|
Name |
Accession |
Description |
Interval |
E-value |
| Uds1 |
pfam15456 |
Up-regulated During Septation; Uds1 is a domain family is found mostly in fungi, and is ... |
21-151 |
8.97e-25 |
|
Up-regulated During Septation; Uds1 is a domain family is found mostly in fungi, and is typically between 120 and 138 amino acids in length. The GO annotation for the S.pombe protein describes the protein as barrier septum assembly involved in cell cycle cytokinesis, GO:0071937. Many of the uncharacterized members are listed as being involucrin repeat proteins, but this can not be substantiated.
Pssm-ID: 434730 [Multi-domain] Cd Length: 119 Bit Score: 99.93 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 21 LLIETAIFDSSSYDILSHEEVDQLKREETTLNGRIEALKRKLLLETKVRDAAQSLSRLQSPKHVESSlnsptsfltggfN 100
Cdd:pfam15456 1 LLVETALLDSQEFEILSFEEVEELKKELRALDSRLEYLRRKLALETKLRDAARSLHRLYSSYLRSPR------------N 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 526195852 101 KSAFDHTTLASTELGSSIAKCNAIDSDIRKLESDLWRLQRRLLRHTSRVLA 151
Cdd:pfam15456 69 SKFSESLLKAEEELAESDRKIDELAQELEKLENRRAEVRRRLLEHTAAVLQ 119
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
471-808 |
4.10e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 471 QMSSKQDAISLNLKQEISKLQSELDSKDSRYQRQLEELEDRLSIQKTEFEDrfevfsktslnnehhLQEKVRMMDEELNR 550
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE---------------LRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 551 SNRALEDSLLTLKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEI 630
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 631 QIFEYKSNNERLAVWAEEykttdvaQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKT 710
Cdd:TIGR02168 366 ELEELESRLEELEEQLET-------LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 711 QSAMDTsllleleiLSKQNEELLKANVALQAKLSEASGTKTgESEADHQILKDNCDRLQKELA---DMLLDYEKLMKASV 787
Cdd:TIGR02168 439 QAELEE--------LEEELEELQEELERLEEALEELREELE-EAEQALDAAERELAQLQARLDsleRLQENLEGFSEGVK 509
|
330 340
....*....|....*....|.
gi 526195852 788 NFEAERVRLEAQVDTLQDKIE 808
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLSELIS 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
473-810 |
2.65e-10 |
|
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: 64.69 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 473 SSKQDAISLNLKQEISKLQSELDskdsRYQRQLEELEDRLSIQKTEFEDRFEVFSKTsLNNEHHLQEKVRMMDEELNRSN 552
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIE----ELEEKIAELEKALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 553 RALEDSLLTLKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEIQI 632
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 633 FEYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDeeasSQRQIEEirnqaaatLQAEKGKTQS 712
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE----LESELEA--------LLNERASLEE 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 713 AMDTSLLLELEILSKQNeELLKANVALQAKLSEAsGTKTGESEADHQILKDNCDRLQKELADML-LDYEKLMKASVNFEA 791
Cdd:TIGR02168 888 ALALLRSELEELSEELR-ELESKRSELRRELEEL-REKLAQLELRLEGLEVRIDNLQERLSEEYsLTLEEAEALENKIED 965
|
330
....*....|....*....
