|
Name |
Accession |
Description |
Interval |
E-value |
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
10-182 |
9.97e-66 |
|
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar proteins; Gipie, also called coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing.
Pssm-ID: 411801 Cd Length: 170 Bit Score: 219.70 E-value: 9.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 10 RDFLSGSLATWALGLAGLVGEAEESSGTEEEEEEEEegPLCTERRFLKLISGDLLLRVLGIIAPSSRGRLQMvKGHDGPA 89
Cdd:cd22230 1 EEFMSGALVTWALGFEGLVGEEEDSLGFPEEEEEEG--TLDAEKRFLRLSNGDLLNRVMGIIDPSPRGGPRM-RGDDGPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 90 ACRIWNLYHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPFSEEAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDV 169
Cdd:cd22230 78 AHRVQNLHILWGRLRDFYQEELQQLILSPPPDLQVMGRDPFTEEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDV 157
|
170
....*....|...
gi 2778277499 170 QSELAAAIQEVTQ 182
Cdd:cd22230 158 QAELAEAIQEVTQ 170
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-182 |
3.24e-42 |
|
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration. Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B (CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. It acts as a positive regulator of T-cell maturation and inflammatory function. As a microtubule-binding protein, Gipie regulates lytic granule clustering and NK cell killing. All family members contain a conserved globular Hook domain which folds as a variant of the helical calponin homology (CH) domain.
Pssm-ID: 411794 Cd Length: 149 Bit Score: 151.59 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 12 FLSGSLATWALGLAGLVGEaeessgteeeeeeeeegplctERRFLKLISGDLLLRVLGIIAPSSRGrLQMVKGHDGPAAC 91
Cdd:cd22223 1 FLSSPLVTWAKTFADDGSA---------------------ELSYTDLVDGVFLNNVMLQIDPRPFS-EVSNRNVDDDVNA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 92 RIWNLYHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPFSEEAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQS 171
Cdd:cd22223 59 RIQNLDLLLRNIKSFYQEVLQQLIVMKLPDILTIGREPESEQSLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQH 138
|
170
....*....|.
gi 2778277499 172 ELAAAIQEVTQ 182
Cdd:cd22223 139 ALVACIQEVTD 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
728-1297 |
3.74e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.51 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 728 QALRDEVAQLRREVVSLeaKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAA 807
Cdd:COG1196 216 RELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 808 SREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDR 887
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 888 LEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALmKLKARALQLEEELIQLRQypvdQATEVR 967
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEE----ALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 968 AEprtvetQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELH 1047
Cdd:COG1196 449 EE------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1048 RKLGVLEEEVRVARRAQEETRGQqqallrdhEALVQLQRRQETELEGLLVRHRDLKANmRALELAHRELQGRHEQLQAQR 1127
Cdd:COG1196 523 AGAVAVLIGVEAAYEAALEAALA--------AALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1128 ASVEAQEVALLAERERLMQDGHRQRGLEEELRRLqnEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQS 1207
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTL--VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1208 QKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRRE 1287
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570
....*....|
gi 2778277499 1288 KQKLVEKIMD 1297
Cdd:COG1196 752 ALEELPEPPD 761
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
55-182 |
2.52e-22 |
|
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). It acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits. It also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS. In addition, Girdin plays an essential role in cell migration.
Pssm-ID: 411800 Cd Length: 156 Bit Score: 94.86 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 55 FLKLISGDLLLRVLGIIAPSSRGRlQMVKGHDGPAACRIWNLYHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPFSEEA 134
Cdd:cd22229 30 YVALVDGVFLNEVMLQINPKSSNQ-RVNKKVNNDASLRIQNLSILVKQIKLYYQETLQQLIMMSLPNVLVLGRNPLSEQG 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2778277499 135 VDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEVTQ 182
Cdd:cd22229 109 TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEVTH 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
726-1266 |
7.97e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELE 805
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 806 AASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELG 885
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 886 DRLEHLQRELEQAALERQKFLQERESQHQ---RYQHLEQRLEAELQAAstnkEEALMKLKARALQLEEELIQLRQYPVDQ 962
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEaleEAAEEEAELEEEEEAL----LELLAELLEEAALLEAALAELLEELAEA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 963 ATEVRAEPRTVETQNGRLIEVERnnATLVAEKAALQGQLqHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQ 1042
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAV-AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1043 GQELHRKLGVL---EEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGR 1119
Cdd:COG1196 567 KAAKAGRATFLpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRL 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1120 HEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELE 1199
Cdd:COG1196 647 REVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL 726
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 1200 RAQLEIQSQKLRESNQQLDlsacrlttqcelltQLRSAQEEENRQLLAEVQALSREnRELLERSLES 1266
Cdd:COG1196 727 EEQLEAEREELLEELLEEE--------------ELLEEEALEELPEPPDLEELERE-LERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
726-1204 |
5.31e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEEL---------AQARRTEAEAHLEVEARAREQARLREA 796
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleeeleeLEEELEEAEEELEEAEAELAEAEEALL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 797 VDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQ-----VEAAEQQVQALESQVRCHLEEAEREHLEKQALR 871
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEallerLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 872 EELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQrLEAELQAASTNKEEALMKLKARALQLEEE 951
Cdd:COG1196 449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE-AEADYEGFLEGVKAALLLAGLRGLAGAVA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 952 LIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSR 1031
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1032 LQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALEL 1111
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1112 AHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRS 1191
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
490
....*....|...
gi 2778277499 1192 RLARLELERAQLE 1204
Cdd:COG1196 768 ELERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
834-1290 |
2.67e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 834 RLRAQVEAAEQ----QVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQER 909
Cdd:COG1196 204 PLERQAEKAERyrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 910 ESQHQRYQHLEQRLEAE------LQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEV 983
Cdd:COG1196 284 EEAQAEEYELLAELARLeqdiarLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 984 ERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRA 1063
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1064 QEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVeaQEVALLAERER 1143
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV--KAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1144 LMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACR 1223
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 1224 LTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQK 1290
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
726-1295 |
1.37e-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: 92.43 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELE 805
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 806 AASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAvvRGQELG 885
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQ 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 886 DRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEaelqaaSTNKEEALMKLKARALQLEEELIQLRQYPVDQATE 965
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALD------AAERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 966 VRAEPRTVETQNGRLIEVERNNATLVAekAALQGQLQHLEGQLGSLQGRAQELLLQS----------------------- 1022
Cdd:TIGR02168 514 NQSGLSGILGVLSELISVDEGYEAAIE--AALGGRLQAVVVENLNAAKKAIAFLKQNelgrvtflpldsikgteiqgndr 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1023 ----------------------------------------QRAQEHSSRLQAEKSMMEIQG------------------- 1043
Cdd:TIGR02168 592 eilkniegflgvakdlvkfdpklrkalsyllggvlvvddlDNALELAKKLRPGYRIVTLDGdlvrpggvitggsaktnss 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1044 -QELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ 1122
Cdd:TIGR02168 672 iLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1123 LQAQRASVEAQEVALLAERERLMQDGHRqrgLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQ 1202
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1203 LEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLH---REQREYLD 1279
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelsEELRELES 908
|
650
....*....|....*.
gi 2778277499 1280 QLNALRREKQKLVEKI 1295
Cdd:TIGR02168 909 KRSELRRELEELREKL 924
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
55-182 |
7.48e-17 |
|
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) and similar proteins; Protein Daple, also called coiled-coil domain-containing protein 88C (CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling.
Pssm-ID: 411799 Cd Length: 153 Bit Score: 79.20 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 55 FLKLISGDLLLRVLGIIAPSSRGrlQMVKGH-DGPAACRIWNLYHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPFSEE 133
Cdd:cd22228 27 YMDLVDGVFLNKIMLQIDPRPTN--QRVNKHvNNDVNLRIQNLTILVRHIKTYYQEVLQQLIVMNLPNVLMIGKDPLSGK 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2778277499 134 AVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEVTQ 182
Cdd:cd22228 105 SMEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEVTH 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-955 |
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: 86.26 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 262 QLTNAKAQLRRLRQEVEEKAELLLDSQAEVQGLESEIRRLRQETQALSGQAKRAELYREEAEALRERAG-RLPRLQEELR 340
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 341 RCRERLhaaEVFKGQLEEERVLSGALEASKVLLEEQLEiarERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVE 420
Cdd:TIGR02168 348 ELKEEL---ESLEAELEELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 421 ENVELELELQR------SLEPPPGSPGETSLPGAAPSLQDEVREAEAgRLRTVEQENRTLRGQLQMLREQLDSQRPLLEE 494
Cdd:TIGR02168 422 EIEELLKKLEEaelkelQAELEELEEELEELQEELERLEEALEELRE-ELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 495 QSKDSMLPVTNGAPAAPLALDHSP--KSLACQIGGEGPGSLDLPSPASYSGITRLSECLQAPDSHPELDSPFQMVSQDPQ 572
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDS 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 573 TSDQTQESDPTGEAHQ---------SLEKSGHRVSV-------QSPIVWDPPQGAEIRIDVQEL-------GET-GSREA 628
Cdd:TIGR02168 581 IKGTEIQGNDREILKNiegflgvakDLVKFDPKLRKalsyllgGVLVVDDLDNALELAKKLRPGyrivtldGDLvRPGGV 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 629 SEGESVPEAQVL---KQENPECRPRSAEFILLEPLKDQK--TLEPELELSKQQTE---TGGHEQRPKGLVNKLVLQKPQQ 700
Cdd:TIGR02168 661 ITGGSAKTNSSIlerRREIEELEEKIEELEEKIAELEKAlaELRKELEELEEELEqlrKELEELSRQISALRKDLARLEA 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 701 TSEGPPDAWSREEpipgETLATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAH 780
Cdd:TIGR02168 741 EVEQLEERIAQLS----KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 781 LEVEARAREQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESqvrcHLEEA 860
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE----ALALL 892
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 861 EREHLEKQALREELEKAVvrgQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMK 940
Cdd:TIGR02168 893 RSELEELSEELRELESKR---SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEE 969
|
730
....*....|....*
gi 2778277499 941 LKARALQLEEELIQL 955
Cdd:TIGR02168 970 ARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
880-1203 |
3.60e-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: 84.72 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 880 RGQELgDRLEHLQRELEQAALERQKFLQERESQHQRYQ---HLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLR 956
Cdd:TIGR02168 675 RRREI-EELEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 957 QYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEK 1036
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1037 SMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHREL 1116
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1117 QGRHEQLQAQRASVEAQEVALLAERERLMQdghrqrgleeelrRLQNEHdraQMLLAEVSRERGELQGERGELRSRLARL 1196
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQE-------------RLSEEY---SLTLEEAEALENKIEDDEEEARRRLKRL 977
|
....*..
gi 2778277499 1197 ELERAQL 1203
Cdd:TIGR02168 978 ENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
717-1291 |
3.28e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.64 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 717 GETLATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQ--ARRTEAEAHLE--VEARAREQAR 792
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnNEIERLEARLErlEDRRERLQQE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 793 LREAVDAASL-ELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQV-----RCHLEEAEREHLE 866
Cdd:TIGR02168 423 IEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELaqlqaRLDSLERLQENLE 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 867 ------KQALREELEKAVVRGQ-----------------ELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRL 923
Cdd:TIGR02168 503 gfsegvKALLKNQSGLSGILGVlselisvdegyeaaieaALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIK 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 924 EAELQAASTNKEEALMKLKARALQLEEELIQLRQ---------YPVD---QATEVRAE---------------------- 969
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvLVVDdldNALELAKKlrpgyrivtldgdlvrpggvit 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 970 PRTVETQNGRLiEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRK 1049
Cdd:TIGR02168 663 GGSAKTNSSIL-ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1050 LGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQ---AQ 1126
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeeaAN 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1127 RASVEAQEVALLAERERLMQDGHRQ-RGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEI 1205
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQiEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1206 QSQKLRESNQQLDLSACRLTTQcelLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALR 1285
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREK---LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....*.
gi 2778277499 1286 REKQKL 1291
Cdd:TIGR02168 979 NKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1204 |
4.29e-14 |
|
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: 77.80 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 859 EAEREHLEKQALREELEKAVVRgqELGDRLEHLQRELEQAalERQKFLQERESQHQRYQHLEQRLEAELQAASTNK---- 934
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIID--EKRQQLERLRREREKA--ERYQALLKEKREYEGYELLKEKEALERQKEAIERqlas 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 935 -EEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPrtvetqngrlievERNNATLVAEKAALQGQLQHLEGQLGSLQG 1013
Cdd:TIGR02169 249 lEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLG-------------EEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1014 RAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELE 1093
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1094 GLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLmqdGHRQRGLEEELRRLQNEHDRAQMLLA 1173
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLSKYEQELY 472
|
330 340 350
....*....|....*....|....*....|.
gi 2778277499 1174 EVSRERGELQGERGELRSRLARLELERAQLE 1204
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
778-1287 |
8.04e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 8.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 778 EAHLEVEaRAREQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREgpRLRAQVEAAEQQVQALESQvrchL 857
Cdd:COG4913 239 RAHEALE-DAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAE----L 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 858 EEAEREHLEKQALREELEKAvvRGQELGDRLEHLQRELEQAALErqkfLQERESQHQRYQHLEQRLEAELQAASTNKEEA 937
Cdd:COG4913 312 ERLEARLDALREELDELEAQ--IRGNGGDRLEQLEREIERLERE----LEERERRRARLEALLAALGLPLPASAEEFAAL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 938 LMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNN----ATLVAEKAALQGQLQHLEGQL----- 1008
Cdd:COG4913 386 RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEAELpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1009 ----------------GSLQGRAQELL---------------------LQSQRAQEHSSRLQAEK-------SMMEIQG- 1043
Cdd:COG4913 466 lievrpeeerwrgaieRVLGGFALTLLvppehyaaalrwvnrlhlrgrLVYERVRTGLPDPERPRldpdslaGKLDFKPh 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1044 -------QELHRKLGVL----EEEVRVARRA--------QEETRGQ---QQALLRDH----EALVQLQRRQEtELEGLLV 1097
Cdd:COG4913 546 pfrawleAELGRRFDYVcvdsPEELRRHPRAitragqvkGNGTRHEkddRRRIRSRYvlgfDNRAKLAALEA-ELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1098 RHRDLKANMRALELAHRELQGRHEQLQAQR---------ASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRA 1168
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1169 QMLLAEVSRERGELQGERGELRSRLARLE-----LERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR 1243
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQdrleaAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNR 784
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2778277499 1244 QLLAEVQALSRENRELLERSLESRDHLhREQREYLDQLNALRRE 1287
Cdd:COG4913 785 AEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEED 827
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
55-182 |
1.56e-13 |
|
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor proteins, Hook-related proteins and nuclear mitotic apparatus protein (NuMA). They share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain with an extended alpha-helix. The Hook domain is responsible for the binding of microtubule. The Hook family includes microtubule-binding proteins, Hook1-3. Hook1 is required for spermatid differentiation. Hook2 contributes to the establishment and maintenance of centrosome function. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking, and is involved in Golgi and endosome transport. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. The Hook-related protein (HkRP) family includes Daple, Girdin and Gipie. Daple, also called Dvl-associating protein with a high frequency of leucine residues, or coiled-coil domain-containing protein 88C(CCDC88C), or Hook-related protein 2 (HkRP2), is a novel non-receptor nucleotide exchange factor (GEF) required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Girdin, also called Akt phosphorylation enhancer (APE), or coiled-coil domain-containing protein 88A (CCDC88A), or G alpha-interacting vesicle-associated protein (GIV), or Girders of actin filament, or Hook-related protein 1 (HkRP1), is a bifunctional modulator of guanine nucleotide-binding proteins (G proteins). Gipie, also called GRP78-interacting protein induced by ER stress, or coiled-coil domain-containing protein 88B(CCDC88B), or brain leucine zipper domain-containing protein, or Hook-related protein 3 (HkRP3), is a novel actin cytoskeleton-binding protein and Akt substrate that regulates cell migratory responses in various biological contexts. NuMA, also called nuclear mitotic apparatus protein 1, or nuclear matrix protein-22 (NMP-22), or SP-H antigen, is a microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignment and the segregation of chromosomes during mitotic cell division.
