTSTLE-LQ 972
Cdd:PRK02224 648 -------IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL----EELEELRERREAL--ENRVEALEaLY 714
|
410 420
....*....|....*....|....*..
gi 1622953339 973 NQLDEYKEKNRRELAEMqRQLKEKTLE 999
Cdd:PRK02224 715 DEAEELESMYGDLRAEL-RQRNVETLE 740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
603-1197 |
5.88e-14 |
|
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: 77.19 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 603 SNSTSEVKDLLEQKSKLTTEVAElqrQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQ-RLEESEGELRK 681
Cdd:pfam12128 318 AKDRSELEALEDQHGAFLDADIE---TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSkIKEQNNRDIAG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 682 NLEELFQVKMEREQHQTEIR-DLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRER-- 758
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEdDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERie 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 759 ELTALKGALKEEVSSHDQEMDKLKEQYDAELQALREsveeATKNVEVLASRSNTSEQD---QAGTemrvkLLQEENEKLQ 835
Cdd:pfam12128 475 RAREEQEAANAEVERLQSELRQARKRRDQASEALRQ----ASRRLEERQSALDELELQlfpQAGT-----LLHFLRKEAP 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 836 GRSEELEQRV--AQLQRQIEDLKGDEAKAKETLKKY---------------------EGEIRQLEEALVQARREEKEAVS 892
Cdd:pfam12128 546 DWEQSIGKVIspELLHRTDLDPEVWDGSVGGELNLYgvkldlkridvpewaaseeelRERLDKAEEALQSAREKQAAAEE 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 893 ARRALENELEAAQRNLSRTTQEQKQlseklkeeseQKEQLRRLKNEMENerwhlgktiEKLQKEMAdiVEASRTSTLELQ 972
Cdd:pfam12128 626 QLVQANGELEKASREETFARTALKN----------ARLDLRRLFDEKQS---------EKDKKNKA--LAERKDSANERL 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 973 NQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLemeleeernnsDLLSERISRSREQmeqvrnell 1052
Cdd:pfam12128 685 NSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQL-----------ALLKAAIAARRSG--------- 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1053 qeRAARQDlecdkiSLERQNK-DLKSRIIhlegsyrssKEGLVVQMEARIAELEDRLESEERDRASLqlsnRRLERKVKE 1131
Cdd:pfam12128 745 --AKAELK------ALETWYKrDLASLGV---------DPDVIAKLKREIRTLERKIERIAVRRQEV----LRYFDWYQE 803
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1132 LVMQvddehlsltdQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLN 1197
Cdd:pfam12128 804 TWLQ----------RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLS 859
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
561-1079 |
7.07e-14 |
|
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: 76.60 E-value: 7.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 561 NYLKEGSADNDDATKRKVNLVFEKIQTLKsraagsaQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEvKNQQNI 640
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEK-------EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE-SQISEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 641 KEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRS 720
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 721 EDRE-KGALIEELLQAKQDLQDL---------LIAK-EEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEqydaEL 789
Cdd:TIGR04523 304 KEQDwNKELKSELKNQEKKLEEIqnqisqnnkIISQlNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK----EN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 790 QALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKY 869
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 870 EGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKT 949
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 950 IEKLQKEMADIVEASRTSTLE-----LQNQLDEYKEKNRRELAEmQRQLKE--KTLEAEKSRLTAMKMQDEDKVSQLEME 1022
Cdd:TIGR04523 540 ISDLEDELNKDDFELKKENLEkeideKNKEIEELKQTQKSLKKK-QEEKQEliDQKEKEKKDLIKEIEEKEKKISSLEKE 618
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 1023 LEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRI 1079
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
613-1091 |
7.82e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.96 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 613 LEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNK--KVEENSTLQQRLEESEGELR---KNLEELF 687
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAelpERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKgalIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGAL 767
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLAT---EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 KE-EVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRV----------KLLQEENEKLQG 836
Cdd:COG4717 230 EQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAllflllarekASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 837 RSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAvsARRALENELEAAQRNLSRTTQEQ- 915
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEEl 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 916 KQLSEKLKEESEQKEQLRRLKNEMENerwHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKE 995
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEE---LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 996 ktLEAEKsRLTAMKMQDEDKVSQLEmELEEERNNSDLLSERISRSREQMEQVRNELLQERAAR--QDLECDKISLERQNK 1073
Cdd:COG4717 465 --LEEDG-ELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREERLPPVLERASEyfSRLTDGRYRLIRIDE 540
|
490
....*....|....*...
gi 1622953339 1074 DLKSRIIHLEGSYRSSKE 1091
Cdd:COG4717 541 DLSLKVDTEDGRTRPVEE 558
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
739-1207 |
1.02e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 739 LQDLLIAK--EEQEDLLRKRERELTALKGALKEEvsshDQEMDKLKEQYDaELQALRESVEEATKNVEVLASRSNTSEQD 816
Cdd:COG4717 43 IRAMLLERleKEADELFKPQGRKPELNLKELKEL----EEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 817 QAGTEMRVKLLQEENEKlqgrsEELEQRVAQLQRQIEDLKgdeaKAKETLKKYEGEIRQLEEALVQARREEKEAV-SARR 895
Cdd:COG4717 118 LEKLEKLLQLLPLYQEL-----EALEAELAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLeQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 896 ALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLgKTIEKLQKEMADIVEASRTSTLELQNQL 975
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 976 DEYKEKNRRELAEMQRQL----------KEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQME 1045
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLlallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1046 QVRNELLQERAARQDLECDKISLERQNkDLKSRIIHLEGSYRSskegLVVQMEARIAELEDRLESEERDRASLQLSNRRL 1125
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAA-LLAEAGVEDEEELRA----ALEQAEEYQELKEELEELEEQLEELLGELEELL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1126 ERKVKElvmQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSkkklqRELEEQMDMNEHLQGQLNSMKKDLSR 1205
Cdd:COG4717 423 EALDEE---ELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRELAEEWAA 494
|
..
gi 1622953339 1206 LK 1207
Cdd:COG4717 495 LK 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
603-1056 |
1.51e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 603 SNSTSEVKDLLEQKSKLTTEVAELQRQLQ-LEVKNQQ--NIKEERERMRANLEELRSQHnKKVEENSTLQQRLEESEGEL 679
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEERIKeLEEKEERleELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 680 R-KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDsaKRSEDREKGalIEELLQAKQD--LQDLLIAKEEQEDLLRKR 756
Cdd:PRK03918 382 TgLTPEKLEKELEELEKAKEEIEEEISKITARIGELK--KEIKELKKA--IEELKKAKGKcpVCGRELTEEHRKELLEEY 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 757 ERELtalkgalkEEVSSHDQEMDKLKEQYDAELqalrESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQG 836
Cdd:PRK03918 458 TAEL--------KRIEKELKEIEEKERKLRKEL----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 837 RSEELEQRVAQLQRQIEDLKGDEAKAKEtlkkYEGEIRQLEEALVQARREEKEAVsarRALENELEAAQRNLSRTTQEQK 916
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELL---KELEELGFESVEELEERLKELE 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 917 QLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEAS-RTSTLELQNQLDEYKEKnRRELAEMQRQLke 995
Cdd:PRK03918 599 PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRkELEELEKKYSEEEYEEL-REEYLELSREL-- 675
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 996 KTLEAEKSRLTAMKMQDEDKVSQLEMELeEERNNSDLLSERISRSREQMEQVRNELLQERA 1056
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEEL-EEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1208 |
5.05e-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: 73.95 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 845 VAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALvQARREEKEAVSARRALENELEAAqrnlsrttqEQKQLSEKLKE 924
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-ERLRREREKAERYQALLKEKREY---------EGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 925 ESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEasrtstlelqnQLDEYKEKNRRELAEMQRQLKEKTLEaeksr 1004
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ-----------LLEELNKKIKDLGEEEQLRVKEKIGE----- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1005 LTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEG 1084
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1085 SYRSSKEGLVvQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDehlsLTDQKDQLSLRLKAMKRQVEEA 1164
Cdd:TIGR02169 379 EFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINELEEEKEDKALEIKKQ 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622953339 1165 EEEidrLESSKKKLQRELEEQMDMNE---HLQGQLNSMKKDLSRLKK 1208
Cdd:TIGR02169 454 EWK---LEQLAADLSKYEQELYDLKEeydRVEKELSKLQRELAEAEA 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
541-1035 |
6.29e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 541 KGQQELTQQTNEETAKQILYNYLKEGSADNDDATKRKVNLVFEKIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQKSKlt 620
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-- 1392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 621 teVAELQRQLQLEVKNQQNIKE-ERERMRANLEELRSQHNKKVEEnstLQQRLEESEG--ELRKNLEElfQVKMEREQHQ 697
Cdd:PTZ00121 1393 --ADEAKKKAEEDKKKADELKKaAAAKKKADEAKKKAEEKKKADE---AKKKAEEAKKadEAKKKAEE--AKKAEEAKKK 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 698 TEIRDLQDQLSEMHDELDSA-----KRSEDREKGALIEELLQAKQDLQDLLIAKEEQE-DLLRKRERELTALKGALKEEV 771
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKAdeakkKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKaDEAKKAEEAKKADEAKKAEEK 1545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 772 SSHDqEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKL---QGRSEELEQRVAQL 848
Cdd:PTZ00121 1546 KKAD-ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeEAKKAEEAKIKAEE 1624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 849 QRQIEDLK----------GDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQL 918
Cdd:PTZ00121 1625 LKKAEEEKkkveqlkkkeAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 919 SEKLKEESEQKEQLRRLKNEMENERWhlgKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTL 998
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKI---KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622953339 999 EAEksrltaMKMQDEDKVSQLEMELEEERNNSDLLSE 1035
Cdd:PTZ00121 1782 EEE------LDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
604-1233 |
9.20e-13 |
|
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: 73.16 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 604 NSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQN-IKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKN 682
Cdd:TIGR00606 269 NEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 683 LEELfQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKG-----ALIEELLQAK--------QDLQDLLIAKEEQ 749
Cdd:TIGR00606 349 QGRL-QLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQiknfhTLVIERQEDEaktaaqlcADLQSKERLKQEQ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 750 EDLLRKRERELTALKGALKEEVSSHDQE--------------MDKLKEQYDAELQALRE-SVEEATKNVEVLASRSNTSE 814
Cdd:TIGR00606 428 ADEIRDEKKGLGRTIELKKEILEKKQEElkfvikelqqlegsSDRILELDQELRKAERElSKAEKNSLTETLKKEVKSLQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 815 QDQAGTEMRVKLLQEENEKLQGRSEELEQ------RVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEK 888
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEIN 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 889 EAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEmENERWHLGKTIEKLQKEMADIVEASRTST 968
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIEKSSKQRAMLAGATAVYS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 969 lelqNQLDEYKEKNRRELAEMQRQLK-EKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQV 1047
Cdd:TIGR00606 667 ----QFITQLTDENQSCCPVCQRVFQtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1048 RNELLQERAARQDLECDkisLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAEledrleseerdraSLQLSNRRLER 1127
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRD---IQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIME-------------RFQMELKDVER 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1128 KVKELVMQVDDEHLSLTDQKdqlslrlkaMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLK 1207
Cdd:TIGR00606 807 KIAQQAAKLQGSDLDRTVQQ---------VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIG 877
|
650 660
....*....|....*....|....*.
gi 1622953339 1208 KLPNKVLDDMDDDDDLSTDGGSLYEA 1233
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSLIRE 903
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
610-1200 |
1.84e-12 |
|
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: 72.39 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 610 KDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQV 689
Cdd:TIGR00606 366 RDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 690 KMEREQHQTEIRDLQDQLSEMHDELDSAKRSEdrekgaliEELLQAKQDLQdlLIAKEEQEDLLRKRERELTALKGALKE 769
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSSDRILELD--------QELRKAERELS--KAEKNSLTETLKKEVKSLQNEKADLDR 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 770 EVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQ--DQAGTEMRVKLLQEENEKLQGRSEELEQRVAQ 847
Cdd:TIGR00606 516 KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEltSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 848 LQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRaLENELEAAQRN---LSRTTQEQKQLSEKLKE 924
Cdd:TIGR00606 596 LNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLER-LKEEIEKSSKQramLAGATAVYSQFITQLTD 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 925 ESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSR 1004
Cdd:TIGR00606 675 ENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1005 LTAMKMQD-----EDKVSQLEMELEEERNNSDLLSER--ISRSREQMEQVRNELLQERAARQ----DLECDKISLERQNK 1073
Cdd:TIGR00606 755 KVNRDIQRlkndiEEQETLLGTIMPEEESAKVCLTDVtiMERFQMELKDVERKIAQQAAKLQgsdlDRTVQQVNQEKQEK 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1074 DLKSRIIHLEGSyrsSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRR---LERKVKELVMQVDDEHLSLTDQKDQL 1150
Cdd:TIGR00606 835 QHELDTVVSKIE---LNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRrqqFEEQLVELSTEVQSLIREIKDAKEQD 911
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1151 SLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEeqmDMNEHLQGQLNSMK 1200
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKVN---DIKEKVKNIHGYMK 958
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
873-1208 |
3.00e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 71.25 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 873 IRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEK 952
Cdd:PRK03918 132 IRQGEIDAILESDESREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 953 LQKEMADIVEasrtstlELQNQLDEYK--EKNRRELAEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNS 1030
Cdd:PRK03918 212 ISSELPELRE-------ELEKLEKEVKelEELKEEIEELEKELES--LEGSKRKLEEKIRELEERIEELKKEIEELEEKV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1031 DLLSErISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEgsyrsskeglvvQMEARIAELEDRLES 1110
Cdd:PRK03918 283 KELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE------------EKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1111 EERDRAslqlsnrRLERKVKELvmqvdDEHLSLTDQKDQLSLRLKAmkRQVEEAEEEIDRLESSKKKLQRELEEQMDMNE 1190
Cdd:PRK03918 350 LEKRLE-------ELEERHELY-----EEAKAKKEELERLKKRLTG--LTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
330
....*....|....*...
gi 1622953339 1191 HLQGQLNSMKKDLSRLKK 1208
Cdd:PRK03918 416 ELKKEIKELKKAIEELKK 433
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
532-995 |
4.22e-12 |
|
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: 70.82 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 532 NTQATPDLLKGQQELTQQTNEETAKQILYNYLKEGSADNDDATKRKVNLVFEKIQTLKsraagsaQGNNQASNSTSEVKD 611
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK-------ELEKQLNQLKSEISD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 612 LLEQKSklttevAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVE-----------ENSTLQQRLEESEGELR 680
Cdd:TIGR04523 300 LNNQKE------QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISqlkkeltnsesENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 681 KnleelfqVKMEREQHQTEIRDLQDQLSEMHDELDSAKrsedrekgalieellQAKQDLQDLLIAKEEQEDLLRKREREL 760
Cdd:TIGR04523 374 K-------LKKENQSYKQEIKNLESQINDLESKIQNQE---------------KLNQQKDEQIKKLQQEKELLEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 761 TALKGALKEEVSSHDQEMDKLKEQYDaELQALRESVEeatKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEE 840
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIK-NLDNTRESLE---TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 841 LEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALvqarrEEKEAVSARRALENELEAAQRNLSRTTQEQKQLSE 920
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL-----NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKK 582
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 921 KLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNqLDEYKEKNRRELAEMQRQLKE 995
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN-IKSKKNKLKQEVKQIKETIKE 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
828-1057 |
5.88e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 828 QEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALvqarreekeavsarRALENELEAAQRN 907
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI--------------RALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 908 LSRTTQEQKQLSEKLKEESEQ-KEQLRRLKNEMENERWHLG------KTIEKLQKEMADIVEASRTSTLELQNQLDEYKE 980
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953339 981 KnRRELAEMQRQLKE--KTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAA 1057
Cdd:COG4942 165 L-RAELEAERAELEAllAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
769-1208 |
6.64e-12 |
|
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: 70.20 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 769 EEVSSHDQEMDKLKEQydaELQALRESVEEATKNVEVLASRSNTSEQDQAGT-------EMRVKLLQEENE------KLQ 835
Cdd:pfam01576 5 EEMQAKEEELQKVKER---QQKAESELKELEKKHQQLCEEKNALQEQLQAETelcaeaeEMRARLAARKQEleeilhELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 836 GRSEELEQRVAQL-------QRQIEDLKG-----DEAKAKETLKKY--EGEIRQLEEALVQARREEKEAVSARRALENEL 901
Cdd:pfam01576 82 SRLEEEEERSQQLqnekkkmQQHIQDLEEqldeeEAARQKLQLEKVttEAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 902 EAAQRNLSRTTQEQKQLS--------------EKLKEESEQKEQLRRLKNEMENE------------------RWHLGKT 949
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSklknkheamisdleERLKKEEKGRQELEKAKRKLEGEstdlqeqiaelqaqiaelRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 950 IEKLQKEMADIVE--ASRTSTL----ELQNQLDEYK-----EKNRRELAEMQRQLKEKTLEAEKSRL------TA----M 1008
Cdd:pfam01576 242 EEELQAALARLEEetAQKNNALkkirELEAQISELQedlesERAARNKAEKQRRDLGEELEALKTELedtldtTAaqqeL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1009 KMQDEDKVSQLEMELEEE-RNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSyR 1087
Cdd:pfam01576 322 RSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA-K 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1088 SSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERK---VKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEA 1164
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSElesVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 1165 EEE-------IDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:pfam01576 481 TRQklnlstrLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
608-1208 |
1.30e-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: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEE-NSTLQQRLEESEGELRKNLEEL 686
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREaKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 687 FQVKMEREQHQTEIRDLQDQLSEMHDELdsakrsEDREKGALIEEllqakqdlqdlliakeEQEDLLRKRERELTALKGA 766
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKLLADL------HKREKELSLEK----------------EQNKRLWDRDTGNSITIDH 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 767 LKEEVSSHDQEMDKLkeqyDAELQALRESVEEAtknvevlasrsntseqdqagtemrvklLQEENEKLQGRSEELEqRVA 846
Cdd:pfam15921 417 LRRELDDRNMEVQRL----EALLKAMKSECQGQ---------------------------MERQMAAIQGKNESLE-KVS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 QLQRQIEdlkgdeaKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEES 926
Cdd:pfam15921 465 SLTAQLE-------STKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLK 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 927 EQKEQLRRLKNEMENERWHLG---KTIEKLQKEMADIVEA----SRTSTLELQNQLDEYKEKNRRELaemqrQLKEktLE 999
Cdd:pfam15921 538 NEGDHLRNVQTECEALKLQMAekdKVIEILRQQIENMTQLvgqhGRTAGAMQVEKAQLEKEINDRRL-----ELQE--FK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1000 AEKSRLTAMKMQDEDKVSQLEMELEEERNNSdllSERIsRSREQMEQVRNELLQE-RAARQDLEcdkiSLERQNKDLKSR 1078
Cdd:pfam15921 611 ILKDKKDAKIRELEARVSDLELEKVKLVNAG---SERL-RAVKDIKQERDQLLNEvKTSRNELN----SLSEDYEVLKRN 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1079 IIHLEGSYRSSKEGLVVQMEARIAELEdrleseeRDRASLQlSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMK 1158
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELE-------QTRNTLK-SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLE 754
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1159 RQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:pfam15921 755 EAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1079 |
1.33e-11 |
|
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: 67.87 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREekeavsaRRALENELEAAQRNLSRTTQEQKQL 918
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 919 SEKLKEESEQ-KEQLRRLKNEMENERWHLGKTIEklqkemaDIVEASRTSTLelqnqLDEYKEKNRRELAEMQRQLKEkt 997
Cdd:COG4942 96 RAELEAQKEElAELLRALYRLGRQPPLALLLSPE-------DFLDAVRRLQY-----LKYLAPARREQAEELRADLAE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 998 LEAEKSRLTAMKmqdeDKVSQLEMELEEERNNsdlLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKS 1077
Cdd:COG4942 162 LAALRAELEAER----AELEALLAELEEERAA---LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
..
gi 1622953339 1078 RI 1079
Cdd:COG4942 235 EA 236
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
692-906 |
1.96e-11 |
|
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: 67.48 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 692 EREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGAL------IEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKG 765
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalerrIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 ALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRV 845
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 846 AQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQR 906
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
643-1081 |
2.42e-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: 68.61 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 643 ERERMRANLEELRSQ--------------HNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLS 708
Cdd:pfam15921 427 EVQRLEALLKAMKSEcqgqmerqmaaiqgKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 709 EMHDELDsAKRSEDREKGALIEELLQAKQDLQDlliakeeQEDLLRKRERELTALKGALKEEvsshdqemdklkeqyDAE 788
Cdd:pfam15921 507 EKERAIE-ATNAEITKLRSRVDLKLQELQHLKN-------EGDHLRNVQTECEALKLQMAEK---------------DKV 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 789 LQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKK 868
Cdd:pfam15921 564 IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSE 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 869 YEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEE----SEQKEQLRRLKNEMENERW 944
Cdd:pfam15921 644 RLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQlksaQSELEQTRNTLKSMEGSDG 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 945 HLGKTIEKLQKEmadiVEASRTSTLELQNQLDEYKEKnrrelaeMQRQLKEKT-LEAEKSRLTAMKMQDEDKVSQLEMEL 1023
Cdd:pfam15921 724 HAMKVAMGMQKQ----ITAKRGQIDALQSKIQFLEEA-------MTNANKEKHfLKEEKNKLSQELSTVATEKNKMAGEL 792
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 1024 EEERNNSDLLSERISRSreqmeqvrnELLQERAARQDLECDKISLERQNKDLKSRIIH 1081
Cdd:pfam15921 793 EVLRSQERRLKEKVANM---------EVALDKASLQFAECQDIIQRQEQESVRLKLQH 841
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
538-866 |
3.44e-11 |
|
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: 68.16 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 538 DLLKGQQELTQQTNE-ETAKQILYNYLKEGSADNDDA--TKRKVNLVFEKIQTLKSRAAGSAQGNNQASnstSEVKDLLE 614
Cdd:TIGR02168 685 KIEELEEKIAELEKAlAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEAEVEQLEERIAQLS---KELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 615 QKSKLTTEVAELQR----------QLQLEVKNQQN----IKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELR 680
Cdd:TIGR02168 762 EIEELEERLEEAEEelaeaeaeieELEAQIEQLKEelkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 681 KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAkrseDREKGALIEELLQAKQDLQDLliakEEQEDLLRKREREL 760
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEAL----LNERASLEEALALLRSELEEL----SEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 761 TALKGALKEEVSSHDQEMDKLKEQYDAELQALResvEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLqGR--- 837
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLS---EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL-GPvnl 989
|
330 340 350
....*....|....*....|....*....|....
gi 1622953339 838 -----SEELEQRVAQLQRQIEDLKgdeaKAKETL 866
Cdd:TIGR02168 990 aaieeYEELKERYDFLTAQKEDLT----EAKETL 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
780-1005 |
1.37e-10 |
|
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: 64.79 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 780 KLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDE 859
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 860 AKAKETLKKYEGEIRQL------------EEALVQARREE--KEAVSARRALENELEAAQRNLSRT----TQEQKQLSEK 921
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqpplalllspEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALraelEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 922 LKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEAsrtstlelQNQLDEYKEKNRRELAEMQRQLKEKTLEAE 1001
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE--------AEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....
gi 1622953339 1002 KSRL 1005
Cdd:COG4942 252 KGKL 255
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
607-1212 |
1.42e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.15 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRA--NLEELRSQHNKKVEENSTLQQRLEESEGELRKNLE 684
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQeiEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 685 ELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKgalIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALK 764
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEE---IEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 765 GALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEvLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQR 844
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE-LARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 845 VAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSR-------------- 910
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKdgvggriisahgrl 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 911 -------------TTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTL----ELQN 973
Cdd:pfam02463 532 gdlgvavenykvaISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILnlaqLDKA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 974 QLDEYKEKNRRELAEMQRQLKEKTLEAEK--------------SRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISR 1039
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESakakesglrkgvslEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1040 SREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEG-LVVQMEARIAELEDRLESEERDRASL 1118
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKiDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1119 QLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNS 1198
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
650
....*....|....
gi 1622953339 1199 MKKDLSRLKKLPNK 1212
Cdd:pfam02463 852 AEEELERLEEEITK 865
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
828-1204 |
1.62e-10 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 65.70 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 828 QEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAK-AKETLKKYegEIRQLEEALVQARREEKEAVSARRALENEL----- 901
Cdd:PRK11281 79 KEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEeTRETLSTL--SLRQLESRLAQTLDQLQNAQNDLAEYNSQLvslqt 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 902 --EAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRR-LKNEMENERWHLGKTIEKLQKEMADiveasrTSTLE--LQNQLD 976
Cdd:PRK11281 157 qpERAQAALYANSQRLQQIRNLLKGGKVGGKALRPsQRVLLQAEQALLNAQNDLQRKSLEG------NTQLQdlLQKQRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 977 EYKEKNRR---ELAEMQ-------RQLKEKTLEAEKSRLTAMKMQDEDKVSQlemELEEERNnsdlLSERISRSREQMeq 1046
Cdd:PRK11281 231 YLTARIQRlehQLQLLQeainskrLTLSEKTVQEAQSQDEAARIQANPLVAQ---ELEINLQ----LSQRLLKATEKL-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1047 vrNELLQER-AARQDLEcdkiSLERQNKDLKSRIIHLEGSYRSSK-----------EGLVVQMEARIAELedRLE----S 1110
Cdd:PRK11281 302 --NTLTQQNlRVKNWLD----RLTQSERNIKEQISVLKGSLLLSRilyqqqqalpsADLIEGLADRIADL--RLEqfeiN 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1111 EERDraslQLSN-----RRLERKVKELVmqVDDEHLSLTD-----QK--DQLSLRLKAmkrQVEEA-EEEIDR--LESSK 1175
Cdd:PRK11281 374 QQRD----ALFQpdayiDKLEAGHKSEV--TDEVRDALLQllderREllDQLNKQLNN---QLNLAiNLQLNQqqLLSVS 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1622953339 1176 KKLQRELEEQ---------MDMN------EHLQGQLNSMKKDLS 1204
Cdd:PRK11281 445 DSLQSTLTQQifwvnsnkpMDLDwlkafpQALKDQFKSLKITVS 488
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
619-1024 |
1.82e-10 |
|
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: 64.92 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 619 LTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELfqvkmerEQHQT 698
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------EEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 699 EIRDLQDQLSEMHDELDSAKrsedREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKgalKEEVSSHDQEM 778
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQR----AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR---KEEEAERKQLQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 779 DKLkEQYDAELQALRESVEEAtknvevlasRSNTSEQDQagtemRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGD 858
Cdd:pfam07888 178 AKL-QQTEEELRSLSKEFQEL---------RNSLAQRDT-----QVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 859 EAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARraleneLEAAQRNLsrttqEQKQLSEKLKEESEQKEQLRR-LKN 937
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR------LQAAQLTL-----QLADASLALREGRARWAQEREtLQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 938 EMENERWHLGKTIEKLQKeMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKE-----KTLEAEKSRLTAMKMQD 1012
Cdd:pfam07888 312 SAEADKDRIEKLSAELQR-LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkaslRVAQKEKEQLQAEKQEL 390
|
410
....*....|..
gi 1622953339 1013 EDKVSQLEMELE 1024
Cdd:pfam07888 391 LEYIRQLEQRLE 402
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
869-1207 |
1.97e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 869 YEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGK 948
Cdd:TIGR02169 140 LQGDVTDFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 949 TIEKLQKEMADIVEASRTSTLELQNQLDEYkeknRRELAEMQRQLKEKTLEAEksrltamkmQDEDKVSQLEMELEeern 1028
Cdd:TIGR02169 220 KREYEGYELLKEKEALERQKEAIERQLASL----EEELEKLTEEISELEKRLE---------EIEQLLEELNKKIK---- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1029 nsDLLSERISRSREQMEQVRNEllQERAARQDLECdkislERQNKDLKSRIIHLEGSYRSSKEglvvqmeaRIAELEDRL 1108
Cdd:TIGR02169 283 --DLGEEEQLRVKEKIGELEAE--IASLERSIAEK-----ERELEDAEERLAKLEAEIDKLLA--------EIEELEREI 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1109 ESEERDRASLQLSNRRLERKVKELVMQVDDEhlsltdqkdqlSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDM 1188
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEV-----------DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
330
....*....|....*....