gi 526195852 792 ERVRLEAQVDTLQDKIEGL 810
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
452-811 |
4.67e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 452 EQQIVGLTNSLSHTMNELSQMSSKQDAISLNLKqEISKLQSELDSKDSRYQRQLEELEDRLSIQKTEFEDrfevfSKTSL 531
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN-----VKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 532 NnehHLQEKVRMMDEELNRSNRALEDslLTLKNKEKENQEQQENMNSLRTEMSRSEVVAS---AEESQRLLDRKIVDDLD 608
Cdd:TIGR02169 761 K---ELEARIEELEEDLHKLEEALND--LEARLSHSRIPEIQAELSKLEEEVSRIEARLReieQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 609 RKLQVQktrILELEDDIKLKEIQIFEYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASS 688
Cdd:TIGR02169 836 QELQEQ---RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 689 QRQiEEIRNQAAATLQAEKGktqsamdtsllleleilskQNEELLKANVALQAKLSEasgtktgesEADHQILKDNCDRL 768
Cdd:TIGR02169 913 EKK-RKRLSELKAKLEALEE-------------------ELSEIEDPKGEDEEIPEE---------ELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 526195852 769 QKELADM-------LLDYEKLMKASVNFEAERVRLEAQVDTLQDKIEGLE 811
Cdd:TIGR02169 964 EEEIRALepvnmlaIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
482-815 |
1.70e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 482 NLKQEISKLQSELDSKDSR---YQRQLEELEDRLSIQKTEFEdRFEVFSKTSLNNEHHLQEKVRMMDEELNRSNRALEDS 558
Cdd:COG1196 236 ELEAELEELEAELEELEAEleeLEAELAELEAELEELRLELE-ELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 559 LLTLKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEIQIFEYKSN 638
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 639 NERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQSAMDTSL 718
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 719 LLELEILSKQNEELLKANVALQAKLSEASGTKTGESEADHqiLKDNCDRLQKELADMLLDYEKLMKASVNFEAERV--RL 796
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL--LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnIV 552
|
330
....*....|....*....
gi 526195852 797 EAQVDTLQDKIEGLESNLA 815
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKA 571
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
553-822 |
1.02e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 553 RALEDSLLTLKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEIQI 632
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 633 FEYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQS 712
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 713 AmdtsllLELEILSKQNEELLKANVALQAKLSEASGTKTGESEADHQILKDnCDRLQKELADMLLDYEKLMKASVNFEAE 792
Cdd:COG1196 392 L------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE-EEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270
....*....|....*....|....*....|
gi 526195852 793 RVRLEAQVDTLQDKIEGLESNLADEKIRLL 822
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
489-823 |
3.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 489 KLQSELDSKDSRYQ-RQLEELEDRLSIQKTEFEDrfevfsktslnnehhLQEKVRMMDEELNRSNRALEDSLLTLKNKEK 567
Cdd:COG1196 217 ELKEELKELEAELLlLKLRELEAELEELEAELEE---------------LEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 568 ENQEQQENMNSLRTEMSRSE--VVASAEESQRLLDRKivDDLDRKLQVQKTRILELEDDIKLKEIQIFEyksnnerlavw 645
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEqdIARLEERRRELEERL--EELEEELAELEEELEELEEELEELEEELEE----------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 646 AEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQSamDTSLLLELEIL 725
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--LERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 726 SKQNEELLKANVALQAKLSEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQD 805
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330
....*....|....*...
gi 526195852 806 KIEGLESNLADEKIRLLG 823
Cdd:COG1196 507 LEGVKAALLLAGLRGLAG 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
562-893 |
5.77e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 562 LKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEIQIFEYKSNNER 641
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 642 LAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQSAMDTSLLLE 721
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 722 LEILSKQNEELLKANVALQAKLSEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVD 801