Pssm-ID: 411792 Cd Length: 145 Bit Score: 69.23 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 55 FLKLISGDLLLRVLGIIAPSS-RGRLQMVKGHDGPAACRIWNLYHLWGRLRDFYQEEL-QLLILSPPPDLQTLgfdpFSE 132
Cdd:cd22211 20 LDDLSDGVVLAEILSQIDPSYfDSEWLESRDSSDNWVLKLNNLKKLYRSLSKYYREVLgQQLSDLPLPDLSAI----ARD 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2778277499 133 EAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEVTQ 182
Cdd:cd22211 96 GDEEEIVKLLELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
857-1189 |
1.68e-13 |
|
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: 75.86 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 857 LEEAER--EHLEKQAlreeleKAVVRGQELGDRLEHLQRELEQAALER-QKFLQERESQHQRYQHLEQRLEAELqaasTN 933
Cdd:TIGR02168 195 LNELERqlKSLERQA------EKAERYKELKAELRELELALLVLRLEElREELEELQEELKEAEEELEELTAEL----QE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 934 KEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQG 1013
Cdd:TIGR02168 265 LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1014 RAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELE 1093
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1094 GLL-----VRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRA 1168
Cdd:TIGR02168 425 ELLkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
330 340
....*....|....*....|.
gi 2778277499 1169 QMLLAEVSRERGELQGERGEL 1189
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-1303 |
4.51e-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: 74.33 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLE---AKLQAQAQRLEARSAEAVSLSEELA-QARRTEAEAHLEVEARAR----EQARLREAV 797
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEeelEKLTEEISELEKRLEEIEQLLEELNkKIKDLGEEEQLRVKEKIGeleaEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 798 DAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKA 877
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 878 VVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLeAELQAASTNKEEALMKLKARALQLEEELIQLRQ 957
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 958 ypvdqatEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGqlqhlegqlGSLQGRAQELLLQSQRAQEHSSRLQ---- 1033
Cdd:TIGR02169 470 -------ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE---------RVRGGRAVEEVLKASIQGVHGTVAQlgsv 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1034 AEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQ------------QALLRDHEA------------LVQLQRRQE 1089
Cdd:TIGR02169 534 GERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKagratflplnkmRDERRDLSIlsedgvigfavdLVEFDPKYE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1090 TEL-----EGLLVRH----RDLKANMRALELA-----------------------HRELQGRHEQLQAQRASVEAQEVAL 1137
Cdd:TIGR02169 614 PAFkyvfgDTLVVEDieaaRRLMGKYRMVTLEgelfeksgamtggsraprggilfSRSEPAELQRLRERLEGLKRELSSL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1138 LAERERL----------MQDGHRQ-RGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQ 1206
Cdd:TIGR02169 694 QSELRRIenrldelsqeLSDASRKiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEED 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1207 SQKLREsnQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQAL-SRENRELLERSL--ESRDHLHREQREYLDQLNA 1283
Cdd:TIGR02169 774 LHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYleKEIQELQEQRIDLKEQIKS 851
|
650 660
....*....|....*....|
gi 2778277499 1284 LRREKQKLVEKIMDQYRVLE 1303
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELE 871
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
726-1323 |
2.02e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.40 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVS-----LSEELAQARRTEAEAHLEVEARAREQARLREAVDAA 800
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 801 SLELEAASREREALAEALAAAGRERRQWEREG-----------------PRLRAQVEAAEQQVQALESqvrchleeaere 863
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSegvkallknqsglsgilGVLSELISVDEGYEAAIEA------------ 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 864 hlekqALREELEKAVVRGqelgdrlehlqrelEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKA 943
Cdd:TIGR02168 542 -----ALGGRLQAVVVEN--------------LNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 944 RALQLEEELIQLRqypvdqatevraepRTVETQNGRLIEVER-NNATLVAEKAALQGQLQHLEGQLGSLQGraqelLLQS 1022
Cdd:TIGR02168 603 VAKDLVKFDPKLR--------------KALSYLLGGVLVVDDlDNALELAKKLRPGYRIVTLDGDLVRPGG-----VITG 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1023 QRAQEHSSRLQAEKSMMEIQGQ--ELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHR 1100
Cdd:TIGR02168 664 GSAKTNSSILERRREIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1101 DLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRG----LEEELRRLQNEHDRAQMLLAEVS 1176
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAELTLLNEEAANLR 823
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1177 RERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSREN 1256
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2778277499 1257 RELLERSLESRdHLHREQREYLDQLNA--------LRREKQKLVEKIMDQYRVLEPGPLPRTKKGSWLADKVKRL 1323
Cdd:TIGR02168 904 RELESKRSELR-RELEELREKLAQLELrleglevrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
259-924 |
3.32e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 259 LALQLTNAKAQLRRLRQEVEEKAELLLDSQAEVQGLESEIRRLRQETQALS--GQAKRAELYREEAEalreragrLPRLQ 336
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEleLEEAQAEEYELLAE--------LARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 337 EELRRCRERLHAAEVFKGQLEEERVlsgALEASKVLLEEQLEIARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLE 416
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 417 QLVEENVELELELQRslepppgspgETSLPGAAPSLQDEVREAEAGRLRTVEQENRTLRGQLQMLREQLDSQRPLLEEQS 496
Cdd:COG1196 379 EELEELAEELLEALR----------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 497 KDsmlpvtngapAAPLALDHSpkslacqiggegpgSLDLPSPASYSGITRLSECLQAPDSHPELDSPFQMVSQDPQTSDQ 576
Cdd:COG1196 449 EE----------EAELEEEEE--------------ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 577 tQESDPTGEAHQSLEKSGHRVSVQSPIVWDPPQGAEIRIDVQELGETGSREaSEGESVPEAQVLKQEnpecRPRSAEFIL 656
Cdd:COG1196 505 -GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE-DDEVAAAAIEYLKAA----KAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 657 LEPLKDQKTLEPELELSKQQTETGGHEQRPKGLVNKLVLqkpqqtsegppdawsREEPIPGETLATAIPEEQALRDEVAQ 736
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV---------------LGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 737 LRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAAsrerealae 816
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE--------- 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 817 alaaagrERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKavvrgqelgdRLEHLQRELE 896
Cdd:COG1196 715 -------ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER----------ELERLEREIE 777
|
650 660 670
....*....|....*....|....*....|....
gi 2778277499 897 Q------AALErqkflqERESQHQRYQHLEQRLE 924
Cdd:COG1196 778 AlgpvnlLAIE------EYEELEERYDFLSEQRE 805
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
729-1264 |
3.87e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 729 ALRDEVAQLRREVVSLEAKLQAQAQRLEA----------RSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVD 798
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEadevleeheeRREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 799 ---------AASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQ-----VEAAEQQVQALESQVRCHLEEAEREH 864
Cdd:PRK02224 290 eleeerddlLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahneeAESLREDADDLEERAEELREEAAELE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 865 LEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQK---FLQERESQHQRYQHLEQRLEAELQAASTNKEEalmkl 941
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNaedFLEELREERDELREREAELEATLRTARERVEE----- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 942 kARALQLEEELIQLRQyPVDQATEVraepRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEgQLGSLQGRAQELLLQ 1021
Cdd:PRK02224 445 -AEALLEAGKCPECGQ-PVEGSPHV----ETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1022 SQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhRD 1101
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL----ER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1102 LKANMRALELAHRELQGRHEQLqAQRASVEAQevallaERERLMQDGHRQRGLEEE-----LRRLQNEHDRAQMLLAEVS 1176
Cdd:PRK02224 594 IRTLLAAIADAEDEIERLREKR-EALAELNDE------RRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVE 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1177 RERGELQGERGELRSRLARLELERAQLEiqsqKLRESNQQLDLSACRLTTQCELLTQLrsaqEEENRQLLAEvqaLSREN 1256
Cdd:PRK02224 667 EKLDELREERDDLQAEIGAVENELEELE----ELRERREALENRVEALEALYDEAEEL----ESMYGDLRAE---LRQRN 735
|
....*...
gi 2778277499 1257 RELLERSL 1264
Cdd:PRK02224 736 VETLERML 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-1282 |
5.01e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 728 QALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQA--------RRTEAEAHLEVEARAREQARLREAVDA 799
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERERRRARLEALLAA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 800 ASLELEAASREREALAEALAaagRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHleEAEREHLEK---------QAL 870
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAA---ALLEALEEELEALEEALAEAEAALRDLRRELREL--EAEIASLERrksniparlLAL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 871 REELEKAVVRGQE----LGDRLEHLQRELE-QAALER----QKFL----QERESQHQRY---QHLEQRLEAElQAASTNK 934
Cdd:COG4913 446 RDALAEALGLDEAelpfVGELIEVRPEEERwRGAIERvlggFALTllvpPEHYAAALRWvnrLHLRGRLVYE-RVRTGLP 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 935 EEALMKLKARALQ-------------LEEELIQLRQYP-VDQATEVRAEPRTVeTQNGrlievernnatlvaekaalqgq 1000
Cdd:COG4913 525 DPERPRLDPDSLAgkldfkphpfrawLEAELGRRFDYVcVDSPEELRRHPRAI-TRAG---------------------- 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1001 LQHLEGQLGSLQGR---AQELLLQSQRAQehssRLQAeksmmeiqgqeLHRKLGVLEEEVRVARRAQEETRGQQQALLRD 1077
Cdd:COG4913 582 QVKGNGTRHEKDDRrriRSRYVLGFDNRA----KLAA-----------LEAELAELEEELAEAEERLEALEAELDALQER 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1078 HEALVQLQRRQETEL--EGLLVRHRDLKANMRALELAHRELqgrhEQLQAQRASVEAQEVALLAERERLMQdghRQRGLE 1155
Cdd:COG4913 647 REALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKG---EIGRLE 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1156 EELRRLQNEHDRAQMLLAEVsrERGELQGERGELRSRLARLELERAQLEIQsQKLRESNQQLDLSACRLTTQCE-LLTQL 1234
Cdd:COG4913 720 KELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNRAEEELErAMRAF 796
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2778277499 1235 RSAQEEENRQLLAEVQALsRENRELLERsLEsRDHLHREQREYLDQLN 1282
Cdd:COG4913 797 NREWPAETADLDADLESL-PEYLALLDR-LE-EDGLPEYEERFKELLN 841
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
852-1204 |
6.48e-12 |
|
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: 70.87 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 852 QVRCHLEEAEREhleKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEaELQAAS 931
Cdd:TIGR02169 678 RLRERLEGLKRE---LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 932 TNKEEALMKLKARALQLEEELIQLRqypvDQATEVRAEPRTVETQngrliEVERNNATLVAEKAALQGQLQHLEGQLGSL 1011
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLE----EALNDLEARLSHSRIP-----EIQAELSKLEEEVSRIEARLREIEQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1012 QGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVrvarraqEETRGQQQALLRDHEALVQLQRRQETE 1091
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-------EELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1092 LEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQ---RGLEEELRRLQNEHDRA 1168
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQaelQRVEEEIRALEPVNMLA 977
|
330 340 350
....*....|....*....|....*....|....*.
gi 2778277499 1169 QMLLAEVSRERGELQGERgelrsrlARLELERAQLE 1204
Cdd:TIGR02169 978 IQEYEEVLKRLDELKEKR-------AKLEEERKAIL 1006
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
727-1295 |
1.87e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 727 EQALRDEVAQLRREVVSLEAKLQAQAQR--LEARSAEAVSLSEElaqARRTEAEAHLEvEARAREQARLREAVDAASlel 804
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDARKAEA---ARKAEEERKAE-EARKAEDAKKAEAVKKAE--- 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 805 EAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALES-QVRCHLEEAEREHLEKQALREELEKAVVRGQE 883
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 884 L--GDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEAlmKLKARALQLEEELIQLRQYPVD 961
Cdd:PTZ00121 1314 AkkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA--EKKKEEAKKKADAAKKKAEEKK 1391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 962 QATEV--RAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQlGSLQGRAQELLLQSQ---RAQEHSSRLQAEK 1036
Cdd:PTZ00121 1392 KADEAkkKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKADEAKKKAEeakKAEEAKKKAEEAK 1470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1037 SMMEIQGQ-ELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELegllvrhRDLKANMRALELAHRE 1115
Cdd:PTZ00121 1471 KADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-------KKAEEAKKADEAKKAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1116 LQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLL--------------AEVSRERGE 1181
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeekkmkaeeakkAEEAKIKAE 1623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1182 LQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQCE----LLTQLRSAQEEENRQllaeVQALSRENR 1257
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkKAEEAKKAEEDEKKA----AEALKKEAE 1699
|
570 580 590
....*....|....*....|....*....|....*...
gi 2778277499 1258 EllERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:PTZ00121 1700 E--AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-1295 |
2.12e-11 |
|
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: 68.94 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELE 805
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 806 AASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQ---VRCHLEEAEREHLEKQALREELEKAVVRGQ 882
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEkedKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 883 E----LGDRLEHLQRELeqAALERQKFLQERESQHQRYQHL-------------------EQRLEAELQAASTNKEEALM 939
Cdd:TIGR02169 476 EeydrVEKELSKLQREL--AEAEAQARASEERVRGGRAVEEvlkasiqgvhgtvaqlgsvGERYATAIEVAAGNRLNNVV 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 940 ----KLKARALQLeeeliqLRQYPVDQAT-----EVRAEPRTVE--TQNG------RLIEVERNNA---------TLVAE 993
Cdd:TIGR02169 554 veddAVAKEAIEL------LKRRKAGRATflplnKMRDERRDLSilSEDGvigfavDLVEFDPKYEpafkyvfgdTLVVE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 994 KAAL------QGQLQHLEGQL--------------GSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVL 1053
Cdd:TIGR02169 628 DIEAarrlmgKYRMVTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1054 EEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALElahrelqGRHEQLQAQRASVEAQ 1133
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE-------ARIEELEEDLHKLEEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1134 EVALLAererlMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQsqklRES 1213
Cdd:TIGR02169 781 LNDLEA-----RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----IKS 851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1214 NQQldlsacrltTQCELLTQLRSAQEEEnrqllaevqalsrENRELLERSLESR-DHLHREQREYLDQLNALRREKQKLV 1292
Cdd:TIGR02169 852 IEK---------EIENLNGKKEELEEEL-------------EELEAALRDLESRlGDLKKERDELEAQLRELERKIEELE 909
|
...
gi 2778277499 1293 EKI 1295
Cdd:TIGR02169 910 AQI 912
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
992-1323 |
2.22e-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: 68.93 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 992 AEKA----ALQGQLQHLEGQLgslqgraqeLLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEET 1067
Cdd:TIGR02168 209 AEKAerykELKAELRELELAL---------LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1068 RGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERErlmqd 1147
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE----- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1148 ghrqrGLEEELRRLQNEhdraqmlLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQ 1227
Cdd:TIGR02168 355 -----SLEAELEELEAE-------LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1228 CELLTQLRSAQE--------EENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALrREKQKLVEKIMDQY 1299
Cdd:TIGR02168 423 IEELLKKLEEAElkelqaelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENL 501
|
330 340
....*....|....*....|....
gi 2778277499 1300 RVLEPGPLPRTKKGSWLADKVKRL 1323
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVL 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
998-1303 |
2.93e-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: 68.54 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 998 QGQLQHLEGQLGSLQGRAQELLLQSQRAQEHssrlqaeksmMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRD 1077
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAEKAERY----------KELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1078 HEALvqlqRRQETELEGLLVRHRDLKANMRALElahRELQGRHEQLQAQRASVEAQEVALLAERERLMQDghrQRGLEEE 1157
Cdd:TIGR02168 255 LEEL----TAELQELEEKLEELRLEVSELEEEI---EELQKELYALANEISRLEQQKQILRERLANLERQ---LEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1158 LRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELE-----------RAQLEIQSQKLRESNQQLDLSACRLTT 1226
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrleelEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 1227 QCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1303
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1098-1298 |
3.69e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1098 RHRDLKANMRALELAHRELqgRHEQLQAQRASVEAQEVALLAERERLMQdghRQRGLEEELRRLQNEHDRAQMLLAEVSR 1177
Cdd:COG1196 214 RYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1178 ERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENR 1257
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2778277499 1258 ELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1298
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
274-1131 |
4.01e-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: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 274 RQEVEEKAELLLDSQAEVQGLESEIRRlrqETQALSGQAKRAELYREEAEALRERAGRLprLQEELRRCRERLHAAEVFK 353
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELER---QLKSLERQAEKAERYKELKAELRELELAL--LVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 354 GQLEEERVlsgALEASKVLLEEQLEIAR----ERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELEL 429
Cdd:TIGR02168 249 KEAEEELE---ELTAELQELEEKLEELRlevsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 430 QRSLEpppgSPGETSLpgAAPSLQDEVREAEAgRLRTVEQENRTLRGQLQMLREQLDSQRPLLEEQSKDSmlpvtngapa 509
Cdd:TIGR02168 326 EELES----KLDELAE--ELAELEEKLEELKE-ELESLEAELEELEAELEELESRLEELEEQLETLRSKV---------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 510 apLALDHSPKSLACQIGGEGPGSLDLPSPASySGITRLSECLQAPDSHPELDSPFQMVSQDPQTSDQTQESDPTGEAHQS 589
Cdd:TIGR02168 389 --AQLELQIASLNNEIERLEARLERLEDRRE-RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 590 LEKSGHRVSVQSPIVWDPPQGAEIRIDVQElgetGSREASEGESVPEAQVLKQEN--PECRPRSAEFILLEPlKDQKTLE 667
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEGFSEGVKALLKNQSglSGILGVLSELISVDE-GYEAAIE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 668 PELELSKQQTETGGhEQRPKGLVNKLVLQKPQQTSEGPPDAwsreepIPGETLATAIPEEQALRDEVAQLRREVVSLEAK 747
Cdd:TIGR02168 541 AALGGRLQAVVVEN-LNAAKKAIAFLKQNELGRVTFLPLDS------IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 748 LQAQAQRLEARSAEAVSLSEELAQARRT-----------------------EAEAHLEVEARAREQARLREAVDAASLEL 804
Cdd:TIGR02168 614 LRKALSYLLGGVLVVDDLDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 805 EAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKavvrgqel 884
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE-------- 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 885 gdrlehLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAeLQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQAT 964
Cdd:TIGR02168 766 ------LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 965 EVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQ 1044
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1045 ELHRKLGVLEEEVRVAR----RAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKA-----NMRALElAHRE 1115
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEvridNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvNLAAIE-EYEE 997
|
890
....*....|....*.
gi 2778277499 1116 LQGRHEQLQAQRASVE 1131
Cdd:TIGR02168 998 LKERYDFLTAQKEDLT 1013
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
92-180 |
7.09e-11 |
|
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes Hook1-3. Hook1 is a microtubule-binding protein required for spermatid differentiation. Hook2, also a microtubule-binding protein, contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook proteins are components of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex. Hook adaptor proteins share an N-terminal conserved globular Hook domain, which folds as a variant of the helical calponin homology (CH) domain, and contacts the helix alpha1 of dynein light intermediate chain 1 (LIC1) in a hydrophobic groove.