gi 1622953339 1189 NEHLQGQLNSMKKDLSRLK 1207
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIE 433
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
678-1208 |
1.99e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 65.38 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 678 ELRKNLEELFQVKMEREQHQTEIRDLQDQLsemhdeldsaKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRE 757
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQE----------LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 758 RELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESveeatknvevlasrsntseqdqagtEMRVKLLQEENEKLQGR 837
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE-------------------------EKEKKLQEEELKLLAKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 838 SEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQ 917
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 918 LSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEmadiveasrtstleLQNQLDEYKEKNRRELAEM-------- 989
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL--------------ARQLEDLLKEEKKEELEILeeeeesie 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 990 -------QRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLE 1062
Cdd:pfam02463 441 lkqgkltEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1063 CDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLS 1142
Cdd:pfam02463 521 GGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEID 600
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1143 LTDQKDQLSLRlkAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:pfam02463 601 PILNLAQLDKA--TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
614-863 |
2.09e-10 |
|
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: 64.01 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 614 EQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNleelfqvKMER 693
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-------EKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 694 EQHQTEIRDLQDQLSEMhdeLDSAKRSEDREKGALI------EELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGAL 767
Cdd:COG4942 93 AELRAELEAQKEELAEL---LRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 KEEVsshdQEMDKLKEQYDAELQALRESVEEATKNVEVLasrsntsEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQ 847
Cdd:COG4942 170 EAER----AELEALLAELEEERAALEALKAERQKLLARL-------EKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....*.
gi 1622953339 848 LQRQIEDLKGDEAKAK 863
Cdd:COG4942 239 AAERTPAAGFAALKGK 254
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
697-1185 |
3.71e-10 |
|
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: 64.38 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 697 QTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSH-- 774
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNrl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 775 ----DQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQR 850
Cdd:pfam05557 81 kkkyLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 851 QIEDLKGDEAKAKETlkKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLsRTTQEQKQLsekLKEESEQKE 930
Cdd:pfam05557 161 QQSSLAEAEQRIKEL--EFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHL-NENIENKLL---LKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 931 QLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEykeknRRELAEMQRqlKEKTLEAEKSRLTAMKM 1010
Cdd:pfam05557 235 RKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDL-----SRRIEQLQQ--REIVLKEENSSLTSSAR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1011 QDEDKVSQLEMELEEERNNsdLLSERISRsREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYR-SS 1089
Cdd:pfam05557 308 QLEKARRELEQELAQYLKK--IEDLNKKL-KRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERiEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1090 KEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQKdqlslrLKAMKRQVEEAEEEID 1169
Cdd:pfam05557 385 AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEE------VDSLRRKLETLELERQ 458
|
490
....*....|....*.
gi 1622953339 1170 RLESSKKKLQRELEEQ 1185
Cdd:pfam05557 459 RLREQKNELEMELERR 474
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
606-1023 |
4.23e-10 |
|
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: 64.22 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 606 TSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEE 685
Cdd:TIGR00618 527 TRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 686 lfqVKMEREQHQTEIRDLQDQLSEMHdeldsakrsedrekgaLIEELLQAKQDLQDLLIAKE-EQEDLLRKRERELTALK 764
Cdd:TIGR00618 607 ---EDMLACEQHALLRKLQPEQDLQD----------------VRLHLQQCSQELALKLTALHaLQLTLTQERVREHALSI 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 765 GALKEEvsshdqemdkLKEQYDAELQALRESVEEATKNVEVLASRSNtseqdqagtemrvkLLQEENEKLQGRSEELEQR 844
Cdd:TIGR00618 668 RVLPKE----------LLASRQLALQKMQSEKEQLTYWKEMLAQCQT--------------LLRELETHIEEYDREFNEI 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 845 VAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSrttQEQKQLSEKLKE 924
Cdd:TIGR00618 724 ENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQ---FFNRLREEDTHL 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 925 ESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSR 1004
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
410 420
....*....|....*....|
gi 1622953339 1005 LTAMKMQ-DEDKVSQLEMEL 1023
Cdd:TIGR00618 881 INQIKIQfDGDALIKFLHEI 900
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
608-956 |
4.86e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREK-----------GALIEELLQAKQDLQD--------------- 741
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliAAALLALLGLGGSLLSliltiagvlflvlgl 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 742 --LLIAKEEQEDLLRKRERELTALKGALKEEvssHDQEMDKLKEQYDAELQALRESVEEATKNVEVLasRSNTSEQDQAG 819
Cdd:COG4717 286 laLLFLLLAREKASLGKEAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLELLDRIEEL--QELLREAEELE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 820 TEMRVKLLQEENEKLQGRS-----EELEQRVAQLQRQiEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEK--EAVS 892
Cdd:COG4717 361 EELQLEELEQEIAALLAEAgvedeEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEELEEEleELEE 439
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 893 ARRALENELEAAQRNLSRTTQEQKQLSEKlKEESEQKEQLRRLKNEMENE----------RWHLGKTIEKLQKE 956
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELaeewaalklaLELLEEAREEYREE 512
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
599-1208 |
5.04e-10 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 64.33 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 599 NNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEV-KNQQNIKEERERMRANLEELRSQH--NKKVEENSTLQQRLEES 675
Cdd:COG5022 828 REKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLlKKETIYLQSAQRVELAERQLQELKidVKSISSLKLVNLELESE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 676 EGELRKNLEELFqvkMEREQHQTE-IRDLQDQLSEMHDELDSAKrseDREKGALIEELLQAKQDLQDLLiakEEQEDLLR 754
Cdd:COG5022 908 IIELKKSLSSDL---IENLEFKTElIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKETS---EEYEDLLK 978
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KRERELTALKGAlKEEVSSHDQEMDKLKEQYDAeLQALRESVEEatKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKL 834
Cdd:COG5022 979 KSTILVREGNKA-NSELKNFKKELAELSKQYGA-LQESTKQLKE--LPVEVAELQSASKIISSESTELSILKPLQKLKGL 1054
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 835 QGRS-EELEQRVAQLQRQIEDLKGDEaKAKETLKKYEGEIRQLEEALVQArrEEKEAVSARRALENeLEAAQRNLSRTTQ 913
Cdd:COG5022 1055 LLLEnNQLQARYKALKLRRENSLLDD-KQLYQLESTENLLKTINVKDLEV--TNRNLVKPANVLQF-IVAQMIKLNLLQE 1130
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 914 EQKQLSEKL-------KEESEQKEQLRRLKNEMENERWHLGK----TIEKLQKEMADIVEASRTSTLELQNQLDEYKEKN 982
Cdd:COG5022 1131 ISKFLSQLVntlepvfQKLSVLQLELDGLFWEANLEALPSPPpfaaLSEKRLYQSALYDEKSKLSSSEVNDLKNELIALF 1210
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 983 RRELAEMQRQLKEKTLEAEKSRLTAMKMqdedkvsqlemELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLE 1062
Cdd:COG5022 1211 SKIFSGWPRGDKLKKLISEGWVPTEYST-----------SLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEE 1279
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1063 -----CDKISLERQNKDLKSRIIHLEGSYRSSkegLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQvD 1137
Cdd:COG5022 1280 evlpaTINSLLQYINVGLFNALRTKASSLRWK---SATEVNYNSEELDDWCREFEISDVDEELEELIQAVKVLQLLKD-D 1355
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1138 DEHLS--LTDQKDQLSLRLKAMKRQVEEAEEE-------IDRLESS--KKKLQRELEEQMDMNEHLQgQLNSMKKDLSRL 1206
Cdd:COG5022 1356 LNKLDelLDACYSLNPAEIQNLKSRYDPADKEnnlpkeiLKKIEALliKQELQLSLEGKDETEVHLS-EIFSEEKSLISL 1434
|
..
gi 1622953339 1207 KK 1208
Cdd:COG5022 1435 DR 1436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
623-943 |
5.57e-10 |
|
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: 63.60 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 623 VAELQRQLQLEVKNQQNIKEERERM------RANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQH 696
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKareverRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 697 QTEIRDLQDQLSEMHdELDSAKRSEDREKGALIEELLQAKQdlqdlliAKEEQEDLLRKRERELTALKGALKEEVSSHDQ 776
Cdd:pfam17380 364 RIRQEEIAMEISRMR-ELERLQMERQQKNERVRQELEAARK-------VKILEEERQRKIQQQKVEMEQIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 777 EMDKLKEQYDAELQALRESVEEATKNVEVLasrsntseQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLK 856
Cdd:pfam17380 436 EVRRLEEERAREMERVRLEEQERQQQVERL--------RQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 857 GDEAKAKETLKKYEGEIRQLEEALVQARREEKEavsarraleneleaaQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLK 936
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEE---------------ERRKQQEMEERRRIQEQMRKATEERSRLEAME 572
|
....*..
gi 1622953339 937 NEMENER 943
Cdd:pfam17380 573 REREMMR 579
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
663-896 |
6.28e-10 |
|
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: 62.47 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 663 EENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAkrseDREKGALIEELLQAKQDLQDL 742
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 743 LIAKEEQEDLLRKREREL--TALKGALKEEVSSHD-QEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQag 819
Cdd:COG4942 96 RAELEAQKEELAELLRALyrLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER-- 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 820 temrvKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRA 896
Cdd:COG4942 174 -----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
747-1054 |
7.63e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 7.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 747 EEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAeLQALRESVEEATKNVEVLASRSNTSEQdqagtemrVKL 826
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-LQRLAEYSWDEIDVASAEREIAELEAE--------LER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 827 LQEEN---EKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQArrEEKEAVSARRALENELEA 903
Cdd:COG4913 680 LDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 904 AQRNlSRTTQEQKQLSEKLKEESEQKEQLRrlknemenerwhlgktiEKLQKEMADIVEASRTSTLELQNQLDEYkeknr 983
Cdd:COG4913 758 ALGD-AVERELRENLEERIDALRARLNRAE-----------------EELERAMRAFNREWPAETADLDADLESL----- 814
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 984 RELAEMQRQLKEKTLEAEKSRLTAMKMQDED-KVSQLEMELEEERnnsdllsERIsrsREQMEQVrNELLQE 1054
Cdd:COG4913 815 PEYLALLDRLEEDGLPEYEERFKELLNENSIeFVADLLSKLRRAI-------REI---KERIDPL-NDSLKR 875
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
601-1202 |
9.41e-10 |
|
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: 63.53 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 601 QASNSTSEVKDLLEQKSKLTTEVAELQRQ--------LQLEVKNQQNIKEERERMRANLEELRSQHNKKVEEnstlqqrL 672
Cdd:TIGR00606 462 ELQQLEGSSDRILELDQELRKAERELSKAeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT-------R 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 673 EESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMhDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDL 752
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 753 LRKRERELTALKGALKEEVSSHDQEMDklkeqydaeLQALRESVEEATKNVEVLASRSNTSEQdqagtemRVKLLQEENE 832
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDVCGSQDEESD---------LERLKEEIEKSSKQRAMLAGATAVYSQ-------FITQLTDENQ 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 833 KLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEalvqaRREEkeavsarraLENELEAAQRNLSRTT 912
Cdd:TIGR00606 678 SCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEK-----RRDE---------MLGLAPGRQSIIDLKE 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 913 QEQKQLSEKLKEESEQkeqLRRLKNEMENERWHLGKTIEKLqkEMADIVEASRTSTLELQNQLDEykekNRRELAEMQRQ 992
Cdd:TIGR00606 744 KEIPELRNKLQKVNRD---IQRLKNDIEEQETLLGTIMPEE--ESAKVCLTDVTIMERFQMELKD----VERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 993 LKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNnsdlLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQN 1072
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK----LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQL 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1073 KDLKSRIIHLEGSYRSSKEglvvQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTD------- 1145
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKE----QDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDienkiqd 966
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 1146 ----QKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKD 1202
Cdd:TIGR00606 967 gkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRE 1027
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
834-1125 |
9.76e-10 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 62.01 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 834 LQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQ 913
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 914 EQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQL 993
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 994 KEKT-----LEAEKSRLTAMKMQDEDKVSQL----EMELEEERNNSDLLSERISRSREqMEQVRNELLQERAARQDLECD 1064
Cdd:pfam19220 241 AERAslrmkLEALTARAAATEQLLAEARNQLrdrdEAIRAAERRLKEASIERDTLERR-LAGLEADLERRTQQFQEMQRA 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 1065 KISLERQNKDLKSRIihlegsyrSSKEGLVVQMEARIAELEDRLESEER----DRASLQLSNRRL 1125
Cdd:pfam19220 320 RAELEERAEMLTKAL--------AAKDAALERAEERIASLSDRIAELTKrfevERAALEQANRRL 376
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
599-941 |
1.08e-09 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 62.74 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 599 NNQASNSTSEVKDLLEQKSKLTTEVAELQRQLqlevkNQQNIKEerermRANLEELRSQHNKKveenstLQQRLEESege 678
Cdd:pfam05667 195 TAQPSSRASVVPSLLERNAAELAAAQEWEEEW-----NSQGLAS-----RLTPEEYRKRKRTK------LLKRIAEQ--- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 679 lrknLEELFQVKMEREQHQTEIR-DLQDQLSEMHDeldSAKRSEDREKGALI--EELLQAKQDLQ----DLLIAKEEQED 751
Cdd:pfam05667 256 ----LRSAALAGTEATSGASRSAqDLAELLSSFSG---SSTTDTGLTKGSRFthTEKLQFTNEAPaatsSPPTKVETEEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 752 LLRKRERELTALKG---ALKEEVSSHDQEMDKLK---EQYDAELQALRESVEEATKNVEVlasrsntseqdqagTEMRVK 825
Cdd:pfam05667 329 LQQQREEELEELQEqleDLESSIQELEKEIKKLEssiKQVEEELEELKEQNEELEKQYKV--------------KKKTLD 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 826 LLQ--EEN-EKLQGRSEELEQRVAQLQRQIEdlkgdeaKAKETLKKyegEIRQLEEAlvQARREEKeavsarralenele 902
Cdd:pfam05667 395 LLPdaEENiAKLQALVDASAQRLVELAGQWE-------KHRVPLIE---EYRALKEA--KSNKEDE-------------- 448
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622953339 903 aAQRNLSrttqEQKQLSEKLKEESE---QKEQL-RRLKNEMEN 941
Cdd:pfam05667 449 -SQRKLE----EIKELREKIKEVAEeakQKEELyKQLVAEYER 486
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
492-1073 |
1.11e-09 |
|
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: 63.14 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 492 KKEEEVKTATATLMLQNRAAATSpdsgAKKISVKtfpSASNTQAtpDLLKGQQELTQQTNEEtakqilyNYLKEGSADND 571
Cdd:TIGR00606 475 ELDQELRKAERELSKAEKNSLTE----TLKKEVK---SLQNEKA--DLDRKLRKLDQEMEQL-------NHHTTTRTQME 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 572 DATKRKVNlVFEKIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANL 651
Cdd:TIGR00606 539 MLTKDKMD-KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESK 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 652 EELRSQHNKKVEE---NSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEdrekgal 728
Cdd:TIGR00606 618 EEQLSSYEDKLFDvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTE------- 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 729 iEELLQAKQDLQDLLIA----KEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKE------QYDAELQALRESVEE 798
Cdd:TIGR00606 691 -AELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPElrnklqKVNRDIQRLKNDIEE 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 799 ATKNVEVLASRSNTSEQDQAGtemrVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYE-GEIRQLE 877
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTD----VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHElDTVVSKI 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 878 EALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEM 957
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 958 ADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQlkEKTLEAEKSRltaMKMQDEDKVSQLEMELEEERNNSDLLSERI 1037
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI--ENKIQDGKDD---YLKQKETELNTVNAQLEECEKHQEKINEDM 1000
|
570 580 590
....*....|....*....|....*....|....*...
gi 1622953339 1038 SRSREQME--QVRNELLQERAARQDLECDKISLERQNK 1073
Cdd:TIGR00606 1001 RLMRQDIDtqKIQERWLQDNLTLRKRENELKEVEEELK 1038
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
486-938 |
1.43e-09 |
|
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: 62.43 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 486 SLGAQSKKEEEVKTATATLMLQNRAAATSPDSGAKKISVKTFPSA---SNTQATPDLLKGQQELTQqtNEETAKQILYNY 562
Cdd:pfam05483 308 SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTefeATTCSLEELLRTEQQRLE--KNEDQLKIITME 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 563 LKEGSADNDDATKRKVN--LVFEKIQTLKSRAAGSAQGNNQASNSTSEVKD-------LLEQKSKlttEVAELQRQLQLE 633
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNkeVELEELKKILAEDEKLLDEKKQFEKIAEELKGkeqelifLLQAREK---EIHDLEIQLTAI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 634 VKNQQNIKEERERMRANLE-------ELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQ 706
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEkeklkniELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 707 LSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALK-----------------GALKE 769
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKkqienknknieelhqenKALKK 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 770 EVSSHDQEMDKLK---EQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQgrsEELEQRVa 846
Cdd:pfam05483 623 KGSAENKQLNAYEikvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQ---KEIDKRC- 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 qlQRQIEDLKGDEAKAKEtlkKYEGEIRQLEEALVQARREEKEAVSARRALENEleaaqrnLSRTTQEQKQLSEKLKEES 926
Cdd:pfam05483 699 --QHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAKAALEIE-------LSNIKAELLSLKKQLEIEK 766
|
490
....*....|..
gi 1622953339 927 EQKEQLRRLKNE 938
Cdd:pfam05483 767 EEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
805-1007 |
1.96e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 805 VLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQAR 884
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 885 REEKEAVSARRALENELE----AAQRN------------------------LSRTTQEQKQLSEKLKeesEQKEQLRRLK 936
Cdd:COG4942 90 KEIAELRAELEAQKEELAellrALYRLgrqpplalllspedfldavrrlqyLKYLAPARREQAEELR---ADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 937 NEMENERWHLGKTIEKLQKEMADIvEASRTSTLELQNQLDEYKEKNRRELAEMQRQlkEKTLEAEKSRLTA 1007
Cdd:COG4942 167 AELEAERAELEALLAELEEERAAL-EALKAERQKLLARLEKELAELAAELAELQQE--AEELEALIARLEA 234
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
600-876 |
1.97e-09 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 62.01 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 600 NQASNSTSEVKD----LLEQKSKLTTEVAELQRQLQ--LEVKNQQNIKEERERMRANLEELRsQHNKKVEENSTLQQRLE 673
Cdd:COG4192 37 NSLSNQIRYILDdslpKLQASLKLEENSNELVAALPefAAATNTTERSQLRNQLNTQLADIE-ELLAELEQLTQDAGDLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 674 ESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLL 753
Cdd:COG4192 116 AAVADLRNLLQQLDSLLTQRIALRRRLQELLEQINWLHQDFNSELTPLLQEASWQQTRLLDSVETTESLRNLQNELQLLL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 754 RkRERELTALKGALKE-EVSSHDQEMDKLKEQYDaelqalrESVEEATKNVEVLASRSNTSEQDQAGTEMRV-------- 824
Cdd:COG4192 196 R-LLAIENQIVSLLREvAAARDQADVDNLFDRLQ-------YLKDELDRNLQALKNYPSTITLRQLIDELLAigsgeggl 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 825 -KLLQEE---NEKLQGRSEELEQRVAQLQRQIEDLKGdeaKAKETLKKYEGEIRQL 876
Cdd:COG4192 268 pSLRRDElaaQATLEALAEENNSILEQLRTQISGLVG---NSREQLVALNQETAQL 320
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
879-1131 |
2.67e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 879 ALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMA 958
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 959 diveasrtstlELQNQLDEYKEKNRRELAEMQRQlkektleAEKSRLTAMKMQDEdkVSQLEMELEeernnsdLLSERIS 1038
Cdd:COG4942 94 -----------ELRAELEAQKEELAELLRALYRL-------GRQPPLALLLSPED--FLDAVRRLQ-------YLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1039 RSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEgSYRSSKEGLVVQMEARIAELEDRLESEERDRASL 1118
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|...
gi 1622953339 1119 QLSNRRLERKVKE 1131
Cdd:COG4942 226 EALIARLEAEAAA 238
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
719-943 |
3.41e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.19 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 719 RSEDREKGALI-EELLQAKQDLQdlliaKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDaeLQALRESVE 797
Cdd:COG3206 143 TSPDPELAAAVaNALAEAYLEQN-----LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 798 EATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQ--RVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQ 875
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953339 876 LEEALVQARRE-EKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENER 943
Cdd:COG3206 296 LRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAR 364
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
600-898 |
3.75e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 600 NQASNSTSEVKDLLEQKSKLTTEVAELqrqlqlevknqqniKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGEL 679
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEEL--------------KEKRDELNEELKELAEKRDELNAQVKELREEAQELREKR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 680 RKNLEELFQVKMEREQHQTEIRDLQDQLSE---MHDELDSAKRSEDREKGALieELLQAKQDLQDLLIAKEEQedlLRKR 756
Cdd:COG1340 67 DELNEKVKELKEERDELNEKLNELREELDElrkELAELNKAGGSIDKLRKEI--ERLEWRQQTEVLSPEEEKE---LVEK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 757 ERELTALKGALKEEVSSHDQEMDKLkeqydAELQALRESVEEATKNVEVLAsrsntSEQDQAGTEMrVKLLQEEnEKLQG 836
Cdd:COG1340 142 IKELEKELEKAKKALEKNEKLKELR-----AELKELRKEAEEIHKKIKELA-----EEAQELHEEM-IELYKEA-DELRK 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 837 RSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALE 898
Cdd:COG1340 210 EADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEE 271
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
638-1050 |
4.01e-09 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 60.64 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 638 QNIKEERERMRANLEELRSQHnkkvEENSTLQQRLEESEGELRKNLEElfqvkmEREQHQTEIRDLQDQLSEMHDELDSA 717
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESE----EKNREEVEELKDKYRELRKTLLA------NRFSYGPAIDELEKQLAEIEEEFSQF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 718 krSEDREKGALI---EELLQAKQDLQDLLIAKEEQEDLLRKRERELtalKGALkEEVSSHDQEMdkLKEQY-------DA 787
Cdd:pfam06160 166 --EELTESGDYLearEVLEKLEEETDALEELMEDIPPLYEELKTEL---PDQL-EELKEGYREM--EEEGYalehlnvDK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 788 ELQALRESVEEATKNVEVLasrsntsEQDQAGTEMrvkllqeeneklqgrsEELEQRVAQLQRQIEDlkgdEAKAKETLK 867
Cdd:pfam06160 238 EIQQLEEQLEENLALLENL-------ELDEAEEAL----------------EEIEERIDQLYDLLEK----EVDAKKYVE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 868 KYEGEIRQ-LEEALVQAR--REEKEAVSARRAL-ENELEAAQ---RNLSRTTQEQKQLSEKLKEE----SEQKEQLRRLK 936
Cdd:pfam06160 291 KNLPEIEDyLEHAEEQNKelKEELERVQQSYTLnENELERVRgleKQLEELEKRYDEIVERLEEKevaySELQEELEEIL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 937 NEMEnerwhlgkTIEKLQKEMADIVEASRTSTLELQNQLDEYKeknrRELAEMQRQLkektleaEKSRLT-------AMK 1009
Cdd:pfam06160 371 EQLE--------EIEEEQEEFKESLQSLRKDELEAREKLDEFK----LELREIKRLV-------EKSNLPglpesylDYF 431
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1622953339 1010 MQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNE 1050
Cdd:pfam06160 432 FDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEK 472
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
724-1062 |
4.21e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.13 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 724 EKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLK------------EQYDAELQA 791
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqtalrqqekiERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 792 LRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLkgdeAKAKETLKKYEG 871
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL----ERAKQLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 872 EIRQLEEALVQARREEKEAVSARRALENELeaaqrnlsrttqeqkQLSEKLKEESEQKEQL-RRLKNEME-NERWHLGKt 949
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKL---------------SVAQAAHSQFEQAYQLvRKIAGEVSrSEAWDVAR- 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 950 iEKLQKEMADIVEASRTStlELQNQLDEYkeknRRELAEMQRQlkEKTLEAEKSRLTAMkMQDEDKVSQLEMELEEERNN 1029
Cdd:PRK04863 500 -ELLRRLREQRHLAEQLQ--QLRMRLSEL----EQRLRQQQRA--ERLLAEFCKRLGKN-LDDEDELEQLQEELEARLES 569
|
330 340 350
....*....|....*....|....*....|...
gi 1622953339 1030 sdlLSERISRSREQMEQVRNELLQERAARQDLE 1062
Cdd:PRK04863 570 ---LSESVSEARERRMALRQQLEQLQARIQRLA 599
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
531-1184 |
5.34e-09 |
|
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: 60.51 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 531 SNTQATPDLLKGQQELTQQTNEETAKQILYnyLKEGSADNDDATKRKvNLVFEKIQTLKSRAAGSAQGNNQASNSTSEVK 610
Cdd:pfam05483 106 NKLQENRKIIEAQRKAIQELQFENEKVSLK--LEEEIQENKDLIKEN-NATRHLCNLLKETCARSAEKTKKYEYEREETR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 611 ----DLLEQKSKLTTEVAELQRQLQ-LEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELrKNLEE 685
Cdd:pfam05483 183 qvymDLNNNIEKMILAFEELRVQAEnARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM-KDLTF 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 686 LFQVKMEREQHQTEIRDLQDQ------------LSEMHDELDSAKRSEDREKgALIEELLQAKQDLQDLLIAKEEQEDLL 753
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDEnlkeliekkdhlTKELEDIKMSLQRSMSTQK-ALEEDLQIATKTICQLTEEKEAQMEEL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 754 RKRE-------RELTALKGALKEEVSSHDQEMDKLKEQYD---AELQALRESVEEATK---NVEVLASRSNTSEQDQAGT 820
Cdd:pfam05483 341 NKAKaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQLKiitMELQKKSSELEEMTKfknNKEVELEELKKILAEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 821 EMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENE 900
Cdd:pfam05483 421 LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLE 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 901 LEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMadiveasRTSTLELQNQLDEYKE 980
Cdd:pfam05483 501 NKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF-------IQKGDEVKCKLDKSEE 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 981 KNRRELAEMQRqlKEKTLEAEKSRLTAMKMQDEDKVSQLEmELEEERNNSDLLSERISRSREQMEQVRNELLQERAA--- 1057
Cdd:pfam05483 574 NARSIEYEVLK--KEKQMKILENKCNNLKKQIENKNKNIE-ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASakq 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1058 ---------RQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEgLVVQMEARIAELEDRLES---------EERDRASLQ 1119
Cdd:pfam05483 651 kfeeiidnyQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE-IDKRCQHKIAEMVALMEKhkhqydkiiEERDSELGL 729
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 1120 LSNRRLERKvkelvmqvdDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEidrlessKKKLQRELEE 1184
Cdd:pfam05483 730 YKNKEQEQS---------SAKAALEIELSNIKAELLSLKKQLEIEKEE-------KEKLKMEAKE 778
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
607-1114 |
6.23e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRanlEELRSQHNKKVEENSTLQQ--RLEESEGELRKNLE 684
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLS---IEYNNAMDDYNNLKSALNElsSLEDMKNRYESEIK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 685 ELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRErELTALK 764
Cdd:PRK01156 260 TAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS-VLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 765 G---ALKEEVSSHDQEMDKLKEQYD------AELQALRESVEEATKNVEVLASRSNTSEQDQAGT---------EMRVKL 826
Cdd:PRK01156 339 NdyiKKKSRYDDLNNQILELEGYEMdynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDpdaikkelnEINVKL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 827 LQEENE--KLQGRSEELEQRVAQLQRQIEDLKGD-----------EAKAKETLKKYEGEIRQLEEALVQARREEKEAVSA 893
Cdd:PRK01156 419 QDISSKvsSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 894 RRALENELE-AAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIVEASRTSTLELQ 972
Cdd:PRK01156 499 IVDLKKRKEyLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE----EIKNRYKSLKLEDLDSKRTSWLNAL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 973 NQLDEYK-EKNRRELAEMQRQLK--EKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERiSRSREQMEQVRN 1049
Cdd:PRK01156 575 AVISLIDiETNRSRSNEIKKQLNdlESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQEN-KILIEKLRGKID 653
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 1050 ELLQERAARQDLECDKISLERQNKDLKSRIIHLEG------SYRSSKEGLVVQMEARIAELEDRLESEERD 1114
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKalddakANRARLESTIEILRTRINELSDRINDINET 724
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
637-881 |
1.27e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 637 QQNIKEERERMRANLEELRSQhnkkVEEnstLQQRLEESEGELR--KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDEL 714
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQ----LPE---LRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 715 DSAKRSEDREKGALIEELLQAKQDLQDLLIAK-EEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALR 793
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVIQQlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 794 ESVEeatKNVEVLASRSNTSEQDQAGTEMRVKLLQEenekLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEI 873
Cdd:COG3206 316 ASLE---AELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
....*...