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 802 TLQDKIEGLESNLADEKIRLLGNgspiktastqsnsiptpisstgeamtMSVLRAEFKKMMRDMRSEHSKALKGEQEARR 881
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNL--------------------------QERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330
....*....|..
gi 526195852 882 RVEsELRQYRKE 893
Cdd:TIGR02168 973 RLK-RLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-698 |
1.12e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 419 LAKDKGELAEKLHQVSVQIqldaDAYEVTKSGQEQQIVGLTNSLSHTMNELSQMSSKQDAIS---LNLKQEISKLQSE-- 493
Cdd:TIGR02168 230 LVLRLEELREELEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQQkq 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 494 --------LDSKDSRYQRQLEELEDRLSIQKTEFEDRFEVFSKtslnnehhLQEKVRMMDEELNRSNRALEDslltLKNK 565
Cdd:TIGR02168 306 ilrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEE--------LKEELESLEAELEELEAELEE----LESR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 566 EKENQEQQENMNSLRTEMSRSEVVASAEesQRLLDRKIvDDLDRKLQVQKTRILELEDDIKLKEIQIFEyksnnERLAVW 645
Cdd:TIGR02168 374 LEELEEQLETLRSKVAQLELQIASLNNE--IERLEARL-ERLEDRRERLQQEIEELLKKLEEAELKELQ-----AELEEL 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 526195852 646 AEEYKTTDVAQKSRISNLEgEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQ 698
Cdd:TIGR02168 446 EEELEELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
377-708 |
1.15e-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: 52.76 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 377 EAILQDLlsAAVSENTPRADIHERSV----ERLgQKVKSLVERSLRLAKDKGELAEKLHQVSVQIqLDADAYEVTK--SG 450
Cdd:TIGR02169 173 EKALEEL--EEVEENIERLDLIIDEKrqqlERL-RREREKAERYQALLKEKREYEGYELLKEKEA-LERQKEAIERqlAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 451 QEQQIVGLT----------NSLSHTMNELS-QMSSKQDAISLNLKQEISKLQSE---LDSKDSRYQRQLEELEDRLsiQK 516
Cdd:TIGR02169 249 LEEELEKLTeeiselekrlEEIEQLLEELNkKIKDLGEEEQLRVKEKIGELEAEiasLERSIAEKERELEDAEERL--AK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 517 TEFEDRFEVFSKTSLNNE-HHLQEKVRMMDEELNRSNRALEDSLLTLKNKEKENQEQQENMNSLRTEMSrsEVVASAEES 595
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE--KLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 596 QRLLDRkivddLDRKLQVQKTRILELEDDIKLKEIQIFEYKSNNE--RLAVWAEEYKTTDVAQKsrisnLEGEIERLIRE 673
Cdd:TIGR02169 405 KRELDR-----LQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkALEIKKQEWKLEQLAAD-----LSKYEQELYDL 474
|
330 340 350
....*....|....*....|....*....|....*
gi 526195852 674 SEKLRiRLEDEEASSQRQIEEIRNQAAATLQAEKG 708
Cdd:TIGR02169 475 KEEYD-RVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
492-900 |
2.48e-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: 51.61 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 492 SELDSKDSRYQRQLEELEDRLsiqktefeDRFEVFsktslnnehhLQEKVRMMDEELNRSNRALEDSLLTLKNKEKENQE 571
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENI--------ERLDLI----------IDEKRQQLERLRREREKAERYQALLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 572 QQENMNSLRTEMSRSEV-VASAEESQrlldrkivDDLDRKLQVQKTRILELEDDIKLKEIQIfEYKSNNERLAVwaeeyk 650
Cdd:TIGR02169 228 LLKEKEALERQKEAIERqLASLEEEL--------EKLTEEISELEKRLEEIEQLLEELNKKI-KDLGEEEQLRV------ 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 651 ttdvaqKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQSAMDTSLLLELEILSKQNE 730
Cdd:TIGR02169 293 ------KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 731 ELLKANValqaklseasgtktGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKIEGL 810
Cdd:TIGR02169 367 EDLRAEL--------------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 811 ESNLADEKIRLLGNGSPIKTASTQSNSIptpisstgeamtmsvlraefKKMMRDMRSEHSKalkgEQEARRRVESELRQY 890
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQL--------------------AADLSKYEQELYD----LKEEYDRVEKELSKL 488
|
410
....*....|
gi 526195852 891 RKEYPQSQKQ 900
Cdd:TIGR02169 489 QRELAEAEAQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
605-834 |
2.99e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 605 DDLDRKLQVQKTRILELEDDIKLKEIQIFEYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDE 684