Pssm-ID: 411793 Cd Length: 147 Bit Score: 61.88 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 92 RIWNLYHLWGRLRDFYQEEL-QLLILSPPPDLQTLGfdpfSEEAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQ 170
Cdd:cd22222 60 KVSNLKKILKGIVDYYSEVLgQQISGFTMPDVNAIA----EKEDPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQ 135
|
90
....*....|
gi 2778277499 171 SELAAAIQEV 180
Cdd:cd22222 136 HVVMEAIQEL 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
730-1298 |
1.12e-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: 66.62 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 730 LRDEVAQLRREVVSLEAK---------LQAQAQRLEARSA--EAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVD 798
Cdd:TIGR02168 191 LEDILNELERQLKSLERQaekaerykeLKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 799 aaslELEAASREREALAEALAAA------------GRERRQWEREgPRLRAQVEAAEQQVQALESQVRCHLEEAER---- 862
Cdd:TIGR02168 271 ----ELRLEVSELEEEIEELQKElyalaneisrleQQKQILRERL-ANLERQLEELEAQLEELESKLDELAEELAEleek 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 863 -EHLEKQ--ALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLE---QRLEAELQAASTNKEE 936
Cdd:TIGR02168 346 lEELKEEleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 937 ALMKLKARALQ-LEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVE-------RNNATLVAEKAALQGQLQHLEG-- 1006
Cdd:TIGR02168 426 LLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEqaldaaeRELAQLQARLDSLERLQENLEGfs 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1007 -----------QLGSLQGRAQELL-------------LQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARR 1062
Cdd:TIGR02168 506 egvkallknqsGLSGILGVLSELIsvdegyeaaieaaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1063 AQ-------EETRGQQQALLRDHEALVQL----------------------QRRQETE------LEGLLVRHRDL----- 1102
Cdd:TIGR02168 586 IQgndreilKNIEGFLGVAKDLVKFDPKLrkalsyllggvlvvddldnaleLAKKLRPgyrivtLDGDLVRPGGVitggs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1103 ----------KANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQR----GLEEELRRLQNEHDRA 1168
Cdd:TIGR02168 666 aktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisALRKDLARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1169 QMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLsacRLTTQCELLTQLRSAQEEENRQL--L 1246
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE---ELKALREALDELRAELTLLNEEAanL 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 2778277499 1247 AEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1298
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
992-1221 |
1.12e-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: 65.17 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 992 AEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQ 1071
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1072 QALLRdhealvQLQRRQETELEGLLVRHRDLKANMRALELAH---RELQGRHEQLQAQRASVEAQEVALLAERERLMQDg 1148
Cdd:COG4942 107 AELLR------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEAL- 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2778277499 1149 hrQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSA 1221
Cdd:COG4942 180 --LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
726-1312 |
1.54e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELE 805
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 806 AASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVrchlEEAEREHLEKQALREELEKAvvrgQELG 885
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----EEAKKKADAAKKKAEEKKKA----DEAK 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 886 DRLEHLQR---ELEQAALERQKF--LQERESQHQRYQHLEQRLEaELQAASTNKEEALMKLKARALQLEEEliqlRQYPV 960
Cdd:PTZ00121 1398 KKAEEDKKkadELKKAAAAKKKAdeAKKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAE----EAKKA 1472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 961 DQATEVRAEPRTVETQNGRLIEVERNNATLvaeKAALQGQLQHLEGQLGSLQGRAQELllqsQRAQEHSSRLQAEKSMME 1040
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEA---KKAAEAKKKADEAKKAEEAKKADEA----KKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1041 IQGQELHRKLGVLE-EEVRVARRAQEETRGQQQAlLRDHEALVQLQRRQETELEGLLVRHRDLKAnmralELAHRELQGR 1119
Cdd:PTZ00121 1546 KKADELKKAEELKKaEEKKKAEEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKA-----EEAKKAEEAK 1619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1120 HEQLQAQRASVEAQEVALLAERErlmqdghrqrglEEELRR---LQNEHDRAQMLLAEVSRERGELQGERGELRsrlaRL 1196
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKE------------AEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAK----KA 1683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1197 ELERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAqEEENRQLLAEVQALSRENR---ELLERSLESRDHLHRE 1273
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHL 1762
|
570 580 590
....*....|....*....|....*....|....*....
gi 2778277499 1274 QREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKK 1312
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
834-1323 |
1.61e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 834 RLRAQVEAAEQQVQALEsQVRCHLEEAEREHLEKQALREELEKAVV-----RGQELGDRLEHLQRELEQAALERQKFLQE 908
Cdd:COG4913 239 RAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 909 RESQHQRYQHLEQRL-------EAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATE----VRAEPRTVETQN 977
Cdd:COG4913 318 LDALREELDELEAQIrgnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEfaalRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 978 GRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEhssrlqaeksmmeiqgqELHRKLGVLEEEV 1057
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD-----------------ALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1058 RVAR-----RAQEET---------RGQQQALLRDHEALVQL-----QRRQETELEGLLVRHRDLKANMRALE---LAHR- 1114
Cdd:COG4913 461 PFVGelievRPEEERwrgaiervlGGFALTLLVPPEHYAAAlrwvnRLHLRGRLVYERVRTGLPDPERPRLDpdsLAGKl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1115 -----ELQGRHEQLQAQRAS---VEAQEvALLAERERLMQDGHRQRG----------------------------LEEEL 1158
Cdd:COG4913 541 dfkphPFRAWLEAELGRRFDyvcVDSPE-ELRRHPRAITRAGQVKGNgtrhekddrrrirsryvlgfdnraklaaLEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1159 RRLQNEHDRAQMLLAEVSRERGELQGERGELRS---------RLARLELERAQLEIQSQKLRESNQQLDlsacRLTTQCE 1229
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDDLA----ALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1230 LLTQLRSAQEEENRQLLAEVQALSRENRELLErslesrdhlhrEQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPR 1309
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEE-----------ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVE 764
|
570
....*....|....
gi 2778277499 1310 TKKGSWLADKVKRL 1323
Cdd:COG4913 765 RELRENLEERIDAL 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
769-1243 |
3.04e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 769 LAQARRTEAEAHLEVEARA--REQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQV 846
Cdd:COG4717 39 LLAFIRAMLLERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 847 QALESQVRCH-----LEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALE-RQKFLQERESQHQRYQHLE 920
Cdd:COG4717 119 EKLEKLLQLLplyqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 921 QRLEaELQAASTNKEEALMKLKARALQLEEELIQLR-QYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQG 999
Cdd:COG4717 199 EELE-ELQQRLAELEEELEEAQEELEELEEELEQLEnELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1000 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLE----EEVRVARRAQEETRGQQQALL 1075
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspEELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1076 RDHEALvqLQRRQETELEGLLvrhRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRgLE 1155
Cdd:COG4717 358 ELEEEL--QLEELEQEIAALL---AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-LE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1156 EELRRLQNEhdraqmlLAEVSRERGELQGERGELRSRLARLELER--AQLEIQSQKLRESNQQLDLSACRLTTQCELLTQ 1233
Cdd:COG4717 432 EELEELEEE-------LEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
490
....*....|
gi 2778277499 1234 LRSAQEEENR 1243
Cdd:COG4717 505 AREEYREERL 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
744-1298 |
7.00e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 744 LEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEahleVEARAREQARLREAVdaASLELEAASREREALAEALAAAGR 823
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEK----LEKEVKELEELKEEI--EELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 824 ERRqweregprlraqVEAAEQQVQALESQVRcHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEqaALERQ 903
Cdd:PRK03918 265 EER------------IEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 904 kfLQERESQHQRYQHLEQRLEAELQAASTNKEEAlmKLKARALQLEEELIQLRQypvdqatevRAEPRTVETQNGRLIEV 983
Cdd:PRK03918 330 --IKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKK---------RLTGLTPEKLEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 984 ERnnatlvaEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQEHSSRLQAEKSMMEIQGQELHRklgvlEEEVRVARRA 1063
Cdd:PRK03918 397 EK-------AKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGKCPVCGRELTE-----EHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1064 QEETRGQQQALLRDHEALVQLqRRQETELEGLLVRHRDLKANMRALELAhRELQGRHEQLQAQRASVEAQEVALLAER-- 1141
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQL-KELEEKLKKYNLEELEKKAEEYEKLKEKli 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1142 ------ERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGER-GELRSRLARLE-LERAQLEIQS--QKLR 1211
Cdd:PRK03918 536 klkgeiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEpFYNEYLELKDaeKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1212 ESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKL 1291
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
....*..
gi 2778277499 1292 VEKIMDQ 1298
Cdd:PRK03918 696 LEKLKEE 702
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
722-1162 |
2.19e-09 |
|
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: 62.66 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 722 TAIPEEQALRDEVAQLRREVVS-LEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAA 800
Cdd:COG3096 246 EAIRVTQSDRDLFKHLITEATNyVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 801 SLELEAASREREALAEALAAAGR-ERRQWEregprLRAQVEAAEQQVQAlesqvrchLEEAEREHLEKQALREELEKAVv 879
Cdd:COG3096 326 EQDYQAASDHLNLVQTALRQQEKiERYQED-----LEELTERLEEQEEV--------VEEAAEQLAEAEARLEAAEEEV- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 880 rgQELGDRLEHLQRELEQaalerqkfLQERESQ-HQRYQHLE--QRLEAELQAASTNKEEALMKLKARALQLEEELIQLR 956
Cdd:COG3096 392 --DSLKSQLADYQQALDV--------QQTRAIQyQQAVQALEkaRALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 957 QYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVA--------EKAALQGQLQHLEGQLGSLQGRAQelllQSQRAQEh 1028
Cdd:COG3096 462 QKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTArellrryrSQQALAQRLQQLRAQLAELEQRLR----QQQNAER- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1029 ssrlqaeksmmeiQGQELHRKLGvleeEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRA 1108
Cdd:COG3096 537 -------------LLEEFCQRIG----QQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2778277499 1109 LELAHRELQGRHEQLQAQ--------------RASVEAQEVALLAERERLMQdghRQRGLEEELRRLQ 1162
Cdd:COG3096 600 RAPAWLAAQDALERLREQsgealadsqevtaaMQQLLEREREATVERDELAA---RKQALESQIERLS 664
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
861-1295 |
4.23e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 861 EREHLEKQALR-EELEKAVvrgqelgDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAelqaastnKEEALM 939
Cdd:PRK03918 146 SREKVVRQILGlDDYENAY-------KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEE--------VLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 940 KLKARALQLEEELiqlrqypvdqaTEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL 1019
Cdd:PRK03918 211 EISSELPELREEL-----------EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1020 LQSQRAQE------HSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQEtELE 1093
Cdd:PRK03918 280 EKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE-ELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1094 G---LLVRHRDLKANMRALE-----LAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELR------ 1159
Cdd:PRK03918 359 ErheLYEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkc 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1160 ----RLQNEHDRAQmLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLResnqqldlsacRLTTQCELLTQLR 1235
Cdd:PRK03918 439 pvcgRELTEEHRKE-LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES-----------ELIKLKELAEQLK 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1236 SAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREyLDQLNALRREKQKLVEKI 1295
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKL 565
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
650-1295 |
5.66e-09 |
|
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: 61.14 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 650 RSAEFILLEPLKDQKTLEPELELSKQQTETGGHEQRPKGLVNKLVLQKPQqtSEGPPDAWSREEPIPGETLATAIPEEQA 729
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLR--SQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 730 LRDEVAQLRREvvslEAKLQAQAQRLEARSAEAVSLSEELAQARRTEA-EAHLEVEARAREQARLREAVDAASLELEAAS 808
Cdd:TIGR00618 231 LREALQQTQQS----HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAqEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 809 REREALAEALAAAGRERRQwEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRL 888
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAK-LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 889 EHLQRELEQAALERQKFLQERESQHQR-YQHLEQR-LEAELQAASTNKEEALMKLKARALQLEEELIQLRQ---YPVDQA 963
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIdTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLekiHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 964 TEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQS------QRAQEHSSRLQAEKS 1037
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1038 MMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQ 1117
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1118 GRHEQLQAQRASVEAQEVALLA---ERERLMQDGHRQRGL------EEELRRLQNEHDRAQMLLAEVSRERGELQGERGE 1188
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTAlhaLQLTLTQERVREHALsirvlpKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1189 LRSRLARLELERAQLEIQSQKLRESNQQLdlsACRLTTQCELLTQLRsAQEEENRQLLAEVQALSRENRELLERSLESRD 1268
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDL---AAREDALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
650 660
....*....|....*....|....*..