gi 1622953339 874 RQLEEALV 881
Cdd:COG3206 389 RVIDPAVV 396
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
628-943 |
1.28e-08 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 58.54 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 628 RQLQLEVKNQQnIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQL 707
Cdd:pfam19220 49 RLLELEALLAQ-ERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 708 SEMHDELdsakRSEDREKGALIEELLQAKQDLQDL---LIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQ 784
Cdd:pfam19220 128 AAETEQN----RALEEENKALREEAQAAEKALQRAegeLATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 785 YDAELQALRESveEATKNVEVLASRSNTSEQDQAGTEMRVKL--LQEENEKLQGRSEELEQRVAQ----LQRQIEDLKGD 858
Cdd:pfam19220 204 LDATRARLRAL--EGQLAAEQAERERAEAQLEEAVEAHRAERasLRMKLEALTARAAATEQLLAEarnqLRDRDEAIRAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 859 EAKAKET---LKKYEGEIRQLEEALVQARREEKEAVSARRALENELE---------------AAQRNLSRTTQEQKQLSE 920
Cdd:pfam19220 282 ERRLKEAsieRDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmltkalaakdaalerAEERIASLSDRIAELTKR 361
|
330 340
....*....|....*....|...
gi 1622953339 921 KLKEESEQKEQLRRLKNEMENER 943
Cdd:pfam19220 362 FEVERAALEQANRRLKEELQRER 384
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
865-1185 |
1.35e-08 |
|
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: 59.37 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 865 TLKKYE-----GEIRQLEEALVQARREEKEAVSARRALENELeaaQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEM 939
Cdd:pfam17380 229 TLAPYEkmerrKESFNLAEDVTTMTPEYTVRYNGQTMTENEF---LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEK 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 940 EnerwHLGKTIEKLQKemadIVEASRTSTLELQNQLDEYKEKNR------RELAEMQRQLKEKTLEAEKSRLTAMKMQDE 1013
Cdd:pfam17380 306 E----EKAREVERRRK----LEEAEKARQAEMDRQAAIYAEQERmamereRELERIRQEERKRELERIRQEEIAMEISRM 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1014 DKVSQLEMELEEERnnsdllseriSRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSriihlegsyrSSKEGL 1093
Cdd:pfam17380 378 RELERLQMERQQKN----------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE----------ARQREV 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1094 VVQMEARIAELED-RLESEERDRASLQLSNRRLERKVKELVMQVDDEhlsltDQKDQLSLRLKAMKRQVEEAEEEIDRLE 1172
Cdd:pfam17380 438 RRLEEERAREMERvRLEEQERQQQVERLRQQEEERKRKKLELEKEKR-----DRKRAEEQRRKILEKELEERKQAMIEEE 512
|
330
....*....|...
gi 1622953339 1173 SSKKKLQRELEEQ 1185
Cdd:pfam17380 513 RKRKLLEKEMEER 525
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
764-1109 |
1.39e-08 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 59.53 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 764 KGALKEEVSSHDQEMDKLKEQYDAELQALRESVEeatknvevLASRSNTSEQDQAGTEM-RVKLLQEENEKLQGRSEELE 842
Cdd:PLN02939 52 KNIAPKQRSSNSKLQSNTDENGQLENTSLRTVME--------LPQKSTSSDDDHNRASMqRDEAIAAIDNEQQTNSKDGE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 843 QrvaQLQRQIEDLKGdeakakeTLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKL 922
Cdd:PLN02939 124 Q---LSDFQLEDLVG-------MIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 923 KEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEAS---RTSTLELQNQLDEYKEKNRRELA-EMQRQLKEKTL 998
Cdd:PLN02939 194 IHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENmllKDDIQFLKAELIEVAETEERVFKlEKERSLLDASL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 999 EAEKSRLTAMKmQDEDKVSQLEMELeeernnsdllserisrsreQMEQVRN-ELLQERAARQdLECDKISLErQNKDLKS 1077
Cdd:PLN02939 274 RELESKFIVAQ-EDVSKLSPLQYDC-------------------WWEKVENlQDLLDRATNQ-VEKAALVLD-QNQDLRD 331
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622953339 1078 RIIHLEGS------YRSSKEgLVVQMEARIAELEDRLE 1109
Cdd:PLN02939 332 KVDKLEASlkeanvSKFSSY-KVELLQQKLKLLEERLQ 368
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
969-1183 |
1.41e-08 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 57.85 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 969 LELQNQ-LDEYKEKNRRELaemqrQLKEKTLEAEKSRLTAmkmQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQV 1047
Cdd:pfam09787 2 LESAKQeLADYKQKAARIL-----QSKEKLIASLKEGSGV---EGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1048 RNElLQERAARQDLECDkiSLERQNKDLKSRIIhlegSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLER 1127
Cdd:pfam09787 74 RTE-LQELEAQQQEEAE--SSREQLQELEEQLA----TERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1128 KVKELVMQVDDEHLSlTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELE 1183
Cdd:pfam09787 147 EIEKLRNQLTSKSQS-SSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLE 201
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
559-1213 |
1.54e-08 |
|
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: 59.68 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 559 LYNYL----KEGSADN-DDATK-----RKVNLVFEKIQ-----TLKSRAAGSAQGNNQASNSTSEVK-----DLLEQKSK 618
Cdd:TIGR01612 676 LYNELssivKENAIDNtEDKAKlddlkSKIDKEYDKIQnmetaTVELHLSNIENKKNELLDIIVEIKkhihgEINKDLNK 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 619 LTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENST----LQQRLEES----------EGELRKNLE 684
Cdd:TIGR01612 756 ILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIkdedAKQNYDKSkeyiktisikEDEIFKIIN 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 685 ELFQVKME-----------REQHQTEIRDLQDQLSEMHDELD---SAKRSEDREKG-----ALIEELLQAkqdlqdllIA 745
Cdd:TIGR01612 836 EMKFMKDDflnkvdkfinfENNCKEKIDSEHEQFAELTNKIKaeiSDDKLNDYEKKfndskSLINEINKS--------IE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 746 KEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRES--VEEATKNVEVLASRSNTSEQDQAGTEMR 823
Cdd:TIGR01612 908 EEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESnlIEKSYKDKFDNTLIDKINELDKAFKDAS 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 824 VKLLQEENEklqgrseeleqrvaQLQRQIEDLKGDEAKAKETLkkyegeirqleeaLVQARREEKEAVSArraLENELEA 903
Cdd:TIGR01612 988 LNDYEAKNN--------------ELIKYFNDLKANLGKNKENM-------------LYHQFDEKEKATND---IEQKIED 1037
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 904 AQRNLSRTtqeqkqlseklkeESEQKEQLRRLKNEMENErwhLGKTIEKLQKEMADIVEASRTSTLELQNQLDEY----- 978
Cdd:TIGR01612 1038 ANKNIPNI-------------EIAIHTSIYNIIDEIEKE---IGKNIELLNKEILEEAEINITNFNEIKEKLKHYnfddf 1101
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 979 -KEKNRR---ELAEMQRQLKEKTLEAEK--SRLTAMKMQDEDKVSQLEMELE--EERNNSDLLSERISRSREQMEQV--- 1047
Cdd:TIGR01612 1102 gKEENIKyadEINKIKDDIKNLDQKIDHhiKALEEIKKKSENYIDEIKAQINdlEDVADKAISNDDPEEIEKKIENIvtk 1181
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1048 ----------RNELLQERAarqDLECDKISLER-------QNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELED-RLE 1109
Cdd:TIGR01612 1182 idkkkniydeIKKLLNEIA---EIEKDKTSLEEvkginlsYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEiKEK 1258
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1110 SEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQ--LSLRLKAMKrqVEEAEEEIDRLESSKKKLQRELEEQMD 1187
Cdd:TIGR01612 1259 SPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEniSDIREKSLK--IIEDFSEESDINDIKKELQKNLLDAQK 1336
|
730 740 750
....*....|....*....|....*....|.
gi 1622953339 1188 MNEHLQGQLNSMKK-----DLSRLKKLPNKV 1213
Cdd:TIGR01612 1337 HNSDINLYLNEIANiynilKLNKIKKIIDEV 1367
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
607-1047 |
2.23e-08 |
|
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: 58.68 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEEL 686
Cdd:pfam10174 289 NKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 687 FQVKMEREQHQTEIRDLQDQLsemhdelDSAKRSedrekgalIEELLQAKQDLQDLLIAKEEQEDLLRKREREL------ 760
Cdd:pfam10174 369 QDLTEEKSTLAGEIRDLKDML-------DVKERK--------INVLQKKIENLQEQLRDKDKQLAGLKERVKSLqtdssn 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 761 --TALkGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRS 838
Cdd:pfam10174 434 tdTAL-TTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSG 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEdlkgdeaKAKETLKKYEGEIRQLEEALVQARREEkEAVSARRALENELEAAQRNLSRTTQEQKQL 918
Cdd:pfam10174 513 LKKDSKLKSLEIAVE-------QKKEECSKLENQLKKAHNAEEAVRTNP-EINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 919 SEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNqlDEYKEKNRRELAEMQRQLKEKTL 998
Cdd:pfam10174 585 LGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLE--EARRREDNLADNSQQLQLEELMG 662
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 999 EAEKSR--LTAMKMqdedKVSQLEMELEE-ERNNSDLLSERisrsREQMEQV 1047
Cdd:pfam10174 663 ALEKTRqeLDATKA----RLSSTQQSLAEkDGHLTNLRAER----RKQLEEI 706
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
821-981 |
2.32e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 821 EMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSAR--RALE 898
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 899 NELEAAQRnlsrttqEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEY 978
Cdd:COG1579 96 KEIESLKR-------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
...
gi 1622953339 979 KEK 981
Cdd:COG1579 169 AAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
602-865 |
2.64e-08 |
|
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: 57.98 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 602 ASNSTSEVKD-LLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELR 680
Cdd:pfam07888 109 SSEELSEEKDaLLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 681 KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEdrekgALIEELLQAKQDLQDLLIAKEEQEDLLRKREREL 760
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE-----AENEALLEELRSLQERLNASERKVEGLGEELSSM 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 761 TALKG-------------------------ALKEEVSSHDQE---------MDKLK-EQYDAELQALRESVEEATKNVEV 805
Cdd:pfam07888 264 AAQRDrtqaelhqarlqaaqltlqladaslALREGRARWAQEretlqqsaeADKDRiEKLSAELQRLEERLQEERMEREK 343
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 806 L---------ASRSNTSEQDQAGTEMR--VKLLQEENEKLQGRSEELEQRVAQLQRQIE---DLKGDEAKAKET 865
Cdd:pfam07888 344 LevelgrekdCNRVQLSESRRELQELKasLRVAQKEKEQLQAEKQELLEYIRQLEQRLEtvaDAKWSEAALTST 417
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
609-1155 |
2.71e-08 |
|
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: 58.29 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 609 VKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLE---ESEGELRKNLEE 685
Cdd:pfam10174 249 IRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLEtltNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 686 LFQVKMEREQH----QTEIRDLQDQLSEMHDELDSAKRSEDR---EKGALIEELlqakQDLQDLLIAKEEQEDLLRKRER 758
Cdd:pfam10174 329 LKESLTAKEQRaailQTEVDALRLRLEEKESFLNKKTKQLQDlteEKSTLAGEI----RDLKDMLDVKERKINVLQKKIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 759 EltalkgaLKEEVSSHDQEMDKLKEQydaelqalresveeatknveVLASRSNTSEQDQAGTEMRVKLLQEEN--EKLQG 836
Cdd:pfam10174 405 N-------LQEQLRDKDKQLAGLKER--------------------VKSLQTDSSNTDTALTTLEEALSEKERiiERLKE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 837 RSEELEQrvaQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQK 916
Cdd:pfam10174 458 QREREDR---ERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECS 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 917 QLSEKLKEESEQKEQLRrlKNEMENERwhlgktIEKLQKEMADIVEASRTSTLELQNQLDEYKEknrrelAEMQRQLKEK 996
Cdd:pfam10174 535 KLENQLKKAHNAEEAVR--TNPEINDR------IRLLEQEVARYKEESGKAQAEVERLLGILRE------VENEKNDKDK 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 997 TL-EAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQE-----RAARQDLECDKISLER 1070
Cdd:pfam10174 601 KIaELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEElmgalEKTRQELDATKARLSS 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1071 QNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRlERKVKELVMQVDDEHLSLTDQ-KDQ 1149
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAAISEKDANIALLELSSSK-KKKTQEEVMALKREKDRLVHQlKQQ 759
|
....*.
gi 1622953339 1150 LSLRLK 1155
Cdd:pfam10174 760 TQNRMK 765
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
608-1207 |
2.84e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEE------NSTLQQRLEESEGELRK 681
Cdd:pfam02463 343 ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkseeekEAQLLLELARQLEDLLK 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 682 NLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQD-------LLIAKEEQEDLLR 754
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLqeqlellLSRQKLEERSQKE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KRERELTALKGALKE--EVSSHDQEMDKLKEQYDAE------------LQALRESVEEATKNVEVLASRSNTSEQDQAGT 820
Cdd:pfam02463 503 SKARSGLKVLLALIKdgVGGRIISAHGRLGDLGVAVenykvaistaviVEVSATADEVEERQKLVRALTELPLGARKLRL 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 821 EMRVKLLQ-------EENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSA 893
Cdd:pfam02463 583 LIPKLKLPlksiavlEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 894 RRALENELEAAQRNLSRTTQE-QKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQ 972
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEkAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 973 NQLDEYKE-------KNRRELAEM-QRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQM 1044
Cdd:pfam02463 743 QKIDEEEEeeeksrlKKEEKEEEKsELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1045 EQVRNELLQERAARQDLECDKISLERQNKDlksriihLEGSYRSSKEGLVVQMEARiaELEDRLESEERDRASLQLSNRR 1124
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEEQKLEKLA-------EEELERLEEEITKEELLQE--LLLKEEELEEQKLKDELESKEE 893
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1125 LERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLS 1204
Cdd:pfam02463 894 KEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
...
gi 1622953339 1205 RLK 1207
Cdd:pfam02463 974 KVN 976
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
814-983 |
2.86e-08 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 58.11 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 814 EQDQAGTEMRVKLLQEENEKLQ-GRSEELEQrvaqLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARRE----EK 888
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQqQREEELEE----LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQneelEK 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 889 EAVSARRALEnELEAAQRNLSRTTQEQKQLSEKLKEESEQKE-----------QLRRLKNEMENERWHLGKTIEKLQKEM 957
Cdd:pfam05667 385 QYKVKKKTLD-LLPDAEENIAKLQALVDASAQRLVELAGQWEkhrvplieeyrALKEAKSNKEDESQRKLEEIKELREKI 463
|
170 180
....*....|....*....|....*.
gi 1622953339 958 ADIVEASRTSTLELQNQLDEYKEKNR 983
Cdd:pfam05667 464 KEVAEEAKQKEELYKQLVAEYERLPK 489
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
675-1228 |
4.13e-08 |
|
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: 58.13 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 675 SEG-ELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHD-ELDSAKRSEDREKGALIEELLQAKQDL----QDLLIAKEE 748
Cdd:TIGR00606 166 SEGkALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEhQMELKYLKQYKEKACEIRDQITSKEAQlessREIVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 749 QEDLLRKRERELTALKGALKE------EVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEqdqagtEM 822
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSKIMKldneikALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREK------ER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 823 RVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEAL--------------------VQ 882
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLeldgfergpfserqiknfhtLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 883 ARREEKEAVSARR---ALENELEAAQRNLSRTTQEQKQLSEKLKEESE----QKEQLRRLKNEMENERWHLGKTIEK--- 952
Cdd:TIGR00606 400 IERQEDEAKTAAQlcaDLQSKERLKQEQADEIRDEKKGLGRTIELKKEilekKQEELKFVIKELQQLEGSSDRILELdqe 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 953 LQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKT--LEAEKSRLTAMKMQDEDKVSQLEMELEEERNNS 1030
Cdd:TIGR00606 480 LRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMeqLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHS 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1031 DLLSERI------SRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLV-----VQMEA 1099
Cdd:TIGR00606 560 DELTSLLgyfpnkKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFdvcgsQDEES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1100 RIAELEDRLESEERDRASL------------QLSNR------------RLERKVKELVMQVDDEHLSLTDQKDQLSLRLK 1155
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLagatavysqfitQLTDEnqsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELK 719
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 1156 AMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKKLPNKVLDDMDDDDDLSTDGG 1228
Cdd:TIGR00606 720 KKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT 792
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
816-956 |
5.06e-08 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 57.17 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 816 DQAGTEMRVKLLQEENEKL-------QGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEK 888
Cdd:COG2433 379 EEALEELIEKELPEEEPEAerekeheERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 889 EAVSARR---ALENELEAAQRNLSRTTQEQKQLSEKLkeeseqkEQLRRLKnEMENERWHLG-KTIEKLQKE 956
Cdd:COG2433 459 REIRKDReisRLDREIERLERELEEERERIEELKRKL-------ERLKELW-KLEHSGELVPvKVVEKFTKE 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
566-784 |
6.13e-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: 56.31 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 566 GSADNDDATKRKVNLVFEKIQTLKSRAAgsaQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERE 645
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA---ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 646 RMRANLEELRSQHNK------KVEENSTLQQRLE-ESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAK 718
Cdd:COG4942 94 ELRAELEAQKEELAEllralyRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 719 rsedREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQ 784
Cdd:COG4942 174 ----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
740-970 |
6.58e-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: 56.31 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 740 QDLLIAKEEQEDLLRKRERELTALKGALKEEvsshdqemdklKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAG 819
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKE-----------EKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 820 TEMRVKLLQEEnekLQGRSEELEQRVAQLQRQIED------LKGDEAKAKETLKKYEG-----------EIRQLEEALVQ 882
Cdd:COG4942 88 LEKEIAELRAE---LEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKylaparreqaeELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 883 ARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKL-KEESEQKEQLRRLKNEMENerwhLGKTIEKLQKEMADIV 961
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEE----LEALIARLEAEAAAAA 240
|
....*....
gi 1622953339 962 EASRTSTLE 970
Cdd:COG4942 241 ERTPAAGFA 249
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
608-1136 |
6.68e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 57.27 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLqlevknqqnikEERERMRANLEELRSQHNKKV-------EENSTLQQRLEESEGELR 680
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRL-----------RQQQNAERLLEEFCQRIGQQLdaaeeleELLAELEAQLEELEEQAA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 681 KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRsedrekgaLIEELLQAKQDLQDLLIAKEEQEDLLRKRERE- 759
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALER--------LREQSGEALADSQEVTAAMQQLLEREREATVEr 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 760 --LTALKGALKEEVS-------SHDQEMDKLKEQYDAELqaLRE-----SVEEA-------------------TKNVEVL 806
Cdd:COG3096 647 deLAARKQALESQIErlsqpggAEDPRLLALAERLGGVL--LSEiyddvTLEDApyfsalygparhaivvpdlSAVKEQL 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 807 ASRSNT-------------------------------SEQDQ--------------AGTEMRVKLLQEENEKLQGRSEEL 841
Cdd:COG3096 725 AGLEDCpedlyliegdpdsfddsvfdaeeledavvvkLSDRQwrysrfpevplfgrAAREKRLEELRAERDELAEQYAKA 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 842 EQRVAQLQR---QIEDLKGD------EAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTT 912
Cdd:COG3096 805 SFDVQKLQRlhqAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN 884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 913 Q-EQKQLSEKLKEESEQKEQLRRLKNEMeneRWHlGKTIEKLQkEMADIVEASRTSTLELQNQLDEYKEKnrrelaemQR 991
Cdd:COG3096 885 LlADETLADRLEELREELDAAQEAQAFI---QQH-GKALAQLE-PLVAVLQSDPEQFEQLQADYLQAKEQ--------QR 951
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 992 QLKEKT--LEAEKSRLTAMKMQDEdkvsqlEMELEEERNNSDLLSERI-------SRSREQMEQVRNELLQERAARQDLE 1062
Cdd:COG3096 952 RLKQQIfaLSEVVQRRPHFSYEDA------VGLLGENSDLNEKLRARLeqaeearREAREQLRQAQAQYSQYNQVLASLK 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1063 CDKISLERQNKDLKSRIIHLE-----------GSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKE 1131
Cdd:COG3096 1026 SSRDAKQQTLQELEQELEELGvqadaeaeeraRIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQ 1105
|
....*
gi 1622953339 1132 LVMQV 1136
Cdd:COG3096 1106 EREQV 1110
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
672-1227 |
7.25e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 672 LEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLsemhDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEE--- 748
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI----ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNElss 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 749 QEDLLRKRERELTALKGALK---EEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASR----SNTSEQDQAGTE 821
Cdd:PRK01156 247 LEDMKNRYESEIKTAESDLSmelEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKkqilSNIDAEINKYHA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 822 MRVKLlqEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEE--------------ALVQARREE 887
Cdd:PRK01156 327 IIKKL--SVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEyskniermsafiseILKIQEIDP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 888 KEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQL------------------RRLKNEMENERWHLGKT 949
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeeksNHIINHYNEKKSRLEEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 950 IEKLQKEMADIVEASRtstlELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKsrltamkmqDEDKVSQLEmelEEERNN 1029
Cdd:PRK01156 485 IREIEIEVKDIDEKIV----DLKKRKEYLESEEINKSINEYNKIESARADLED---------IKIKINELK---DKHDKY 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1030 SDLLSERISRSREQMEQVRNELLQERAARQDLECDKI-----SLERQNKDLKSRIIHLEGSYRSSKEglvvQMEARIAEL 1104
Cdd:PRK01156 549 EEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNrsrsnEIKKQLNDLESRLQEIEIGFPDDKS----YIDKSIREI 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1105 EDRLESEERDRASLQLSNRRLER---KVKELVMQVdDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRE 1181
Cdd:PRK01156 625 ENEANNLNNKYNEIQENKILIEKlrgKIDNYKKQI-AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLEST 703
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1622953339 1182 LEEQMDMNEHLQGQLNSMKKDLSRLKKLPNKVLDDMDDDDDLSTDG 1227
Cdd:PRK01156 704 IEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSG 749
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
664-1062 |
9.06e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.88 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 664 ENSTLQQRLEESEGELRKNLEELFQVKMEREQhqteiRDLQDQL-SEMHDELDSAKRSEDREKGALIEELLQAKQDLQDL 742
Cdd:COG3096 223 ENSGVRKAFQDMEAALRENRMTLEAIRVTQSD-----RDLFKHLiTEATNYVAADYMRHANERRELSERALELRRELFGA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 743 LIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLK------------EQYDAELQALRESVEEAtknvevlasrs 810
Cdd:COG3096 298 RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNlvqtalrqqekiERYQEDLEELTERLEEQ----------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 811 ntseqdqagtEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKgdeaKAKETLKKYEGEIRQLEEALVQARREEKEA 890
Cdd:COG3096 367 ----------EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQ----QALDVQQTRAIQYQQAVQALEKARALCGLP 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 891 VSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQ-------LRRLKNEMENERWHlGKTIEKLQKEMADIVEA 963
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQfekayelVCKIAGEVERSQAW-QTARELLRRYRSQQALA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 964 SRTSTLELQnqldeYKEKNRRElaemQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERnnsDLLSERISRSREQ 1043
Cdd:COG3096 512 QRLQQLRAQ-----LAELEQRL----RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQL---EELEEQAAEAVEQ 579
|
410
....*....|....*....
gi 1622953339 1044 MEQVRNELLQERAARQDLE 1062
Cdd:COG3096 580 RSELRQQLEQLRARIKELA 598
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
738-1186 |
9.72e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 56.24 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 738 DLQDLLIAKEEqedlLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDaELQALRESVEEATKNVEVLASRsntseqdq 817
Cdd:pfam05622 1 DLSEAQEEKDE----LAQRCHELDQQVSLLQEEKNSLQQENKKLQERLD-QLESGDDSGTPGGKKYLLLQKQ-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 818 agtemrVKLLQEENEKLQG-------RSEELEQRVAQLQRQIEDLKG--DEAKA-----------KETLKKYEGEI---- 873
Cdd:pfam05622 68 ------LEQLQEENFRLETarddyriKCEELEKEVLELQHRNEELTSlaEEAQAlkdemdilresSDKVKKLEATVetyk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 874 RQLEEaLVQARR-----EEKEAVSARRALENELEAAQRNLSRTTQE--QKQLSE---KLKEES--------------EQK 929
Cdd:pfam05622 142 KKLED-LGDLRRqvkllEERNAEYMQRTLQLEEELKKANALRGQLEtyKRQVQElhgKLSEESkkadklefeykkleEKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 930 EQLRRLKNEMENERWHLGKTIEKL-----------QKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEmQRQLKEKTL 998
Cdd:pfam05622 221 EALQKEKERLIIERDTLRETNEELrcaqlqqaelsQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHE-NKMLRLGQE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 999 EAEKSRLTAMKMQDEDKVSQLEmELEEErnnSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLksr 1078
Cdd:pfam05622 300 GSYRERLTELQQLLEDANRRKN-ELETQ---NRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKL--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1079 iiHLEGSYRSSKEGLV--------VQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEhlsltdQKDQL 1150
Cdd:pfam05622 373 --HEAQSELQKKKEQIeelepkqdSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPK------QNPAS 444
|
490 500 510
....*....|....*....|....*....|....*...
gi 1622953339 1151 SLRLKAMKRQVEEAEEEIDRLESSKK--KLQRELEEQM 1186
Cdd:pfam05622 445 PPEIQALKNQLLEKDKKIEHLERDFEksKLQREQEEKL 482
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
618-1027 |
1.13e-07 |
|
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: 56.12 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 618 KLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQ 697
Cdd:COG5185 209 ESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 698 TEIRDLQDQLSEMHDELDSAKRSEDrekgalIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQE 777
Cdd:COG5185 289 KQFENTKEKIAEYTKSIDIKKATES------LEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 778 MDKLKEQYDAELqaLRESVEEATKNVEVLASRSNTSEQDQAGTEmrvkllQEENEKLQGRSEELEQRVAQLQRQIEdlkg 857
Cdd:COG5185 363 IENIVGEVELSK--SSEELDSFKDTIESTKESLDEIPQNQRGYA------QEILATLEDTLKAADRQIEELQRQIE---- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 858 deaKAKETLKKYEGEIRQLEEALVQARREEKEAVSARraleneLEAAQRNLSRTTQEQKqlsEKLKEESEQ-KEQLRRLK 936
Cdd:COG5185 431 ---QATSSNEEVSKLLNELISELNKVMREADEESQSR------LEEAYDEINRSVRSKK---EDLNEELTQiESRVSTLK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 937 NEMENERWHLGKTIEKLQKEMaDIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKV 1016
Cdd:COG5185 499 ATLEKLRAKLERQLEGVRSKL-DQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYL 577
|
410
....*....|.
gi 1622953339 1017 SQLEMELEEER 1027
Cdd:COG5185 578 STIESQQARED 588
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
583-808 |
1.17e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 583 EKIQTLKSRAAGSAQgnnqasnstsEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEER-----ERMRANLEELRSQ 657
Cdd:COG4913 610 AKLAALEAELAELEE----------ELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 658 HNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAkq 737
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA-- 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 738 dlqdlLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLAS 808
Cdd:COG4913 758 -----ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDR 823
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
608-884 |
1.19e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQlqlEVKNQQNIKEERERMRAnLEELRSQHNkkVEENSTLQQRLEEsegeLRKNLEELF 687
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQ---EQQQRSQLEQAKEGLSA-LNRLLPRLN--LLADETLADRVEE----IREQLDEAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQ-------------DQLSEMHDELDSAKRSEDREKGALiEELLQ-----AKQDLQDLLIAKEEQ 749
Cdd:PRK04863 908 EAKRFVQQHGNALAQLEpivsvlqsdpeqfEQLKQDYQQAQQTQRDAKQQAFAL-TEVVQrrahfSYEDAAEMLAKNSDL 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 750 EDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQY---DAELQALRESVEEATKNVEVLASRSNtseqdqAGTEMRVKL 826
Cdd:PRK04863 987 NEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLaslKSSYDAKRQMLQELKQELQDLGVPAD------SGAEERARA 1060
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 827 LQEEnekLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQAR 884
Cdd:PRK04863 1061 RRDE---LHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAK 1115
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
689-845 |
1.36e-07 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 56.24 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 689 VKMEREQHQTEIRDLQDQLSEMHDELDSAKRSED---REKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKG 765
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDeasFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 ALKEEVSSHDQEMDKLKEQYDAELQALRESVEEAtkNV-EVLASRsntseqdqagTEMRV-KLLQEENEKLQGRSEELEQ 843
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREEVTEE--DIaEVVSRW----------TGIPVgKLLEGEREKLLNLEEELHE 549
|
..