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 685 EASSQRQIEEIRNQAAATLQAEkgKTQSAMDTSLLLELEILSKQNEELLKANVALQAKLSEASGTKTGESEADHQI--LK 762
Cdd:COG1196 322 EEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAaeLA 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526195852 763 DNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKIEGLESNLADEKIRLLGNGSPIKTASTQ 834
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-629 |
1.21e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 397 IHERSVERLGQKVKSLVERSLRLAKDKGELAEKLHQVSVQIQLDadayevtksgqEQQIVGLTNSLSHTMNELSQMSSKQ 476
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL-----------EEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 477 DAISLNLKQEISKLQSELDSKDSRYQRQLEELEDRLSIQKTEFEDRfevfsktslNNEHHLQEKVRMMDEELNRSNRALE 556
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE---------EAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526195852 557 DSLLTLKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKE 629
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
420-632 |
3.25e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 420 AKDKGELAEKLHQVSVQIQLDADAYEVTKSgQEQQIVGLTNSLSHTMNELSQMSSKQDAISLNLKQEISKLQSELDSKDS 499
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKK-EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 500 RYQRQLEELEDRL-SIQKTEFEDRFEV-FSKTSLNNEHHLQEKVRMMDEELNRSNRALEDSLLTLKNKEKENQEQQENMN 577
Cdd:COG4942 98 ELEAQKEELAELLrALYRLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 526195852 578 SLRTEMSRSEVVASAEESQRlldRKIVDDLDRKLQVQKTRILELEDDIKLKEIQI 632
Cdd:COG4942 178 ALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
453-808 |
5.49e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 453 QQIVGLTNSLSHTMNELSQMSSKQDaislNLKQEISKLQSELDskdsRYQRQLEELEDRLSIQKTEFED----RFEVFSK 528
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQN----KIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEISDlnnqKEQDWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 529 TSLNNEHHLQEKVRMMDEELNRSNRALEDSLLTLKNKEKENQEQQENMNSLRTEMSR--SEVVASAEESQRLLDRkiVDD 606
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqNEIEKLKKENQSYKQE--IKN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 607 LDRKLQVQKTRILELEDDIKLKEIQIFEYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEI---ERLIRESEKLRIRLED 683
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDsvkELIIKNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 684 EEASSQRQIEEIRNQAAATLQAEKGKTQ-----SAMDTSLLLELEILSKQNEELLKANVALQAKLSE--------ASGTK 750
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKelkklNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisdlEDELN 548
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 526195852 751 TGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKIE 808
Cdd:TIGR04523 549 KDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
399-821 |
5.74e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 399 ERSVERLGQKVKSLVERSLRLA--KDKGELAEKLHQVSVQIQLDADAYEVTKSGQEQQIvgltNSLSHTMNELSQMSSKq 476
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI----NGIEERIKELEEKEER- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 477 daislnlKQEISKLQSELDSKDSRYQRQLEELEDRLSI--QKTEFEDRFEVFSKTSLNNEHHLQEKVRmmdEELNRSNRA 554
Cdd:PRK03918 340 -------LEELKKKLKELEKRLEELEERHELYEEAKAKkeELERLKKRLTGLTPEKLEKELEELEKAK---EEIEEEISK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 555 LEDSLLTLKNKEKENQEQQENMNSLR----------TEMSRSEVVA--SAEESQRLLDRKIVDDLDRKLQVQKTRI---- 618
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelTEEHRKELLEeyTAELKRIEKELKEIEEKERKLRKELRELekvl 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 619 LELEDDIKLKEI--QIFEYKS-----NNERLAVWAEEYKTTdvaqKSRISNLEGEIERLIRESEKLRiRLEDEEASSQRQ 691
Cdd:PRK03918 490 KKESELIKLKELaeQLKELEEklkkyNLEELEKKAEEYEKL----KEKLIKLKGEIKSLKKELEKLE-ELKKKLAELEKK 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 692 IEEIRNQAAATLQAEKGKTQSAMDTSLLLELEILSKQNE--ELLKANVALQAKLSEASGTKT--GESEADHQILKDNCDR 767
Cdd:PRK03918 565 LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEelDKAFEELAETEKRLEE 644
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 526195852 768 LQKELADMLL-----DYEKLMKASVNFEAERVRLEAQVDTLQDKIEGLESNLADEKIRL 821