gi 2778277499 1269 HLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
825-1169 |
6.50e-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: 60.85 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 825 RRQWEREGPRLRAQVEAAEQQVQALESQVrchleeaerehlekQALREELEKAVVRGQELGDRLEHLQRELEQAALERQK 904
Cdd:TIGR02169 218 KEKREYEGYELLKEKEALERQKEAIERQL--------------ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 905 FLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQypvdqatEVRAEPRTVETQNGRlieve 984
Cdd:TIGR02169 284 LGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA-------EIEELEREIEEERKR----- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 985 rnnatlvaeKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQ 1064
Cdd:TIGR02169 352 ---------RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1065 EETRgqqqallrdhealvqlqrrqeTELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERl 1144
Cdd:TIGR02169 423 ADLN---------------------AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR- 480
|
330 340
....*....|....*....|....*
gi 2778277499 1145 mqdghrqrgLEEELRRLQNEHDRAQ 1169
Cdd:TIGR02169 481 ---------VEKELSKLQRELAEAE 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
720-1285 |
7.49e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.52 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 720 LATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAE----AHLEVEARAREQARLRE 795
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEqlrkMMLSHEGVLQEIRSILV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 796 AVDAASLE--LEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREH--------- 864
Cdd:pfam15921 195 DFEEASGKkiYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHqdrieqlis 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 865 ---LEKQALREELEKAVVRGQELGDRLEHLQR--------------ELEQAALERQKFLQERESQHQ-RYQHLEQRL--- 923
Cdd:pfam15921 275 eheVEITGLTEKASSARSQANSIQSQLEIIQEqarnqnsmymrqlsDLESTVSQLRSELREAKRMYEdKIEELEKQLvla 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 924 EAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNG--------------RLIEVERNNAT 989
Cdd:pfam15921 355 NSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhlrrelddRNMEVQRLEAL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 990 LVAEKAALQGQlqhLEGQLGSLQGRAQELllqsQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRG 1069
Cdd:pfam15921 435 LKAMKSECQGQ---MERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1070 QQQALLRDHEALVQLQRRQETELEGLlvrhRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGH 1149
Cdd:pfam15921 508 KERAIEATNAEITKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1150 RQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQL-EIQSQKLR---ESNQQLDlsacrlt 1225
Cdd:pfam15921 584 TAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvNAGSERLRavkDIKQERD------- 656
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1226 tqcELLTQLRSAQEEENrQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALR 1285
Cdd:pfam15921 657 ---QLLNEVKTSRNELN-SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
836-1295 |
1.11e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 836 RAQVEAAEQQVQALESQVrchlEEAEREhleKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQR 915
Cdd:PRK02224 250 REELETLEAEIEDLRETI----AETERE---REELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 916 YQHLEQRLEAELQAASTNKEEAlMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEvernnatlvaeka 995
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEA-ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE------------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 996 alqgqlqhLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSmmeiqgqELHRKLGVLEEEVRVARRAQEETrgqqqall 1075
Cdd:PRK02224 389 --------LEEEIEELRERFGDAPVDLGNAEDFLEELREERD-------ELREREAELEATLRTARERVEEA-------- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1076 rdhEALVQLQRRQETElegllvrhRDLKANMRALELAHRElqGRHEQLQAQRASVEAQEVALLAERERLMQdghrQRGLE 1155
Cdd:PRK02224 446 ---EALLEAGKCPECG--------QPVEGSPHVETIEEDR--ERVEELEAELEDLEEEVEEVEERLERAED----LVEAE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1156 EELRRLQNEHDRAQMLLAEvSRERGELQGERGE-LRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQcelLTQL 1234
Cdd:PRK02224 509 DRIERLEERREDLEELIAE-RRETIEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK---LAEL 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2778277499 1235 RSAQEEENRqlLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:PRK02224 585 KERIESLER--IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
762-1130 |
1.17e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 762 AVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAAsrerealaealaaagrerrqwEREGPRLRAQVEA 841
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA---------------------SRKIGEIEKEIEQ 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 842 AEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQ-AALERQKFLQERESQHQRYQHLE 920
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEV 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 921 QRLEAELQAASTnKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNA----TLVAEKAA 996
Cdd:TIGR02169 808 SRIEARLREIEQ-KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaalrDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 997 LQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRvARRAQEETRGQQQALLR 1076
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEE 965
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2778277499 1077 DHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASV 1130
Cdd:TIGR02169 966 EIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
739-1186 |
1.48e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 739 REVVSLEAKLQAQAQRLEARSAEAVSLSEelAQARRTEAEA---HLEVEARAREQARLREAVDAASLELEAASREREALA 815
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE--LEEELEELEAeleELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 816 EALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKqalREELEKAVvrgQELGDRLEHLQREL 895
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE---LEELQQRL---AELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 896 EQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVET 975
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 976 QNGRLIEVERNNATlvaEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRK-----L 1050
Cdd:COG4717 303 EAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1051 GVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHrDLKANMRALELAHRELQGRHEQLQAQRASV 1130
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-ELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 1131 EaQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGER 1186
Cdd:COG4717 459 E-AELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
882-1295 |
7.36e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 882 QELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRL-EAELQAASTNKEEAlmKLKARALQLEEELIQLRQypv 960
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgEIEKEIEQLEQEEE--KLKERLEELEEDLSSLEQ--- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 961 dqatevraeprtvetqngRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLqgraqelllqsqraqehssrlqaEKSMME 1040
Cdd:TIGR02169 752 ------------------EIENVKSELKELEARIEELEEDLHKLEEALNDL-----------------------EARLSH 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1041 IQGQELHRKLGVLEEEVRvarraqeETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRH 1120
Cdd:TIGR02169 791 SRIPEIQAELSKLEEEVS-------RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1121 EQLQAQRASVEAQEvallaererlmqdghrqRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLEler 1200
Cdd:TIGR02169 864 EELEEELEELEAAL-----------------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK--- 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1201 AQLEIQSQKLREsnqqLDLSACRLTTQCELLTQLRSAQEEENRqLLAEVQALSRENRelleRSLESRDHLHREQREYLDQ 1280
Cdd:TIGR02169 924 AKLEALEEELSE----IEDPKGEDEEIPEEELSLEDVQAELQR-VEEEIRALEPVNM----LAIQEYEEVLKRLDELKEK 994
|
410
....*....|....*
gi 2778277499 1281 LNALRREKQKLVEKI 1295
Cdd:TIGR02169 995 RAKLEEERKAILERI 1009
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
724-1209 |
1.07e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.05 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 724 IPEEQAlRDEVAQLRREVVSLEAKL-QAQAQRLEARSA---EAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDA 799
Cdd:pfam15921 303 IIQEQA-RNQNSMYMRQLSDLESTVsQLRSELREAKRMyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 800 ASLELEAASREREALAEalaaagRERRQWEREG------PRLRAQVEAAEQQVQALESQVRCHLEEA----EREHLEKQA 869
Cdd:pfam15921 382 LLADLHKREKELSLEKE------QNKRLWDRDTgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECqgqmERQMAAIQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 870 LREELEKAVVRGQELGDRLEHLQRELEQAALERQKFlqerESQHQRYQHLEQRL-EAELQAASTNKEeaLMKLKARA-LQ 947
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL----ESSERTVSDLTASLqEKERAIEATNAE--ITKLRSRVdLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 948 LEEelIQLRQYPVDQATEVRAEPRTVETQ---NGRLIEVER----NNATLVAEKAALQGQLQ----HLEGQLGSLQGRAQ 1016
Cdd:pfam15921 530 LQE--LQHLKNEGDHLRNVQTECEALKLQmaeKDKVIEILRqqieNMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQ 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1017 ELLLQSQRAQEHSSRLQAEKSMMEIQ-------GQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQE 1089
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEkvklvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1090 TELEGLLVRHR-DLKANMRALELAHRELQ--------------GRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGL 1154
Cdd:pfam15921 688 EEMETTTNKLKmQLKSAQSELEQTRNTLKsmegsdghamkvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFL 767
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2778277499 1155 EEELRRLQNEhdraqmlLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQK 1209
Cdd:pfam15921 768 KEEKNKLSQE-------LSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
835-1219 |
2.49e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.29 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 835 LRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVvrgQELGDRLEHLQRELEQAaleRQKfLQERESQHQ 914
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQR---RELESRVAELKEELRQS---REK-HEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 915 RYQHLEQRLEAELQAASTNKEEAlmklKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVErnnatlvAEK 994
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAH----EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE-------AER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 995 AALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQ-- 1072
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERkv 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1073 -ALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ-LQAQRASVEAqevallaERERLMQDGHR 1150
Cdd:pfam07888 254 eGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQeRETLQQSAEA-------DKDRIEKLSAE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 1151 QRGLEEelrRLQNEHDRAQMLLAEVSRER-------GELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDL 1219
Cdd:pfam07888 327 LQRLEE---RLQEERMEREKLEVELGREKdcnrvqlSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
732-1163 |
3.60e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 732 DEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELA--QARRTEAEAHLeveARAREQARLREAVDAASLELEAASr 809
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESdlEQDYQAASDHL---NLVQTALRQQEKIERYQADLEELE- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 810 erealaealaaagrerrqweregPRLRAQVEA-AEQQVQALESQVRchLEEAEREHLEKQAlreelekavvrgqELGDRl 888
Cdd:PRK04863 362 -----------------------ERLEEQNEVvEEADEQQEENEAR--AEAAEEEVDELKS-------------QLADY- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 889 ehlqreleQAALERQkflQERESQHQRYQHLEQRLEAELQAAS---TNKEEALMKLKARALQLEEELIQLrqypvDQATE 965
Cdd:PRK04863 403 --------QQALDVQ---QTRAIQYQQAVQALERAKQLCGLPDltaDNAEDWLEEFQAKEQEATEELLSL-----EQKLS 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 966 VRAEPRTVETQNGRLI-----EVERNNATLVAEKAALQG-QLQHLEGQLGSLQGRAQEL--LLQSQRAQEhssRLQAEKS 1037
Cdd:PRK04863 467 VAQAAHSQFEQAYQLVrkiagEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRLSELeqRLRQQQRAE---RLLAEFC 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1038 MMEIQGQElhrklgvLEEEVrvarraqEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQ 1117
Cdd:PRK04863 544 KRLGKNLD-------DEDEL-------EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ 609
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1118 GRHEQLQAQ-------RASVEA-------QEVALLAERERLmqdGHRQRGLEEELRRLQN 1163
Cdd:PRK04863 610 DALARLREQsgeefedSQDVTEymqqlleRERELTVERDEL---AARKQALDEEIERLSQ 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
911-1136 |
4.82e-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: 54.00 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 911 SQHQRYQHLEQRLEaELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATL 990
Cdd:COG4942 17 AQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 991 VAEKAALQGQLQHLEGQLGSLQGRAQ-ELLLQSQRAQEHSSRLQAEKSMMEI---QGQELHRKLGVLEEEVRVARRAQEE 1066
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1067 TRGQQQALLRDHEALVQLQRRQETELegllvrhRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVA 1136
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLL-------ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
856-1280 |
5.06e-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: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 856 HLEEAeREHLEKQA-LREELEKAVVRGQELGDRLEHLQRELEQaalerqkfLQERESQhqryqhleqrLEAELQAAStnk 934
Cdd:COG3096 276 HANER-RELSERALeLRRELFGARRQLAEEQYRLVEMARELEE--------LSARESD----------LEQDYQAAS--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 935 eEALMKLKArALQLEEElIQLRQYPVDQATEVRAEprtvetQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQgr 1014
Cdd:COG3096 334 -DHLNLVQT-ALRQQEK-IERYQEDLEELTERLEE------QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQ-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1015 aQELLLQSQRAQEHSSRLQA-EKSMMEIQGQELHRKLGVLEEEvrvARRAQEETRGQQQALLRDHEALVQLQRRQETELE 1093
Cdd:COG3096 403 -QALDVQQTRAIQYQQAVQAlEKARALCGLPDLTPENAEDYLA---AFRAKEQQATEEVLELEQKLSVADAARRQFEKAY 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1094 GLLVRHRDLKANMRALELAhREL--QGRHEQLQAQRASVEAQEvalLAERERLMqdgHRQRGLEEELRRLQNEHDRAQML 1171
Cdd:COG3096 479 ELVCKIAGEVERSQAWQTA-RELlrRYRSQQALAQRLQQLRAQ---LAELEQRL---RQQQNAERLLEEFCQRIGQQLDA 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1172 LAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRsaqeEENRQLLAEVQA 1251
Cdd:COG3096 552 AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLR----EQSGEALADSQE 627
|
410 420 430
....*....|....*....|....*....|..
gi 2778277499 1252 LSRENRELLERSLE---SRDHLhREQREYLDQ 1280
Cdd:COG3096 628 VTAAMQQLLEREREatvERDEL-AARKQALES 658
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1053-1267 |
5.17e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1053 LEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEA 1132
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1133 QevalLAERERLMQDGHRQRGLEEELRRLQ-NEHDRAQMLLAEVSRER----GELQGERGELRSRLARLELERAQLEIQS 1207
Cdd:COG4942 105 E----LAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1208 QKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1267
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
738-1287 |
5.76e-07 |
|
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: 54.36 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 738 RREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAhlevEARAREQArlrEAVDAASLELEAASREREALAEA 817
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEA----EEALREQA---ELNRLKKKYLEALNKKLNEKESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 818 LAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRC---HLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRE 894
Cdd:pfam05557 99 LADAREVISCLKNELSELRRQIQRAELELQSTNSELEElqeRLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 895 LEQAALERQ--KFLQERESQHQRYQHLEQRLEAELQAASTNKEEAL------------------MKLKARALQLEEELIQ 954
Cdd:pfam05557 179 IQSQEQDSEivKNSKSELARIPELEKELERLREHNKHLNENIENKLllkeevedlkrklereekYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 955 LR-QYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQgraQELLLQSQRAQEHSSRLQ 1033
Cdd:pfam05557 259 QElQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELE---QELAQYLKKIEDLNKKLK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1034 AEKSMMEiqgqELHRKLGVLEEEvRVARRAQEETRGQQQALlrdHEALVQLQRRQEtELEGLLVRHRDLKANMRA-LELA 1112
Cdd:pfam05557 336 RHKALVR----RLQRRVLLLTKE-RDGYRAILESYDKELTM---SNYSPQLLERIE-EAEDMTQKMQAHNEEMEAqLSVA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1113 HRELQGrheqlQAQRASVEAQEVALLAERERLMQDGHRQRGLEeelrrlqnehdraqmllaEVSRERGELQGERGELRSR 1192
Cdd:pfam05557 407 EEELGG-----YKQQAQTLERELQALRQQESLADPSYSKEEVD------------------SLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1193 LARLELERAQLEIQsqklresnQQLDLSACR-LTTQCELLTQLRSAQEEENRQLLAEVQALSRENReLLERSLESRDHLH 1271
Cdd:pfam05557 464 KNELEMELERRCLQ--------GDYDPKKTKvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLK-KLEDDLEQVLRLP 534
|
570
....*....|....*..
gi 2778277499 1272 REQREYLDQ-LNALRRE 1287
Cdd:pfam05557 535 ETTSTMNFKeVLDLRKE 551
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
743-1218 |
1.85e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 52.66 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 743 SLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAASREREALAEALAAAG 822
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 823 RERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAER--EHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAAL 900
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARllELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 901 ERQKFLQERES-QHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGR 979
Cdd:TIGR00618 536 TYAQLETSEEDvYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 980 LIEVERNNATLVAEKAALQGQLQHLEGQ-LGSLQGRAQELLLQSQRAQEHSSRLQAEKSmmeiqGQELHRKLGVLEEEVR 1058
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCSQELALkLTALHALQLTLTQERVREHALSIRVLPKEL-----LASRQLALQKMQSEKE 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1059 VARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQG-RHEQLQAQRASVEAQEVAL 1137
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqARTVLKARTEAHFNNNEEV 770
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1138 LAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGE-----------LQGERGELRSRLARLELERAQLEIQ 1206
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdedilnlqcetLVQEEEQFLSRLEEKSATLGEITHQ 850
|
490
....*....|..
gi 2778277499 1207 SQKLRESNQQLD 1218
Cdd:TIGR00618 851 LLKYEECSKQLA 862
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
834-1218 |
2.28e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 834 RLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQ--ALREELEKAVVRGQELGD---RLEHLQRELEQAALERQKFLQE 908
Cdd:pfam01576 624 RDRAEAEAREKETRALSLARALEEALEAKEELERTnkQLRAEMEDLVSSKDDVGKnvhELERSKRALEQQVEEMKTQLEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 909 RESQHQRYQHLEQRLEAELQAASTNKEEalmKLKARALQLEEELIQLrqypVDQATEVRAEprtvetqngrLIEVERNNA 988
Cdd:pfam01576 704 LEDELQATEDAKLRLEVNMQALKAQFER---DLQARDEQGEEKRRQL----VKQVRELEAE----------LEDERKQRA 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 989 TLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQehssrlqaeksmmeIQGQELHRKLgvleEEVRVARraqeetr 1068
Cdd:pfam01576 767 QAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQ--------------AQMKDLQREL----EEARASR------- 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1069 gqqqallrdhEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQdg 1148
Cdd:pfam01576 822 ----------DEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEA-- 889
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2778277499 1149 hRQRGLEEELRRLQNE----HDRAQMLLAEVSRERGELQGErgelRSRLARLELERAQLEIQSQKLRESNQQLD 1218
Cdd:pfam01576 890 -RIAQLEEELEEEQSNtellNDRLRKSTLQVEQLTTELAAE----RSTSQKSESARQQLERQNKELKAKLQEME 958
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
728-931 |
2.67e-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: 51.30 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 728 QALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARareQARLREAVDAASLELEAA 807
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ---KEELAELLRALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 808 SREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVrchlEEAEREHLEKQALREELEKAVVRGQELGDR 887
Cdd:COG4942 121 PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR----AELEAERAELEALLAELEEERAALEALKAE 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2778277499 888 LEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAAS 931
Cdd:COG4942 197 RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
782-1277 |
2.80e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 782 EVEARAREQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRcHLEEAE 861
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 862 REHLEKQALREELEKAVVRGQELGDRLEHLQRELEqaALERQkfLQERESQHQRYQHLEQRLEAELQAASTNKEEAlmKL 941
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEER--IKELEEKEERLEELKKKLKELEKRLEELEERH--EL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 942 KARALQLEEELIQLRQypvdqatevRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQEL--- 1018
Cdd:PRK03918 364 YEEAKAKKEELERLKK---------RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkka 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1019 -----LLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQ-------- 1085
Cdd:PRK03918 435 kgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKeleeklkk 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1086 ------RRQETELEGLLVRHRDLKANMRALEL---AHRELQGRHEQLQAQRASVEAQEVALLAERE-------------- 1142
Cdd:PRK03918 515 ynleelEKKAEEYEKLKEKLIKLKGEIKSLKKeleKLEELKKKLAELEKKLDELEEELAELLKELEelgfesveeleerl 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1143 -----------RLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERaqleiqsqkLR 1211
Cdd:PRK03918 595 kelepfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE---------LR 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2778277499 1212 ESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALS--RENRELLERSLESRDHLHREQREY 1277
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREkaKKELEKLEKALERVEELREKVKKY 733
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
720-957 |
5.61e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 720 LATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEArsaeavslSEELAQARRTEaeahlevearareqarlreaVDA 799
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREA--------LQRLAEYSWDE--------------------IDV 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 800 ASLEleaasrerealaealaaagRERRQWEREgprlRAQVEAAEQQVQALESQvrchLEEAEREHlekQALREELEKAVV 879
Cdd:COG4913 664 ASAE-------------------REIAELEAE----LERLDASSDDLAALEEQ----LEELEAEL---EELEEELDELKG 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 880 RGQELGDRLEHLQRELEQAALERQKFlqERESQHQRYQHLEQRLEAELQAASTNK-----EEALMKLKARALQLEEELIQ 954
Cdd:COG4913 714 EIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAAALGDAVERElrenlEERIDALRARLNRAEEELER 791
|
...
gi 2778277499 955 LRQ 957
Cdd:COG4913 792 AMR 794
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
712-985 |
5.71e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 712 EEPIPGETLATAipEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARrteaeahlevEARAREQA 791
Cdd:PTZ00121 1531 EEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE----------EARIEEVM 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 792 RLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQAlR 871
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK-A 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 872 EELEKAvvrGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEE 951
Cdd:PTZ00121 1678 EEAKKA---EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2778277499 952 ----LIQLRQYPVDQATEVRAEPRTV------ETQNGRLIEVER 985
Cdd:PTZ00121 1755 ekkkIAHLKKEEEKKAEEIRKEKEAVieeeldEEDEKRRMEVDK 1798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1085-1303 |
6.39e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1085 QRRQETELegllvRHRDLKANMRALELAHRELQGRHEQLQAQ----------RASVEAQEVALLA--------ERERLMQ 1146
Cdd:TIGR02168 172 ERRKETER-----KLERTRENLDRLEDILNELERQLKSLERQaekaerykelKAELRELELALLVlrleelreELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1147 D----GHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSAC 1222
Cdd:TIGR02168 247 ElkeaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1223 RLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLhREQREYLDQLNALRREKQKLVEKIMDQYRVL 1302
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
.