gi 1622953339 844 RV 845
Cdd:COG0542 550 RV 551
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
692-921 |
1.40e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 692 EREQHQTEIRDLQDQLSEMHDELDSAkrseDREKGALIEELLQAKQDLQDLliaKEEQEDLlrkrERELTALKgalkeev 771
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNELQAELEAL---QAEIDKL----QAEIAEAE------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 772 sshdQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRV-KLLQEENEKLQGRSEELEQRVAQLQR 850
Cdd:COG3883 79 ----AEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIaDADADLLEELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 851 QIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEK 921
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
600-939 |
1.41e-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: 55.63 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 600 NQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQqnikeerermranLEELRSQHNKKVEENSTL-----QQRLEE 674
Cdd:pfam06160 175 LEAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQ-------------LEELKEGYREMEEEGYALehlnvDKEIQQ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 675 SEGELRKNLEELFQVKMEREQhqTEIRDLQDQLSEMHDeldsakrsedrekgaLIEELLQAKQDLQDLLIAKEEQEDLLR 754
Cdd:pfam06160 242 LEEQLEENLALLENLELDEAE--EALEEIEERIDQLYD---------------LLEKEVDAKKYVEKNLPEIEDYLEHAE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KRERELTALKGALKEEVSSHDQEMDKLKeQYDAELQALRESVEEATKNVEvlasrsntsEQDQAGTEmrvklLQEENEKL 834
Cdd:pfam06160 305 EQNKELKEELERVQQSYTLNENELERVR-GLEKQLEELEKRYDEIVERLE---------EKEVAYSE-----LQEELEEI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 835 QGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEealvqaRREEK--------EAVSARRALENELEAAQR 906
Cdd:pfam06160 370 LEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIK------RLVEKsnlpglpeSYLDYFFDVSDEIEDLAD 443
|
330 340 350
....*....|....*....|....*....|...
gi 1622953339 907 NLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEM 939
Cdd:pfam06160 444 ELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
768-1193 |
1.80e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.75 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 KEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSeELEQRVAQ 847
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL-KKQQLLKQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 848 LQRQIEDLKGDEAKAKETLKK---------YEGEIRQLEEALVQARREEKEAVSARRALENELEAAQrNLSRTTQEQKQL 918
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERinrarkaapLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA-AHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 919 SEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQ--KEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQ---- 992
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFrdlq 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 993 ----LKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERIsrsrEQMEQVRNELLQERAARQDLECDKISL 1068
Cdd:TIGR00618 424 gqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE----QQLQTKEQIHLQETRKKAVVLARLLEL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1069 ERQNKDLKSRIIHLEGSYRSS--KEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERkVKELVMQVDDEHLSLTDQ 1146
Cdd:TIGR00618 500 QEEPCPLCGSCIHPNPARQDIdnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS-LKEQMQEIQQSFSILTQC 578
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1147 KDQLSLRLKAMKRQVEEAEEEID---RLESSKKKLQRELEEQMDMNEHLQ 1193
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEklsEAEDMLACEQHALLRKLQPEQDLQ 628
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
729-1209 |
1.90e-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: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 729 IEELLQAKQDLQDLLIakeeQEDLLRKRERELTalkGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLAS 808
Cdd:pfam06160 12 IDELEERKNELMNLPV----QEELSKVKKLNLT---GETQEKFEEWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 809 RsntseqdqagtemrvKLLQEENEKLQgrseELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEK 888
Cdd:pfam06160 85 K---------------KALDEIEELLD----DIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 889 EAVSArraLENELEAAQRNLSRTtqeqkqlsEKLKEES---EQKEQLRRLKNEMEnerwhlgktieKLQKEMADIVEASR 965
Cdd:pfam06160 146 PAIDE---LEKQLAEIEEEFSQF--------EELTESGdylEAREVLEKLEEETD-----------ALEELMEDIPPLYE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 966 TSTLELQNQLDEYKEkNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSdlLSERISRSREQME 1045
Cdd:pfam06160 204 ELKTELPDQLEELKE-GYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEALEE--IEERIDQLYDLLE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1046 QvrnellqERAARQDLE--CDKIS-----LERQNKDLKSRIIHLEGSYRSSKEGLVVQM--EARIAELEDRLESEERDRA 1116
Cdd:pfam06160 281 K-------EVDAKKYVEknLPEIEdylehAEEQNKELKEELERVQQSYTLNENELERVRglEKQLEELEKRYDEIVERLE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1117 SLQLSNRRLERKVKELVMQVDDehlsLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQ----------- 1185
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEE----IEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKSnlpglpesyld 429
|
490 500
....*....|....*....|....*....
gi 1622953339 1186 -----MDMNEHLQGQLNSMKKDLSRLKKL 1209
Cdd:pfam06160 430 yffdvSDEIEDLADELNEVPLNMDEVNRL 458
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
812-1007 |
2.13e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 812 TSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAV 891
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 892 SA--------------------------RRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWH 945
Cdd:COG3883 93 RAlyrsggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 946 LGKTIEKLQKEMADIVEASRtstlELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTA 1007
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEA----AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
840-1207 |
2.80e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.84 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 840 ELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREekeaVSARR--------ALENELEAAQRNLSRT 911
Cdd:PRK04778 109 EIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKS----LLANRfsfgpaldELEKQLENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 912 tqeqkqlsEKLKEE---SEQKEQLRRLKNEMENerwhlgktiekLQKEMADIVEASRTSTLELQNQLDEYKEKNRrelaE 988
Cdd:PRK04778 185 --------VELTESgdyVEAREILDQLEEELAA-----------LEQIMEEIPELLKELQTELPDQLQELKAGYR----E 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 989 MQRQ---LKEKTLEaekSRLTAMKMQDEDKVSQL-EMELEEERNNSDLLSERISRSREQMEQvrnellqERAARQDLE-- 1062
Cdd:PRK04778 242 LVEEgyhLDHLDIE---KEIQDLKEQIDENLALLeELDLDEAEEKNEEIQERIDQLYDILER-------EVKARKYVEkn 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1063 CDKIS-----LERQNKDLKSRIIHLEGSYR-SSKEGLVV-QMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQ 1135
Cdd:PRK04778 312 SDTLPdflehAKEQNKELKEEIDRVKQSYTlNESELESVrQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQ 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1136 VDDehlsLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELE---------EQMDMNEHLQGQLNSMKKDLSRL 1206
Cdd:PRK04778 392 LEE----IEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEksnlpglpeDYLEMFFEVSDEIEALAEELEEK 467
|
.
gi 1622953339 1207 K 1207
Cdd:PRK04778 468 P 468
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
582-939 |
3.24e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 582 FEKIQTLKSraagsaQGN-NQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQqnikeerermranLEELRSQHNK 660
Cdd:PRK04778 181 FSQFVELTE------SGDyVEAREILDQLEEELAALEQIMEEIPELLKELQTELPDQ-------------LQELKAGYRE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 661 KVEEN-----STLQQRLEESEGELRKNLEELFQVKMEREQhqTEIRDLQDQLSEMHDELD---SAKRSEDREKGALIEEL 732
Cdd:PRK04778 242 LVEEGyhldhLDIEKEIQDLKEQIDENLALLEELDLDEAE--EKNEEIQERIDQLYDILErevKARKYVEKNSDTLPDFL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 733 LQAKQDLQDLliakeeQEDLLRKRER-ELTalkgalkeevsshDQEMDKLKeQYDAELQALRESVEEATKNVEvlasrsn 811
Cdd:PRK04778 320 EHAKEQNKEL------KEEIDRVKQSyTLN-------------ESELESVR-QLEKQLESLEKQYDEITERIA------- 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 812 tsEQDQAGTEmrvklLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLeealvqARREEK--- 888
Cdd:PRK04778 373 --EQEIAYSE-----LQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEI------KRYLEKsnl 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 889 -----EAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEM 939
Cdd:PRK04778 440 pglpeDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEEL 495
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
747-903 |
3.48e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 747 EEQEDLLR-----KRERELTALKGALKEEVSSHDQEMDKLKEQYDA---ELQALRESVEEATKNVEVLASR--SNTSEQD 816
Cdd:COG1579 4 EDLRALLDlqeldSELDRLEHRLKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARikKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 817 QAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEI----RQLEEALVQARREEKEAVS 892
Cdd:COG1579 84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELeekkAELDEELAELEAELEELEA 163
|
170
....*....|.
gi 1622953339 893 ARRALENELEA 903
Cdd:COG1579 164 EREELAAKIPP 174
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
618-997 |
3.56e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 618 KLTTEVAELQRQLQLevknqqnIKEERERMRANLEELRSQHnkkvEENSTLQQRLEESEGELRKNLEElfqvkmEREQHQ 697
Cdd:PRK04778 102 KAKHEINEIESLLDL-------IEEDIEQILEELQELLESE----EKNREEVEQLKDLYRELRKSLLA------NRFSFG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 698 TEIRDLQDQLSEMHDELDSAKR---SEDREKGAliEELLQAKQDLQDLLIAKEEQEDLLRKRERELTA----LKGALKEE 770
Cdd:PRK04778 165 PALDELEKQLENLEEEFSQFVElteSGDYVEAR--EILDQLEEELAALEQIMEEIPELLKELQTELPDqlqeLKAGYREL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 771 VSSH--------DQEMDKLKEQYDAELQALRE-SVEEATKNVEVLASRSNTSeQDQAGTEMRVK-LLQEENEKLQGRSEE 840
Cdd:PRK04778 243 VEEGyhldhldiEKEIQDLKEQIDENLALLEElDLDEAEEKNEEIQERIDQL-YDILEREVKARkYVEKNSDTLPDFLEH 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 841 LEQRVAQLQRQIEDLKGD---EAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQ 917
Cdd:PRK04778 322 AKEQNKELKEEIDRVKQSytlNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEK 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 918 LSEKL----KEESEQKEQLRRLKNEMENERWHLGKT-IEKLQKEMADIVEASRTSTLELQNQLDEYK---EKNRRELAEM 989
Cdd:PRK04778 402 LSEMLqglrKDELEAREKLERYRNKLHEIKRYLEKSnLPGLPEDYLEMFFEVSDEIEALAEELEEKPinmEAVNRLLEEA 481
|
410
....*....|.
gi 1622953339 990 Q---RQLKEKT 997
Cdd:PRK04778 482 TedvETLEEET 492
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
600-1136 |
4.24e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 600 NQASNSTSEVKDLLEQkskLTTEVAELQRQLQLEVKNQQnikEERERMRANLEELRSQHN---KKVEENSTLQ---QRLE 673
Cdd:PRK04863 543 CKRLGKNLDDEDELEQ---LQEELEARLESLSESVSEAR---ERRMALRQQLEQLQARIQrlaARAPAWLAAQdalARLR 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 674 ESEGEL---RKNLEELFQVKMEREQHQTEIRDL----QDQLSEMHDELDSAKRSEDrekgaliEELLQAKQDLQDLLIAk 746
Cdd:PRK04863 617 EQSGEEfedSQDVTEYMQQLLERERELTVERDElaarKQALDEEIERLSQPGGSED-------PRLNALAERFGGVLLS- 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 747 EEQEDLLRKRERELTALKGALKEE--VSSHDQEMDKLKEQYD---------AELQALRESVEEATKNVEVLASRSNTSEQ 815
Cdd:PRK04863 689 EIYDDVSLEDAPYFSALYGPARHAivVPDLSDAAEQLAGLEDcpedlylieGDPDSFDDSVFSVEELEKAVVVKIADRQW 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 816 -----------DQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGD---------EAKAKETLKKYEGEIRQ 875
Cdd:PRK04863 769 rysrfpevplfGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFigshlavafEADPEAELRQLNRRRVE 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 876 LEEALVQARREEKEAVSARRALENELEAAQRNLSRT--------TQEQKQLSEKLKEESEQKEQLRRlknemenerwhLG 947
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLnlladetlADRVEEIREQLDEAEEAKRFVQQ-----------HG 917
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 948 KTIEKLQKEMADIVEAsrtstlelQNQLDEYKEkNRRELAEMQRQLKEKT--LEAEKSRLTAMKMQDEDKVsqlemeLEE 1025
Cdd:PRK04863 918 NALAQLEPIVSVLQSD--------PEQFEQLKQ-DYQQAQQTQRDAKQQAfaLTEVVQRRAHFSYEDAAEM------LAK 982
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1026 ERNNSDLLSERI-------SRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRI--------IHLEGSYRSSK 1090
Cdd:PRK04863 983 NSDLNEKLRQRLeqaeqerTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELqdlgvpadSGAEERARARR 1062
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1622953339 1091 EGLVVQMEA---RIAELEDRLESEERDRASLQLSNRRLERKVKELVMQV 1136
Cdd:PRK04863 1063 DELHARLSAnrsRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
618-883 |
4.91e-07 |
|
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: 54.57 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 618 KLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRS-QHNKKVEENSTLQQRLEesegELRKNLEELFQVKMEREQH 696
Cdd:COG3096 840 ALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKlLPQANLLADETLADRLE----ELREELDAAQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 697 QTEIRDLQDQLS------EMHDEL-------DSAKRSEDREKGALIE--------------ELLQAKQDLQDLLIAKEEQ 749
Cdd:COG3096 916 GKALAQLEPLVAvlqsdpEQFEQLqadylqaKEQQRRLKQQIFALSEvvqrrphfsyedavGLLGENSDLNEKLRARLEQ 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 750 EDLLRKREREltALKGAlKEEVSSHDQEMDKLKEQYDAELQALRESVEEaTKNVEVlasrsntseQDQAGTEMRVKllqE 829
Cdd:COG3096 996 AEEARREARE--QLRQA-QAQYSQYNQVLASLKSSRDAKQQTLQELEQE-LEELGV---------QADAEAEERAR---I 1059
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 830 ENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQA 883
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
970-1185 |
5.39e-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: 53.23 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 970 ELQNQLDEYKEKNRRELAEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRN 1049
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1050 ELLQERAARQDL----------ECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQ 1119
Cdd:COG4942 98 ELEAQKEELAELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1120 LSNRRLERKVKELVMQVDDEhlslTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQ 1185
Cdd:COG4942 178 ALLAELEEERAALEALKAER----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
876-1205 |
5.47e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.14 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 876 LEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQK 955
Cdd:PLN02939 10 LSHGCGPIRSRAPFYLPSRRRLAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 956 EMAD-------IVEASRTSTLELQNQLDEYKEKNR------RELAEMQRQLKEKTLEAEKSRLTAMKMQD---------E 1013
Cdd:PLN02939 90 STSSdddhnraSMQRDEAIAAIDNEQQTNSKDGEQlsdfqlEDLVGMIQNAEKNILLLNQARLQALEDLEkiltekealQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1014 DKVSQLEMELEEERNNSDLLSE---RISRSREQMEQVRNELLQERAARQDLEcdkISLERQNKDLKSRIIHLEGSYRSSK 1090
Cdd:PLN02939 170 GKINILEMRLSETDARIKLAAQekiHVEILEEQLEKLRNELLIRGATEGLCV---HSLSKELDVLKEENMLLKDDIQFLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1091 EGLVvqmeaRIAELEDRLESEERDRASLQLSNRRLERKVkeLVMQVDDEHLS------LTDQKDQLSLRLKAMKRQVEEA 1164
Cdd:PLN02939 247 AELI-----EVAETEERVFKLEKERSLLDASLRELESKF--IVAQEDVSKLSplqydcWWEKVENLQDLLDRATNQVEKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 1165 ----------EEEIDRLESSKK--KLQRELEEQMDMnehLQGQLNSMKKDLSR 1205
Cdd:PLN02939 320 alvldqnqdlRDKVDKLEASLKeaNVSKFSSYKVEL---LQQKLKLLEERLQA 369
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
610-1019 |
5.67e-07 |
|
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: 54.19 E-value: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 610 KDLLEQKSKLTTE---VAELQRQLQLEVKNQQNIKEERERMRANLEELRS--QHNKKVEenstlqqRLEESEGELRKNLE 684
Cdd:COG3096 292 RELFGARRQLAEEqyrLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEKIE-------RYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 685 ELFQVKMEREQHQTEirdLQDQLSEMHDELDSAKRS-EDREKGalIEEL----LQAKQDLQdlliAKEEQEDLLRKRERE 759
Cdd:COG3096 365 EQEEVVEEAAEQLAE---AEARLEAAEEEVDSLKSQlADYQQA--LDVQqtraIQYQQAVQ----ALEKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 760 LTALKG---ALKEEVSSHDQEMDKLKEQYDAElQALRESVEEATKNVEVLASRSNTSEQDQAGTEmrvkLLQeeneklQG 836
Cdd:COG3096 436 PENAEDylaAFRAKEQQATEEVLELEQKLSVA-DAARRQFEKAYELVCKIAGEVERSQAWQTARE----LLR------RY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 837 RSEE-LEQRVAQLQRQIEDLKGDEAKAKETlkkyegeIRQLEEALVQARREekeaVSARRALENELEAAQrnlsrttQEQ 915
Cdd:COG3096 505 RSQQaLAQRLQQLRAQLAELEQRLRQQQNA-------ERLLEEFCQRIGQQ----LDAAEELEELLAELE-------AQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 916 KQLSEKLKEESEQKEQLRRlknemenERWHLGKTIEKLQKEmADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQL-K 994
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQ-------QLEQLRARIKELAAR-APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLeR 638
|
410 420
....*....|....*....|....*
gi 1622953339 995 EKTLEAEKSRLTAMKMQDEDKVSQL 1019
Cdd:COG3096 639 EREATVERDELAARKQALESQIERL 663
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
828-1174 |
7.65e-07 |
|
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: 53.59 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 828 QEENEKLQgrSEELEQRVAQLQRQIEDLKgdeaKAKETLKKYEGEIRQleEALVQARrEEKEAVSARRALEN-ELEAAQR 906
Cdd:pfam17380 290 QEKFEKME--QERLRQEKEEKAREVERRR----KLEEAEKARQAEMDR--QAAIYAE-QERMAMERERELERiRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 907 NLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKnrrel 986
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR----- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 987 aEMQRQLKEKTLEAEKSRLTAMKMQDEdkVSQLEMElEEERNNSDLLSERISRSREQMEQVRNELlqeraarqdlecdki 1066
Cdd:pfam17380 436 -EVRRLEEERAREMERVRLEEQERQQQ--VERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKI--------------- 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1067 sLERQNKDLKSRIIHlEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRrleRKVKELVMQVDDEHLSLTDQ 1146
Cdd:pfam17380 497 -LEKELEERKQAMIE-EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEER---RRIQEQMRKATEERSRLEAM 571
|
330 340
....*....|....*....|....*...
gi 1622953339 1147 KdqlslRLKAMKRQVEEAEEEIDRLESS 1174
Cdd:pfam17380 572 E-----REREMMRQIVESEKARAEYEAT 594
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
708-1080 |
7.96e-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: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 708 SEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGAL--KEEVSSHDQEMDKLKEQY 785
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQreKEELKKLKLEAEELLADR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 786 DAELQ--ALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAK 863
Cdd:pfam02463 727 VQEAQdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 864 ETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENER 943
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 944 WHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDkvsqlemel 1023
Cdd:pfam02463 887 ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE--------- 957
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 1024 EEERNNSDLLSERISRSREQMEQVRNELLQERaaRQDLECDKISLERQNKDLKSRII 1080
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEER--YNKDELEKERLEEEKKKLIRAII 1012
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
855-1002 |
8.09e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 855 LKGDEAKAKETLKKYEGEIRQL-EEALVQARREEKEAvsaRRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLR 933
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIkKEALLEAKEEIHKL---RNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 934 RLKNEMENERWHLGKTIEKLQKEMADIVEASRTstlELQN------------QLDEYKEKNRRELAEMQRQLKEK-TLEA 1000
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIEEQLQ---ELERisgltaeeakeiLLEKVEEEARHEAAVLIKEIEEEaKEEA 186
|
..
gi 1622953339 1001 EK 1002
Cdd:PRK12704 187 DK 188
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
839-926 |
9.05e-07 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 53.55 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEDLKGDEAKA-KETLKKYEGEIRQLEEALVQAR---REEKEAVSARRALENELEAAQRNLSRTTQE 914
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90
....*....|..
gi 1622953339 915 QKQLSEKLKEES 926
Cdd:COG0542 494 LAELEEELAELA 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
608-758 |
1.03e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHN--KKVEENSTLQQRLEESEGELRKNLEE 685
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 686 LFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLliAKEEQEDLLRKRER 758
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL--AAKIPPELLALYER 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
614-995 |
1.09e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 614 EQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELR-------------SQHNKKVEENSTLQQRLEESEGELR 680
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleqdyqaaSDHLNLVQTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 681 KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAK--------RSEDREKGAL-----IEELLQAKQ--DLQDLLIA 745
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqALDVQQTRAIqyqqaVQALERAKQlcGLPDLTAD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 746 K-EEQEDLLRKRERELTALKGALKEEVSSHDQemdkLKEQYDAELQALRESVEEATKNvevlasrsntseqdQAGTEMRV 824
Cdd:PRK04863 439 NaEDWLEEFQAKEQEATEELLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRS--------------EAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 825 KLLQEENEKLQGrseeleQRVAQLQRQIEDLKGD---EAKAKETLKKYEGEIRQ--LEEALVQARREEKEAvsARRALEN 899
Cdd:PRK04863 501 LLRRLREQRHLA------EQLQQLRMRLSELEQRlrqQQRAERLLAEFCKRLGKnlDDEDELEQLQEELEA--RLESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 900 ELEAAQRNLSRTTQEQKQLSEKLkEESEQKEQlrrlknemeneRWH-LGKTIEKLQKEMADIVEASRTSTLELQNQLDEY 978
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARI-QRLAARAP-----------AWLaAQDALARLREQSGEEFEDSQDVTEYMQQLLERE 640
|
410
....*....|....*....
gi 1622953339 979 KE--KNRRELAEMQRQLKE 995
Cdd:PRK04863 641 REltVERDELAARKQALDE 659
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
776-928 |
1.59e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 776 QEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQL--QRQIE 853
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 854 DLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQ 928
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
583-851 |
1.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 583 EKIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQksklttEVAELQRQLQLevknqqnIKEERERMRANLEELrsqhNKKV 662
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK------EIQELQEQRID-------LKEQIKSIEKEIENL----NGKK 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 663 EEnstLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDsakrsedrekgalieellQAKQDLQDL 742
Cdd:TIGR02169 864 EE---LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE------------------KKRKRLSEL 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 743 LIAKEEQEDllrkrerELTALKGALKEEVSSHDQEMDKLKeqydaeLQALRESVEEAtknVEVLASRSNTSEQDQAGTEM 822
Cdd:TIGR02169 923 KAKLEALEE-------ELSEIEDPKGEDEEIPEEELSLED------VQAELQRVEEE---IRALEPVNMLAIQEYEEVLK 986
|
250 260
....*....|....*....|....*....
gi 1622953339 823 RVKLLQEENEKLQGRSEELEQRVAQLQRQ 851
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
678-889 |
1.82e-06 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 52.37 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 678 ELRKNLEELFQvkmereqhqTEIRDLQDQLSEMHDELDSAKRSEDREKGALIE---ELLQAKQDLQDLLIAKEEQEDLLR 754
Cdd:pfam13166 268 ERKAALEAHFD---------DEFTEFQNRLQKLIEKVESAISSLLAQLPAVSDlasLLSAFELDVEDIESEAEVLNSQLD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KRERELTAlkgalKEEVSSHDQEMDklkeQYDAELQALRESVeeatKNVEVLASRSN--TSEQDQAGTEMRVKLLQEENE 832
Cdd:pfam13166 339 GLRRALEA-----KRKDPFKSIELD----SVDAKIESINDLV----ASINELIAKHNeiTDNFEEEKNKAKKKLRLHLVE 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 833 KLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKE 889
Cdd:pfam13166 406 EFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1034-1214 |
2.05e-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: 51.69 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1034 SERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVvQMEARIAELEDRLESEER 1113
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-ALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1114 DRASLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQR---ELEEQMDMNE 1190
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAlraELEAERAELE 177
|
170 180
....*....|....*....|....
gi 1622953339 1191 HLQGQLNSMKKDLSRLKKLPNKVL 1214
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLL 201
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1103-1214 |
2.30e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1103 ELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDehLSLT-DQKDQ----LSLRLKAMKRQVEE---AEEEIDRLESS 1174
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEE--LEAElEEKDErierLERELSEARSEERReirKDREISRLDRE 473
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1622953339 1175 KKKLQRELEEQMDMNEHLQGQLNSMK---KDLSRLKKLPNKVL 1214
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLKelwKLEHSGELVPVKVV 516
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
603-864 |
2.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 603 SNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQN------IKEERERMRA-NLEELRsqhnKKVEENSTLQQRLEES 675
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLkelaeqLKELEEKLKKyNLEELE----KKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 676 EGELR---KNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDL 752
Cdd:PRK03918 538 KGEIKslkKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 753 LRKRERELTALKGALKE------EVSSHDQEMDKLKEQYDAE-LQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVK 825
Cdd:PRK03918 618 EKELKKLEEELDKAFEElaetekRLEELRKELEELEKKYSEEeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622953339 826 LLQEENEKLQG---RSEELEQRVAQLQRQIEDLKGDEAKAKE 864
Cdd:PRK03918 698 KLKEELEEREKakkELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
678-1182 |
2.87e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.57 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 678 ELRKNLE-ELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRsedrekgaLIEEL-----------LQAKQDLQDLLIA 745
Cdd:pfam05701 35 ERRKLVElELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKR--------LIEELklnleraqteeAQAKQDSELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 746 KEEQEDLLRKRER-----ELTALKGALKEEVS---SHDQEMDKLKEQYDAelqaLRESVEEATKNVEVLASRSNTSEqdq 817
Cdd:pfam05701 107 VEEMEQGIADEASvaakaQLEVAKARHAAAVAelkSVKEELESLRKEYAS----LVSERDIAIKRAEEAVSASKEIE--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 818 agtemrvKLLQEENEKLQGRSEELEQ-RVAQLQRQIEDLKGDEAKAKETLKkYEGEIRQLEEALVQARREekeaVSARRA 896
Cdd:pfam05701 180 -------KTVEELTIELIATKESLESaHAAHLEAEEHRIGAALAREQDKLN-WEKELKQAEEELQRLNQQ----LLSAKD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 897 LENELEAAQRNL------------SRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIE------------- 951
Cdd:pfam05701 248 LKSKLETASALLldlkaelaaymeSKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAKDevnclrvaaaslr 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 952 -KLQKEMADIVEASRTSTL------ELQNQLD---------EYKEKNRRE-LAEMQRQLKEKTLEAEKSRLTAMKMQDED 1014
Cdd:pfam05701 328 sELEKEKAELASLRQREGMasiavsSLEAELNrtkseialvQAKEKEAREkMVELPKQLQQAAQEAEEAKSLAQAAREEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1015 KVSQLEMelEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLegsyrsskeglv 1094
Cdd:pfam05701 408 RKAKEEA--EQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKALQESESSAESTNQEDSPRGVTL------------ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1095 vqmeariaELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLtDQKDQLSLRLKAMKRQVEEAEEEIDRLESS 1174
Cdd:pfam05701 474 --------SLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSL-EKLEEVNREMEERKEALKIALEKAEKAKEG 544
|
....*...
gi 1622953339 1175 KKKLQREL 1182
Cdd:pfam05701 545 KLAAEQEL 552
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
642-1077 |
3.37e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 642 EERERMRANLEELRSQHNKKVEENSTLQQRLEEsegELRKNLEELFQVKmerEQHQTEIRD----LQDQLSEMHDELDS- 716
Cdd:NF041483 728 QERERAREQSEELLASARKRVEEAQAEAQRLVE---EADRRATELVSAA---EQTAQQVRDsvagLQEQAEEEIAGLRSa 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 717 AKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEE-VSSHDQEMDKLKEQYDAELQALRES 795
Cdd:NF041483 802 AEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAERtVSEAIAEAERLRSDASEYAQRVRTE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 796 VEEATKNVEVLASRSNTSEQDQAgTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEI-- 873
Cdd:NF041483 882 ASDTLASAEQDAARTRADAREDA-NRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQae 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 874 RQLEEALVQARREEKEAV----SARRALENELEAAQRNLSRTTQEQKQLSEKLKEESE------QKEQLRRLKNEMENER 943
Cdd:NF041483 961 QLIAEATGEAERLRAEAAetvgSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADrtldeaRKDANKRRSEAAEQAD 1040
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 944 WHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRelaEMQRQLKEKTLEA----EKSRLTAMKMqdedkvsql 1019
Cdd:NF041483 1041 TLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARK---EAERIVAEATVEGnslvEKARTDADEL--------- 1108
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 1020 emeLEEERNNSDLLSERISRSREQMEQVRNElLQERAARQDLECDKISLERQNKDLKS 1077
Cdd:NF041483 1109 ---LVGARRDATAIRERAEELRDRITGEIEE-LHERARRESAEQMKSAGERCDALVKA 1162
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
553-806 |
3.46e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 553 ETAKQILYNYLKEGSADNDDATKRKVNLVFEKIQTLKSRAAGSA------QGNNQASNSTSEVKDLLEQKSKLTTEVAEL 626
Cdd:COG3206 152 AVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEaaleefRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 627 QRQLQLEVKNQQNIKEERERMRANLEELRsqhnkkveeNSTLQQRLEESEGELRKNLEELfqVKMEREQHQtEIRDLQDQ 706
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELL---------QSPVIQQLRAQLAELEAELAEL--SARYTPNHP-DVIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 707 LSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKgalkeevsshdQEMDKLKEQYD 786
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLE-----------REVEVARELYE 368
|
250 260
....*....|....*....|...