Cdd:PRK03918 645 LRKELEELEKkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
277-816 |
7.17e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 277 KKSAQANLVAISMGSEEEGSQKSTSDtpnsSDSLFEKQIACLELGLAQIQSSVldQPANRYSANDPKQFDKEqktlsLLW 356
Cdd:pfam15921 285 EKASSARSQANSIQSQLEIIQEQARN----QNSMYMRQLSDLESTVSQLRSEL--REAKRMYEDKIEELEKQ-----LVL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 357 ETLNYYESSLENETPSGDSG--EAILQDLLsaavsentprADIHERSVERLGQKV--KSLVERSLRLAKDKGELAEKLHQ 432
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGnlDDQLQKLL----------ADLHKREKELSLEKEqnKRLWDRDTGNSITIDHLRRELDD 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 433 VSVQIQLDADAYEVTKS---GQEQQIVGLTNSLSHTMNELSQMSSKQDAISLNLKQEISKLQSELDSKDSRyQRQLEELE 509
Cdd:pfam15921 424 RNMEVQRLEALLKAMKSecqGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLT 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 510 DRLSIQKTEFEDRFEVFSKTSLNNEHHLQEKVRMMDEELNRSNRALEDSLLTLKNKEKEN-----QEQQENMNSLRTEMS 584
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKvieilRQQIENMTQLVGQHG 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 585 RSEVVASAEESQrlLDRKIVDdldRKLQVQKTRILELEDDIKLKEIQifeyksnnerlavwaeeykttdvaqkSRISNLE 664
Cdd:pfam15921 583 RTAGAMQVEKAQ--LEKEIND---RRLELQEFKILKDKKDAKIRELE--------------------------ARVSDLE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 665 GEIERLIRE-SEKLRirledeeasSQRQIEEIRNQAAATLQAEKGKTQSamdtsllleleilSKQNEELLKANVALQakl 743
Cdd:pfam15921 632 LEKVKLVNAgSERLR---------AVKDIKQERDQLLNEVKTSRNELNS-------------LSEDYEVLKRNFRNK--- 686
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526195852 744 SEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKIEGLESNLAD 816
Cdd:pfam15921 687 SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN 759
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
305-889 |
1.38e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 305 NSSDSLFEKQIACLELGLAQIQSSVLDQPANRYSANDPKQFDKE---------QKTLSLLWETLNYYESSLENETPSGD- 374
Cdd:pfam15921 95 NESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQsqedlrnqlQNTVHELEAAKCLKEDMLEDSNTQIEq 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 375 ------SGEAILQDLLSAAVS-ENTPRADIHERS------VERLGQKV-KSLVERSLRLAKDKGEL-----------AEK 429
Cdd:pfam15921 175 lrkmmlSHEGVLQEIRSILVDfEEASGKKIYEHDsmstmhFRSLGSAIsKILRELDTEISYLKGRIfpvedqlealkSES 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 430 LHQVSVQIQLDADAYEVTKSGQEQQIVGLT----------NSLSHTMNELSQMSSKQDAISL----NLKQEISKLQSELD 495
Cdd:pfam15921 255 QNKIELLLQQHQDRIEQLISEHEVEITGLTekassarsqaNSIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 496 SKDSRYQRQLEELEDRLSIQKTEF-EDRFE--VFSKTSLNNEHHLQ---------EKVRMMDEELNRS------------ 551
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELtEARTErdQFSQESGNLDDQLQklladlhkrEKELSLEKEQNKRlwdrdtgnsiti 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 552 ---NRALEDSLLT-------LKNKEKENQEQQE-NMNSLRTEMSRSEVVASAE---ESQRLLDRKIVDDLDRK---LQVQ 614
Cdd:pfam15921 415 dhlRRELDDRNMEvqrlealLKAMKSECQGQMErQMAAIQGKNESLEKVSSLTaqlESTKEMLRKVVEELTAKkmtLESS 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 615 KTRILELEDDIKLKEIQIFEYKSNNERLAVWAEeyktTDVAQKSRISNLEGEIERLIRESEKLRIRLedeeASSQRQIEE 694
Cdd:pfam15921 495 ERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKLQELQHLKNEGDHLRNVQTECEALKLQM----AEKDKVIEI 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 695 IRNQAAATLQ--AEKGKTQSAMDTSLLLELEILSKQNEELLKANV----------ALQAKLSEASGTKTGESEADHQIL- 761
Cdd:pfam15921 567 LRQQIENMTQlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkdkkdakirELEARVSDLELEKVKLVNAGSERLr 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 762 -----KDNCDRL-------QKELADMLLDYEKLMKasvNFEAERVRLEAQVDTLQDKIEGLESNLADEKIRL-------- 821
Cdd:pfam15921 647 avkdiKQERDQLlnevktsRNELNSLSEDYEVLKR---NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLksmegsdg 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 822 ------LGNGSPIKTASTQSNSIPTPISSTGEAMTMS-----VLRAEFKKMMRDMRS--EHSKALKGEQEARRRVESELR 888
Cdd:pfam15921 724 hamkvaMGMQKQITAKRGQIDALQSKIQFLEEAMTNAnkekhFLKEEKNKLSQELSTvaTEKNKMAGELEVLRSQERRLK 803
|
.