gi 2778277499 1303 E 1303
Cdd:TIGR02168 406 E 406
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
882-1295 |
6.90e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 882 QELGDRLEHLQRELEQAaLERQKFLQERESQHQRYQHLEQRLEAELQAAS---TNKEEALMKLKARALQLEEELIQLRqy 958
Cdd:pfam01576 5 EEMQAKEEELQKVKERQ-QKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHELE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 959 pvdqatevraeprtvetqnGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSM 1038
Cdd:pfam01576 82 -------------------SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1039 MEIQGQELHRKLGVLEE---EVRVARRAQEETRGQQQALLRDHEALV-QLQRRQETELEGllvrHRDLKANMRALELAHR 1114
Cdd:pfam01576 143 LEDQNSKLSKERKLLEErisEFTSNLAEEEEKAKSLSKLKNKHEAMIsDLEERLKKEEKG----RQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1115 ELQGRHEQLQAQ----RASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQmllAEVSRERGelQGERGELR 1190
Cdd:pfam01576 219 DLQEQIAELQAQiaelRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ---EDLESERA--ARNKAEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1191 SRLARLELERAQLEIQSqKLRESNQQLDLSACRLTTqcelLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHL 1270
Cdd:pfam01576 294 RRDLGEELEALKTELED-TLDTTAAQQELRSKREQE----VTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQA 368
|
410 420
....*....|....*....|....*
gi 2778277499 1271 HREQREYLDQLNALRREKQKLVEKI 1295
Cdd:pfam01576 369 KRNKANLEKAKQALESENAELQAEL 393
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
726-1275 |
1.17e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.17 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVA--QLRREVVSLEAKLQAQAQRLEARSAEAVSLSEE--LAQARRTEAEAHL-EVEARAREQARLREAVDAA 800
Cdd:pfam01576 109 EEQLDEEEAArqKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKErkLLEERISEFTSNLaEEEEKAKSLSKLKNKHEAM 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 801 SLELEaasREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEE--AEREHLEKQALREELEKAV 878
Cdd:pfam01576 189 ISDLE---ERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEElqAALARLEEETAQKNNALKK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 879 VRgqELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEealmkLKARAlqlEEELIQLRQY 958
Cdd:pfam01576 266 IR--ELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE-----LRSKR---EQEVTELKKA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 959 PVDQATEVRAE--------PRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSS 1030
Cdd:pfam01576 336 LEEETRSHEAQlqemrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1031 RLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEAL-VQLQRRQETeLEGLLVRHRDLKANMRAL 1109
Cdd:pfam01576 416 ELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLeSQLQDTQEL-LQEETRQKLNLSTRLRQL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1110 ELAHRELQGRHEQLQAQRASVEAQ----EVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGE 1185
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQlstlQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1186 RGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSREnrelLERSLE 1265
Cdd:pfam01576 575 KNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARA----LEEALE 650
|
570
....*....|
gi 2778277499 1266 SRDHLHREQR 1275
Cdd:pfam01576 651 AKEELERTNK 660
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
308-964 |
1.66e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 308 LSGQAKRAELYREEAEALRERAGRLprlqeelrrcreRLHAAEVFKGQLEEERVLSGALEASKVLLEEQLEIARERSARL 387
Cdd:COG1196 205 LERQAEKAERYRELKEELKELEAEL------------LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 388 HETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEpppgspgetslpgaapSLQDEVREAEAgRLRTV 467
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE----------------ELEEELAELEE-ELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 468 EQENRTLRGQLQMLREQLDSQRPLLEEQSKdsmlpvtngapaaplALDHSPKSLAcqiggegpgsldlpspasySGITRL 547
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEE---------------ALLEAEAELA-------------------EAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 548 SECLQApdshpeldspfQMVSQDPQTSDQTQESDPTGEAHQSLEKsghrvsvqspivwdppqgaEIRIDVQELGETGSRE 627
Cdd:COG1196 382 EELAEE-----------LLEALRAAAELAAQLEELEEAEEALLER-------------------LERLEEELEELEEALA 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 628 ASEGESVPEAQVLKQENPECRPRSAEFILLEPLKDQKTLEPELELSKQQTETGGHEQRpkgLVNKLVLQKPQQTSEGPPD 707
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA---AARLLLLLEAEADYEGFLE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 708 AWSREEPIPGETLATAiPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARA 787
Cdd:COG1196 509 GVKAALLLAGLRGLAG-AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAA 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 788 REQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEK 867
Cdd:COG1196 588 LAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 868 QALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQ 947
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
650
....*....|....*..
gi 2778277499 948 LEEELIQLRQYPVDQAT 964
Cdd:COG1196 748 LEEEALEELPEPPDLEE 764
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
862-1140 |
1.83e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 862 REH-LEKQALREELEKAVvrgqELGDRLEHLQRELEQAAlERQKFLQERESQHQRYQHLEQRLeAELQAastnkeealMK 940
Cdd:COG4913 214 REYmLEEPDTFEAADALV----EHFDDLERAHEALEDAR-EQIELLEPIRELAERYAAARERL-AELEY---------LR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 941 LKARALQLEEELIQLRQypvdqatevraeprtvetqngrliEVERNNAtlvaEKAALQGQLQHLEGQLGSLQGRAQELll 1020
Cdd:COG4913 279 AALRLWFAQRRLELLEA------------------------ELEELRA----ELARLEAELERLEARLDALREELDEL-- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1021 QSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHR 1100
Cdd:COG4913 329 EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2778277499 1101 DLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAE 1140
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1032-1298 |
2.40e-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: 48.97 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1032 LQAEKSMMEIQGQElhrklgvleeevRVARRAQEETRGQQQALLRDHEALVQLQ-----RRQETELEGLLVRHRDLKANM 1106
Cdd:pfam17380 278 VQHQKAVSERQQQE------------KFEKMEQERLRQEKEEKAREVERRRKLEeaekaRQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1107 RALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLM----QDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGEL 1182
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1183 QGERGELRSR-LARLELERAQlEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEvqalsrENRELLE 1261
Cdd:pfam17380 426 RAEQEEARQReVRRLEEERAR-EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE------QRRKILE 498
|
250 260 270
....*....|....*....|....*....|....*..
gi 2778277499 1262 RSLESRDHLHREQreyldqlnalrREKQKLVEKIMDQ 1298
Cdd:pfam17380 499 KELEERKQAMIEE-----------ERKRKLLEKEMEE 524
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1123-1331 |
2.42e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1123 LQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQ 1202
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1203 LEIQSQKLRESNQQLDLSACRLTTQCEL---------------------LTQLRSAQEEENRQLLAEVQALsrenRELLE 1261
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLalllspedfldavrrlqylkyLAPARREQAEELRADLAELAAL----RAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1262 RSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKKGSWLADKVKRLIRPRREGA 1331
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
265-434 |
2.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 265 NAKAQLRRLRQEVEEKAELLLDSQAEVQGLESEIRRLRQETQALSG--------------QAKRAELyREEAEALRERAG 330
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaEREIAEL-EAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 331 RLPRLQEELRRCRERLHAAEVFKGQLEEERvlsGALEASKVLLEEQLEIARERSARLHETQRE--NLLLRTRLGEAHAD- 407
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERFAAALGDa 762
|
170 180
....*....|....*....|....*...
gi 2778277499 408 -LDSLRHQLEQLVEENVELELELQRSLE 434
Cdd:COG4913 763 vERELRENLEERIDALRARLNRAEEELE 790
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
737-1255 |
2.82e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 737 LRREVVSLEAKLQAQAQRLeARSAEAVSLseelAQARRTEAEAHLEvEARAREQARLREAVDAASL-ELEAASREREALa 815
Cdd:PRK10246 424 LRQRLVALHGQIVPQQKRL-AQLQVAIQN----VTQEQTQRNAALN-EMRQRYKEKTQQLADVKTIcEQEARIKDLEAQ- 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 816 ealaaagRERRQWEREGPRLRAQVEAAEQQVQALESQVrchlEEAEREHLEKQALREELEKAVVRGQelgdrLEHLQREL 895
Cdd:PRK10246 497 -------RAQLQAGQPCPLCGSTSHPAVEAYQALEPGV----NQSRLDALEKEVKKLGEEGAALRGQ-----LDALTKQL 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 896 EQAALERQKFLQERESQHQRYQHLEQRLEAELQAAstnkeEALMKLKARALQLEEELIQLRQYPVDQATevraeprtvet 975
Cdd:PRK10246 561 QRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQ-----DDIQPWLDAQEEHERQLRLLSQRHELQGQ----------- 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 976 QNGRLIEVERNNATLVAEKAALQGQLQHLEGqlgSLQGRAQELLLQSQRAQEHSsrlqaeksmmeiQGQELHRKLGVLEE 1055
Cdd:PRK10246 625 IAAHNQQIIQYQQQIEQRQQQLLTALAGYAL---TLPQEDEEASWLATRQQEAQ------------SWQQRQNELTALQN 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1056 evRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLlvrhrDLKANMRALELAHRELQGRHEQLQAQ-----RASV 1130
Cdd:PRK10246 690 --RIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCL-----SLHSQLQTLQQQDVLEAQRLQKAQAQfdtalQASV 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1131 EAQEVALLAErerLMQDGHRQRgLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKL 1210
Cdd:PRK10246 763 FDDQQAFLAA---LLDEETLTQ-LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQL 838
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2778277499 1211 RESNqqldlsacrlTTQCELLTQLRsaQEEENRQ----LLAEVQALSRE 1255
Cdd:PRK10246 839 RENT----------TRQGEIRQQLK--QDADNRQqqqaLMQQIAQATQQ 875
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
718-930 |
2.84e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 718 ETLATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAV 797
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 798 DAASLELEAASREREALaealaaagrerrqweregpRLRAQVEAAEQQVQALESQvrchleEAEREHLEKQalREELEKA 877
Cdd:COG3883 103 SYLDVLLGSESFSDFLD-------------------RLSALSKIADADADLLEEL------KADKAELEAK--KAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2778277499 878 VVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAA 930
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
665-1011 |
4.27e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 665 TLEPELeLSKQQTETGGHEQRPKGLVNKLVLQKPQQTSEGPPDAWSREEPIPGETLATAIPEEQALRDEVAQLRREVVSL 744
Cdd:TIGR02169 643 TLEGEL-FEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 745 EAK---LQAQAQRLEARSAEAVSLSEELAQARrteAEAHLEVEARAREQARLREAVDAASLELEAAsrerealaealaaa 821
Cdd:TIGR02169 722 EKEieqLEQEEEKLKERLEELEEDLSSLEQEI---ENVKSELKELEARIEELEEDLHKLEEALNDL-------------- 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 822 grERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALE 901
Cdd:TIGR02169 785 --EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 902 RQKFLQERESQHQRYQHLEQRLEaELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATevraeprTVETQNGRLI 981
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLG-DLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA-------KLEALEEELS 934
|
330 340 350
....*....|....*....|....*....|....*.
gi 2778277499 982 EVERNNATLVAEKAA------LQGQLQHLEGQLGSL 1011
Cdd:TIGR02169 935 EIEDPKGEDEEIPEEelsledVQAELQRVEEEIRAL 970
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
840-1201 |
4.66e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 840 EAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHqryqhl 919
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 920 EQRLEAELQAASTNKEEALMKLKARaLQLEEELIQLRQYPVDQATEVRAeprtvetqngrLIEVERnnATLVAEKAALQG 999
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQE-IEKEEEKLAQVLKENKEEEKEKK-----------LQEEEL--KLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1000 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDH- 1078
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKk 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1079 EALVQLQRRQETELEGLLVRHRDLKANMRALELAHRElqgrhEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEEL 1158
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL-----EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2778277499 1159 RRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERA 1201
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
840-1217 |
4.95e-05 |
|
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: 47.76 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 840 EAAEQQVQALESQVRCHLEEAEREHLEKQALRE---ELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRY 916
Cdd:pfam05622 10 DELAQRCHELDQQVSLLQEEKNSLQQENKKLQErldQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKC 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 917 QHLEQRLeAELQaastNKEEALMKLKARALQLEEELIQLRQyPVDQATEVRAeprTVETQNGRLievernnatlvaekaa 996
Cdd:pfam05622 90 EELEKEV-LELQ----HRNEELTSLAEEAQALKDEMDILRE-SSDKVKKLEA---TVETYKKKL---------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 997 lqGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEI---QGQELHRKLgvlEEEVRVARRAQEETR---GQ 1070
Cdd:pfam05622 145 --EDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETykrQVQELHGKL---SEESKKADKLEFEYKkleEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1071 QQALLRDHEALV----------------QLQRRQETELEGLLVRHRDLKANMRAlELAHRELQGRHEQLQAQ----RASV 1130
Cdd:pfam05622 220 LEALQKEKERLIierdtlretneelrcaQLQQAELSQADALLSPSSDPGDNLAA-EIMPAEIREKLIRLQHEnkmlRLGQ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1131 EAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHdraqmlLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKL 1210
Cdd:pfam05622 299 EGSYRERLTELQQLLEDANRRKNELETQNRLANQR------ILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKL 372
|
....*..
gi 2778277499 1211 RESNQQL 1217
Cdd:pfam05622 373 HEAQSEL 379
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
983-1183 |
5.32e-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: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 983 VERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ--RAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVA 1060
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1061 RRAQEETRGQQQALLRD------HEALVQLQRRQETELEGLLVRH---RDLKANMRALE-LAHRELQGRHEQLQAQRASV 1130
Cdd:COG3206 246 RAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRaQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2778277499 1131 EAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQ 1183
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
838-1300 |
7.14e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 838 QVEAAEQQVQALESQVR--CHLEEAEREHLEK--QALREELEKAVVRGQELGDRLEHLQREleqaalerqkflQERESQH 913
Cdd:PRK10246 192 QHKSARTELEKLQAQASgvALLTPEQVQSLTAslQVLTDEEKQLLTAQQQQQQSLNWLTRL------------DELQQEA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 914 QRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQlrqypvDQATEVRAEPRTVETQNGRLIEVERNNATLVAE 993
Cdd:PRK10246 260 SRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHWERIQ------EQSAALAHTRQQIEEVNTRLQSTMALRARIRHH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 994 KAALQGQLQHLEGQLGSLQGRAQELLLQSQ-----RAQ-EHSSRLQAEKSMMEIQGQELHRKLGVL--------EEEVRV 1059
Cdd:PRK10246 334 AAKQSAELQAQQQSLNTWLAEHDRFRQWNNelagwRAQfSQQTSDREQLRQWQQQLTHAEQKLNALpaitltltADEVAA 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1060 ARRAQEETRGQQQALLRDHEALVQLQRRQETelegllvrhrdlkaNMRALELAHRELQGRHEQLQAQRASV-----EAQE 1134
Cdd:PRK10246 414 ALAQHAEQRPLRQRLVALHGQIVPQQKRLAQ--------------LQVAIQNVTQEQTQRNAALNEMRQRYkektqQLAD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1135 VALLAERERLMQDghrqrgLEEELRRLQ----------NEHDRAQMLLAEvsrergelqgERGELRSRLARLELERAQLE 1204
Cdd:PRK10246 480 VKTICEQEARIKD------LEAQRAQLQagqpcplcgsTSHPAVEAYQAL----------EPGVNQSRLDALEKEVKKLG 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1205 IQSQKLResnqqldlsacrltTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLER---SLESRDHLH---REQREYL 1278
Cdd:PRK10246 544 EEGAALR--------------GQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASlniTLQPQDDIQpwlDAQEEHE 609
|
490 500
....*....|....*....|..
gi 2778277499 1279 DQLNALrREKQKLVEKIMDQYR 1300
Cdd:PRK10246 610 RQLRLL-SQRHELQGQIAAHNQ 630
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
822-1211 |
7.33e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.44 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 822 GRERRQWEREGPR-LRAQVEAAEQQVQAL---ESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQ 897
Cdd:pfam07111 47 GRRGRSLELEGSQaLSQQAELISRQLQELrrlEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 898 AALERQKFLQERESQHQRYQHLEQRleaELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQN 977
Cdd:pfam07111 127 AEMVRKNLEEGSQRELEEIQRLHQE---QLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 978 GRLIEVERN---NATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLE 1054
Cdd:pfam07111 204 KQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1055 EEvrvarraqeetrgqqqaLLRDHEALVQLQRRQETELEGLLVRHRD----LKANMRALELAHRElqgRHEQLQAQRASV 1130
Cdd:pfam07111 284 EE-----------------LTRKIQPSDSLEPEFPKKCRSLLNRWREkvfaLMVQLKAQDLEHRD---SVKQLRGQVAEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1131 EAQeVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKL 1210
Cdd:pfam07111 344 QEQ-VTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMT 422
|
.
gi 2778277499 1211 R 1211
Cdd:pfam07111 423 R 423
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
58-180 |
8.09e-05 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 44.32 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 58 LISGDLLLRVLGIIAPS--SRGRLQMVKGHDGPA-ACRIWNLYHLWGRLRDFYQEELQLLILSPP-PDLQTLGfdPFSEe 133
Cdd:pfam19047 25 LTDGVAMAQVLHQIDPSwfTEAWLSRIKEDVGDNwRLKVSNLKKILQSVVDYYQDVLGQQISDFLlPDVNLIG--EHSD- 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2778277499 134 aVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEV 180
Cdd:pfam19047 102 -PAELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQEL 147
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
858-1263 |
8.82e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 858 EEAEREHLEKQA-LREELEKAVVRGQELGDRLEHLQRELEQaalerqkfLQERESQhqryqhleqrLEAELQAAST--NK 934
Cdd:PRK04863 278 ANERRVHLEEALeLRRELYTSRRQLAAEQYRLVEMARELAE--------LNEAESD----------LEQDYQAASDhlNL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 935 EEALMKLKARALQLEEELIQLrQYPVDQATEVRAEprtvetQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGR 1014
Cdd:PRK04863 340 VQTALRQQEKIERYQADLEEL-EERLEEQNEVVEE------ADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1015 AqellLQSQRAQehsSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALlRDHEALvqlqRRQETELEG 1094
Cdd:PRK04863 413 A----IQYQQAV---QALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKL-SVAQAA----HSQFEQAYQ 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1095 LLVRHRDLKANMRALELAhRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRR----------LQNE 1164
Cdd:PRK04863 481 LVRKIAGEVSRSEAWDVA-RELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRlgknlddedeLEQL 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1165 HDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDlsacRLTTQC---------------E 1229
Cdd:PRK04863 560 QEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA----RLREQSgeefedsqdvteymqQ 635
|
410 420 430
....*....|....*....|....*....|....