gi 1622953339 787 AELQALRE-SVEEATK--NVEVL 806
Cdd:COG3206 369 SLLQRLEEaRLAEALTvgNVRVI 391
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
694-894 |
3.83e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 694 EQHQTEIRDLQDQLSEMhDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEevss 773
Cdd:COG1579 3 PEDLRALLDLQELDSEL-DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 774 hDQEmdKLKEQYDA-ELQALRESVEEATKnvevlasrsntseqdqagtemRVKLLQEENEKLQGRSEELEQRVAQLQRQI 852
Cdd:COG1579 78 -YEE--QLGNVRNNkEYEALQKEIESLKR---------------------RISDLEDEILELMERIEELEEELAELEAEL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622953339 853 EDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSAR 894
Cdd:COG1579 134 AELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
638-804 |
3.91e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 638 QNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDEldsa 717
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 718 krsedREKGAL---IEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRE 794
Cdd:COG1579 89 -----KEYEALqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
170
....*....|
gi 1622953339 795 SVEEATKNVE 804
Cdd:COG1579 164 EREELAAKIP 173
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
767-1139 |
4.24e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 767 LKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVA 846
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 QLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEES 926
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 927 EQKEQLRRLKNEMENErwHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEmQRQLKEKTLEAEKSRLT 1006
Cdd:COG4372 164 EELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEA-KDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1007 AMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARqdlECDKISLERQNKDLKSRIIHLEGSY 1086
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA---LELKLLALLLNLAALSLIGALEDAL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 1087 RSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDE 1139
Cdd:COG4372 318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
667-905 |
4.97e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.70 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 667 TLQQRLEESEGELRKnlEELFQVKMEREQHQTE-IRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIA 745
Cdd:PRK05771 13 TLKSYKDEVLEALHE--LGVVHIEDLKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 746 KEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLK--EQYDAELQALRESveeatKNVEVLA---SRSNTSEQDQAGT 820
Cdd:PRK05771 91 VEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGF-----KYVSVFVgtvPEDKLEELKLESD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 821 EMRVKLLQEENEK-------LQGRSEELEQRVAQLQRQIEDLKgDEAKAKETLKKYEGEIRQLEEALVQARRE------- 886
Cdd:PRK05771 166 VENVEYISTDKGYvyvvvvvLKELSDEVEEELKKLGFERLELE-EEGTPSELIREIKEELEEIEKERESLLEElkelakk 244
|
250 260
....*....|....*....|
gi 1622953339 887 -EKEAVSARRALENELEAAQ 905
Cdd:PRK05771 245 yLEELLALYEYLEIELERAE 264
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
600-1208 |
5.67e-06 |
|
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: 50.79 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 600 NQASNSTSEVKDLLEQKSKLTTEVaelqRQLQLEVKNQQNIKEERERMRANLEElrsQHNKKVEENSTLQQRLEESEGEL 679
Cdd:TIGR04523 26 NIANKQDTEEKQLEKKLKTIKNEL----KNKEKELKNLDKNLNKDEEKINNSNN---KIKILEQQIKDLNDKLKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 680 RKNLEELFQVKmereqhqTEIRDLQDQLSEMHDELDSAKRsEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERE 759
Cdd:TIGR04523 99 NKLNSDLSKIN-------SEIKNDKEQKNKLEVELNKLEK-QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 760 LTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQdqagtemrVKLLQEENEKLQGRSE 839
Cdd:TIGR04523 171 LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ--------NNQLKDNIEKKQQEIN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 840 ELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQarreekeavsarraLENELEAAQRNLSRTTQEQKQ-L 918
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE--------------LEKQLNQLKSEISDLNNQKEQdW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 919 SEKLKEE-SEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIVEASRTSTLElqnqldeyKEKNRRELAEMQRQLKekT 997
Cdd:TIGR04523 309 NKELKSElKNQEKKLEEIQNQISQNN----KIISQLNEQISQLKKELTNSESE--------NSEKQRELEEKQNEIE--K 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 998 LEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERIsrsreqmeqvrnellqeraarQDLECDKISLERQNKDLKS 1077
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI---------------------KKLQQEKELLEKEIERLKE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1078 RIIhlegsyrsskeglvvqmeariaELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDehlsltdqkdqLSLRLKAM 1157
Cdd:TIGR04523 434 TII----------------------KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV-----------LSRSINKI 480
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 1158 KRQVEEAEEEIDRLESSKKKLQRE---LEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEKLESEKK 534
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
823-1074 |
5.70e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 823 RVKLLQEENEKLQGRSEELEQR---------------VAQLQRQIEDLKGDEAKAketlkkyEGEIRQLEEALVQARREE 887
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARL-------QLELDNLRLAAEDFRQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 888 KEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKeesEQKEQLRRLKNEMENERWHLGKTI--EKLQKEMADIVEASR 965
Cdd:pfam00038 92 EDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIE---SLKEELAFLKKNHEEEVRELQAQVsdTQVNVEMDAARKLDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 966 TSTL-ELQNQLDEYKEKNRRELAEM-QRQLKEKTLEAE---------KSRLTAMKMQdedkVSQLEMELEEERNNSDLLS 1034
Cdd:pfam00038 169 TSALaEIRAQYEEIAAKNREEAEEWyQSKLEELQQAAArngdalrsaKEEITELRRT----IQSLEIELQSLKKQKASLE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622953339 1035 ERIS----RSREQMEQVRNELLQERAARQDLECDkisLERQNKD 1074
Cdd:pfam00038 245 RQLAeteeRYELQLADYQELISELEAELQETRQE---MARQLRE 285
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
768-1208 |
7.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 KEEVSSHDQEMDKLKEQY-DAELQALRESVEEATknvevlasrsntseqdqagTEMRVKLLQEENEKLQGRSEELEQRVA 846
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYkDFDFDAKEDNRADEA-------------------TEEAFGKAEEAKKTETGKAEEARKAEE 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 QLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENElEAAQRNLSRTTQEQKQLSEKLK-EE 925
Cdd:PTZ00121 1120 AKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRKaED 1198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 926 SEQKEQLRRLKNEMENE---RWHLGKTIE---KLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKE---- 995
Cdd:PTZ00121 1199 ARKAEAARKAEEERKAEearKAEDAKKAEavkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAeear 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 996 -----KTLEAEKSRLTAMKMQDEDKVSQLEMELEEERnNSDLLSERISRSREQMEQVRNELLQER----AARQDLECDKI 1066
Cdd:PTZ00121 1279 kadelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKKADAAKKKAEEAKkaaeAAKAEAEAAAD 1357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1067 SLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAElEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQ 1146
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD-EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEA 1436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953339 1147 KDQLSLRLKA--MKRQVEE---AEEEIDRLESSKK--KLQRELEEQMDMNEhLQGQLNSMKKDLSRLKK 1208
Cdd:PTZ00121 1437 KKKAEEAKKAdeAKKKAEEakkAEEAKKKAEEAKKadEAKKKAEEAKKADE-AKKKAEEAKKKADEAKK 1504
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
870-1080 |
7.87e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 870 EGEIRQ-LEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERwhLGK 948
Cdd:PRK10929 25 EKQITQeLEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVP--PNM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 949 TIEKLQKEMADI----VEASRTSTLELQ---------NQLDEYKEKNRRELAEMQRQLKEK---TLEAEKSRLTAMKMQD 1012
Cdd:PRK10929 103 STDALEQEILQVssqlLEKSRQAQQEQDrareisdslSQLPQQQTEARRQLNEIERRLQTLgtpNTPLAQAQLTALQAES 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1013 ---EDKVSQLEME-------LEEERNNSDLLSERISRSREQMEQVRNEL--LQERAARQDLECDKIsLERQNKDLKSRII 1080
Cdd:PRK10929 183 aalKALVDELELAqlsannrQELARLRSELAKKRSQQLDAYLQALRNQLnsQRQREAERALESTEL-LAEQSGDLPKSIV 261
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
969-1143 |
9.16e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 969 LELQnQLDEYKEKNRRELAEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVR 1048
Cdd:COG1579 10 LDLQ-ELDSELDRLEHRLKELPAELAE--LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1049 N--ELlqeraarQDLECDKISLERQNKDLKSRIIHLEGSyRSSKEGLVVQMEARIAELEDRLESEERDR----ASLQLSN 1122
Cdd:COG1579 87 NnkEY-------EALQKEIESLKRRISDLEDEILELMER-IEELEEELAELEAELAELEAELEEKKAELdeelAELEAEL 158
|
170 180
....*....|....*....|.
gi 1622953339 1123 RRLERKVKELVMQVDDEHLSL 1143
Cdd:COG1579 159 EELEAEREELAAKIPPELLAL 179
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
607-762 |
9.16e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQlevknqqNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELR--KNLE 684
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELA-------ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 685 ELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGAL---IEELLQAKQDLQDLLIAKEEQEDLLRKRERELT 761
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELaelEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
.
gi 1622953339 762 A 762
Cdd:COG1579 170 A 170
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
597-1185 |
9.45e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.21 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 597 QGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNikEERERMRANLEELRSQHNKKVEENSTLQQRLE-ES 675
Cdd:NF041483 84 QADQLRADAERELRDARAQTQRILQEHAEHQARLQAELHTEAV--QRRQQLDQELAERRQTVESHVNENVAWAEQLRaRT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 676 EGELRKNLEElfqVKMEREQHQTEIRDLQDQLS-EMHDELDSAKRSEDREKGALieeLLQAKQDLQDLLIAKEEQEDLLR 754
Cdd:NF041483 162 ESQARRLLDE---SRAEAEQALAAARAEAERLAeEARQRLGSEAESARAEAEAI---LRRARKDAERLLNAASTQAQEAT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQ-ALRESVEEATKnveVLASRSNTSEQDQAGTEmrvkllqeenek 833
Cdd:NF041483 236 DHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEeALREARAEAEK---VVAEAKEAAAKQLASAE------------ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 834 lqgrsEELEQRVAQLQRQIEDLKGDEAKAKETLKKyEGEiRQLEEALVQARREEKEAVSARRALENELEAAQrnLSRTTQ 913
Cdd:NF041483 301 -----SANEQRTRTAKEEIARLVGEATKEAEALKA-EAE-QALADARAEAEKLVAEAAEKARTVAAEDTAAQ--LAKAAR 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 914 EQKQLSEKLKEESeqKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVE----ASRTSTLELQNQLDEYKEKNRRELAEM 989
Cdd:NF041483 372 TAEEVLTKASEDA--KATTRAAAEEAERIRREAEAEADRLRGEAADQAEqlkgAAKDDTKEYRAKTVELQEEARRLRGEA 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 990 QRQLKEKTLEAEKSRLTAMK---MQDEDKVSQLEMELEEERNNSDllsERISRSREQMEQVRNELLqERAArqdlecdki 1066
Cdd:NF041483 450 EQLRAEAVAEGERIRGEARReavQQIEEAARTAEELLTKAKADAD---ELRSTATAESERVRTEAI-ERAT--------- 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1067 SLERQNKDLKSRIIHLEGSYRSSKEGLV--VQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLT 1144
Cdd:NF041483 517 TLRRQAEETLERTRAEAERLRAEAEEQAeeVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA 596
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622953339 1145 DQKDQlslrlkaMKRQVEEAEEEIDRLESSKKKLQRELEEQ 1185
Cdd:NF041483 597 DARAE-------AERIRREAAEETERLRTEAAERIRTLQAQ 630
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
561-783 |
9.51e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 561 NYLKEGSADNDDATKRKVNLVFEKIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQ--- 637
Cdd:PHA02562 202 KNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIkmy 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 638 ----------QNIKEERERMranlEELRsqhnkkvEENSTLQQRLEesegELRKNLEELFQVKMEREQHQTEIRDLQDQL 707
Cdd:PHA02562 282 ekggvcptctQQISEGPDRI----TKIK-------DKLKELQHSLE----KLDTAIDELEEIMDEFNEQSKKLLELKNKI 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 708 SEMHDELDSAKRSEDREKGALIEellqakqdLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKE 783
Cdd:PHA02562 347 STNKQSLITLVDKAKKVKAAIEE--------LQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLKD 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
827-1057 |
1.41e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 827 LQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAvsaRRALENELEAAQR 906
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---REELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 907 NLSRTTqeqkqLSEKLKEESEQKEQLRRLKNemenerwhlgktIEKLQKEMADIVEAsrtsTLELQNQLDEYKEKNRREL 986
Cdd:COG3883 98 SGGSVS-----YLDVLLGSESFSDFLDRLSA------------LSKIADADADLLEE----LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 987 AEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAA 1057
Cdd:COG3883 157 AELEALKAE--LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
872-1173 |
1.51e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 872 EIRQLEEALVQARREEKEAVSARRALENELEAA-------------QRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNE 938
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnlvqtalrqQEKIERYQADLEELEERLEEQNEVVEEADEQQEE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 939 MENERWHLGKTIEKLQKEMADIVEAsrtsTLELQNQLDEYKE-KNRRELAEMQRQLKEKTLEAEKSRLTAMKMQdEDKVS 1017
Cdd:PRK04863 381 NEARAEAAEEEVDELKSQLADYQQA----LDVQQTRAIQYQQaVQALERAKQLCGLPDLTADNAEDWLEEFQAK-EQEAT 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1018 QLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQdlecdKISLERQNKDLKsriiHLEGSyrsskeglVVQM 1097
Cdd:PRK04863 456 EELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDV-----ARELLRRLREQR----HLAEQ--------LQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1098 EARIAELEDRLESEERDRASLQLSNRRLERK------VKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRL 1171
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNlddedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL 598
|
..
gi 1622953339 1172 ES 1173
Cdd:PRK04863 599 AA 600
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
746-1062 |
1.64e-05 |
|
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: 49.35 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 746 KEEQEDLLRKREReltalKGALKEEVSSHDQEMDKLKEQYdAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVK 825
Cdd:pfam17380 302 RQEKEEKAREVER-----RRKLEEAEKARQAEMDRQAAIY-AEQERMAMERERELERIRQEERKRELERIRQEEIAMEIS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 826 LLQEEnEKLQGRSEELEQRVAQlqrQIEDLKGDEAKAKETLKKYEGEIRQLEEalVQARREEKEAVSARRaLENELEAAQ 905
Cdd:pfam17380 376 RMREL-ERLQMERQQKNERVRQ---ELEAARKVKILEEERQRKIQQQKVEMEQ--IRAEQEEARQREVRR-LEEERAREM 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 906 RNLSRTTQEQKQLSEKLKeeseQKEQLRRLKN-EMENERWHLGKTIEKLQKEMADIVEASRTSTLElqnqldeykEKNRR 984
Cdd:pfam17380 449 ERVRLEEQERQQQVERLR----QQEEERKRKKlELEKEKRDRKRAEEQRRKILEKELEERKQAMIE---------EERKR 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 985 ELAEMQRQLKEKTL-------EAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLseriSRSREQMEQVrnelLQERAA 1057
Cdd:pfam17380 516 KLLEKEMEERQKAIyeeerrrEAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM----EREREMMRQI----VESEKA 587
|
....*
gi 1622953339 1058 RQDLE 1062
Cdd:pfam17380 588 RAEYE 592
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
676-1052 |
1.66e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.28 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 676 EGELRKNLEelfQVKMEREQHQTEIRD-LQDQLSEMHDELDSAKRSEDREKgaLIEELLQAKQDLQDLLIAKEEQEDLLR 754
Cdd:PRK10929 25 EKQITQELE---QAKAAKTPAQAEIVEaLQSALNWLEERKGSLERAKQYQQ--VIDNFPKLSAELRQQLNNERDEPRSVP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KR------ERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVE------EATKNVEVLASRSNTSEQDQAgtem 822
Cdd:PRK10929 100 PNmstdalEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEarrqlnEIERRLQTLGTPNTPLAQAQL---- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 823 rvKLLQEENEKLQGRSEELEqrVAQLQ---RQ-IEDLKGDEAKaketlKKYE---GEIRQLEEALVQARREEKEavsarR 895
Cdd:PRK10929 176 --TALQAESAALKALVDELE--LAQLSannRQeLARLRSELAK-----KRSQqldAYLQALRNQLNSQRQREAE-----R 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 896 ALEN-ELEAAQ-----RNLSRTTQEQKQLSEKLKEESEQ----KEQLRRLKNEMENERWHLGKTIEKLQkemadiveasr 965
Cdd:PRK10929 242 ALEStELLAEQsgdlpKSIVAQFKINRELSQALNQQAQRmdliASQQRQAASQTLQVRQALNTLREQSQ----------- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 966 tsTLELQNQLDEYKEKNRRELAEMQrqlKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQME 1045
Cdd:PRK10929 311 --WLGVSNALGEALRAQVARLPEMP---KPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRILDAQL 385
|
....*..
gi 1622953339 1046 QVRNELL 1052
Cdd:PRK10929 386 RTQRELL 392
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
551-1193 |
1.68e-05 |
|
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: 49.66 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 551 NEETAKQILYNYLKEGSADNDDATKrKVNLVFEKIQTLKSRAAGSAQG----NNQASNSTSEVKDLLEQKSKLTTEVAEL 626
Cdd:TIGR01612 1087 NEIKEKLKHYNFDDFGKEENIKYAD-EINKIKDDIKNLDQKIDHHIKAleeiKKKSENYIDEIKAQINDLEDVADKAISN 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 627 QRQLQLEvKNQQNIKEERERMRANLEELRSQHNK--KVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTE--IRD 702
Cdd:TIGR01612 1166 DDPEEIE-KKIENIVTKIDKKKNIYDEIKKLLNEiaEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmIKA 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 703 LQDQLSEMhDELDsaKRSEDREKGALIEELLQAKQDLQDL---------LIAKEEQEDLLRKRERELTALKGALKEevsS 773
Cdd:TIGR01612 1245 MEAYIEDL-DEIK--EKSPEIENEMGIEMDIKAEMETFNIshdddkdhhIISKKHDENISDIREKSLKIIEDFSEE---S 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 774 HDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMR--VKLLQEENEKLQGRSEELEQRVAQLQRQ 851
Cdd:TIGR01612 1319 DINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKeyTKEIEENNKNIKDELDKSEKLIKKIKDD 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 852 IeDLKGDEAKAKETL--KKYEGEIRQLEEALVQARREE----------KEAVSARRALENELEAAQRNLSRTTQEQKQ-- 917
Cdd:TIGR01612 1399 I-NLEECKSKIESTLddKDIDECIKKIKELKNHILSEEsnidtyfknaDENNENVLLLFKNIEMADNKSQHILKIKKDna 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 918 ---LSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEA-SRTSTLELQNQLDEYKEKNRRELAEMQRQL 993
Cdd:TIGR01612 1478 tndHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELlNKYSALAIKNKFAKTKKDSEIIIKEIKDAH 1557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 994 KEKTLEAEKSRltamkmQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQ---ERAARQDLECDKISLER 1070
Cdd:TIGR01612 1558 KKFILEAEKSE------QKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKisdIKKKINDCLKETESIEK 1631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1071 QNKDLKsriihlegsyrsskeglVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELvMQVDDEHLSLTDQKDQ- 1149
Cdd:TIGR01612 1632 KISSFS-----------------IDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKEL-DELDSEIEKIEIDVDQh 1693
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1150 -LSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELE-----------EQMDMNEHLQ 1193
Cdd:TIGR01612 1694 kKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEnlissfntndlEGIDPNEKLE 1749
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
860-1016 |
1.72e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 860 AKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQlrrlknem 939
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-------- 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 940 enerwhlgKTIEKLQKEMADIVEASRtstlelQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKV 1016
Cdd:PRK00409 577 --------QAIKEAKKEADEIIKELR------QLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
651-1000 |
2.16e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.18 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 651 LEELRSQHNKKVEENSTL---QQRLEESEGELRKNLEELFQVKMEREQHQtEIRDLQDQLSEMHDELdsakrsedrekga 727
Cdd:COG3096 787 LEELRAERDELAEQYAKAsfdVQKLQRLHQAFSQFVGGHLAVAFAPDPEA-ELAALRQRRSELEREL------------- 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 728 liEELLQAKQDLQDLLIAKEEQEDLLRKrereLTALKGALKEEvsSHDQEMDKLKEQYDAELQALREsVEEATKNVEVLA 807
Cdd:COG3096 853 --AQHRAQEQQLRQQLDQLKEQLQLLNK----LLPQANLLADE--TLADRLEELREELDAAQEAQAF-IQQHGKALAQLE 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 808 SRSNTSEQDQagtemrvkllqEENEKLQGRSEELEQRVAQLQRQIEDLK-----------GDEA-----------KAKET 865
Cdd:COG3096 924 PLVAVLQSDP-----------EQFEQLQADYLQAKEQQRRLKQQIFALSevvqrrphfsyEDAVgllgensdlneKLRAR 992
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 866 LKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRR--LKNEM---- 939
Cdd:COG3096 993 LEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRdeLHEELsqnr 1072
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 940 -------------ENERWHLGKTIEKLQKEMADIVE------ASRTSTLELQNQLDEYKEKNRRELAEM----QRQLKEK 996
Cdd:COG3096 1073 srrsqlekqltrcEAEMDSLQKRLRKAERDYKQEREqvvqakAGWCAVLRLARDNDVERRLHRRELAYLsadeLRSMSDK 1152
|
....
gi 1622953339 997 TLEA 1000
Cdd:COG3096 1153 ALGA 1156
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
598-870 |
2.16e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 598 GNNQASNSTSEVKDLLEQKSKLTTEVAELQRQlqlevKNQQNIKEERERMRANLEELRSQHNKKVEEN---STLQQRLEE 674
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRK-----KNGENIARKQNKYDELVEEAKTIKAEIEELTdelLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 675 SEGELRKNLEELFQVKMEREQHQTEIrdlqdqlsEMHdeldsakrsedrEKGAlieELLQAKQDLqdlliakEEQEDLLR 754
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEQFQKVI--------KMY------------EKGG---VCPTCTQQI-------SEGPDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 KrereltalkgaLKEEVSSHDQEMDKLKEQYDaELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKL 834
Cdd:PHA02562 303 K-----------IKDKLKELQHSLEKLDTAID-ELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622953339 835 QGRSEELEQRVAQLQRQIEDLKgdEAKAKETLKKYE 870
Cdd:PHA02562 371 QAEFVDNAEELAKLQDELDKIV--KTKSELVKEKYH 404
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
860-1000 |
2.36e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 48.60 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 860 AKAKETLKKYEGEIRQLEEALVQARRE-EKEAVSARRALEnELEAAQRNLSRTTQEQKQLSEKLKEESEQK--EQLRRLK 936
Cdd:COG1193 503 ERARELLGEESIDVEKLIEELERERRElEEEREEAERLRE-ELEKLREELEEKLEELEEEKEEILEKAREEaeEILREAR 581
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 937 NEMENerwhLGKTIEKLQKEMADIVEASRtstlELQNQLDEYKEKNRRELAEMQRQLKEKTLEA 1000
Cdd:COG1193 582 KEAEE----LIRELREAQAEEEELKEARK----KLEELKQELEEKLEKPKKKAKPAKPPEELKV 637
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
726-979 |
2.68e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 726 GALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKgalKEEVSSHDQEMDKLKEQYDAELQalresveeatknvev 805
Cdd:PRK12704 17 GAVIGYFVRKKIAEAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNEFEKELR--------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 806 lasrsntseqdqagtemrvkllqEENEKLQGRSEELEQRVAQLQRQIEDLKgdeaKAKETLKKYEGEIRQLEEALVQARR 885
Cdd:PRK12704 79 -----------------------ERRNELQKLEKRLLQKEENLDRKLELLE----KREEELEKKEKELEQKQQELEKKEE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 886 EEKEAVSARRAlenELEaaqrNLSRTTQEQ--KQLSEKLKEESEQK--EQLRRLKNEMENERWHLGKTI--EKLQKEMAD 959
Cdd:PRK12704 132 ELEELIEEQLQ---ELE----RISGLTAEEakEILLEKVEEEARHEaaVLIKEIEEEAKEEADKKAKEIlaQAIQRCAAD 204
|
250 260
....*....|....*....|
gi 1622953339 960 IVEASRTSTLELQNqlDEYK 979
Cdd:PRK12704 205 HVAETTVSVVNLPN--DEMK 222
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1014-1208 |
2.87e-05 |
|
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: 48.35 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1014 DKVSQLEMELEEERNNSDLL-----SERISRSREQMEQVRNELLQERAA--------RQDLECDKISLERQNKDLKSRII 1080
Cdd:pfam07888 4 DELVTLEEESHGEEGGTDMLlvvprAELLQNRLEECLQERAELLQAQEAanrqrekeKERYKRDREQWERQRRELESRVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1081 HLEGSYRSSKEGlVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVddehlsltdqkdqlslrlKAMKRQ 1160
Cdd:pfam07888 84 ELKEELRQSREK-HEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDI------------------KTLTQR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622953339 1161 VEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:pfam07888 145 VLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
699-1062 |
3.58e-05 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 48.19 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 699 EIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEM 778
Cdd:COG2770 266 EIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 779 DKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGD 858
Cdd:COG2770 346 LAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 859 EAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNE 938
Cdd:COG2770 426 AAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEEL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 939 MENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQ 1018
Cdd:COG2770 506 AEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAAL 585
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622953339 1019 LEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLE 1062
Cdd:COG2770 586 LLLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAGAAL 629
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
815-1054 |
3.85e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.11 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 815 QDQAGTEMRVKLLQEENEKLQGR-------SEELEQRVAQLQRQIEDLK--GDEAKAKETLKKYEGEIRQLEEALVQARR 885
Cdd:pfam15905 87 QERGEQDKRLQALEEELEKVEAKlnaavreKTSLSASVASLEKQLLELTrvNELLKAKFSEDGTQKKMSSLSMELMKLRN 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 886 E----EKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKL----KEESEQKEQLRRLKNEMEnerwHLGKTIEKLQKEM 957
Cdd:pfam15905 167 KleakMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLvsteKEKIEEKSETEKLLEYIT----ELSCVSEQVEKYK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 958 ADIVeasrtstlelqnQLDEYKEKNRRELAEMQRQLKEKTLEAEKSrltaMKMQDEdKVSQLEMELEEERNNSDLLSERI 1037
Cdd:pfam15905 243 LDIA------------QLEELLKEKNDEIESLKQSLEEKEQELSKQ----IKDLNE-KCKLLESEKEELLREYEEKEQTL 305
|
250
....*....|....*..
gi 1622953339 1038 SRSREQMEQVRNELLQE 1054
Cdd:pfam15905 306 NAELEELKEKLTLEEQE 322
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
650-1204 |
3.90e-05 |
|
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: 47.89 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 650 NLEELRSQHNKKVEENSTLQQRLEESE-------------GELRKNLEELFQVK----MEREQHQTEIRDLQDQLSEMHd 712
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEMElrietqkqtlgarDESIKKLLEMLQSKglpkKSGEEDWERTRRIAEAEMQLG- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 713 ELDSAKRSEDREKGALIEEL---LQAKQD------LQDLLIAKEEQ----EDLLRKRERELTALK--GALK--------- 768
Cdd:pfam10174 196 HLEVLLDQKEKENIHLREELhrrNQLQPDpaktkaLQTVIEMKDTKisslERNIRDLEDEVQMLKtnGLLHtedreeeik 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 769 --EEVSSHDQEM----DKLKEQY---DAELQALRESVEEAT-------KNVEVLASRSNTSEQdqagtemRVKLLQEENE 832
Cdd:pfam10174 276 qmEVYKSHSKFMknkiDQLKQELskkESELLALQTKLETLTnqnsdckQHIEVLKESLTAKEQ-------RAAILQTEVD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 833 KLQGRSEELEQRVAQLQRQIEDLKGDeakaKETLKkyeGEIRQLEEALVQARREEkeavsarraleNELEAAQRNLsrtt 912
Cdd:pfam10174 349 ALRLRLEEKESFLNKKTKQLQDLTEE----KSTLA---GEIRDLKDMLDVKERKI-----------NVLQKKIENL---- 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 913 qeQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGkTIEKLQKEMADIVEASR----TSTLELQNQLDEYKEKN---RRE 985
Cdd:pfam10174 407 --QEQLRDKDKQLAGLKERVKSLQTDSSNTDTALT-TLEEALSEKERIIERLKeqreREDRERLEELESLKKENkdlKEK 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 986 LAEMQRQLKEKT-----LEAEKSRLTAMKMQDEDKVSQLEMELEEERnnsdllsERISRSREQMEQVRNELLQERAarqd 1060
Cdd:pfam10174 484 VSALQPELTEKEsslidLKEHASSLASSGLKKDSKLKSLEIAVEQKK-------EECSKLENQLKKAHNAEEAVRT---- 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1061 lecdkislerqNKDLKSRIIHLEGSYRSSKEglvvqmEARIAELE-DRLESEERDRASLQLSNrrlERKVKELVMQVDDE 1139
Cdd:pfam10174 553 -----------NPEINDRIRLLEQEVARYKE------ESGKAQAEvERLLGILREVENEKNDK---DKKIAELESLTLRQ 612
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 1140 HLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKK--LQRELEEQMDMNEHLQGQLNSMKKDLS 1204
Cdd:pfam10174 613 MKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
948-1130 |
4.20e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 948 KTIEKLQKEMADIveasRTSTLELQNQLDEYKEKNR-----RELAEMQRQLKEktLEAEKSRLTAMKMQDEDKVSQLEME 1022
Cdd:COG3206 175 KALEFLEEQLPEL----RKELEEAEAALEEFRQKNGlvdlsEEAKLLLQQLSE--LESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1023 LEEERNNSDLL--SERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEAR 1100
Cdd:COG3206 249 LGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190
....*....|....*....|....*....|...