gi 526195852 889 Q 889
Cdd:pfam15921 804 E 804
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
610-903 |
1.64e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 610 KLQVQKT-RILELEDDIKLKEIQIF-----EYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLED 683
Cdd:TIGR02168 206 ERQAEKAeRYKELKAELRELELALLvlrleELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 684 EEASSQRQIEEIrnqaaATLQAEKGKTQSAMDtSLLLELEILSKQNEELLKANVALQAKLSEasgtktgeseadhqiLKD 763
Cdd:TIGR02168 286 LQKELYALANEI-----SRLEQQKQILRERLA-NLERQLEELEAQLEELESKLDELAEELAE---------------LEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 764 NCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKIEGLESNLADEKIRLLGNGSPIktasTQSNSIPTPIS 843
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL----ERLEDRRERLQ 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 844 STGEAMTMSVLRAEFKKMMRDMrSEHSKALKGEQEARRRVESELRQYRKEYPQSQKQFVQ 903
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
449-598 |
2.60e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 449 SGQEQQIvgltNSLSHTMNELSQMSSKQDAISLNLKQEISKLQSELDSKDSRYQRqLEELEDRLSIQKTEFEDRFEVFSK 528
Cdd:PRK09039 49 SGKDSAL----DRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSR-LQALLAELAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526195852 529 tSLNNEHHLQEKVRMMDEELNRSNRALEDSLLTLKN----KEKENQEQQENMNSLRTEMSrsevVASAEESQRL 598
Cdd:PRK09039 124 -ELDSEKQVSARALAQVELLNQQIAALRRQLAALEAaldaSEKRDRESQAKIADLGRRLN----VALAQRVQEL 192
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
646-903 |
3.65e-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: 44.28 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 646 AEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQSAMDTSLLLELEIL 725
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 726 SKQNEELLKANVALQAKLSEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQD 805
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 806 KIEGLESNLADEKIRLLGNGSPIKTASTQSNSIPTPISSTGEAMTMSVLRAEFKKMMRDMRSEHSKALKGEQEA----RR 881
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEElseeLR 904
|
250 260
....*....|....*....|..
gi 526195852 882 RVESELRQYRKEYPQSQKQFVQ 903
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQ 926
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
554-682 |
6.45e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 554 ALEDSLLTLKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLldRKIVDDLDRKLQVQKTRILELEDdiKLKEIQIF 633
Cdd:COG2433 381 ALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERL--EAEVEELEAELEEKDERIERLER--ELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 526195852 634 EYKSNNERLAVwaeeykttdVAQKSRISNLEGEIERLIRESEKLRIRLE 682
Cdd:COG2433 457 ERREIRKDREI---------SRLDREIERLERELEEERERIEELKRKLE 496
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
492-812 |
8.70e-04 |
|
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: 43.09 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 492 SELDSKDSRYQRQLEELEDRLSIQKTEF---EDRFEVFSKTSLNNEHHLQEKVRMMdEELNRSNRALEDSLLTLKNK--E 566
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQEINEKTTEIsntQTQLNQLKDEQNKIKKQLSEKQKEL-EQNNKKIKELEKQLNQLKSEisD 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 567 KENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEIQIFEYKSNNERLAVWA 646
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 647 EEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNqaaatLQAEKGKTQSAMDTSLLLELEILS 726
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-----LKETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 727 KQNEelLKanvalqaKLSEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDK 806
Cdd:TIGR04523 455 IIKN--LD-------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
....*.