gi 2778277499 1230 LLTQLRSAQEEENrQLLAEVQALSRENRELLERS 1263
Cdd:PRK04863 636 LLERERELTVERD-ELAARKQALDEEIERLSQPG 668
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
727-1226 |
9.67e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 727 EQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHlevearareqaRLREAVDAASLELEA 806
Cdd:pfam12128 421 ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIE-----------RAREEQEAANAEVER 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 807 ASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHL-EEAE--REHLEKQALREELEKA----VV 879
Cdd:pfam12128 490 LQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLrKEAPdwEQSIGKVISPELLHRTdldpEV 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 880 RGQELGDRLEHLQRELEQAALerqkflqeresQHQRYQHLEQRLEAELQAAstnkEEALMKLKARALQLEEELIQLRQyP 959
Cdd:pfam12128 570 WDGSVGGELNLYGVKLDLKRI-----------DVPEWAASEEELRERLDKA----EEALQSAREKQAAAEEQLVQANG-E 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 960 VDQA----TEVRAEPRTVETQNGRLIEVERNNAtlVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAE 1035
Cdd:pfam12128 634 LEKAsreeTFARTALKNARLDLRRLFDEKQSEK--DKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1036 KSMMEIQgqelhrklgvleeevrvARRAQEETRGQQQALLRdhealvqlqrrqetelEGLLVRHRDLKANMRALEL-AHR 1114
Cdd:pfam12128 712 ARTEKQA-----------------YWQVVEGALDAQLALLK----------------AAIAARRSGAKAELKALETwYKR 758
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1115 ELQGRheQLQAQRASVEAQEVALLAER-ERLMQDGHRQRGLEEELR-RLQNEHDRAQMLLAEVSRERGELQGERG----E 1188
Cdd:pfam12128 759 DLASL--GVDPDVIAKLKREIRTLERKiERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSNIERAISELQQQLArliaD 836
|
490 500 510
....*....|....*....|....*....|....*...
gi 2778277499 1189 LRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTT 1226
Cdd:pfam12128 837 TKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1121-1289 |
9.91e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 9.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1121 EQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLA--EVSRERGELQGERGELRSRLARLEL 1198
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1199 ERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1278
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|.
gi 2778277499 1279 DQLNALRREKQ 1289
Cdd:COG4717 234 NELEAAALEER 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
728-932 |
1.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 728 QALRDEVAQLRREVVSLEAKLQA--QAQRLEARSAEAVSLSEELA--QARRTEAEAHL-EVEARAREQARLREAVDAASL 802
Cdd:COG3206 178 EFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSelESQLAEARAELaEAEARLAALRAQLGSGPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 803 ELEAASREREALAEALAAAGRERRQWEREGP------RLRAQVEAAEQQVQALESQVrchLEEAEREHLEKQALREELEK 876
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPnhpdviALRAQIAALRAQLQQEAQRI---LASLEAELEALQAREASLQA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2778277499 877 AVvrgQELGDRLEHL-QRELEQAALERqkflqERESQHQRYQHLEQRL-EAELQAAST 932
Cdd:COG3206 335 QL---AQLEARLAELpELEAELRRLER-----EVEVARELYESLLQRLeEARLAEALT 384
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-401 |
1.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 132 EEAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEVTQPGAGVVLALTGPESAELVAEELEMQLRNL 211
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 212 MGTMSRLVRERDLGAQRLAEVLLEREpahlllpeasanasaegpshHLALQLTNAKAQLRRLRQEVEEKAELLLDSQAEV 291
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELE--------------------EAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 292 QGLESEIRRLRQETQALSGQAKRA--ELYREEAEALRERAGRLPRLQEELrrcRERLHAAEVFKGQLEEERVLSGALEAS 369
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALleRLERLEEELEELEEALAELEEEEE---EEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270
....*....|....*....|....*....|..
gi 2778277499 370 KVLLEEQLEIARERSARLHETQRENLLLRTRL 401
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
259-430 |
1.35e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 259 LALQLTNAKAQLRRLRQEVEEKAELlldsQAEVQGLESEIRRLRQETQALSGQAKRAELYREEAEALRERAG---RLPRL 335
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElpeRLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 336 QEELRRCRERLHAAEVFKGQLEE-ERVLSGALEASKVLLEEQLEIARERSARLHETQREnllLRTRLGEAHADLDSLRHQ 414
Cdd:COG4717 152 EERLEELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEELEELQQRLAE---LEEELEEAQEELEELEEE 228
|
170
....*....|....*.
gi 2778277499 415 LEQLVEENVELELELQ 430
Cdd:COG4717 229 LEQLENELEAAALEER 244
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
960-1291 |
1.58e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 960 VDQATEVRAE----PRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQG--RAQElllQSQRAQEHSSRL- 1032
Cdd:PRK04863 285 LEEALELRRElytsRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQE---KIERYQADLEELe 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1033 -QAEKSMMEIQgqELHRKLGVLEEEVRVARRAQEETRGQqqalLRDH-EALVQLQRR--QETELEGLLVRHRDLKANMra 1108
Cdd:PRK04863 362 eRLEEQNEVVE--EADEQQEENEARAEAAEEEVDELKSQ----LADYqQALDVQQTRaiQYQQAVQALERAKQLCGLP-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1109 lELAHRELQGRHEQLQAQRASVeAQEVALLAERERLMQDGHRQ--------RGLEEELRRLQnEHDRAQMLLAEVSRERG 1180
Cdd:PRK04863 434 -DLTADNAEDWLEEFQAKEQEA-TEELLSLEQKLSVAQAAHSQfeqayqlvRKIAGEVSRSE-AWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1181 ELQgERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSacrlTTQCELLTQLRSAQEeenrqllAEVQALSRENRELL 1260
Cdd:PRK04863 511 LAE-QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKN----LDDEDELEQLQEELE-------ARLESLSESVSEAR 578
|
330 340 350
....*....|....*....|....*....|.
gi 2778277499 1261 ERSLESRDHLhreqreylDQLNALRREKQKL 1291
Cdd:PRK04863 579 ERRMALRQQL--------EQLQARIQRLAAR 601
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
92-180 |
1.60e-04 |
|
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a microtubule-binding protein required for spermatid differentiation. It is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411796 Cd Length: 150 Bit Score: 43.69 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 92 RIWNLYHLWGRLRDFYQEELQLLILSPP-PDLQTLG--FDPFseeavdELEGILRLLLGASVQCEHRELFIRHIQGLSLD 168
Cdd:cd22225 61 KMSNLKKILQGIVDYYHEFLDQQISEFLlPDLNRIAehSDPV------ELGRLLQLILGCAVNCEKKQEHIQNIMTLEES 134
|
90
....*....|..
gi 2778277499 169 VQSELAAAIQEV 180
Cdd:cd22225 135 VQHVVMTAIQEL 146
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1109-1221 |
1.90e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 45.42 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1109 LELAHRELQGRHEQLQAQRASVEAQEVALLAE---RERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAE--VSRErgELQ 1183
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAElgaEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVSQQ--ELD 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 2778277499 1184 GERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSA 1221
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQA 189
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
739-1162 |
2.44e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 739 REVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAASREREALAEAL 818
Cdd:COG5278 96 RSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAAL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 819 AAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQA 898
Cdd:COG5278 176 LLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 899 ALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNG 978
Cdd:COG5278 256 ALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALAT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 979 RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVR 1058
Cdd:COG5278 336 ALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1059 VARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALL 1138
Cdd:COG5278 416 ASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAA 495
|
410 420
....*....|....*....|....
gi 2778277499 1139 AERERLMQDGHRQRGLEEELRRLQ 1162
Cdd:COG5278 496 AAALSLALALAALLLAAAEAALAA 519
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
823-1158 |
2.49e-04 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 45.57 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 823 RERRQWEREgpRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALER 902
Cdd:COG3447 291 AERRRQRLR--ERELALRAALELLALGLLLAALDDALLLLNARGLLLLALSLAALLLLRLALLLLLLALDALLLLLADDD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 903 QKFLQERESQHQRYQHLEQRLEAELQ-AASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLI 981
Cdd:COG3447 369 RGELRGDLLRRRGATRLGAVVARLLRrSGGRGEEVVVLLVIAQVEEALELALRERREERLLERLALALELLAITAALLAA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 982 EVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ---RAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVR 1058
Cdd:COG3447 449 ALLLALADLLLLLLAEAAQLLARALLLGLDRLLADAALAALAalaDLLGALLSAGLRRRGGRRLGARLIRSLLSRVLAEL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1059 VARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALL 1138
Cdd:COG3447 529 GAVELLLALIADLTEVALGAEALERLLERLLLALLGLGLAVAALLATLGLLLALLAALALSGAAALLALGAALLLAAAIL 608
|
330 340
....*....|....*....|
gi 2778277499 1139 AERERLMQDGHRQRGLEEEL 1158
Cdd:COG3447 609 GLAAALLALLRLLGERARLL 628
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
887-1285 |
2.62e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 887 RLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAA-STNKEEALMKLKARALQLEEELIQLRQYPVDQATE 965
Cdd:COG3096 786 RLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 966 VRAEPRTVETQNGrlievernnatlvaekaaLQGQLQHLEGQlgSLQGRAQELLLQSQRAQEhssrlqAEKSMmeiqgQE 1045
Cdd:COG3096 866 LDQLKEQLQLLNK------------------LLPQANLLADE--TLADRLEELREELDAAQE------AQAFI-----QQ 914
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1046 LHRKLGVLEEEVRVARRAQEetrgQQQALLRDHEALVQLQRRQETELEGLlvrhRDLKANMRAL--ELAHRELQGRHEQL 1123
Cdd:COG3096 915 HGKALAQLEPLVAVLQSDPE----QFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQRRPHFsyEDAVGLLGENSDLN 986
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1124 QAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGEL------------QGERGELRS 1191
Cdd:COG3096 987 EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadaeaeeraRIRRDELHE 1066
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1192 RLARLELERAQLEIQSQKLRESNQQLdlsACRLTTQCELLTQLRSaQEEENRQLLAEVQALSRENRelLERSLESRDHLH 1271
Cdd:COG3096 1067 ELSQNRSRRSQLEKQLTRCEAEMDSL---QKRLRKAERDYKQERE-QVVQAKAGWCAVLRLARDND--VERRLHRRELAY 1140
|
410
....*....|....*...
gi 2778277499 1272 ---REQREYLDQ-LNALR 1285
Cdd:COG3096 1141 lsaDELRSMSDKaLGALR 1158
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-489 |
2.91e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 276 EVEEKAELLLDSQAEVQGLESEIRRLRQETQALsgqakraelyreeaEALRERAGRLPRLQEELRRCRERLHAAEVFKGQ 355
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELL--------------EPIRELAERYAAARERLAELEYLRAALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 356 LEEERV--LSGALEASKVLLEEQLEIARERSARLHETQREnlLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQR-- 431
Cdd:COG4913 288 RRLELLeaELEELRAELARLEAELERLEARLDALREELDE--LEAQIRGNGGDRLEQLEREIERLERELEERERRRARle 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 432 ------SLEPPPGSPGETSLPGAAPSLQDEVREAEAG---RLRTVEQENRTLRGQLQMLREQLDSQR 489
Cdd:COG4913 366 allaalGLPLPASAEEFAALRAEAAALLEALEEELEAleeALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
785-1017 |
3.03e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 785 ARAREQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQvrchLEEAEReh 864
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEK-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 865 lEKQALREELEKavvRGQELGDRLEHLQRELEQAALErQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKAR 944
Cdd:COG4942 91 -EIAELRAELEA---QKEELAELLRALYRLGRQPPLA-LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2778277499 945 ALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQE 1017
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
839-1268 |
3.47e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 839 VEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQ---R 915
Cdd:pfam05483 263 LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 916 YQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRaepRTVETQNGRLIEVERNNaTLVAEKA 995
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE---EMTKFKNNKEVELEELK-KILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 996 ALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALL 1075
Cdd:pfam05483 419 KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1076 RDHEALVQ--------LQRRQETELEGLLVRHRDLKA--NMRALELAHR-ELQGRHEQLQAQRASVEAQevaLLAERERL 1144
Cdd:pfam05483 499 LENKELTQeasdmtleLKKHQEDIINCKKQEERMLKQieNLEEKEMNLRdELESVREEFIQKGDEVKCK---LDKSEENA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1145 MQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRS--------------RLARLELERA--------- 1201
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKkgsaenkqlnayeiKVNKLELELAsakqkfeei 655
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2778277499 1202 ----QLEIQSQKLRESNQQLDLSACRLTTqcELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRD 1268
Cdd:pfam05483 656 idnyQKEIEDKKISEEKLLEEVEKAKAIA--DEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERD 724
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
978-1291 |
3.88e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 978 GRLIEVERNNATLVAEKAALQGQL----QHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVL 1053
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQRekekERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1054 EEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQ----------- 1122
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrslske 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1123 LQAQRASVEAQEVALLAERERLMQDGHR-----QRGLE-----EELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSR 1192
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKlttahRKEAEneallEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1193 LARLELERAQLEIQsqkLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHR 1272
Cdd:pfam07888 274 LHQARLQAAQLTLQ---LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGR 350
|
330
....*....|....*....
gi 2778277499 1273 EQREYLDQLNALRREKQKL 1291
Cdd:pfam07888 351 EKDCNRVQLSESRRELQEL 369
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
746-981 |
4.48e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 746 AKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAASREREALAEALAAAGRER 825
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 826 RQWERE-GPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELgDRLEHLQRELEQAALERQK 904
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-AELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 905 FLQERESQHQRYQHLE---QRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPrtVETQNGRLI 981
Cdd:COG4942 179 LLAELEEERAALEALKaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG--FAALKGKLP 256
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
782-1201 |
4.52e-04 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 44.85 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 782 EVEARAREQARLREAV-----DAASLELEAASREREALAEALAAAGRERRQWERE------------------GPRLRAQ 838
Cdd:COG1020 887 EIEAALLQHPGVREAVvvareDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPpymvpaavvlllplpltgNGKLDRL 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 839 VEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQH 918
Cdd:COG1020 967 ALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAA 1046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 919 LEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQ 998
Cdd:COG1020 1047 AAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALR 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 999 GQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDH 1078
Cdd:COG1020 1127 ARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLL 1206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1079 EALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEEL 1158
Cdd:COG1020 1207 LLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARA 1286
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2778277499 1159 RRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERA 1201
Cdd:COG1020 1287 RAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
725-957 |
4.58e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 725 PEEQALRDEVAQLRREVVSLEAKLQAQAQRLEArSAEAVS-----------LSEELAQARRTEAEAHLEvEARAREQARL 793
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQ-LKEQLQllnkllpqanlLADETLADRLEELREELD-AAQEAQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 794 REAVDAASLELEAASREREALAEALAAAGRERRQWEREgpRLRAQVEAAEQQVQALEsqvrcHL--EEAEREHLEKQA-- 869
Cdd:COG3096 914 QHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQR--RLKQQIFALSEVVQRRP-----HFsyEDAVGLLGENSDln 986
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 870 --LREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEA-ELQAAStnkeEALMKLKARAL 946
Cdd:COG3096 987 ekLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElGVQADA----EAEERARIRRD 1062
|
250
....*....|.
gi 2778277499 947 QLEEELIQLRQ 957
Cdd:COG3096 1063 ELHEELSQNRS 1073
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
726-985 |
5.38e-04 |
|
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: 44.73 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEA--RSAEAVSLSEELAQARRTEAEaHLEVEARAREQARLREAVDAASL- 802
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELE-RIRQEERKRELERIRQEEIAMEIs 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 803 ---------------------ELEAASREREALAEALaaagRERRQWEREGPRLRAQVEAAEQ-QVQALESQVRCHLEEA 860
Cdd:pfam17380 376 rmrelerlqmerqqknervrqELEAARKVKILEEERQ----RKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 861 EREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMK 940
Cdd:pfam17380 452 RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2778277499 941 LKARALQLEEeliQLRQYPVDQATEVRAEPRTVETQNGRLIEVER 985
Cdd:pfam17380 532 EERRREAEEE---RRKQQEMEERRRIQEQMRKATEERSRLEAMER 573
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
760-1198 |
5.58e-04 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 44.85 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 760 AEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQV 839
Cdd:COG1020 899 REAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 840 EAAEQQVQAlesqvrchLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHL 919
Cdd:COG1020 979 AAAPPAEEE--------EEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAA 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 920 EQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVEtQNGRLIEVERNNATLVAEKAALQG 999
Cdd:COG1020 1051 AAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLL-LLLLALLLLLALLLALLAALRARR 1129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1000 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHE 1079
Cdd:COG1020 1130 AVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 1209
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1080 ALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELR 1159
Cdd:COG1020 1210 LLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAA 1289
|
410 420 430
....*....|....*....|....*....|....*....