gi 1622953339 1101 IAELEDRLESEERDRASLQLSN---RRLERKVK 1130
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEaelRRLEREVE 361
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
624-993 |
4.23e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 624 AELQRQLQlEVKNQQNIKEERERMRANLEE---LRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVK-----MEREQ 695
Cdd:PRK11281 39 ADVQAQLD-ALNKQKLLEAEDKLVQQDLEQtlaLLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKddndeETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 696 HQT-EIRDLQDQLSEMHDELDSAKrsedrekgaliEELLQAKQDLQDLLIAKEEQEDLL---RKRERELTALKGALK--E 769
Cdd:PRK11281 118 LSTlSLRQLESRLAQTLDQLQNAQ-----------NDLAEYNSQLVSLQTQPERAQAALyanSQRLQQIRNLLKGGKvgG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 770 EVSSHDQemdklKEQYDAELQAL-------RESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEE-NEKlqgRSEEL 841
Cdd:PRK11281 187 KALRPSQ-----RVLLQAEQALLnaqndlqRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAiNSK---RLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 842 EQRVAQLQRQiedlkgDEAKAKET--LKKYEGEI-RQLEEALVQARREEKEAV----SARRALENeLEAAQRN------- 907
Cdd:PRK11281 259 EKTVQEAQSQ------DEAARIQAnpLVAQELEInLQLSQRLLKATEKLNTLTqqnlRVKNWLDR-LTQSERNikeqisv 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 908 ------LSRTTQEQKQLSEKLKEESEQKEQLR--RLK----NEMENERWHLGKTIEKLQKEMADIVEAsrtstlELQNQL 975
Cdd:PRK11281 332 lkgsllLSRILYQQQQALPSADLIEGLADRIAdlRLEqfeiNQQRDALFQPDAYIDKLEAGHKSEVTD------EVRDAL 405
|
410
....*....|....*...
gi 1622953339 976 DEYKEKNRRELAEMQRQL 993
Cdd:PRK11281 406 LQLLDERRELLDQLNKQL 423
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
734-997 |
4.58e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 47.68 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 734 QAKQDLQDLL--IAKEEQEDLLRKRERELTALKGALKE--EVSSHDQEMDKLKEQYDAELQA-LRESVEEATKNVEVLAS 808
Cdd:pfam13779 463 EALDEVADLLweLALRIEDGDLSDAERRLRAAQERLSEalERGASDEEIAKLMQELREALDDyMQALAEQAQQNPQDLQQ 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 809 RsntseQDQAGTEMRVKLLQEENEKLQ-----GRSEELEQRVAQLQRQIEDLKgdeakaketlkkyegeirqleealvQA 883
Cdd:pfam13779 543 P-----DDPNAQEMTQQDLQRMLDRIEelarsGRRAEAQQMLSQLQQMLENLQ-------------------------AG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 884 RREEkeavsARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRrlkNEMENERWHLGKTIEKLQKEMADIVEA 963
Cdd:pfam13779 593 QPQQ-----QQQQGQSEMQQAMDELGDLLREQQQLLDETFRQLQQQGGQQ---QGQPGQQGQQGQGQQPGQGGQQPGAQM 664
|
250 260 270
....*....|....*....|....*....|....
gi 1622953339 964 SRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKT 997
Cdd:pfam13779 665 PPQGGAEALGDLAERQQALRRRLEELQDELKELG 698
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
623-901 |
5.08e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.33 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 623 VAELQRQLQlEVK-NQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEES-------EGELRKNLEELFQVKMERE 694
Cdd:pfam05701 295 LASAKKELE-EVKaNIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMAsiavsslEAELNRTKSEIALVQAKEK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 695 QHQTEIRDLQDQLSEMHDELDSAKrsedrekgalieELLQAKQDlqDLLIAKEEQEDLLRKRERELTALKGALKEEVSSH 774
Cdd:pfam05701 374 EAREKMVELPKQLQQAAQEAEEAK------------SLAQAARE--ELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 775 DQEMDKLkeqydAELQALRESveeatknvevlasRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQ----RVAQLQR 850
Cdd:pfam05701 440 ASEKLAL-----AAIKALQES-------------ESSAESTNQEDSPRGVTLSLEEYYELSKRAHEAEElankRVAEAVS 501
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 851 QIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENEL 901
Cdd:pfam05701 502 QIEEAKESELRSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQEL 552
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
768-939 |
9.01e-05 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 46.96 E-value: 9.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 KEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTseqdqagtemrvklLQEENEKLQGRSEELEQRvaq 847
Cdd:pfam10168 556 REEIQKRVKLLKLQKEQQLQELQSLEEERKSLSERAEKLAEKYEE--------------IKDKQEKLMRRCKKVLQR--- 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 848 LQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEavsARRALENELEAAQRN-LSRTTQEQKQLSEKLKEES 926
Cdd:pfam10168 619 LNSQLPVLSDAEREMKKELETINEQLKHLANAIKQAKKKMNY---QRYQIAKSQSIRKKSsLSLSEKQRKTIKEILKQLG 695
|
170
....*....|....*..
gi 1622953339 927 ----EQKEQLRRLKNEM 939
Cdd:pfam10168 696 seidELIKQVKDINKHV 712
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
649-886 |
1.03e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 649 ANLEELRSQHNKKVEENSTLQQRLEE---SEGELRKNLEEL-FQVKmereqhqtEIRDLQDQLSEMhDELDsakrsEDRE 724
Cdd:COG0497 151 AGLEELLEEYREAYRAWRALKKELEElraDEAERARELDLLrFQLE--------ELEAAALQPGEE-EELE-----EERR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 725 KGALIEELLQAKQDLQDLLiAKEEQ--EDLLRKRERELtalkgalkEEVSSHDQEMDKLKEQydaeLQALRESVEEATKN 802
Cdd:COG0497 217 RLSNAEKLREALQEALEAL-SGGEGgaLDLLGQALRAL--------ERLAEYDPSLAELAER----LESALIELEEAASE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 803 VEVLASRSNTSEQDQAGTEMRVKLLQE-------ENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYegeiRQ 875
Cdd:COG0497 284 LRRYLDSLEFDPERLEEVEERLALLRRlarkygvTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAEL----LE 359
|
250
....*....|.
gi 1622953339 876 LEEALVQARRE 886
Cdd:COG0497 360 AAEKLSAARKK 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
534-758 |
1.03e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 534 QATPDLLKGQQELTQQTNEETAKQILYNYLKEGSADNDDATKRKVNLVFEKIQTLKSRAAGSAQGNNQASNSTSEVKDLL 613
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 614 EQKSKLTTEVAEL-------QRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEEL 686
Cdd:TIGR02168 866 ELIEELESELEALlneraslEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 687 fqvkmeREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGAL----------IEELLQAKQDLQDLliaKEEQEDLLRKR 756
Cdd:TIGR02168 946 ------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnlaaIEEYEELKERYDFL---TAQKEDLTEAK 1016
|
..
gi 1622953339 757 ER 758
Cdd:TIGR02168 1017 ET 1018
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
608-964 |
1.07e-04 |
|
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: 46.67 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQnikeERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:pfam09731 45 EVVLYALGEDPPLAPKPKTFRPLQPSVVSAV----TGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIrdLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKREREL------- 760
Cdd:pfam09731 121 KSEQEKEKALEEV--LKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALaeklkev 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 761 -TALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVL--ASRSNTSEQDQAGTEMrVKLLQE-------- 829
Cdd:pfam09731 199 iNLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVdqYKELVASERIVFQQEL-VSIFPDiipvlked 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 830 ---ENEKLQGRSEELEQRVAQLQRQIEDLKGDE-AKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELE--- 902
Cdd:pfam09731 278 nllSNDDLNSLIAHAHREIDQLSKKLAELKKREeKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREree 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 903 --AAQRNLSRTTQEQKQ--LSEKLKEESEQKEQ------LRRLKNEMENERWHLGKTIEKLQKEMADIVEAS 964
Cdd:pfam09731 358 irESYEEKLRTELERQAeaHEEHLKDVLVEQEIelqrefLQDIKEKVEEERAGRLLKLNELLANLKGLEKAT 429
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
614-1058 |
1.07e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 614 EQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMrANLEELRSQHNKKVEENSTLQQRLEESEGELRKnlEELFQVKM-- 691
Cdd:PRK10246 216 EQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWL-TRLDELQQEASRRQQALQQALAAEEKAQPQLAA--LSLAQPARql 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 692 ----EREQHQTE-IRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQeDLLRKRERELTALKGA 766
Cdd:PRK10246 293 rphwERIQEQSAaLAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEH-DRFRQWNNELAGWRAQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 767 LKEEVSSHDQeMDKLKEQYDAELQALrESVEEATKNV---EVLASRSNTSEQdqagTEMRVKLLQeenekLQGRSEELEQ 843
Cdd:PRK10246 372 FSQQTSDREQ-LRQWQQQLTHAEQKL-NALPAITLTLtadEVAAALAQHAEQ----RPLRQRLVA-----LHGQIVPQQK 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 844 RVAQLQRQIEDLKGDEAKAKETL----KKY----------------EGEIRQLEE--ALVQARR-------EEKEAVSAR 894
Cdd:PRK10246 441 RLAQLQVAIQNVTQEQTQRNAALnemrQRYkektqqladvkticeqEARIKDLEAqrAQLQAGQpcplcgsTSHPAVEAY 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 895 RALenELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEA---SRTSTLEL 971
Cdd:PRK10246 521 QAL--EPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlniTLQPQDDI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 972 QNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELE-------EERNNSDLLSERISRSRE-Q 1043
Cdd:PRK10246 599 QPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltlpQEDEEASWLATRQQEAQSwQ 678
|
490
....*....|....*
gi 1622953339 1044 MEQVRNELLQERAAR 1058
Cdd:PRK10246 679 QRQNELTALQNRIQQ 693
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
601-882 |
1.15e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 601 QASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNI------KEERERMRANLEE---LRSQHNKKVEENSTLQQR 671
Cdd:PRK10246 559 QLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIqpwldaQEEHERQLRLLSQrheLQGQIAAHNQQIIQYQQQ 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 672 LEESEGELRKNL------------EELFQVKMERE-----QHQTEIRDLQDQLSEMHDELDSAKRSEDREKGA---LIEE 731
Cdd:PRK10246 639 IEQRQQQLLTALagyaltlpqedeEASWLATRQQEaqswqQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEetvALDN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 732 LLQAKQD---LQDLLIAKEEQEDLLRKRERELTA-LKGALKEEVSShDQEM---DKLKEQYDAELQALRESVEEATKNVE 804
Cdd:PRK10246 719 WRQVHEQclsLHSQLQTLQQQDVLEAQRLQKAQAqFDTALQASVFD-DQQAflaALLDEETLTQLEQLKQNLENQRQQAQ 797
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 805 VLASRSNtsEQDQAGTEMRVKLLQEeneklQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKyEGEIRQLEEALVQ 882
Cdd:PRK10246 798 TLVTQTA--QALAQHQQHRPDGLDL-----TVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQ-DADNRQQQQALMQ 867
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
737-936 |
1.38e-04 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 45.26 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 737 QDLQDLLiaKEEQEDLLRKRERE--------LTALKGALKEEVSS-----------HDQEMDKLKEQYDAELQALRESVE 797
Cdd:cd16269 93 KKLMEQL--EEKKEEFCKQNEEAsskrcqalLQELSAPLEEKISQgsysvpggyqlYLEDREKLVEKYRQVPRKGVKAEE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 798 EATKNVEVLASRSNTSEQ-DQAGTEMRVKLLQEE--NEKLQGRSEELEQRVAQLQRQIEDLKgdeakaketlKKYEGEIR 874
Cdd:cd16269 171 VLQEFLQSKEAEAEAILQaDQALTEKEKEIEAERakAEAAEQERKLLEEQQRELEQKLEDQE----------RSYEEHLR 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 875 QLEEALVQARREEKEAvsARRALENELeaaqrnlsrttQEQKQLSEK-LKEESEQ-KEQLRRLK 936
Cdd:cd16269 241 QLKEKMEEERENLLKE--QERALESKL-----------KEQEALLEEgFKEQAELlQEEIRSLK 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1017-1209 |
1.55e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1017 SQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDlecdkISLERQNKDLKSRIIHLEGSYRSSKEGLVvQ 1096
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL-----VDLSEEAKLLLQQLSELESQLAEARAELA-E 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1097 MEARIAELEDRLESEERDRASLQLSNR---------RLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEE 1167
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPViqqlraqlaELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622953339 1168 IDRLESSKKKLQRELEEQMdmnEHLQGQLNSMKKDLSRLKKL 1209
Cdd:COG3206 318 LEAELEALQAREASLQAQL---AQLEARLAELPELEAELRRL 356
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
569-870 |
1.69e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 569 DNDDATKRKVNLVFEKIQTLKSRaagSAQGNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMR 648
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEK---RDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 649 ANLEELRSQHNKKVEENSTLQQRlEESEGELRKNLEELfqvkmeREQHQTEI------RDLQDQLSEMHDELDSAKrsed 722
Cdd:COG1340 85 EKLNELREELDELRKELAELNKA-GGSIDKLRKEIERL------EWRQQTEVlspeeeKELVEKIKELEKELEKAK---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 723 rekgalieELLQAKQDLQDLLiakeEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDaelqALRESVEEATKN 802
Cdd:COG1340 154 --------KALEKNEKLKELR----AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD----ELRKEADELHKE 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 803 VEVLASRSNTSEQDQAGTEMRVKLLQEENEKLqgrseELEQRVAQLQRQIEDLKGDEAKAKETLKKYE 870
Cdd:COG1340 218 IVEAQEKADELHEEIIELQKELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEKLKKGE 280
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
619-732 |
1.75e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 619 LTTEVAELQRQLQLEVKNQQNIKEERERMRANL---EELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKmEREQ 695
Cdd:PRK09039 58 LNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS-ARAL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622953339 696 HQTE-----IRDLQDQLSEMHDELDSAKrSEDREKGALIEEL 732
Cdd:PRK09039 137 AQVEllnqqIAALRRQLAALEAALDASE-KRDRESQAKIADL 177
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
612-924 |
1.79e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 612 LLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKM 691
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 692 EREQHQTEIRDLQDQLSEMHDELDSAKrsedREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEV 771
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQ----KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 772 SSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQ 851
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 852 IEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKE 924
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
793-943 |
2.28e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 793 RESVEEATKNVEVLASRSNTSEQDQagtemrvkllQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKyege 872
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL----------EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---- 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 873 irQLEEALVQARREEKEAVSARRALENELEAAQRnLSRTTQEQKQLSEKLKE-ESEQKEQLRRLKNEMENER 943
Cdd:PRK00409 574 --EAQQAIKEAKKEADEIIKELRQLQKGGYASVK-AHELIEARKRLNKANEKkEKKKKKQKEKQEELKVGDE 642
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
801-1187 |
2.52e-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: 45.27 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 801 KNVEVLASRSNTSEQDQAGTEMRvkLLQEENEKLQGRSEELEQRVAQLqrqiedlkgdeakaketLKKYEGEIRQLEEAL 880
Cdd:pfam07888 1 KPLDELVTLEEESHGEEGGTDML--LVVPRAELLQNRLEECLQERAEL-----------------LQAQEAANRQREKEK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 881 VQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADI 960
Cdd:pfam07888 62 ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 961 VEasrtSTLELQNQLDEYKEKNRRelaeMQRQLKEKtlEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRS 1040
Cdd:pfam07888 142 TQ----RVLERETELERMKERAKK----AGAQRKEE--EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1041 REQMEQVRNELLQerAARQDLEcdkisLERQNKDLKSRIIHLEGSYRSSK------EGLVVQMEARIAEL-EDRLESEE- 1112
Cdd:pfam07888 212 QDTITTLTQKLTT--AHRKEAE-----NEALLEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELhQARLQAAQl 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1113 -------------------RDRASLQLSN--------------RRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKR 1159
Cdd:pfam07888 285 tlqladaslalregrarwaQERETLQQSAeadkdrieklsaelQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRR 364
|
410 420
....*....|....*....|....*...
gi 1622953339 1160 QVEEAEEEIDRLESSKKKLQRELEEQMD 1187
Cdd:pfam07888 365 ELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
876-1042 |
2.59e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 876 LEEALvqARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMEnerwhlgKTIEKLQK 955
Cdd:COG2433 378 IEEAL--EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD-------ERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 956 EmadiveasrtstlelqnqLDEYKEKNRRELAEmqrqlkektlEAEKSRLtamkmqdEDKVSQLEMELEEERNNSDLLSE 1035
Cdd:COG2433 449 E------------------LSEARSEERREIRK----------DREISRL-------DREIERLERELEEERERIEELKR 493
|
....*..
gi 1622953339 1036 RISRSRE 1042
Cdd:COG2433 494 KLERLKE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1208 |
2.77e-04 |
|
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: 43.76 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1094 VVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDehlsltDQKDQLSLR----LKAMKRQVEEAEEEID 1169
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------YEEQLGNVRnnkeYEALQKEIESLKRRIS 106
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622953339 1170 RLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKA 145
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
602-913 |
3.06e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.69 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 602 ASNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEErerMRANLEELRSQHNKKVEENSTLQQRLEESEGELRK 681
Cdd:pfam04108 12 ANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREG---LEKVLNELKKDFKQLLKDLDAALERLEETLDKLRN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 682 NLEELFQVKMEREQH-------QTEIRDLQDQLSEMHDELDSAKRSEDRekgaLIEELLQAKQDLQDLLIAKEEQedllr 754
Cdd:pfam04108 89 TPVEPALPPGEEKQKtlldfidEDSVEILRDALKELIDELQAAQESLDS----DLKRFDDDLRDLQKELESLSSP----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 755 kreRELTALKGALKEEVSSHDQEM----DKLKEQYDAELQALRESVEEATKNVEVLasrsntsEQDQAGTEMRVKLLQEe 830
Cdd:pfam04108 160 ---SESISLIPTLLKELESLEEEMasllESLTNHYDQCVTAVKLTEGGRAEMLEVL-------ENDARELDDVVPELQD- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 831 neklqgRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKyegeIRQLEEALVQARREEKEavsARRALENELEAAQRNLSR 910
Cdd:pfam04108 229 ------RLDEMENNYERLQKLLEQKNSLIDELLSALQL----IAEIQSRLPEYLAALKE---FEERWEEEKETIEDYLSE 295
|
...
gi 1622953339 911 TTQ 913
Cdd:pfam04108 296 LED 298
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
879-1131 |
3.07e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 879 ALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQkeqlrrlknemenerwhlgktIEKLQKEMA 958
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---------------------LEALQAEID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 959 diveasrtstlELQNQLDEYKEknrrELAEMQRQLKEktleaeksRLTAMKMQDEDkVSQLEMELEEErNNSDLLSeRIS 1038
Cdd:COG3883 69 -----------KLQAEIAEAEA----EIEERREELGE--------RARALYRSGGS-VSYLDVLLGSE-SFSDFLD-RLS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1039 RSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLEgSYRSSKEGLVVQMEARIAELEDRLESEERDRASL 1118
Cdd:COG3883 123 ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE-AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
250
....*....|...
gi 1622953339 1119 QLSNRRLERKVKE 1131
Cdd:COG3883 202 EAELAAAEAAAAA 214
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
688-1002 |
3.24e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGAL 767
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 KEEVSSHDQEMDKLK------EQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEEL 841
Cdd:COG4372 83 EELNEQLQAAQAELAqaqeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 842 EQRVAQLQRQIEDLkgDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEK 921
Cdd:COG4372 163 QEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 922 LKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAE 1001
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
.
gi 1622953339 1002 K 1002
Cdd:COG4372 321 L 321
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
648-988 |
3.34e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 648 RANLEELRSQHNKKVEENSTLQQRleESEGELRKNLEELFQVK-------MEREQHQTEIRDLQDQLSEMHDELDSAKRS 720
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQR--SSNSKLQSNTDENGQLEntslrtvMELPQKSTSSDDDHNRASMQRDEAIAAIDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 721 EDREKGALIEELLQAKqdLQDLL-IAKEEQEDLLRKRERELTALkgalkeevsshdQEMDKL---KEQYDAELQALRESV 796
Cdd:PLN02939 114 EQQTNSKDGEQLSDFQ--LEDLVgMIQNAEKNILLLNQARLQAL------------EDLEKIlteKEALQGKINILEMRL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 797 EEATknvevlaSRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAK---ETLKKYEGEI 873
Cdd:PLN02939 180 SETD-------ARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKddiQFLKAELIEV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 874 RQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQ-----------KQLSEKLKEESEQK----EQLRRLKNE 938
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQydcwwekvenlQDLLDRATNQVEKAalvlDQNQDLRDK 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 939 MENERWHLGKT---------IEKLQK--------------EMADIVEASRTSTLELQNQLDEYKEKNRRELAE 988
Cdd:PLN02939 333 VDKLEASLKEAnvskfssykVELLQQklklleerlqasdhEIHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
610-924 |
3.50e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 610 KDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELrsqhnkkveenstlqQRLEESEGElrknLEELFQv 689
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL---------------EAAALQPGE----EEELEE- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 690 kmERE--QHQTEIRDLqdqLSEMHDELDsakrseDREKGALieellqakqdlqdlliakeeqeDLLRKRERELtalkgal 767
Cdd:COG0497 214 --ERRrlSNAEKLREA---LQEALEALS------GGEGGAL----------------------DLLGQALRAL------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 768 kEEVSSHDQEMDKLKEQydaeLQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQ 847
Cdd:COG0497 254 -ERLAEYDPSLAELAER----LESALIELEEAASELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEELLAYAEE 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 848 LQRQIEDLKGDEakakETLKKYEGEIRQLEEALvqarREEKEAVSARRAlenelEAAQRnLSrttqeqKQLSEKLKE 924
Cdd:COG0497 329 LRAELAELENSD----ERLEELEAELAEAEAEL----LEAAEKLSAARK-----KAAKK-LE------KAVTAELAD 385
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
839-1113 |
3.74e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQrnlsrttQEQKQL 918
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK-------EERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 919 SEKLKEESEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIVEASRTS--TLELQNQLDEYKEKNRRELAEMQRQLKEK 996
Cdd:COG1340 84 NEKLNELREELDELRKELAELNKAG----GSIDKLRKEIERLEWRQQTEvlSPEEEKELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 997 T-LEAEKSRLTAMKMQDED---KVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQN 1072
Cdd:COG1340 160 EkLKELRAELKELRKEAEEihkKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622953339 1073 KDLKSRI-IHLEGSYRSSKEGLVVQMEARIAELEDRLESEER 1113
Cdd:COG1340 240 RELRKELkKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEK 281
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1035-1208 |
4.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1035 ERISRSREQMEQVRN--ELLQE-RAARQDLECDKISLERQnKDLKSRIIHLEGsyrsskeglvvqmEARIAELEDRLESE 1111
Cdd:COG4913 235 DDLERAHEALEDAREqiELLEPiRELAERYAAARERLAEL-EYLRAALRLWFA-------------QRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1112 ERDRASLQLSNRRLERKVKELvmqvDDEHLSLTDQKDQLSLRlkamkrQVEEAEEEIDRLESSKKKLQRELEEQMDMNEH 1191
Cdd:COG4913 301 RAELARLEAELERLEARLDAL----REELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARLEALLAA 370
|
170
....*....|....*..
gi 1622953339 1192 LQGQLNSMKKDLSRLKK 1208
Cdd:COG4913 371 LGLPLPASAEEFAALRA 387
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
905-1060 |
4.57e-04 |
|
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: 44.67 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 905 QRNLSRTTQEQKQLSEKLKeeseqKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTlELQNQLDEYKEKNRr 984
Cdd:pfam05911 668 DGPLVSGSNDLKTEENKRL-----KEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIA-ELRSELASLKESNS- 740
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953339 985 eLAEMQ-RQLKE--KTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQD 1060
Cdd:pfam05911 741 -LAETQlKCMAEsyEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADQE 818
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
831-1172 |
4.87e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 831 NEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLsr 910
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 911 tTQEQKQLSEKLKEESEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIvEASRTSTLELQNQLDEYKEKNRRELAEMQ 990
Cdd:COG4372 83 -EELNEQLQAAQAELAQAQEELESLQEEAEELQ----EELEELQKERQDL-EQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 991 RQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLER 1070
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1071 QNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQL 1150
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
330 340
....*....|....*....|..
gi 1622953339 1151 SLRLKAMKRQVEEAEEEIDRLE 1172
Cdd:COG4372 317 LLAALLELAKKLELALAILLAE 338
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
567-869 |
5.30e-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: 44.44 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 567 SADNDDATKRKVNLVFEKIQTLKSRAAGSAQGNNQAsNSTSEVKDLLEQKSKLTTEVAEL-QRQLQLEVKNQQNIKEE-- 643
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQA-NGELEKASREETFARTALKNARLdLRRLFDEKQSEKDKKNKal 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 644 RERMRANLEELRS-QHNKKVEENStLQQRLEESEGELRKNleelfqvKMEREQHQTE-IRDLQDQLSEMHDELDSAKRSE 721
Cdd:pfam12128 674 AERKDSANERLNSlEAQLKQLDKK-HQAWLEEQKEQKREA-------RTEKQAYWQVvEGALDAQLALLKAAIAARRSGA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 722 DREKGALIE----ELLQAKQDLQDLLIAKEEQEDLLRKRER-----------------ELTALKGALKEEVSSHDQEMDK 780
Cdd:pfam12128 746 KAELKALETwykrDLASLGVDPDVIAKLKREIRTLERKIERiavrrqevlryfdwyqeTWLQRRPRLATQLSNIERAISE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 781 LKEQydaeLQALRESVEEATKNVEvLASRSNTSEQDQAGTEMR-VKLLQEE--NEKLQGRSEELEQRVAQLQRQIEDLKG 857
Cdd:pfam12128 826 LQQQ----LARLIADTKLRRAKLE-MERKASEKQQVRLSENLRgLRCEMSKlaTLKEDANSEQAQGSIGERLAQLEDLKL 900
|
330
....*....|..
gi 1622953339 858 DEAKAKETLKKY 869
Cdd:pfam12128 901 KRDYLSESVKKY 912
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
839-1112 |
5.32e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQR----QIEDLKGDEAKAKetLKKYEGEIRQLEEALVQARR---------------EEKEAVSARRALEN 899
Cdd:PRK05771 16 SYKDEVLEALHElgvvHIEDLKEELSNER--LRKLRSLLTKLSEALDKLRSylpklnplreekkkvSVKSLEELIKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 900 ELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKN---EMENER---------WHLGKTIEKLQKEMADIVEASRTS 967
Cdd:PRK05771 94 ELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNfdlDLSLLLgfkyvsvfvGTVPEDKLEELKLESDVENVEYIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 968 TLELQN-----QLDEYKEKNRRELAEMQ-RQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSR 1041
Cdd:PRK05771 174 TDKGYVyvvvvVLKELSDEVEEELKKLGfERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALY 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622953339 1042 EQMEqvrNELLQERAARQDLECDKISL------ERQNKDLKSRIihlegsyRSSKEGLVVqmearIAELEDRLESEE 1112
Cdd:PRK05771 254 EYLE---IELERAEALSKFLKTDKTFAiegwvpEDRVKKLKELI-------DKATGGSAY-----VEFVEPDEEEEE 315
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
598-807 |
5.34e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 598 GNNQASNSTSEVKDLLEQKSKlttEVAELQRQLQLEVKnqqnikEERERMRANLEELRSQHNKKVEEnstLQQRLEESEG 677
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK---EAEAIKKEALLEAK------EEIHKLRNEFEKELRERRNELQK---LEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 678 ELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMhdeldsakrsedrekgalieellqakqdlqdlliaKEEQEDLLRKRE 757
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQELEKK-----------------------------------EEELEELIEEQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 758 RELTALKGALKEEVSShdQEMDKLKEQYDAELQAL-RESVEEATKNVEVLA 807
Cdd:PRK12704 142 QELERISGLTAEEAKE--ILLEKVEEEARHEAAVLiKEIEEEAKEEADKKA 190
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
701-1002 |
5.57e-04 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 43.44 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 701 RDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKR----ERELTALKGALKEEVSSHDQ 776
Cdd:pfam14915 2 CMLQDEIAMLRLEIDTIKNQNQEKEKKYLEDIEILKEKNDDLQKTLKLNEETLTKTvfqyNGQLNVLKAENTMLNSKLEN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 777 EMDKlKEQYDAELQALRESVEEATKNVEvlasRSNTSEQDQAGTemrvklLQEENEKLQGRSEELEQRVAQLQRQIEDLK 856
Cdd:pfam14915 82 EKQN-KERLETEVESYRSRLAAAIQDHE----QSQTSKRDLELA------FQRERDEWLRLQDKMNFDVSNLRDENEILS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 857 GDEAKAKETLKKYEGEIRQLEEALVQ-------ARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQK 929
Cdd:pfam14915 151 QQLSKAESKANSLENELHRTRDALREktlllesVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQESLEERLAQLQSEN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622953339 930 EQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTlELQNQLDEykEKNrRELAEMQRQLKEKTLEAEK 1002
Cdd:pfam14915 231 MLLRQQLEDAQNKADAKEKTVIDIQDQFQDIVKKLQAES-EKQVLLLE--ERN-KELINECNHLKERLYQYEK 299
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1214 |
5.60e-04 |
|
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: 44.19 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 900 ELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYK 979
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 980 EKNRRELAEMQRQLKEKTLEAEKSRLTamKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQ 1059
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQEAVLE--ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1060 DLECDKISLERQNKDLKSRII-HLEGSYRSSKEGLVVQMEARIAELEDRL----ESEERDRASLQLSNRRLErKVKELVM 1134
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSqEIHIRDAHEVATSIREISCQQHTLTQHIhtlqQQKTTLTQKLQSLCKELD-ILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1135 QVDDEHLSLTDQKDQLSLRLKAMKRQVEEAE------EEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
....*.