gi 526195852 807 IEGLES 812
Cdd:TIGR04523 526 IEKLES 531
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
687-895 |
1.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 687 SSQRQIEEIRNQAAAtLQAEKGKTQSAMdtsllleleilsKQNEELLKANVALQAKLSEASgtKTGESEADHQILKDNCD 766
Cdd:COG4913 607 DNRAKLAALEAELAE-LEEELAEAEERL------------EALEAELDALQERREALQRLA--EYSWDEIDVASAEREIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 767 RLQKELADMLLDYEKLMKASVNFE---AERVRLEAQVDTLQDKIEGLESNLADEKIRllgngspIKTASTQSNSIPTPIS 843
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLEeleAELEELEEELDELKGEIGRLEKELEQAEEE-------LDELQDRLEAAEDLAR 744
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 526195852 844 STGEAMTMSVLRAE-----FKKMMRDMRSEHSKALKGEQEARRRVESELRQYRKEYP 895
Cdd:COG4913 745 LELRALLEERFAAAlgdavERELRENLEERIDALRARLNRAEEELERAMRAFNREWP 801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
482-697 |
1.66e-03 |
|
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: 42.31 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 482 NLKQEISKLQSE---LDSKDSRYQRQLEELEDRLSIQKTEFEdrfeVFSKTSLNNEHHLQEKVRMMDE------ELNRSN 552
Cdd:TIGR04523 430 RLKETIIKNNSEikdLTNQDSVKELIIKNLDNTRESLETQLK----VLSRSINKIKQNLEQKQKELKSkekelkKLNEEK 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 553 RALEDSLLTLKNKEKENQEQQENMNSLRTEMSR------SEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIK 626
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdleDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526195852 627 LKEIQIFEYKSNNERLAVWAEEYKTTdvaqksrISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRN 697
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEKK-------ISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
444-817 |
1.68e-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: 42.02 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 444 YEVTKSGQEQQIVGLTNSLSHTMNELSQMSSKQDAISLNLKQEISKLQSELDSKDSRYQRQLEELEDRLS---IQKTEFE 520
Cdd:pfam05483 174 YEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSlllIQITEKE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 521 DRFEVFS---KTSLNNEHHLQEKVRMMDEELNRSNR--------------ALEDSLLTLKNKEKENQEQQENMNSL---- 579
Cdd:pfam05483 254 NKMKDLTfllEESRDKANQLEEKTKLQDENLKELIEkkdhltkeledikmSLQRSMSTQKALEEDLQIATKTICQLteek 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 580 RTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKTRILELEDDIKLKEIQIFEYKSNNERLA-------VWAEEYKTT 652
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfknnkeVELEELKKI 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 653 dVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQAEKGKTQSAMDTSLLLeleilskQNEEL 732
Cdd:pfam05483 414 -LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL-------EKEKL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 733 lkanvalqaklseasgtKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKieglES 812
Cdd:pfam05483 486 -----------------KNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK----EM 544
|
....*
gi 526195852 813 NLADE 817
Cdd:pfam05483 545 NLRDE 549
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
583-825 |
1.69e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 583 MSRSEVVASAEESQRLLDRKIvDDLDRKLQVQKTRILELEDDIKLKEIQIfeyKSNNERLAvwaeeykttdvAQKSRISN 662
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRI---AALARRIR-----------ALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 663 LEGEIERLIRESEKLRIRLEDEEASSQRQIEEI----RNQAAATLQAEKGKTQSAMDTSLLLELEILSKQNEELLKANVA 738
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 739 LQAKLSEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLEAQVDTLQDKIEGLESNLADEK 818
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*..
gi 526195852 819 IRLLGNG 825
Cdd:COG4942 241 ERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
483-709 |
1.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 483 LKQEISKLQSELDSKDSRY---QRQLEELEDRLSiqktefedrfevfsktslnnehHLQEKVRMMDEELNRSNRALEDSL 559
Cdd:COG4942 32 LQQEIAELEKELAALKKEEkalLKQLAALERRIA----------------------ALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 560 LTLKNKEKENQEQQENMNSLRTEMSRS------EVVASAEESQRLL------------DRKIVDDLDRKLQVQKTRILEL 621
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLgrqpplALLLSPEDFLDAVrrlqylkylapaRREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 622 EDDIKLKEIQIFEYKSNNERLAVWAEEYKTTDVAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIrnqAAA 701
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT---PAA 246
|
....*...