gi 2778277499 1160 RLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLEL 1198
Cdd:COG1020 1290 RTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
775-1312 |
6.32e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 775 TEAEAHLEVEARAREQARLREAVDAASLELEAASREREALAEALAAAGRE--------RRQWEREGPRLRAQVEAAEQQV 846
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEearkaedaRKAEEARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 847 QALESQVRCHLEEAEREHLEKQAlrEELEKAV-VRGQELGDRLEHLQR-ELEQAALERQKFLQERESQHQRYQHLEQRLE 924
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKA--EEVRKAEeLRKAEDARKAEAARKaEEERKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 925 AELQAAST--NKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEvERNNATLVAEKAALQGQLQ 1002
Cdd:PTZ00121 1240 EEAKKAEEerNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE-EKKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1003 HLEGQLGSLQGRAQELllqSQRAQEHSSRLQAEKSMMEIQGQELHRKlgvlEEEVRVARRAQEETRGQQQALLRDHEalv 1082
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEAEAA----EEKAEAAEKKKEEAKKKADAAKKKAE--- 1388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1083 qlQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQ 1162
Cdd:PTZ00121 1389 --EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1163 NEHDRAQML--LAEVSRERGELQGERGELRSRLARLElERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEE 1240
Cdd:PTZ00121 1467 EEAKKADEAkkKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2778277499 1241 ENRQLLAEVQALSRENRellERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPGPLPRTKK 1312
Cdd:PTZ00121 1546 KKADELKKAEELKKAEE---KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
837-1063 |
7.73e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 837 AQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRY 916
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 917 QHLEQRLEAELQAASTNKEEALMKL---------KARALQLEEELIQLRQypvDQATEVRAEPRTVETQNGRLievERNN 987
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALllspedfldAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAEL---EAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 988 ATLVAEKAALQGQLQHLEGQLgslqgRAQELLLQSQRAQEhsSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRA 1063
Cdd:COG4942 174 AELEALLAELEEERAALEALK-----AERQKLLARLEKEL--AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
823-1019 |
8.29e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 823 RERRQW-EREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQ--ALREELEKAVVRGQELGDRLEHLQRELEQAA 899
Cdd:COG3206 174 RKALEFlEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQlsELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 900 LERQKFLQERESQ--HQRYQHLEQRLeAELQAASTNKEEALMKLKARALQLEEELIQLRQypvdqatevraeprtvetqn 977
Cdd:COG3206 254 DALPELLQSPVIQqlRAQLAELEAEL-AELSARYTPNHPDVIALRAQIAALRAQLQQEAQ-------------------- 312
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2778277499 978 GRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELL 1019
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
266-414 |
8.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 266 AKAQLRRLRQEVEEKAELLLDSQAEVQGLESEIRRLRQETQALSGQAK---RAELYREEAEaLRERAGRLPRLQEELRRC 342
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeqlEREIERLERE-LEERERRRARLEALLAAL 371
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2778277499 343 RERL-HAAEVFKGQLEEERVLSGALEASKVLLEEQLeiaRERSARLHEtqrenllLRTRLGEAHADLDSLRHQ 414
Cdd:COG4913 372 GLPLpASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRD-------LRRELRELEAEIASLERR 434
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
219-372 |
9.24e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 219 VRERDLGAQRLAEVLLEREPAHLLLPEASAnasaEGPSHHLALQLTNAKAQLRRLRQEVEEKAELLLDSQAEVQGLESEI 298
Cdd:COG2433 368 VKARVIRGLSIEEALEELIEKELPEEEPEA----EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI 443
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2778277499 299 RRLRQETQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLhaaevfKGQLEEER-----VLSGALEASKVL 372
Cdd:COG2433 444 ERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEEL------KRKLERLKelwklEHSGELVPVKVV 516
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
725-1164 |
9.95e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 725 PEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLEL 804
Cdd:PRK02224 307 ADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 805 EAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALE---SQVRCHLEEAER-----------EHLEKQAL 870
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEatlRTARERVEEAEAlleagkcpecgQPVEGSPH 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 871 REELEKAVVRGQELGDRLEHLQRELE--QAALERQKFLQERESQHQRYQHLEQRLE---AELQAASTNKEEALMKLKARA 945
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEevEERLERAEDLVEAEDRIERLEERREDLEeliAERRETIEEKRERAEELRERA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 946 LQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATLvAEKAALQGQLQHLEGQLGSLQGRAQELllqSQRA 1025
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL---AELN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1026 QEHSSRLQAEKsmmeiqgqELHRKLGVLEEEVRVArRAQEETRGQQQALLRDHEALVQLqRRQETELEGLLVRHRDLKAN 1105
Cdd:PRK02224 623 DERRERLAEKR--------ERKRELEAEFDEARIE-EAREDKERAEEYLEQVEEKLDEL-REERDDLQAEIGAVENELEE 692
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2778277499 1106 MRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLmqdghRQRGLeEELRRLQNE 1164
Cdd:PRK02224 693 LEELRERREALENRVEALEALYDEAEELESMYGDLRAEL-----RQRNV-ETLERMLNE 745
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1126-1275 |
1.03e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1126 QRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRaqmllaEVSRERGELQGERGELR-------SRLARLEL 1198
Cdd:PRK12705 29 QRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQ------EARREREELQREEERLVqkeeqldARAEKLDN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 1199 ERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRsaQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQR 1275
Cdd:PRK12705 103 LENQLEEREKALSARELELEELEKQLDNELYRVAGLT--PEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
728-1262 |
1.05e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 728 QALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAA 807
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKN 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 808 ---SREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHlEEAEREHLEKQALREELEKAvvrgQEL 884
Cdd:PRK01156 273 nyyKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKY-HAIIKKLSVLQKDYNDYIKK----KSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 885 GDRLEHLQRELEQAALERQKFLQERESQHQRYQhlEQRLEAELQAASTNKEEALMKLKARALQLEEELIqlrqypvdqat 964
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKKIE--EYSKNIERMSAFISEILKIQEIDPDAIKKELNEI----------- 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 965 evraeprtvetqNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRL----QAEKSMME 1040
Cdd:PRK01156 415 ------------NVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIinhyNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1041 IQGQELHRKLGVLEEEVRVARRAQEETRGQQ-------QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAH 1113
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEYLESEEinksineYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1114 RE--------------------LQGRHEQLQAQRASVEA--QEVALLAERERLMQDGHRQRgLEEELRRLQNEHDRAQml 1171
Cdd:PRK01156 563 LDskrtswlnalavislidietNRSRSNEIKKQLNDLESrlQEIEIGFPDDKSYIDKSIRE-IENEANNLNNKYNEIQ-- 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1172 laEVSRERGELQGERGELRSRLARL-ELERAQLEIQSQkLRESNQQLDLSACRLTTQCELLTQLRSaQEEENRQLLAEVQ 1250
Cdd:PRK01156 640 --ENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITSR-INDIEDNLKKSRKALDDAKANRARLES-TIEILRTRINELS 715
|
570
....*....|..
gi 2778277499 1251 ALSRENRELLER 1262
Cdd:PRK01156 716 DRINDINETLES 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1143-1304 |
1.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1143 RLMQDGHRQRGLEEELRRLQNEhdraqmlLAEVSRERGELQGERGELRSRLARLELERAQLEiqsQKLRESNQQL----- 1217
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDE-------LAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLgnvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1218 --DLSAcrLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:COG1579 88 nkEYEA--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 2778277499 1296 MDQYRVLEP 1304
Cdd:COG1579 166 EELAAKIPP 174
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
828-1286 |
1.47e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 43.32 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 828 WEREGPrlRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQ 907
Cdd:COG3321 868 FQREDA--AAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLAL 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 908 ERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNN 987
Cdd:COG3321 946 AAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALA 1025
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 988 ATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEET 1067
Cdd:COG3321 1026 ALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAA 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1068 RGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQD 1147
Cdd:COG3321 1106 LLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1148 GHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQ 1227
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALL 1265
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2778277499 1228 CELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRR 1286
Cdd:COG3321 1266 AAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAA 1324
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1023-1295 |
1.71e-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: 42.81 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1023 QRAQEHSSRLQAEKSMMEIqgqELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDL 1102
Cdd:pfam05557 5 IESKARLSQLQNEKKQMEL---EHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1103 KANMRALELAHRElqgrHEQLQAqrasvEAQEVallaererlmqdghrQRGLEEELRRLQNEHDRAQMLLAEVSRERGEL 1182
Cdd:pfam05557 82 KKYLEALNKKLNE----KESQLA-----DAREV---------------ISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1183 QGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR--QLLAEVQAL-------- 1252
Cdd:pfam05557 138 QERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLrehnkhln 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2778277499 1253 -SRENRELLERSLES-RDHLHREQrEYLDQLNALRREKQKLVEKI 1295
Cdd:pfam05557 218 eNIENKLLLKEEVEDlKRKLEREE-KYREEAATLELEKEKLEQEL 261
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
892-1151 |
1.80e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 892 QRELEQAALERQkfLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEpR 971
Cdd:pfam05667 223 EEEWNSQGLASR--LTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGS-R 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 972 TVETQNGRLIEVERNNATLVAEKAALQGQLQ-HLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKL 1050
Cdd:pfam05667 300 FTHTEKLQFTNEAPAATSSPPTKVETEEELQqQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1051 GVLEEEVRVARRAQE---ETRGQQQALLRDHEA----LVQLQRRQETELEGLLVRHRDLK--ANMRALELAHR--ELQGR 1119
Cdd:pfam05667 380 EELEKQYKVKKKTLDllpDAEENIAKLQALVDAsaqrLVELAGQWEKHRVPLIEEYRALKeaKSNKEDESQRKleEIKEL 459
|
250 260 270
....*....|....*....|....*....|....*
gi 2778277499 1120 HEQLQ---AQRASVEAQEVALLAERERLMQDGHRQ 1151
Cdd:pfam05667 460 REKIKevaEEAKQKEELYKQLVAEYERLPKDVSRS 494
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
736-1058 |
1.84e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 736 QLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAhleveARAREQARLREAvdaaslelEAASREREALA 815
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA-----RTALKNARLDLR--------RLFDEKQSEKD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 816 EALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEK-QALREELEKAVVR-GQELGDRLEHLQR 893
Cdd:pfam12128 668 KKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYwQVVEGALDAQLALlKAAIAARRSGAKA 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 894 ELEQAALERQKFLQERESQHQRYQHLEQR---LEAELQAASTNKEEAlmkLKARALQLEEELIQlRQYPVDQATEVRAEP 970
Cdd:pfam12128 748 ELKALETWYKRDLASLGVDPDVIAKLKREirtLERKIERIAVRRQEV---LRYFDWYQETWLQR-RPRLATQLSNIERAI 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 971 RTVETQNGRLI-EVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsQRAQEHSSRLQAEKSMMEI--QGQELH 1047
Cdd:pfam12128 824 SELQQQLARLIaDTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL----ATLKEDANSEQAQGSIGERlaQLEDLK 899
|
330
....*....|.
gi 2778277499 1048 RKLGVLEEEVR 1058
Cdd:pfam12128 900 LKRDYLSESVK 910
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
617-1217 |
1.86e-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: 42.79 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 617 VQELGETGSREASEGESVPEAQVLKQENPECRPRSAEFILLEPLKDQKTLEPELELS----KQQTETGGHEQRPKGLVnK 692
Cdd:pfam05483 224 IQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQdenlKELIEKKDHLTKELEDI-K 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 693 LVLQKPQQTSEgppdAWSREEPIPGETLATAIPEEQALRDE-----------VAQLRREVVSLEAKLQAQAQRLEARSAE 761
Cdd:pfam05483 303 MSLQRSMSTQK----ALEEDLQIATKTICQLTEEKEAQMEElnkakaahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 762 AVSLSEELaQARRTEAEahleveararEQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEA 841
Cdd:pfam05483 379 LKIITMEL-QKKSSELE----------EMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 842 AEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQ 921
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 922 RLEAELQAASTnkeealmkLKARALQLEEELIQLRQYPVDQATEVRAEPRTVEtQNGRLIEVErnnatlvaekaalqgqL 1001
Cdd:pfam05483 528 QEERMLKQIEN--------LEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-ENARSIEYE----------------V 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1002 QHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEAL 1081
Cdd:pfam05483 583 LKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1082 VQLQRRQEtelEGLLVRHRDLKANMRALELAHRELQGRHEQLQAqrasveaqEVALLAERERLMQDghrqRGLEEELRRL 1161
Cdd:pfam05483 663 IEDKKISE---EKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIA--------EMVALMEKHKHQYD----KIIEERDSEL 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 1162 QNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQL 1217
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
760-1201 |
1.88e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.08 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 760 AEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAASREREALAEALAAAGRER-------------- 825
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELalrlaaalapfwfl 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 826 RQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQAALERQKF 905
Cdd:COG3903 558 RGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAA 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 906 LQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVER 985
Cdd:COG3903 638 AAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAA 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 986 NNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQE 1065
Cdd:COG3903 718 AAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAA 797
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1066 ETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLM 1145
Cdd:COG3903 798 AAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAA 877
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 1146 QDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERA 1201
Cdd:COG3903 878 AAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
750-1129 |
1.90e-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: 43.02 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 750 AQAQRLEARSAEAVSLSEELAQARrteaeahleveARAREQARLREAVDAAsLELEAASREREALAEALAAAGRERRQWE 829
Cdd:COG3096 782 AREKRLEELRAERDELAEQYAKAS-----------FDVQKLQRLHQAFSQF-VGGHLAVAFAPDPEAELAALRQRRSELE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 830 REGPRLRAQVEAAEQQVQALESQVrchleeaerehlekQALREELEKAVVRGQE-LGDRLEHLQRELEQaALERQKFLQe 908
Cdd:COG3096 850 RELAQHRAQEQQLRQQLDQLKEQL--------------QLLNKLLPQANLLADEtLADRLEELREELDA-AQEAQAFIQ- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 909 resQHQRYQHLEQRLEAELQAASTNKEEalmkLKARALQLEEELIQLRQyPVDQATEV--RAEPRTVETQNGRLIEvern 986
Cdd:COG3096 914 ---QHGKALAQLEPLVAVLQSDPEQFEQ----LQADYLQAKEQQRRLKQ-QIFALSEVvqRRPHFSYEDAVGLLGE---- 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 987 NATLVaekAALQGQLQHLEGQlgslQGRAQELLLQSQ-RAQEHSSRLQAEKSMMEIQGQELHRKLGVLEE-EVRVARRAQ 1064
Cdd:COG3096 982 NSDLN---EKLRARLEQAEEA----RREAREQLRQAQaQYSQYNQVLASLKSSRDAKQQTLQELEQELEElGVQADAEAE 1054
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 1065 EETRGQQQALlrdHEALVQL-QRRQETElEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRAS 1129
Cdd:COG3096 1055 ERARIRRDEL---HEELSQNrSRRSQLE-KQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
132-470 |
1.95e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 132 EEAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEVTQPGAGVVLALTGPESAELVAEELEMQLRNL 211
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 212 MGTMSRLVRERDLGAQRLAEVLLEREPAHLLLPEASANASAEGPSHHLALQLTN-AKAQLRRLRQEVEEKAELLLDSQAE 290
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEvAAAAIEYLKAAKAGRATFLPLDKIR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 291 VQGLESEIRRLRQETQALSGQAKRAELYREEA-------------EALRERAGRLPRLQEELRRcRERLHAAEVFKGQLE 357
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYyvlgdtllgrtlvAARLEAALRRAVTLAGRLR-EVTLEGEGGSAGGSL 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 358 EERVLSGALEASKVLLEEQLEIARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQRSLEPPP 437
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELL 742
|
330 340 350
....*....|....*....|....*....|...
gi 2778277499 438 GSPGETSLPGAAPSLQDEVREAEAGRLRTVEQE 470
Cdd:COG1196 743 EEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
726-1102 |
1.97e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.92 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELE 805
Cdd:COG3899 862 ETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAA 941
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 806 AASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELG 885
Cdd:COG3899 942 AAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLA 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 886 DRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATE 965
Cdd:COG3899 1022 AALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAA 1101
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 966 VRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQE 1045
Cdd:COG3899 1102 AAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAA 1181
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 1046 LHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDL 1102
Cdd:COG3899 1182 LLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALL 1238
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
92-180 |
2.61e-03 |
|
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein for microtubule-dependent intracellular vesicle and protein trafficking. It is involved in Golgi and endosome transport. It acts as a scaffold for the opposite-polarity microtubule-based motors cytoplasmic dynein-1 and the kinesin KIF1C. It may participate in the turnover of the endocytosed scavenger receptor. Hook3 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411797 Cd Length: 153 Bit Score: 39.95 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 92 RIWNLYHLWGRLRDFYQEEL-QLLILSPPPDLQTLGfdpfSEEAVDELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQ 170
Cdd:cd22226 65 KISNLKKILKGILDYNHEILgQQINDFTLPDVNLIG----EHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEESVQ 140
|
90
....*....|
gi 2778277499 171 SELAAAIQEV 180
Cdd:cd22226 141 HVVMTAIQEL 150
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
835-1219 |
2.72e-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: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 835 LRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQA-----ALERQkfLQER 909
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikELEKQ--LNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 910 ESQ-----HQRYQHLEQRLEAELQAASTNKEEA---LMKLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLI 981
Cdd:TIGR04523 294 KSEisdlnNQKEQDWNKELKSELKNQEKKLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 982 EVERNNAT-------LVAEKAALQGQLQH-------LEGQLGSLQGRAQEL-----LLQSQRAQEHS--SRLQAEKSMME 1040
Cdd:TIGR04523 374 KLKKENQSykqeiknLESQINDLESKIQNqeklnqqKDEQIKKLQQEKELLekeieRLKETIIKNNSeiKDLTNQDSVKE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1041 IQGQELHRKLGVLEEEVRVARRAQEETRgqqqallRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRH 1120
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIK-------QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1121 EQLQAQRASVEaQEVALLAERERLMQDGHRQRGLEEELRRLQNE----HDRAQMLLA---EVSRERGELQGERGELRSRL 1193
Cdd:TIGR04523 527 EKLESEKKEKE-SKISDLEDELNKDDFELKKENLEKEIDEKNKEieelKQTQKSLKKkqeEKQELIDQKEKEKKDLIKEI 605
|
410 420
....*....|....*....|....*.