gi 1622953339 1209 LPNKVL 1214
Cdd:TIGR00618 491 VVLARL 496
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
607-943 |
5.85e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQLeVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELrknleel 686
Cdd:PRK04863 314 RELAELNEAESDLEQDYQAASDHLNL-VQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARA------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 687 fqvkmerEQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGAlIEELLQAKQ--DLQDLLIAK-EEQEDLLRKRERELTAL 763
Cdd:PRK04863 386 -------EAAEEEVDELKSQLADYQQALDVQQTRAIQYQQA-VQALERAKQlcGLPDLTADNaEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 764 KGALKEEVSSHDQemdkLKEQYDAELQALRESVEEATKNVevlASRSNTSEQDQAGTEmrvKLLQEENEKLQGRSEELEQ 843
Cdd:PRK04863 458 LLSLEQKLSVAQA----AHSQFEQAYQLVRKIAGEVSRSE---AWDVARELLRRLREQ---RHLAEQLQQLRMRLSELEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 844 RVAQ---LQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELE-----------------A 903
Cdd:PRK04863 528 RLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEqlqariqrlaarapawlA 607
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 904 AQRNLSR--------------TTQEQKQLSEKLKEESEQKEQLRRLKNEMENER 943
Cdd:PRK04863 608 AQDALARlreqsgeefedsqdVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
|
| COG4646 |
COG4646 |
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]; |
667-1202 |
6.60e-04 |
|
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair];
Pssm-ID: 443684 [Multi-domain] Cd Length: 1711 Bit Score: 44.09 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 667 TLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSED-----REKGALIEELLQAKQDLQD 741
Cdd:COG4646 1013 QIAEILKAIKELKAVVRKRFTVKQLESTKKLGAGKLKQLDLLALKDLDVPWEPLDVdqlfgRGSRQGNNNFLVTKMRNVA 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 742 LLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTE 821
Cdd:COG4646 1093 GLAFSDAAKLSDYFGKQRYRDELTAGKGVVVATGTDESNLMYELYTAQAYLQLLLLGKQGLTNFDTWASTLEELVTAAEL 1172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 822 MRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKgDEAKAKETLKKYEGEI---RQLEEALVQARREEKEAVSARRALE 898
Cdd:COG4646 1173 APERTAYRANTREAKAVNLPEEDVMIKEAEDAKTA-DELLLPTPEKISGGVAtkpSEVQKELLEELEERAAIVRKNDGEP 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 899 NELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEM--------ENERWHLGKTIEKLQK--EMADIVEASRTST 968
Cdd:COG4646 1252 DRDNMLVITDDGRKAALDQRLDIKTLPDDEGSLVALCVTNIdriwednpESKLTQLVFCDLSTPKgdGTFNDLEDIREKL 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 969 LELQNQLDEYKEKNRRELAEMQRQLKEK--TLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQ 1046
Cdd:COG4646 1332 IEEEIAELEIAFIHLALDDQEKAELFARdrLGAVEKLRISTAKMGAGTNVRLLLEATHDLDVPWRPRDAEQRAGRGRRQG 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1047 VRNELLQERAARQdlecdkislERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQlsNRRLE 1126
Cdd:COG4646 1412 NENEEVEEIRYVT---------ENTFDAYLWQAAETKQKFIAQIMTSKSPVRSLEDVDEAALSYAERKALAAG--RPKEK 1480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1127 RKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEqMDMNEHLQGQLNSMKKD 1202
Cdd:COG4646 1481 EKMDLDIEVLKLKLLDAAALEQLYAEEDKLRKSYLDEEEALEERIEAATKDLRLARAA-SQEEADEQESASKEAAA 1555
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
779-1131 |
7.33e-04 |
|
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: 43.79 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 779 DKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEmrvklLQEENEKLQGRSEELEQRVAQLQRQIEDLKGD 858
Cdd:COG5185 170 QELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESET-----GNLGSESTLLEKAKEIINIEEALKGFQDPESE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 859 EAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRR---- 934
Cdd:COG5185 245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAaeae 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 935 ----------------LKNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQ-NQLDEYKEKNRRELAEMQRQLKEKT 997
Cdd:COG5185 325 qeleeskretetgiqnLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEElDSFKDTIESTKESLDEIPQNQRGYA 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 998 LEAEKSRLTAMKMQDEDkVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQ--NKDL 1075
Cdd:COG5185 405 QEILATLEDTLKAADRQ-IEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRskKEDL 483
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1076 KSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKE 1131
Cdd:COG5185 484 NEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
603-922 |
7.92e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 603 SNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKN 682
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 683 LEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTA 762
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 763 LKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELE 842
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 843 QRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKL 922
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
824-1207 |
8.93e-04 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.51 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 824 VKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDE----AKAKETLKKYEGEIRQLeealvqarREEKEAVSARralen 899
Cdd:pfam15070 38 VRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEeqppAGPSEEEQRLQEEAEQL--------QKELEALAGQ----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 900 eLEAAQR---NLSRTTQEQKQLSEKLKEE----SEQKEQLRRLKNEMENERwhlgKTIEKlqkemadiveaSRTSTLELQ 972
Cdd:pfam15070 105 -LQAQVQdneQLSRLNQEQEQRLLELERAaerwGEQAEDRKQILEDMQSDR----ATISR-----------ALSQNRELK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 973 NQLDEYKE---KNRRELAEMQRQLK-EKTLEAEKSRltamkmqdedKVSQLEMELEEERNNSDLLSERISRSREQMEQVR 1048
Cdd:pfam15070 169 EQLAELQNgfvKLTNENMELTSALQsEQHVKKELAK----------KLGQLQEELGELKETLELKSQEAQSLQEQRDQYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1049 NELLQERAARQDLECDKISLERQnkdlksriihlegsyrsskegLVVQmeariAELEDRLESEE-RDRASLQLSNRRLER 1127
Cdd:pfam15070 239 AHLQQYVAAYQQLASEKEELHKQ---------------------YLLQ-----TQLMDRLQHEEvQGKVAAEMARQELQE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1128 KVKELVMQV-DDEHLsltdqKDQLSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRL 1206
Cdd:pfam15070 293 TQERLEALTqQNQQL-----QAQLSLLANPGEGDGLESEEEEEEAPRPSLSIPEDFESREAMVAFFNSALAQAEEERAEL 367
|
.
gi 1622953339 1207 K 1207
Cdd:pfam15070 368 R 368
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
823-1131 |
9.27e-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: 42.98 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 823 RVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQ-LEEALVQARREEKEAVSARRALENEL 901
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEiVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 902 EAAQRNLSRTTQEQKQ------------LSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEasrtstL 969
Cdd:pfam13868 133 DEFNEEQAEWKELEKEeereederileyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE------L 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 970 ELQNQLDEYKEKNRRElaemQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERnnsdllSERISRSREQMEQVRN 1049
Cdd:pfam13868 207 RAKLYQEEQERKERQK----EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE------EEFERMLRKQAEDEEI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1050 ELLQERAARQDLECDKISLERQNKDLKSRiihlegsyrsskeglvvQMEARIAELEDRLESEERDRASLQLSNRRLERKV 1129
Cdd:pfam13868 277 EQEEAEKRRMKRLEHRRELEKQIEEREEQ-----------------RAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
..
gi 1622953339 1130 KE 1131
Cdd:pfam13868 340 KE 341
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
621-908 |
9.28e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.99 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 621 TEVAELQRQLQLEVKNQQNIKEERERMRANLEELRsqhnKKVEENSTLQQRLEESEGELRKNLEELFqvkMEREQHQTEI 700
Cdd:pfam00038 54 KEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFR----QKYEDELNLRTSAENDLVGLRKDLDEAT---LARVDLEAKI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 701 RDLQDQLSEM---HDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKREREltalkgalkeevsshdqe 777
Cdd:pfam00038 127 ESLKEELAFLkknHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNRE------------------ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 778 mdKLKEQYDAELQALRESVEeatknvevlasrSNTSEQDQAGTEMrvkllQEENEKLQGRSEELEQRVAQ---LQRQIED 854
Cdd:pfam00038 189 --EAEEWYQSKLEELQQAAA------------RNGDALRSAKEEI-----TELRRTIQSLEIELQSLKKQkasLERQLAE 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622953339 855 LKGDEAKAketLKKYEGEIRQLEEALVQAR-------REEKEAVSARRALENELeAAQRNL 908
Cdd:pfam00038 250 TEERYELQ---LADYQELISELEAELQETRqemarqlREYQELLNVKLALDIEI-ATYRKL 306
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
840-1008 |
9.77e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 840 ELEQRVAQLQRQIedLKGDEAKAKETLKKYEGEIRQLE----------EALVQARREEKEAVSARRALENELEAAQRNLS 909
Cdd:pfam00529 50 QLDPTDYQAALDS--AEAQLAKAQAQVARLQAELDRLQaleselaisrQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 910 RTtqeqKQLSEKLKEESEQKEQLRRLKNEMENErwhLGKTIEKLQKEMADIVEASRtstlELQNQLDEYKEKNRRELAEM 989
Cdd:pfam00529 128 RR----RVLAPIGGISRESLVTAGALVAQAQAN---LLATVAQLDQIYVQITQSAA----ENQAEVRSELSGAQLQIAEA 196
|
170
....*....|....*....
gi 1622953339 990 QRQLKEKTLEAEKSRLTAM 1008
Cdd:pfam00529 197 EAELKLAKLDLERTEIRAP 215
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
635-996 |
9.84e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 635 KNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDEL 714
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 715 DSAKRSEDREKgALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRE 794
Cdd:COG4372 90 QAAQAELAQAQ-EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 795 SVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIR 874
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 875 QLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQ 954
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622953339 955 KEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEK 996
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
647-1209 |
9.85e-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: 43.66 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 647 MRANLEELRSQH--NKKVEENSTLQQRL-EESEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAK----- 718
Cdd:pfam10174 76 IQALQDELRAQRdlNQLLQQDFTTSPVDgEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKqtlga 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 719 RSEDREKgalIEELLQAKQdlqdlLIAKEEQEDLLRKREreltalkgalKEEVSSHDQEMDKLKEQYDAELQALRESVEe 798
Cdd:pfam10174 156 RDESIKK---LLEMLQSKG-----LPKKSGEEDWERTRR----------IAEAEMQLGHLEVLLDQKEKENIHLREELH- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 799 atknvevlasRSNTSEQDQAGTEMRVKLLQEENEKLQgrseELEQRVAQLQRQIEDLKGDEAKAKEtlkKYEGEIRQLEE 878
Cdd:pfam10174 217 ----------RRNQLQPDPAKTKALQTVIEMKDTKIS----SLERNIRDLEDEVQMLKTNGLLHTE---DREEEIKQMEV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 879 ALVQARREEKEAVSARRAL---ENELEAAQRNLSRTTQEQ---KQLSEKLKEESEQKEQLRR-LKNEMENERWHLGK--- 948
Cdd:pfam10174 280 YKSHSKFMKNKIDQLKQELskkESELLALQTKLETLTNQNsdcKQHIEVLKESLTAKEQRAAiLQTEVDALRLRLEEkes 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 949 TIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRR------ELAEMQRQL--KEKTLEAEKSRLTAMKmQDEDKVSQLE 1020
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKinvlqkKIENLQEQLrdKDKQLAGLKERVKSLQ-TDSSNTDTAL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1021 MELEEERNNSDLLSERISRSREQMEQVRNELLQeraarqdlecdkiSLERQNKDLKSRIIHLEGSyRSSKEGLVVQMEAR 1100
Cdd:pfam10174 439 TTLEEALSEKERIIERLKEQREREDRERLEELE-------------SLKKENKDLKEKVSALQPE-LTEKESSLIDLKEH 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1101 IAELEDRLESEERDRASLQLSnrrLERKVKELVMQvddEHLSLTDQKDQLSLRLKA-MKRQVEEAEEEIDRLESSKKKLQ 1179
Cdd:pfam10174 505 ASSLASSGLKKDSKLKSLEIA---VEQKKEECSKL---ENQLKKAHNAEEAVRTNPeINDRIRLLEQEVARYKEESGKAQ 578
|
570 580 590
....*....|....*....|....*....|
gi 1622953339 1180 RELEEQMDMNEHLQGQLNSMKKDLSRLKKL 1209
Cdd:pfam10174 579 AEVERLLGILREVENEKNDKDKKIAELESL 608
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
616-878 |
1.09e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.88 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 616 KSKLTTEVAELQRQLQLEVKNQQNIKEERErmranLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQ 695
Cdd:pfam15905 45 KDASTPATARKVKSLELKKKSQKNLKESKD-----QKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 696 HQTEIRDLQDQLSEMH--DELDSAKRSEDREK---GALIEELLQAKQDL----QDLLIAKEEQEDLLRKRERELTALKG- 765
Cdd:pfam15905 120 LSASVASLEKQLLELTrvNELLKAKFSEDGTQkkmSSLSMELMKLRNKLeakmKEVMAKQEGMEGKLQVTQKNLEHSKGk 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 --ALKEEVSSHDQEMDKLKEQ------YDAELQALRESVEEATKNVEVLASRSNTSEQD--------QAGTEMRVKLLQE 829
Cdd:pfam15905 200 vaQLEEKLVSTEKEKIEEKSEteklleYITELSCVSEQVEKYKLDIAQLEELLKEKNDEieslkqslEEKEQELSKQIKD 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622953339 830 ENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEE 878
Cdd:pfam15905 280 LNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
608-990 |
1.40e-03 |
|
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: 42.75 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 608 EVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQhnkkVEENSTLQQRLEESEGELRKNLEELF 687
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESG----DDSGTPGGKKYLLLQKQLEQLQEENF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 688 QV-------KMEREQHQTEIRDLQDQLSEMH----------DELDSAKRSEDREKG--ALIEELLQAKQDLQDL------ 742
Cdd:pfam05622 77 RLetarddyRIKCEELEKEVLELQHRNEELTslaeeaqalkDEMDILRESSDKVKKleATVETYKKKLEDLGDLrrqvkl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 743 --------LIAKEEQEDLLRKR----------ERELTALKGALKEEVSSHDQ---EMDKLKEQYDA----------ELQA 791
Cdd:pfam05622 157 leernaeyMQRTLQLEEELKKAnalrgqletyKRQVQELHGKLSEESKKADKlefEYKKLEEKLEAlqkekerliiERDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 792 LRESVEE--------ATKNVEVLASRSNTSEQDQAGTEM-------RVKLLQEENEKLQGRSEE-LEQRVAQLQRQIEDl 855
Cdd:pfam05622 237 LRETNEElrcaqlqqAELSQADALLSPSSDPGDNLAAEImpaeireKLIRLQHENKMLRLGQEGsYRERLTELQQLLED- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 856 kgdeakaketlkkyegeirqleealVQARREEkeavsarraLENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRL 935
Cdd:pfam05622 316 -------------------------ANRRKNE---------LETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLL 361
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 936 KNEMENERWHLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRRELAEMQ 990
Cdd:pfam05622 362 KQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMK 416
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
610-931 |
1.54e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 610 KDLLEQKSKltteVAELQRQLQLEVKNQQNIKEERERmranleelrsqhNKKVEENSTLQQRLEESEGELRKNLEELFQV 689
Cdd:NF033838 132 KDTLEPGKK----VAEATKKVEEAEKKAKDQKEEDRR------------NYPTNTYKTLELEIAESDVEVKKAELELVKE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 690 KMEREQHQTEIRDLQDQLSEMHDELDSAKR-SEDREKgalieellqAKQDLQDLLIAKEEQEDLLRKRERELTALKGALK 768
Cdd:NF033838 196 EAKEPRDEEKIKQAKAKVESKKAEATRLEKiKTDREK---------AEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 769 EEVSSHDQEMDKlKEQyDAELQAlrESVEEatknvEVLASRSNTSEQDQAGTEMRVkllQEENEKLQGRSEELEQRVA-- 846
Cdd:NF033838 267 RGVLGEPATPDK-KEN-DAKSSD--SSVGE-----ETLPSPSLKPEKKVAEAEKKV---EEAKKKAKDQKEEDRRNYPtn 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 ---QLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQArreeKEAVSARRALENELEAAQRNLSRTTQEQKQ---LSE 920
Cdd:NF033838 335 tykTLELEIAESDVKVKEAELELVKEEAKEPRNEEKIKQA----KAKVESKKAEATRLEKIKTDRKKAEEEAKRkaaEED 410
|
330
....*....|.
gi 1622953339 921 KLKEESEQKEQ 931
Cdd:NF033838 411 KVKEKPAEQPQ 421
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
572-737 |
1.61e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 572 DATKRKVNLVFEKIQTLKSRAAGSaqgNNQASNSTSEVKDLLEQKSKLTTEVAELQRQLQlevKNQQNIKEERERMRA-- 649
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 650 ------------------------------NLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQTE 699
Cdd:COG3883 93 ralyrsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622953339 700 IRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQ 737
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
993-1135 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 993 LKEKTLEAEKSRLTAMKMQDEDKVSqlEMELEEERNNSDLLSERISRSREQMEQVRNEllqeraarqdlecdKISLERQN 1072
Cdd:COG2433 373 IRGLSIEEALEELIEKELPEEEPEA--EREKEHEERELTEEEEEIRRLEEQVERLEAE--------------VEELEAEL 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 1073 KDLKSRIIHLEGSYRSSKEGL---------VVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQ 1135
Cdd:COG2433 437 EEKDERIERLERELSEARSEErreirkdreISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSG 508
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
604-822 |
2.08e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 604 NSTSEVKDLLEQKSKLTTEVAELQRQLQlEVKNQQNIKEERERMRANLEElrSQHNKKVEENSTLQQRLEESEGELRKNL 683
Cdd:PLN03229 541 NEFSRAKALSEKKSKAEKLKAEINKKFK-EVMDRPEIKEKMEALKAEVAS--SGASSGDELDDDLKEKVEKMKKEIELEL 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 684 EELFQvKMEREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEEL-----LQAKQDLQDLLIAKEEQEDLLRKRER 758
Cdd:PLN03229 618 AGVLK-SMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKIERVirssdLKSKIELLKLEVAKASKTPDVTEKEK 696
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 759 eLTALKGALKEEVSS--HDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEM 822
Cdd:PLN03229 697 -IEALEQQIKQKIAEalNSSELKEKFEELEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRVEV 761
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
770-893 |
2.12e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 770 EVSSHDQEMDKLkeqyDAELQALRESVEEATKnvevlasrsntsEQDQAGTEmRVKLLQEENEKLQGRSEELEQRVAQ-- 847
Cdd:COG0542 405 EIDSKPEELDEL----ERRLEQLEIEKEALKK------------EQDEASFE-RLAELRDELAELEEELEALKARWEAek 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622953339 848 -LQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSA 893
Cdd:COG0542 468 eLIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
583-984 |
2.14e-03 |
|
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: 42.42 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 583 EKIQTLKSRAAGSAQGNNQASNSTSEVKDLLEQKSKLTTEVaELQRQLQLEVKNQQNIKEERERMRANLEELRSqHNKKV 662
Cdd:pfam05557 139 ERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEI-QSQEQDSEIVKNSKSELARIPELEKELERLRE-HNKHL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 663 EENSTLQQRLEESEGELRKNL-------EELFQVKMEREQHQTE------------------------IRDLQDQ---LS 708
Cdd:pfam05557 217 NENIENKLLLKEEVEDLKRKLereekyrEEAATLELEKEKLEQElqswvklaqdtglnlrspedlsrrIEQLQQReivLK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 709 EMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDL---LRKRERELTALKGALKEEVSSHDQEMDklKEQY 785
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALvrrLQRRVLLLTKERDGYRAILESYDKELT--MSNY 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 786 DAELQALRESVEEATKNVEVLASrsntseqdqagtEMRVKLlqeenEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKET 865
Cdd:pfam05557 375 SPQLLERIEEAEDMTQKMQAHNE------------EMEAQL-----SVAEEELGGYKQQAQTLERELQALRQQESLADPS 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 866 LKKYEGEIRQLEEALVQARREEKEavsaRRALENELEAAQRNLSRTTQEQK----QLSEK--LKEESEQKEQLRRLKNEM 939
Cdd:pfam05557 438 YSKEEVDSLRRKLETLELERQRLR----EQKNELEMELERRCLQGDYDPKKtkvlHLSMNpaAEAYQQRKNQLEKLQAEI 513
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1622953339 940 ENERWHLGK---TIEKLQKEMADIVEASRTSTLELQNQLDEYKEKNRR 984
Cdd:pfam05557 514 ERLKRLLKKledDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQR 561
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
619-945 |
2.21e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.01 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 619 LTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELrsqHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMEREQHQT 698
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKEL---YLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMENIKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 699 EIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQaKQDLQDLLIAKEEQEDLLRKRE---RELTALKGALKEEVSSHD 775
Cdd:pfam03528 83 VATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVR-EYEVQFHRRLEQERAQWNQYREsaeREIADLRRRLSEGQEEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 776 QEMDKLKEQYDAElqALRESVEEATKnvEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSE---ELEQRVAQLQRQI 852
Cdd:pfam03528 162 LEDEMKKAQEDAE--KLRSVVMPMEK--EIAALKAKLTEAEDKIKELEASKMKELNHYLEAEKScrtDLEMYVAVLNTQK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 853 EDLKGDEAKAKETL----KKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQ 928
Cdd:pfam03528 238 SVLQEDAEKLRKELhevcHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHK 317
|
330
....*....|....*..
gi 1622953339 929 KEQLRRLKNEMENERWH 945
Cdd:pfam03528 318 RARTHKEKETLKSDREH 334
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
966-1208 |
2.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 966 TSTLELQNQLDEYKEKnRRELAEMQRQLKEK--TLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSRE- 1042
Cdd:COG1340 1 SKTDELSSSLEELEEK-IEELREEIEELKEKrdELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1043 ------QMEQVRNELLQERAARQDLECDKISLERqnkdLKSRIIHLEGSYRSSKEGLVVQME--ARIAELEDRLE----- 1109
Cdd:COG1340 80 rdelneKLNELREELDELRKELAELNKAGGSIDK----LRKEIERLEWRQQTEVLSPEEEKElvEKIKELEKELEkakka 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1110 -------SEERDRA-SLQLSNRRLERKVKELVMQVDDEHLSLTDQK---DQLSLRLKAMKRQVEEAEEEIDRLESSKKKL 1178
Cdd:COG1340 156 lekneklKELRAELkELRKEAEEIHKKIKELAEEAQELHEEMIELYkeaDELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260 270
....*....|....*....|....*....|
gi 1622953339 1179 QRELEEqmdmnehLQGQLNSMKKDLSRLKK 1208
Cdd:COG1340 236 QKELRE-------LRKELKKLRKKQRALKR 258
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
821-1022 |
2.48e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 41.59 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 821 EMRVKLLQEENEKLQGRSEE-------LEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEK---EA 890
Cdd:pfam15742 157 EERIKEASENEAKLKQQYQEeqqkrklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRksdEH 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 891 VSARRALENELEAAQRNLSRTTQEQKQLSEKLKEE--------SEQKEQLRRLKNEMENERWHLGKTIEKLQKEMAdIVE 962
Cdd:pfam15742 237 LKSNQELSEKLSSLQQEKEALQEELQQVLKQLDVHvrkynekhHHHKAKLRRAKDRLVHEVEQRDERIKQLENEIG-ILQ 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 963 ASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQdeDKVSQLEME 1022
Cdd:pfam15742 316 QQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEELIKNNKRTISSVQ--NRVNFLDEE 373
|
|
| cdk7 |
TIGR00570 |
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ... |
898-997 |
2.55e-03 |
|
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). 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: 129661 [Multi-domain] Cd Length: 309 Bit Score: 41.33 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 898 ENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENErwhlgktiEKLQKE--MADIVEASRTSTLELQNQL 975
Cdd:TIGR00570 127 KENKDVIQKNKEKSTREQEELEEALEFEKEEEEQRRLLLQKEEEE--------QQMNKRknKQALLDELETSTLPAAELI 198
|
90 100
....*....|....*....|..
gi 1622953339 976 DEYKEKNRRELAEMQRQLKEKT 997
Cdd:TIGR00570 199 AQHKKNSVKLEMQVEKPKPEKP 220
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
762-1059 |
2.57e-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: 42.05 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 762 ALKGALKEEVSSHDQEMDKLKEQYDAELQAlresVEEATKNVEvlASRSNTSEQDQAGTEMRVKLLQEENEKLQgrseel 841
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQA----VKAHTDSLK--EASDTAEISREKATDSALQKAEALAEKLK------ 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 842 EQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEqkqLSEK 921
Cdd:pfam09731 197 EVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPD---IIPV 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 922 LKE-ESEQKEQLRRLKNEMENErwhlgktIEKLQKEMADIVEASRtstLELQNQLDE-YKEKNRRELAEMQRQLKEKTLE 999
Cdd:pfam09731 274 LKEdNLLSNDDLNSLIAHAHRE-------IDQLSKKLAELKKREE---KHIERALEKqKEELDKLAEELSARLEEVRAAD 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622953339 1000 AEKSRLT---AMKMQDEDKVSQLEMELE------EERNNSDLLSERISRSREQMEQVRNELLQERAARQ 1059
Cdd:pfam09731 344 EAQLRLEferEREEIRESYEEKLRTELErqaeahEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRL 412
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
607-1205 |
2.59e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 607 SEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQ--RLEESEGELRKNLE 684
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEKIERYQEDLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 685 ELfqvkMEREQHQTEIR-DLQDQLSEMHDELDSAKRSEDREKGAL------IEEL----LQAKQDLQdlliAKEEQEDLL 753
Cdd:COG3096 358 EL----TERLEEQEEVVeEAAEQLAEAEARLEAAEEEVDSLKSQLadyqqaLDVQqtraIQYQQAVQ----ALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 754 RKRERELTALKG---ALKEEVSSHDQEMDKLKEQYDAElQALRESVEEATKNVEVLASRSNTSEQDQAGTEM-----RVK 825
Cdd:COG3096 430 GLPDLTPENAEDylaAFRAKEQQATEEVLELEQKLSVA-DAARRQFEKAYELVCKIAGEVERSQAWQTARELlrryrSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 826 LLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEAlvQARREEkeavsarraLENELEAAQ 905
Cdd:COG3096 509 ALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAEL--EAQLEE---------LEEQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 906 RNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERWHLGKTIEKLQKemadiVEASRTSTLELQNQLdeykEKNRRE 985
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE-----VTAAMQQLLEREREA----TVERDE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 986 LAEMQRQLKEKTLE------AEKSRLTAMKMQ------------------------------------------------ 1011
Cdd:COG3096 649 LAARKQALESQIERlsqpggAEDPRLLALAERlggvllseiyddvtledapyfsalygparhaivvpdlsavkeqlagle 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1012 ----------------DEDKVSQLEME-------------------------------LEEERNNSDLLSERISRSR-EQ 1043
Cdd:COG3096 729 dcpedlyliegdpdsfDDSVFDAEELEdavvvklsdrqwrysrfpevplfgraarekrLEELRAERDELAEQYAKASfDV 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1044 MEQVR----------------------NELLQERAARQDLECDKISLERQNKDLKSRIIHLEGSYrSSKEGLVVQM---- 1097
Cdd:COG3096 809 QKLQRlhqafsqfvgghlavafapdpeAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL-QLLNKLLPQAnlla 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1098 ----EARIAELEDRLESEERDRASLQLSNRRLERKVKEL-VMQVDDE-HLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRL 1171
Cdd:COG3096 888 detlADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVaVLQSDPEqFEQLQADYLQAKEQQRRLKQQIFALSEVVQRR 967
|
730 740 750
....*....|....*....|....*....|....*
gi 1622953339 1172 ES-SKKKLQRELEEQMDMNEHLQGQLNSMKKDLSR 1205
Cdd:COG3096 968 PHfSYEDAVGLLGENSDLNEKLRARLEQAEEARRE 1002
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
728-1054 |
2.59e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 728 LIEELLQAK--QDLQDLLIAKEEQEDLLRKRERELTALkgaLKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEV 805
Cdd:pfam13868 11 LNSKLLAAKcnKERDAQIAEKKRIKAEEKEEERRLDEM---MEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 806 LasRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGE--------IRQLE 877
Cdd:pfam13868 88 K--RQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREederileyLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 878 EALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENERwHLGKTIEKLQKEM 957
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKA-RQRQELQQAREEQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 958 ADIVEASRTSTLELQNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERI 1037
Cdd:pfam13868 245 IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
330
....*....|....*..