gi 526195852 702 TLQAEKGK 709
Cdd:COG4942 247 GFAALKGK 254
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
392-747 |
3.51e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 392 TPRADIhERSVERLGQKVKSLVERSLRLAKDK-GELAEKLHQvsvqiQLDADAYEVTKSgqeqqiVGLTNSLSHTMNELS 470
Cdd:PLN03229 429 TPVREL-EGEVEKLKEQILKAKESSSKPSELAlNEMIEKLKK-----EIDLEYTEAVIA------MGLQERLENLREEFS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 471 QMSSKQDAISLNLKQEISKLQSELDSKDSRyQRQLEELEDRLsiqktefeDRFEVFSKTSLNNEHhlQEKVRMMDEELNR 550
Cdd:PLN03229 497 KANSQDQLMHPVLMEKIEKLKDEFNKRLSR-APNYLSLKYKL--------DMLNEFSRAKALSEK--KSKAEKLKAEINK 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 551 SNRALEDslltlknkekeNQEQQENMNSLRTEMSRSEVVASAEesqrlLDRKIVDDLDRklqVQKTRILELEDDIKLKEI 630
Cdd:PLN03229 566 KFKEVMD-----------RPEIKEKMEALKAEVASSGASSGDE-----LDDDLKEKVEK---MKKEIELELAGVLKSMGL 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 631 QIFEYKSNNERLAvwaeeYKTTDVAQKSRISNLEGE----IERLIRESE-KLRI---RLEDEEASSQRQIEEiRNQAAAT 702
Cdd:PLN03229 627 EVIGVTKKNKDTA-----EQTPPPNLQEKIESLNEEinkkIERVIRSSDlKSKIellKLEVAKASKTPDVTE-KEKIEAL 700
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 526195852 703 LQAEKGKTQSAMDTsllleleILSKQNEELLKANVALQAKLSEAS 747
Cdd:PLN03229 701 EQQIKQKIAEALNS-------SELKEKFEELEAELAAARETAAES 738
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
462-713 |
3.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 462 LSHTMNELSQMSSKQDAIslnlKQEISKLQSELDSKDSRYQRQLEELEDrlsiqktefedrfevfsktslnnehhLQEKV 541
Cdd:COG3883 18 IQAKQKELSELQAELEAA----QAELDALQAELEELNEEYNELQAELEA--------------------------LQAEI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 542 RMMDEELNRSNRALEDSLLTLKNKEKENQEQQENMNSLrtemsrsEVVASAEESQRLLDRkiVDDLDRKLQVQKTRILEL 621
Cdd:COG3883 68 DKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYL-------DVLLGSESFSDFLDR--LSALSKIADADADLLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 622 EDDIKLKEIQIFEYKSNNERLAvwaeeykttdvAQKSRISNLEGEIERLIRESEKLRIRLEDEEASSQRQIEEIRNQAAA 701
Cdd:COG3883 139 KADKAELEAKKAELEAKLAELE-----------ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250
....*....|..
gi 526195852 702 TLQAEKGKTQSA 713
Cdd:COG3883 208 AEAAAAAAAAAA 219
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
482-629 |
7.87e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 482 NLKQEISKLQSELDSKDsryqRQLEELEDRLSiqktefedrfevFSKTSLNNEHHLQEKVRMMDEELNRSNRALEDsllt 561
Cdd:COG2433 424 RLEAEVEELEAELEEKD----ERIERLERELS------------EARSEERREIRKDREISRLDREIERLERELEE---- 483
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 526195852 562 lknKEKENQEQQENMNSLRTemsrsevVASAEESQRLLDRKIVDDLDRKlqvqktRILELEDDIKLKE 629
Cdd:COG2433 484 ---ERERIEELKRKLERLKE-------LWKLEHSGELVPVKVVEKFTKE------AIRRLEEEYGLKE 535
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
404-797 |
8.71e-03 |
|
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: 39.95 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 404 RLGQKVKSLVERSLRLAKDKGELAEKLHQVSVQIQLDADAYEVTKSGQEQQIVGLTNSLSHTMNELSQMSSKQDAISLNL 483
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 484 KQEISKLQSELDSKDSRYQRQLEELEDRLSIQKTEFEDRFEVFSKTSLNNEHHLQEKVRMMDEELN--RSNRALEDSLLT 561
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREktEKLKVEEEKEEK 795
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 562 LKNKEKENQEQQENMNSLRTEMSRSEVVASAEESQRLLDRKIVDDLDRKLQVQKtriLELEDDIKLKEIQIFEYKSNNER 641
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE---KLAEEELERLEEEITKEELLQEL 872
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250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526195852 642 LavwAEEYKTTDVAQKSRISNLEGEIERlIRESEKLRIRLEDEEASSQRQIEEIRNQAAATLQaeKGKTQSAMDTSLLLE 721
Cdd:pfam02463 873 L---LKEEELEEQKLKDELESKEEKEKE-EKKELEEESQKLNLLEEKENEIEERIKEEAEILL--KYEEEPEELLLEEAD 946
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330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526195852 722 LEILSKQNEELLKANVALQAKLSEASGTKTGESEADHQILKDNCDRLQKELADMLLDYEKLMKASVNFEAERVRLE 797
Cdd:pfam02463 947 EKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
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