gi 2778277499 1194 ARLELERAQLEIQSQKLRESNQQLDL 1219
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
940-1294 |
2.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 940 KLKARALQLEEELIQLRQYPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSL--QGRAQE 1017
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1018 LLLQSQRAQEHSSRLQAEKSMMEIQGQELHRklgvLEEEVRVARRAQEETRGQQQALLRdhealvQLQRRQETELEGLLV 1097
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLE------QLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1098 RHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALlAERERLMQDGHRQRGL----------EEELRRLQNEHDR 1167
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAaallallglgGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1168 AQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQKLRESNQQLDLSAC-----------RLTTQCELLTQLRS 1236
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDlspeellelldRIEELQELLREAEE 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2778277499 1237 AQEE--------ENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEK 1294
Cdd:COG4717 359 LEEElqleeleqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
717-1032 |
3.03e-03 |
|
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: 42.26 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 717 GETLATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARR-TEAEAHLEVEARAREQARLRE 795
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlTEKLSEAEDMLACEQHALLRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 796 AVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELE 875
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 876 KAVVRGQELGDRLEHLQR---ELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQL---E 949
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDRefnEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgaeL 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 950 EELIQLRQYPVDQATEVRAEPRTVETQNG---------------RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGR 1014
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGqeipsdedilnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
330
....*....|....*...
gi 2778277499 1015 AQELLLQSQRAQEHSSRL 1032
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1000-1144 |
3.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1000 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHRKLGVLEEEVRVARRAQEETRGQQ-------- 1071
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnke 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2778277499 1072 -QALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQR----ASVEAQEVALLAERERL 1144
Cdd:COG1579 91 yEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELdeelAELEAELEELEAEREEL 168
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
728-878 |
3.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 728 QALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREA---------VD 798
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkeYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 799 AASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAV 878
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1039-1217 |
3.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1039 MEIQGQELHRKLGVLEEEVRVARRAQEETRGQQQALLRDHEaLVQLQRRQETELEGLlvrhRDLKANMRALELAHRELQG 1118
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-LVDLSEEAKLLLQQL----SELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1119 RHEQLQAQRASVEAQEVALLAE------RERLMQdghRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGE---- 1188
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQSpviqqlRAQLAE---LEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRilas 317
|
170 180 190
....*....|....*....|....*....|....*.
gi 2778277499 1189 -------LRSRLARLELERAQLEIQSQKLRESNQQL 1217
Cdd:COG3206 318 leaeleaLQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
201-483 |
3.67e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 201 AEELEMQLRNLMGTMSRLVRERDLGAQRLAEVLLEREPAHLllpeasanasaeGPSHHLALQLTNAKAQLRRLRQEVEEK 280
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI------------EEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 281 AEllldsqaEVQGLESEIRRLRQETQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLHAAEVFKGQlEEER 360
Cdd:PTZ00121 1622 AE-------ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK-AAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 361 VLSGALEASKVllEEQLEIARERSARLHETQRENLLLRTRLGEAHADLDSLRHQLEQLVEENVELELELQrsLEPPPGSP 440
Cdd:PTZ00121 1694 LKKEAEEAKKA--EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH--LKKEEEKK 1769
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2778277499 441 GETSLPGAAPSLQDEVREAEAGRLRTVEQENRTLRGQLQMLRE 483
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
842-957 |
4.78e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 842 AEQQVQALESQVRCHLEEAERehlEKQALREELEkavvrgQELGDRLEHLQRELEQAALERQKFLQERESQ-HQRYQHLE 920
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK---EAEAIKKEAL------LEAKEEIHKLRNEFEKELRERRNELQKLEKRlLQKEENLD 99
|
90 100 110
....*....|....*....|....*....|....*..
gi 2778277499 921 QRLEAELQaastnKEEALMKLKARALQLEEELIQLRQ 957
Cdd:PRK12704 100 RKLELLEK-----REEELEKKEKELEQKQQELEKKEE 131
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
262-440 |
5.33e-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: 40.90 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 262 QLTNAKAQLRRLRQEVEEKAELLLDSQAEVQGLESEIRRLRQETQALsgQAKRAELYREEAEALRE--RAGRLPRLQ--- 336
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLRAlyRLGRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 337 ------EELRR-------CRERLHAAEVFKGQLEEERVLSGALEASKVLLEEQLEIARERSARL--HETQRENLL--LRT 399
Cdd:COG4942 127 spedflDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeaLKAERQKLLarLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2778277499 400 RLGEAHADLDSLRHQLEQLVEENVELELELQRSLEPPPGSP 440
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
979-1287 |
5.85e-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: 41.48 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 979 RLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEksmMEIQGQELHRKLGVLEEEVR 1058
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTA---LRQQEKIERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1059 VArrAQEETRGQQQALLRDHEAlvqlqRRQETELEgllvrHRDLKANMRALELAHRELQGRHEQL-QAQRASVEAQEVAL 1137
Cdd:COG3096 363 LE--EQEEVVEEAAEQLAEAEA-----RLEAAEEE-----VDSLKSQLADYQQALDVQQTRAIQYqQAVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1138 LAE-------------RERLMQDGHRQRGLEEELRRLQ---NEHDRAQMLL----AEVSRERG-----ELQGERGELRSR 1192
Cdd:COG3096 431 LPDltpenaedylaafRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVckiaGEVERSQAwqtarELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1193 LARLELERAQLEIQSQKLRESNQqldlsACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHR 1272
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQN-----AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330
....*....|....*
gi 2778277499 1273 EqreyLDQLNALRRE 1287
Cdd:COG3096 586 Q----LEQLRARIKE 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-489 |
6.17e-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: 40.90 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 255 PSHHLALQLTNAKAQLRRLRQEVEEKAELLLDSQAEVQGLESEIRRLRQETQALSGQAKRAELYREEAEA-LRERAGRLP 333
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 334 RLQEELRRCR----ERLHAAEVFKGQLEEERVLSG----ALEASKVLLEEQLEIARERSARLHETQRENLLLRTRLGEAH 405
Cdd:COG4942 94 ELRAELEAQKeelaELLRALYRLGRQPPLALLLSPedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 406 ADLDSLRHQLEQLVEENVELELELQRSLEpppgspgetslpgaapSLQDEvREAEAGRLRTVEQENRTLRGQLQMLREQL 485
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLA----------------RLEKE-LAELAAELAELQQEAEELEALIARLEAEA 236
|
....
gi 2778277499 486 DSQR 489
Cdd:COG4942 237 AAAA 240
|
|
| HAUS6_N |
pfam14661 |
HAUS augmin-like complex subunit 6 N-terminus; This family includes the N-terminus of HAUS ... |
210-327 |
7.05e-03 |
|
HAUS augmin-like complex subunit 6 N-terminus; This family includes the N-terminus of HAUS augmin-like complex subunit 6. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464244 [Multi-domain] Cd Length: 233 Bit Score: 39.94 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 210 NLMGTMSRLVrerdlgaqrLAEVLLEREPAHLLLPE-----ASANASAEGPSHHLALQLTNAKaqlRRLRQEVEEKAELL 284
Cdd:pfam14661 109 ELLLHFSSFV---------LKKVLKTRSKNGGGFPAlaqklALENRGYSGEQAELAALILAHR---SSLLRILEEKDALI 176
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2778277499 285 LDSQAEVQGLESEIRRLRQETQALSGQAKRAELYREEAEALRE 327
Cdd:pfam14661 177 QKYQQFAQLLVKKIRALRAEREKLDALLKKMEKDNRSRSAEQD 219
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
726-1032 |
7.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 726 EEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELE 805
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 806 AASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEK-------QALREELEKAV 878
Cdd:COG4372 126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEllkeanrNAEKEEELAEA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 879 VRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQY 958
Cdd:COG4372 206 EKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2778277499 959 PVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRL 1032
Cdd:COG4372 286 EALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
729-1221 |
8.12e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 41.00 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 729 ALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEARAREQARLREAVDAASLELEAAS 808
Cdd:COG3899 746 ALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGD 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 809 REREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAEREHLEKQALREELEKAVVRGQELGDRL 888
Cdd:COG3899 826 RRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 889 EHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQYPVDQATEVRA 968
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 969 EPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSMMEIQGQELHR 1048
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1049 KLGVLEEEVRVARRAQEETRGQQQALLRDHEALVQLQRRQETELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1128
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALA 1145
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1129 SVEAQEVALLAERERLMQDGHRQRGLEEELRRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQSQ 1208
Cdd:COG3899 1146 LAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLL 1225
|
490
....*....|...
gi 2778277499 1209 KLRESNQQLDLSA 1221
Cdd:COG3899 1226 LLLAALALAAALL 1238
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
887-957 |
8.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 8.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2778277499 887 RLEHLQRELEQAALERQKFLQERESQHQRYQH----LEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQ 957
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEEkkekLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQK 598
|
|
| HkD_Hook2 |
cd22227 |
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a ... |
58-180 |
8.30e-03 |
|
Hook domain found in protein Hook 2 (Hook2) and similar proteins; Hook2 is a microtubule-binding protein that contributes to the establishment and maintenance of centrosome function. It may function in the positioning or formation of aggresomes, which are pericentriolar accumulations of misfolded proteins, proteasomes and chaperones. Hook2 is a component of the FTS/Hook/FHIP complex (FHF complex), which may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting (HOPS) complex.
Pssm-ID: 411798 Cd Length: 150 Bit Score: 38.70 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 58 LISGDLLLRVLGIIAPS--SRGRLQMVKGHDGPA-ACRIWNLYHLWGRLRDFYQEELQLLILSPP-PDLQTLGfdPFSEE 133
Cdd:cd22227 25 LTSGVAIAQVLNRIDPSwfNEAWLGRIKEDTGDNwRLKVSNLKKILQSLLEYYQDVLGHQVSEDHlPDVNLIG--EFSDD 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2778277499 134 AvdELEGILRLLLGASVQCEHRELFIRHIQGLSLDVQSELAAAIQEV 180
Cdd:cd22227 103 T--ELGKLLQLVLGCAISCEKKQEHIQQIMTLEESVQHVVMEAIQEL 147
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
1083-1285 |
8.73e-03 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 40.73 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1083 QLQRRqeteLEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEE----L 1158
Cdd:pfam04632 156 ALRAR----LRARLRDALRLAAAALAGAPGAEAFEAARLRLAADILALEALRSHAAFESPRGRARARALRRLLARmlalL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1159 RRLQNEHDRAQMLLAEVSRERGELQGERGELRSRLARLELERAQLEIQS--QKLRESNQQLDLSACrltTQCELLTQLrs 1236
Cdd:pfam04632 232 PRLRSLARLLARLRTEGAGTVPELAALLDELAAWEAALAAEALQAALAAlrARLRALRPALPLDFD---TAAELLARL-- 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2778277499 1237 aqeeenRQLLAEVQALSRENRELLERSLESRDH----LHREQREYLdqLNALR 1285
Cdd:pfam04632 307 ------ADLLAELAEALASCRALRHPIAQGARParlaRHRDHGAAL--LNGLR 351
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
718-877 |
8.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 718 ETLATAIPEEQALRDEVAQLRREVVSLE------------AKLQAQAQRLEARSAEAVSLSEELAQARRTEAEAHLEVEA 785
Cdd:COG4913 624 EELAEAEERLEALEAELDALQERREALQrlaeyswdeidvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEE 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 786 RAREQARLREAVDAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRCHLEEAERehl 865
Cdd:COG4913 704 LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA--- 780
|
170
....*....|..
gi 2778277499 866 EKQALREELEKA 877
Cdd:COG4913 781 RLNRAEEELERA 792
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
263-489 |
9.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 263 LTNAKAQLRRLRQEVEEKAELllDSQAEVQGLESEIRRLRQETQALSGQAKRAELYREEA----EALRERAGRLPRLQEE 338
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEAdevlEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 339 LRRCRERLHAAEVFKGQLEEErvlsgaleaSKVLLEEQLEIARERSARLHETQRENL---LLRTRLGEAHADLDSLRHQL 415
Cdd:PRK02224 260 IEDLRETIAETEREREELAEE---------VRDLRERLEELEEERDDLLAEAGLDDAdaeAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2778277499 416 EQLVEENVELELELQRSLEpppgspGETSLPGAAPSLQDEVREAEAGrLRTVEQENRTLRGQLQMLREQLDSQR 489
Cdd:PRK02224 331 EECRVAAQAHNEEAESLRE------DADDLEERAEELREEAAELESE-LEEAREAVEDRREEIEELEEEIEELR 397
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
725-1340 |
9.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 725 PEEQALRDEVAQLRREVVSLEAKLQAQaQRLEARSAEAvslseELAQARRTEAEAHLEvearaREQARLREAVDAASLEL 804
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEF-----CKRLGKNLDDEDELE-----QLQEELEARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 805 EAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQqvqaLESQVRCHLEEAER-EHLEKQALREELEKAVVRgqe 883
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR----LREQSGEEFEDSQDvTEYMQQLLERERELTVER--- 647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 884 lgDRLEHLQRELEQaalERQKFLQERESQHQRYQHLEQRLEAELQA---ASTNKEEA---------LM--------KLKA 943
Cdd:PRK04863 648 --DELAARKQALDE---EIERLSQPGGSEDPRLNALAERFGGVLLSeiyDDVSLEDApyfsalygpARhaivvpdlSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 944 RALQLEEEL---IQLRQYPVDQ------ATEVRAEPRTVETqNGRLIEVERNNATLVAEKAA-------LQGQLQHLEGQ 1007
Cdd:PRK04863 723 EQLAGLEDCpedLYLIEGDPDSfddsvfSVEELEKAVVVKI-ADRQWRYSRFPEVPLFGRAArekrieqLRAEREELAER 801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1008 LGSLQGRAQELllqsQRAQEHSSRLQAEKSMMEIQGQElhrklgvlEEEVRVARRAqeetRGQQQALLRDHEALVQLQRR 1087
Cdd:PRK04863 802 YATLSFDVQKL----QRLHQAFSRFIGSHLAVAFEADP--------EAELRQLNRR----RVELERALADHESQEQQQRS 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1088 QETELEGLLVRHRDLKANMRALELAHreLQGRHEQLQAQRASVE------AQEVALLAERER----LMQDGHRQRGLEEE 1157
Cdd:PRK04863 866 QLEQAKEGLSALNRLLPRLNLLADET--LADRVEEIREQLDEAEeakrfvQQHGNALAQLEPivsvLQSDPEQFEQLKQD 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1158 LRRLQNEHDRAQM---LLAEVSRER--------GELQGERGELRSRLarleleRAQLEIQSQKLRESNQQLDLSACRLTT 1226
Cdd:PRK04863 944 YQQAQQTQRDAKQqafALTEVVQRRahfsyedaAEMLAKNSDLNEKL------RQRLEQAEQERTRAREQLRQAQAQLAQ 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1227 QCELLTQLRS---AQEEENRQLLAEVQALS-RENRELLERSLESRDHLH------REQREYLDQ--------LNALRREK 1288
Cdd:PRK04863 1018 YNQVLASLKSsydAKRQMLQELKQELQDLGvPADSGAEERARARRDELHarlsanRSRRNQLEKqltfceaeMDNLTKKL 1097
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1289 QKLVEKIMDQYRVLEPGplprtkKGSWlaDKVKRLIRP--------RREGALHGGPRLGA 1340
Cdd:PRK04863 1098 RKLERDYHEMREQVVNA------KAGW--CAVLRLVKDngverrlhRRELAYLSADELRS 1149
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
718-1024 |
9.56e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 718 ETLATAIPEEQALRDEVAQLRREVVSLEAKLQAQAQRLEARSAEAVSLSEELAQARRteaeahlEVEARAREQARLREAV 797
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE-------QLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 798 DAASLELEAASREREALAEALAAAGRERRQWEREGPRLRAQVEAAEQQVQALESQVRchLEEAEREHLEKQALREELEKA 877
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE--SLQEELAALEQELQALSEAEA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 878 VVRGQELGDRLEHLQRELEQAALERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARALQLEEELIQLRQ 957
Cdd:COG4372 182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2778277499 958 YPVDQATEVRAEPRTVETQNGRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQR 1024
Cdd:COG4372 262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
823-1181 |
9.72e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 823 RERRQWEREGPRLRAQVEAAEQQVQALESqvrchlEEAEREHLEKQALREELEKAVVRGQELGDRLEHLQRELEQA---A 899
Cdd:pfam02029 9 RERRRRAREERRRQKEEEEPSGQVTESVE------PNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRlqeA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 900 LERQKFLQERESQHQRYQHLEQRLEAELQAASTNKEEALMKLKARAlQLEEELIQLRQYPVD--QATEVRAEPRTVETQN 977
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRY-KEEETEIREKEYQENkwSTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 978 GRLIEVERNNATLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQehssrlqaeksmmeiQGQELHRKLGVLEEEV 1057
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQ---------------NGEEEVTKLKVTTKRR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2778277499 1058 RVARRAQEETRGQQQALLRDHEALVQL-QRRQETELEGL-LVRHRDLKAnmrALELAhrELQGRHEqlqaqrasveaqev 1135
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAEQKLEELrRRRQEKESEEFeKLRQKQQEA---ELELE--ELKKKRE-------------- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2778277499 1136 allaERERLMQDGHRQRGLEEELRRLQNEHDRAQMlLAEVSRERGE 1181
Cdd:pfam02029 288 ----ERRKLLEEEEQRRKQEEAERKLREEEEKRRM-KEEIERRRAE 328
|
|
| |