gi 1622953339 1038 SRSREQMEQVRNELLQE 1054
Cdd:pfam13868 325 AERRERIEEERQKKLKE 341
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
767-934 |
2.66e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 42.15 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 767 LKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVA 846
Cdd:pfam09730 21 LLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREARLLQDYS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 847 QLQRQIEDLKGDEAKAKETLKKYEG---EIRQLEEALVQARREEKEAVSARRALENELEAAQrnlsrttqeqkqlsEKLK 923
Cdd:pfam09730 101 ELEEENISLQKQVSVLKQNQVEFEGlkhEITRKEEETELLNSQLEEAIRLREIAERQLDEAL--------------ETLK 166
|
170
....*....|.
gi 1622953339 924 EESEQKEQLRR 934
Cdd:pfam09730 167 TEREQKNSLRK 177
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
839-924 |
2.75e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 39.09 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQL 918
Cdd:pfam13863 20 EEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIEELKSEISKL 99
|
....*.
gi 1622953339 919 SEKLKE 924
Cdd:pfam13863 100 EEKLEE 105
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
698-940 |
2.80e-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: 40.86 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 698 TEIRDLQDQLSEmhdeldsaKRSEDREKGALIEELLQAKQDL-QDlliAKEEQEDLLRKRERELTALKGAlkEEVSSHDQ 776
Cdd:pfam06008 19 YNLENLTKQLQE--------YLSPENAHKIQIEILEKELSSLaQE---TEELQKKATQTLAKAQQVNAES--ERTLGHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 777 EMDKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAGT---EMRVK---LLQEENEKLQGRSEELEQRV-AQLQ 849
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRmlgEIRSRdfgTQLQNAEAELKAAQDLLSRIqTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 850 RQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQK 929
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTARDSL 245
|
250
....*....|.
gi 1622953339 930 EQLRRLKNEME 940
Cdd:pfam06008 246 DAANLLLQEID 256
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
643-982 |
3.06e-03 |
|
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: 41.98 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 643 ERERMRANLEELRSQHNKKVEENSTLQQRLEE---SEGELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMHDELDSAKR 719
Cdd:COG5244 237 ELERLRRQLVSLMSSHGIEVEENSRLKATLEKfqsLELKVNTLQEELYQNKLLKKFYQIYEPFAQAALSSQLQYLAEVIE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 720 SEDREKGALIE--ELLQAKQDLQDLL---IAKEEQEDLLRKRERELTALKGA------LKEEVSSHD----QEMDKLKEQ 784
Cdd:COG5244 317 SENFGKLENIEihIILKVLSSISYALhiyTIKNTPDHLETTLQCFVNIAPISmwlsefLQRKFSSKQetafSICQFLEDN 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 785 YDAE--LQALRESVEE-ATKNVEVLASRSNTSEQD---QAGTEMRVKLLQEENEKlqgrsEELEQRVAQLQRQIEDLKGD 858
Cdd:COG5244 397 KDVTliLKILHPILETtVPKLLAFLRTNSNFNDNDtlcLIGSLYEIARIDKLIGK-----EEISKQDNRLFLYPSCDITL 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 859 EAKAKETLKKYEGEIRQLEEALVQArreekeavsarRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQ-KEQLRRLKN 937
Cdd:COG5244 472 SSILTILFSDKLEVFFQGIESLLEN-----------ITIFPEQPSQQTSDSENIKENSLLSDRLNEENIRlKEVLVQKEN 540
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622953339 938 EMENERwhLGKTIEKLQKEMADIVEASRTSTLELQNQLDEYKEKN 982
Cdd:COG5244 541 MLTEET--KIKIIIGRDLERKTLEENIKTLKVELNNKNNKLKEEN 583
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
603-1214 |
3.06e-03 |
|
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: 41.96 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 603 SNSTSEVKDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERE-RMRAnleELRSQHNKKVEENSTLQQRLEESEGELRK 681
Cdd:TIGR01612 489 SKQDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNIIGFDIDqNIKA---KLYKEIEAGLKESYELAKNWKKLIHEIKK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 682 NLEELFQVKMEREqhqTEIRDLQDQLSEMHDEL---------------------DSAKRSEDREK-----GALIEEL--- 732
Cdd:TIGR01612 566 ELEEENEDSIHLE---KEIKDLFDKYLEIDDEIiyinklklelkekiknisdknEYIKKAIDLKKiiennNAYIDELaki 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 733 --LQAKQDLQDL-LIAKEEQEDLLRKRERELTALKGALKEEVSSHD-------QEMDKLKEQYDAELQALrESVEEATKN 802
Cdd:TIGR01612 643 spYQVPEHLKNKdKIYSTIKSELSKIYEDDIDALYNELSSIVKENAidntedkAKLDDLKSKIDKEYDKI-QNMETATVE 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 803 VEVLASRSNTSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLkgdeAKAKETLKKYEGEIRQL------ 876
Cdd:TIGR01612 722 LHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDY----AKEKDELNKYKSKISEIknhynd 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 877 --------EEALVQARREEKEAVSARRALENELEAAQRNLSRTTQE-----------QKQLSEKLKEESEQ-KEQLRRLK 936
Cdd:TIGR01612 798 qinidnikDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDflnkvdkfinfENNCKEKIDSEHEQfAELTNKIK 877
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 937 NEMENERwhLGKTIEKLQKEMADIVEASRTSTLELQN-----QLDEYKE--KNRRELAE----MQRQLKEK--------- 996
Cdd:TIGR01612 878 AEISDDK--LNDYEKKFNDSKSLINEINKSIEEEYQNintlkKVDEYIKicENTKESIEkfhnKQNILKEIlnknidtik 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 997 -TLEAEKSRLTAMKMQDEDKVSQLEMELEE------ERNNSDLLsERISRSREQMEQVRNELLQERAARQDLECDKIslE 1069
Cdd:TIGR01612 956 eSNLIEKSYKDKFDNTLIDKINELDKAFKDaslndyEAKNNELI-KYFNDLKANLGKNKENMLYHQFDEKEKATNDI--E 1032
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1070 RQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSN-RRLERKVKELVMQ--VDDEHLSLTDQ 1146
Cdd:TIGR01612 1033 QKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNfNEIKEKLKHYNFDdfGKEENIKYADE 1112
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 1147 KDQLSLRLKAMKRQVeeaEEEIDRLESSKKKLQRELEEqmdmnehlqgqlnsMKKDLSRLKKLPNKVL 1214
Cdd:TIGR01612 1113 INKIKDDIKNLDQKI---DHHIKALEEIKKKSENYIDE--------------IKAQINDLEDVADKAI 1163
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
822-924 |
3.09e-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: 40.84 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 822 MRVKLLQEENEKLQGRSEELEQRV-------AQLQRQIEDLKgDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSAR 894
Cdd:pfam15294 133 MEIERLKEENEKLKERLKTLESQAtqaldekSKLEKALKDLQ-KEQGAKKDVKSNLKEISDLEEKMAALKSDLEKTLNAS 211
|
90 100 110
....*....|....*....|....*....|....
gi 1622953339 895 RALENELEAaqrNLSRTTQE----QKQLSEKLKE 924
Cdd:pfam15294 212 TALQKSLEE---DLASTKHEllkvQEQLEMAEKE 242
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
635-944 |
3.12e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 635 KNQQNIKEERERMRANLEELrSQHNKKVEENSTL--QQRLEEsegelrknLEELFQVKMEREQHQTEIRDLQDQLSEMHD 712
Cdd:PLN02939 114 EQQTNSKDGEQLSDFQLEDL-VGMIQNAEKNILLlnQARLQA--------LEDLEKILTEKEALQGKINILEMRLSETDA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 713 ELDSAKRSEdrekgalieellqakqdlqdllIAKEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLKEQ---YDAEL 789
Cdd:PLN02939 185 RIKLAAQEK----------------------IHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEEnmlLKDDI 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 790 QALRESVEEATKNVEVLAsrsnTSEQDQAGTEMRVKLL-------QEENEKLQGRSEE-LEQRVAQLQRQIEDLKGDEAK 861
Cdd:PLN02939 243 QFLKAELIEVAETEERVF----KLEKERSLLDASLRELeskfivaQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 862 AKETLKKY---EGEIRQLEEALVQArREEKEAVSARRALENELEAAQRNLSRTTQE---QKQLSE-----------KLKE 924
Cdd:PLN02939 319 AALVLDQNqdlRDKVDKLEASLKEA-NVSKFSSYKVELLQQKLKLLEERLQASDHEihsYIQLYQesikefqdtlsKLKE 397
|
330 340
....*....|....*....|
gi 1622953339 925 ESEqKEQLRRLKNEMENERW 944
Cdd:PLN02939 398 ESK-KRSLEHPADDMPSEFW 416
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
838-912 |
3.17e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 41.08 E-value: 3.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 838 SEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQ---LEEALVQARREEKEAVSARRALENELEAAQRNLSRTT 912
Cdd:COG0845 56 PPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLKKgavSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTT 133
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
624-857 |
3.18e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 624 AELQRQLQLEVKNQ-QNIKEERERMRANLEELRSQHNKKVEENSTLQqrLEESEGELRKNLEELFQVKMEREQHQTEIRD 702
Cdd:pfam09787 2 LESAKQELADYKQKaARILQSKEKLIASLKEGSGVEGLDSSTALTLE--LEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 703 LQDQLSemhdeldsakrsedrekgaliEELLQAKQDLQDLliakEEQEDLLRKRERELTALKGALKEEVSSHDQEMDKLK 782
Cdd:pfam09787 80 LEAQQQ---------------------EEAESSREQLQEL----EEQLATERSARREAEAELERLQEELRYLEEELRRSK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622953339 783 EQYDAELQAlRESVEEATKNVEVLASRSNTSEQDqagTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKG 857
Cdd:pfam09787 135 ATLQSRIKD-REAEIEKLRNQLTSKSQSSSSQSE---LENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
893-1058 |
3.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 893 ARRALENELEAAQRNLSRTTQEQKQLSEKLKEE--SEQKEQLRRLKNEMENErwhlgktieklqkemadiveasrtstle 970
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEalLEAKEEIHKLRNEFEKE---------------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 971 lqnqldeYKEKnRRELAEMQRQL--KEKTLEAEKSRLTAMK----------MQDEDKVSQLEMELEEERNNSDLLSERIS 1038
Cdd:PRK12704 77 -------LRER-RNELQKLEKRLlqKEENLDRKLELLEKREeelekkekelEQKQQELEKKEEELEELIEEQLQELERIS 148
|
170 180
....*....|....*....|....*.
gi 1622953339 1039 R-SREQ-----MEQVRNELLQERAAR 1058
Cdd:PRK12704 149 GlTAEEakeilLEKVEEEARHEAAVL 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
975-1131 |
3.76e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 975 LDEYKEKNRRELAEmqRQLKEKTLEAE---KSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERISRSREQMEQvRNEL 1051
Cdd:PRK12704 28 IAEAKIKEAEEEAK--RILEEAKKEAEaikKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-KLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1052 LQERaaRQDLECDKISLERQNKDLKSRIIHLEGSYRSSKEGLVVQM-----EARiAELEDRLESEERDRASLQLsnRRLE 1126
Cdd:PRK12704 105 LEKR--EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAK-EILLEKVEEEARHEAAVLI--KEIE 179
|
....*
gi 1622953339 1127 RKVKE 1131
Cdd:PRK12704 180 EEAKE 184
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
610-933 |
3.78e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.43 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 610 KDLLEQKSKLTTEVAELQRQLQLEvknQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQV 689
Cdd:pfam15964 363 SELERQKERLEKELASQQEKRAQE---KEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 690 KMEREQHQTEI-RDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIA--------KEEQEDLLRKRER-- 758
Cdd:pfam15964 440 LASQEMDVTKVcGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLElseskqrlEQAQQDAARAREEcl 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 759 ELTALKGALKEEVSSHDQEMDKLKEQYDAE-----LQALRESVEEATKNVEVLASRSNTSEQDQAGTEMRVKLLQEENEK 833
Cdd:pfam15964 520 KLTELLGESEHQLHLTRLEKESIQQSFSNEakaqaLQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 834 LQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQ 913
Cdd:pfam15964 600 CCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLS 679
|
330 340
....*....|....*....|
gi 1622953339 914 EQKQLSEKLKEESEQKEQLR 933
Cdd:pfam15964 680 KQNQLFKERQNLTEEVQSLR 699
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
962-1195 |
3.89e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.54 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 962 EASRTSTLELQNQLDEYKEKNRRELAE-MQRQLKEKTLEAEKSRLTA-----MKMQDEDKVSQLEMELEEERNNSDLLSE 1035
Cdd:NF033838 39 EVRGGNNPTVTSSGNESQKEHAKEVEShLEKILSEIQKSLDKRKHTQnvalnKKLSDIKTEYLYELNVLKEKSEAELTSK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1036 RISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKsriihlEGSYRSSKEGLVVQMEARIAELEDRLESEERDR 1115
Cdd:NF033838 119 TKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQK------EEDRRNYPTNTYKTLELEIAESDVEVKKAELEL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1116 ASLQLSNRRLERKVKELVMQVDDEHLSLTdqkdqlslRLKAMKRQVEEAEEEidrlesSKKKLQRELEEQMDMNEHLQGQ 1195
Cdd:NF033838 193 VKEEAKEPRDEEKIKQAKAKVESKKAEAT--------RLEKIKTDREKAEEE------AKRRADAKLKEAVEKNVATSEQ 258
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
680-924 |
4.15e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 680 RKNLEELFQVKMEREQH---QTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDlliaKEEQEDLLRKR 756
Cdd:PHA02562 153 RKLVEDLLDISVLSEMDklnKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIAR----KQNKYDELVEE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 757 ERELTALKGALKEEVSSHDQEMdklkEQYDAELQALRESVEEATKNVEVLASRSN---------TSEQDQAGTEMRVKLL 827
Cdd:PHA02562 229 AKTIKAEIEELTDELLNLVMDI----EDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 828 QEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKE---AVSARRALENELEAA 904
Cdd:PHA02562 305 KDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|
gi 1622953339 905 QRNLSRTTqeqKQLSEKLKE 924
Cdd:PHA02562 385 QDELDKIV---KTKSELVKE 401
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
605-792 |
4.19e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 605 STSEVKDLLEQKSKLTTEVAELQRQ---LQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRK 681
Cdd:smart00787 107 ASPDVKLLMDKQFQLVKTFARLEAKkmwYEWRMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 682 NLEELFQVKMEREQH-QTEIRDLQDQLSEMHDELDsakrsedrEKGALIEELLQAKQDLQDLLIAKEEQEDLLRKrerEL 760
Cdd:smart00787 187 ELRQLKQLEDELEDCdPTELDRAKEKLKKLLQEIM--------IKVKKLEELEEELQELESKIEDLTNKKSELNT---EI 255
|
170 180 190
....*....|....*....|....*....|..
gi 1622953339 761 TALKGALKEEVSSHDQEMDKLKEQYDaELQAL 792
Cdd:smart00787 256 AEAEKKLEQCRGFTFKEIEKLKEQLK-LLQSL 286
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
766-858 |
4.31e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 40.36 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 766 ALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRSntSEQDQAGTEMRVKLLQEENEKLQGRSEELEQRV 845
Cdd:pfam03961 142 KTEIEVGVDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKA--RGQLPPEKREQLEKLLETKNKLSEELEELEEEL 219
|
90
....*....|...
gi 1622953339 846 AQLQRQIEDLKGD 858
Cdd:pfam03961 220 KELKEELESLLGE 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
924-1139 |
4.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 924 EESEQKEQLRRLKNEMENERwhlgKTIEKLQKEMADIVEASRTSTLELQnQLDEYKEKNRRELAEMQRQLKEKTlEAEKS 1003
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQ----AELDALQAELEELNEEYNELQAELE-ALQAEIDKLQAEIAEAEAEIEERR-EELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1004 RLTAMKMQDEDkVSQLEMELEEErNNSDLLSeRISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSriihle 1083
Cdd:COG3883 91 RARALYRSGGS-VSYLDVLLGSE-SFSDFLD-RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA------ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622953339 1084 gsyrsskegLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDE 1139
Cdd:COG3883 162 ---------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1108-1214 |
4.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1108 LESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQ-LSLR---LKAMKRQVEEAEEEIDRLESSKKKLQRELE 1183
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKeLRERrneLQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110
....*....|....*....|....*....|.
gi 1622953339 1184 EQMDMNEHLQGQLNSMKKDLSRLKKLPNKVL 1214
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1067-1208 |
4.66e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.53 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1067 SLERQNKDLKSRIIHLEGSYRSSKEGLVVQMEARIAELEDRLESEERDRASLQLSNRRLERKVKELVMQVDDEHLSLTDQ 1146
Cdd:pfam08614 18 LLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLRED 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622953339 1147 kdqlSLRLKAMKRQVEEAEEEIDRLESSKKKLQRELEEQMDMNEHLQGQLNSMKKDLSRLKK 1208
Cdd:pfam08614 98 ----ERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEKLRKLEK 155
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
814-1066 |
4.69e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 814 EQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDlkgdeakAKETLKKYEGEIRQLEEALVQARREEKEavsA 893
Cdd:PRK11637 53 QQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRE-------TQNTLNQLNKQIDELNASIAKLEQQQAA---Q 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 894 RRALENELEAAQRnlsrttQEQKQLSEKL--KEESEQKEQLRRLKNEMENERwhlGKTIEKLQKEmadiveasrTSTLEL 971
Cdd:PRK11637 123 ERLLAAQLDAAFR------QGEHTGLQLIlsGEESQRGERILAYFGYLNQAR---QETIAELKQT---------REELAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 972 QNQLDEYKEKNRRELAEMQRQLKEKTLEAEKSRltamkmqdEDKVSQLEMELEEERNNSDLLSERISRSREQMEQVRNEl 1051
Cdd:PRK11637 185 QKAELEEKQSQQKTLLYEQQAQQQKLEQARNER--------KKTLTGLESSLQKDQQQLSELRANESRLRDSIARAERE- 255
|
250
....*....|....*
gi 1622953339 1052 LQERAARQDLECDKI 1066
Cdd:PRK11637 256 AKARAEREAREAARV 270
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
610-855 |
4.90e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 41.20 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 610 KDLLEQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRL------------EESEG 677
Cdd:pfam15070 200 KELAKKLGQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEKEELHKQYllqtqlmdrlqhEEVQG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 678 --ELRKNLEELFQVKMEREQHQTEIRDLQDQLSEMH-----DELDSAKRSEDREKGAL-IEELLQAKQDLQDLLIAKeeq 749
Cdd:pfam15070 280 kvAAEMARQELQETQERLEALTQQNQQLQAQLSLLAnpgegDGLESEEEEEEAPRPSLsIPEDFESREAMVAFFNSA--- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 750 edlLRKRERELTALKGALKEEvsshdqemdKLKEQYDAELQALRESVEEATKNVEVLASRSNTSEQDQAgtemrvklLQE 829
Cdd:pfam15070 357 ---LAQAEEERAELRRQLKEQ---------KRRCRRLAQQAAPAQEEPEHEAHAPGTGGDSVPVEVHQA--------LQV 416
|
250 260
....*....|....*....|....*.
gi 1622953339 830 ENEKLQGRSEELEQRVAQLQRQIEDL 855
Cdd:pfam15070 417 AMEKLQSRFTELMQEKADLKERVEEL 442
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
615-929 |
5.07e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 615 QKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHN---KKVEENstLQQRLEESEGELRKNLEELFQVKM 691
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQeleEQIEER--EQKRQEEYEEKLQEREQMDEIVER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 692 EREQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDLLIAKEEQEDLLRKRERELTALKGALKEEV 771
Cdd:pfam13868 110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 772 SSHDQEMDKLKEQYDaELQALRESVEEATKNVEVLASRSNTSEQDQAgtEMRVKLLQEENEKLQGRSEELEQRVAQLQRQ 851
Cdd:pfam13868 190 RAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQ--ELQQAREEQIELKERRLAEEAEREEEEFERM 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622953339 852 IEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRnlsrttQEQKQLSEKLKEESEQK 929
Cdd:pfam13868 267 LRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR------EEEAERRERIEEERQKK 338
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
693-1038 |
5.44e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 693 REQHQTEIRDLQDQLSEMHDELDSAKRSEDREKGALIEELLQAKQDLQDL-----LIAKEEQEDLLRKRERELTA----- 762
Cdd:PLN03229 424 REAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKEIDLeyteaVIAMGLQERLENLREEFSKAnsqdq 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 763 -LKGALKEEVsshdqemDKLKEQYDAELQAL--RESVEEATKNVEVLASRSNTSEQDQAGTEMRvkllQEENEKLQgrsE 839
Cdd:PLN03229 504 lMHPVLMEKI-------EKLKDEFNKRLSRApnYLSLKYKLDMLNEFSRAKALSEKKSKAEKLK----AEINKKFK---E 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 840 ELEQrvAQLQRQIEDLKGDEAKAKetLKKYEGEIRQLEEALVQARRE-EKEAVSARRALENELEAAQRNLSRTTQEQ--- 915
Cdd:PLN03229 570 VMDR--PEIKEKMEALKAEVASSG--ASSGDELDDDLKEKVEKMKKEiELELAGVLKSMGLEVIGVTKKNKDTAEQTppp 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 916 --KQLSEKLKEESEQKeqLRRLKNEMEnerwhLGKTIEKLQKEMAdivEASRTSTLELQNQLDEYKEKNRRELAEM--QR 991
Cdd:PLN03229 646 nlQEKIESLNEEINKK--IERVIRSSD-----LKSKIELLKLEVA---KASKTPDVTEKEKIEALEQQIKQKIAEAlnSS 715
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622953339 992 QLKEKTLEAEKSRLTAMKMQDEDKVSQLEMELEEERNNSDLLSERIS 1038
Cdd:PLN03229 716 ELKEKFEELEAELAAARETAAESNGSLKNDDDKEEDSKEDGSRVEVN 762
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
614-809 |
5.89e-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: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 614 EQKSKLTTEVAELQRQLQLEVKNQQNIKEERERMRANLEELRSQHNKKVEENSTLQQRLEESEGELRKNLEELFQVKMER 693
Cdd:pfam05483 573 ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKF 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 694 EQ----HQTEIRDLQDQLSEMHDELDSAKRSED-------------REKGALIEELLQAKQDLQDLLIAKEEQE-DLLRK 755
Cdd:pfam05483 653 EEiidnYQKEIEDKKISEEKLLEEVEKAKAIADeavklqkeidkrcQHKIAEMVALMEKHKHQYDKIIEERDSElGLYKN 732
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622953339 756 RERELTALKGALKEEVSSHDQEMDKLKEQYDAELQALRESVEEATKNVEVLASR 809
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
858-1025 |
6.13e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 858 DEAKAK---ETLKKYEgEIRQLEEALVQARREekeavsaRRALENELEAAqrnlsrttqEQKQLSEKLKEESEQKEQLRR 934
Cdd:COG0542 396 DEAAARvrmEIDSKPE-ELDELERRLEQLEIE-------KEALKKEQDEA---------SFERLAELRDELAELEEELEA 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 935 LKNEMENERwhlgKTIEKLQKEMADIvEASRTSTLELQNQLDEYKEknrrELAEMQRQLKEkTLEAEK-----SRLT--- 1006
Cdd:COG0542 459 LKARWEAEK----ELIEEIQELKEEL-EQRYGKIPELEKELAELEE----ELAELAPLLRE-EVTEEDiaevvSRWTgip 528
|
170 180
....*....|....*....|.
gi 1622953339 1007 AMKM-QDE-DKVSQLEMELEE 1025
Cdd:COG0542 529 VGKLlEGErEKLLNLEEELHE 549
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
839-928 |
7.68e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 839 EELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQl 918
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQ- 216
|
90
....*....|
gi 1622953339 919 seKLKEESEQ 928
Cdd:PRK11448 217 --KRKEITDQ 224
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
654-856 |
7.90e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 40.41 E-value: 7.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 654 LRSQHNKKveenstlqQRLEESEGELRKNLeelfqVKMEREQHQTEIRDLQDQ---LSEMHDELdsAKRSEDrekgalie 730
Cdd:pfam10168 544 FREEYLKK--------HDLAREEIQKRVKL-----LKLQKEQQLQELQSLEEErksLSERAEKL--AEKYEE-------- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 731 ellqakqdlqdlliAKEEQEDLLRKRERELTALKGALKEEVSShDQEMDKLKEQYDAELQALRESVEEATKNVEVLASRS 810
Cdd:pfam10168 601 --------------IKDKQEKLMRRCKKVLQRLNSQLPVLSDA-EREMKKELETINEQLKHLANAIKQAKKKMNYQRYQI 665
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622953339 811 NTSEQDQAGTEMRVKLLQEENEKlqgrsEELEQRVAQLQRQIEDLK 856
Cdd:pfam10168 666 AKSQSIRKKSSLSLSEKQRKTIK-----EILKQLGSEIDELIKQVK 706
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1015-1184 |
8.49e-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: 39.52 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1015 KVSQLEMELEEERNNSDLLSERISRSREQMEQVRNELLQERAARQDLECDKISLERQNKDLKSRIIHLE---GSYRSSKE 1091
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 1092 glvvqMEARIAELEdrleseerdraSLQLSNRRLERKVKELVMQVDDEHLSLTDQKDQLSLRLKAMKRQVEEAEEEIDRL 1171
Cdd:COG1579 91 -----YEALQKEIE-----------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|...
gi 1622953339 1172 ESSKKKLQRELEE 1184
Cdd:COG1579 155 EAELEELEAEREE 167
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
813-995 |
8.55e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 38.97 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 813 SEQDQAGTEMRVKLLQEENEKLQGRSEELEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQLEEALVQARREEKEAVS 892
Cdd:cd00176 24 SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 893 ARRALENELEAAQRNLSRTTQEQKQLSEKLKEES-----EQKEQLRRLKNEMENERWHLGKTIEKLQKEMADIVEASRTS 967
Cdd:cd00176 104 EALDLQQFFRDADDLEQWLEEKEAALASEDLGKDlesveELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEE 183
|
170 180
....*....|....*....|....*...
gi 1622953339 968 TLELQNQLDEYKEKNRRELAEMQRQLKE 995
Cdd:cd00176 184 IEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
841-925 |
9.17e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 37.80 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 841 LEQRVAQLQRQIEDLKGDEAKAKETLKKYEGEIRQ--------LEEALVQARREEKEAVS-ARRALENELEAAQRNLSrt 911
Cdd:cd06503 28 LDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEaraeaqeiIEEARKEAEKIKEEILAeAKEEAERILEQAKAEIE-- 105
|
90
....*....|....
gi 1622953339 912 tQEQKQLSEKLKEE 925
Cdd:cd06503 106 -QEKEKALAELRKE 118
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
872-1038 |
9.20e-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: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 872 EIRQLEEALVQARREEKEAVSARRALENELEAAQRNLSRTTQEQKQLSEKLKEESEQKEQLRRLKNEMENErwhLG---- 947
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGnvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622953339 948 -KTIEKLQKEMADIvEASRTSTLELQNQLDEYKEKNRRELAEMQRQLK--EKTLEAEKSRLtamkmqdEDKVSQLEMELE 1024
Cdd:COG1579 88 nKEYEALQKEIESL-KRRISDLEDEILELMERIEELEEELAELEAELAelEAELEEKKAEL-------DEELAELEAELE 159
|
170
....*....|....
gi 1622953339 1025 EERNNSDLLSERIS 1038
Cdd:COG1579 160 ELEAEREELAAKIP 173
|
|
| |
