|
Name |
Accession |
Description |
Interval |
E-value |
| HkD_Gipie |
cd22230 |
Hook domain found in Gipie (GRP78-interacting protein induced by ER stress) and similar ... |
10-180 |
1.24e-71 |
|
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: 236.65 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 10 RDFLSGSLATWALGLAGLVGEAEDSEGEEEEEEEEPPLWLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMlRGLDGPAAW 89
Cdd:cd22230 1 EEFMSGALVTWALGFEGLVGEEEDSLGFPEEEEEEGTLDAEKRFLRLSNGDLLNRVMGIIDPSPRGGPRM-RGDDGPAAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 90 RVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQS 169
Cdd:cd22230 80 RVQNLHILWGRLRDFYQEELQQLILSPPPDLQVMGRDPFTEEAVQELEKLLRLLLGAAVQCERRELFIRHIQGLDLDVQA 159
|
170
....*....|.
gi 1370459164 170 ELAAAIQEVTQ 180
Cdd:cd22230 160 ELAEAIQEVTQ 170
|
|
| HkD_HkRP |
cd22223 |
Hook domain found in the Hook-related protein (HkRP) family; The HkRP family includes Daple, ... |
12-180 |
1.41e-48 |
|
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: 169.69 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 12 FLSGSLATWALGLAGLVGeaedsegeeeeeeeepplwLEKRFLRLSDGALLLRVLGIIAPSSRGGPRMlRGLDGPAAWRV 91
Cdd:cd22223 1 FLSSPLVTWAKTFADDGS-------------------AELSYTDLVDGVFLNNVMLQIDPRPFSEVSN-RNVDDDVNARI 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 92 WNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSEL 171
Cdd:cd22223 61 QNLDLLLRNIKSFYQEVLQQLIVMKLPDILTIGREPESEQSLEELEKLLLLLLGCAVQCERKEEFIERIKNLDLEVQHAL 140
|
....*....
gi 1370459164 172 AAAIQEVTQ 180
Cdd:cd22223 141 VACIQEVTD 149
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
738-1297 |
5.38e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 116.57 E-value: 5.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 738 RRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEA 817
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 818 LAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQ 897
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 898 AALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALmELKTRALQLEEELFQLRQgpaglgpkkrAEPQLVETQN 977
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-ELEEALAELEEEEEEEEE----------ALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 978 VRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEV 1057
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1058 RAARQSQEETRGQQqallrdhkALAQLQRRQEAELEGLLVRHRDLKANmRALELAHRELQGRHEQLQAQRASVEAQEVAL 1137
Cdd:COG1196 533 EAAYEAALEAALAA--------ALQNIVVEDDEVAAAAIEYLKAAKAG-RATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1138 LAERERlmQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQL 1217
Cdd:COG1196 604 VASDLR--EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1218 DLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMD 1297
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
718-1266 |
5.44e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV 797
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 798 EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEka 877
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE-- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 878 vvrgkELGDRLEHLQRELEQAALERQEFLREKESQHQRyQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQ 957
Cdd:COG1196 411 -----ALLERLERLEEELEELEEALAELEEEEEEEEEA-LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 958 gpaGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKS 1037
Cdd:COG1196 485 ---ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1038 VLEIQGQELHRKLEVL---EEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHR 1114
Cdd:COG1196 562 AIEYLKAAKAGRATFLpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1115 ELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLA 1194
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEEL 721
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370459164 1195 RLELERAQLEMQSQQLRESNQQLDlsacrlttqcelltQLRSAQEEENRQLLAEVQALSREnRELLERSLES 1266
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEE--------------ELLEEEALEELPEPPDLEELERE-LERLEREIEA 778
|
|
| HkD_Girdin |
cd22229 |
Hook domain found in Girdin and similar proteins; Girdin, also called Akt phosphorylation ... |
53-180 |
1.78e-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: 95.63 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 53 FLRLSDGALLLRVLGIIAPSSRGgPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEA 132
Cdd:cd22229 30 YVALVDGVFLNEVMLQINPKSSN-QRVNKKVNNDASLRIQNLSILVKQIKLYYQETLQQLIMMSLPNVLVLGRNPLSEQG 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370459164 133 VEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ 180
Cdd:cd22229 109 TEEMKKLLLLLLGCAVQCERKEEFIERIQTLDFDTKAAVAAHIQEVTH 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
728-1295 |
1.90e-20 |
|
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: 98.59 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 728 EALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESA 807
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 808 SQEREALVEALAAAGRERRQWEREGSRL-----RAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGK 882
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLedrreRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 883 ELGDRLEHLQRELEQAALERQEF---LREKESQHQRYQGLEQRLEAELQAA--------------------ATSKEEAL- 938
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQsglsgilgvlselisvdegyEAAIEAALg 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 939 -------MELKTRALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVER----SNAMLVAEKAALQGQLQHLEGQ 1007
Cdd:TIGR02168 545 grlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgVAKDLVKFDPKLRKALSYLLGG 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1008 L---GSLQGrAQELLLQSQRAQE---------HSSRLQAEKSVLEIQG-QELHRKLEVLEEEVRAARQSQEETRGQQQAL 1074
Cdd:TIGR02168 625 VlvvDDLDN-ALELAKKLRPGYRivtldgdlvRPGGVITGGSAKTNSSiLERRREIEELEEKIEELEEKIAELEKALAEL 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1075 LRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRqrgL 1154
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---A 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1155 EEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQL 1234
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1235 RSAQEEENRQLLAEVQALSRENRELLERSLESRDHLH---REQREYLDQLNALRREKQKLVEKI 1295
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEelsEELRELESKRSELRRELEELREKL 924
|
|
| HkD_Daple |
cd22228 |
Hook domain found in Daple (Dvl-associating protein with a high frequency of leucine residues) ... |
53-180 |
4.93e-20 |
|
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: 88.44 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 53 FLRLSDGALLLRVLGIIAPSSRGgPRMLRGLDGPAAWRVWNLNHLWGRLRDFYQEELQLLILSPPPDLQTLGFDPLSEEA 132
Cdd:cd22228 27 YMDLVDGVFLNKIMLQIDPRPTN-QRVNKHVNNDVNLRIQNLTILVRHIKTYYQEVLQQLIVMNLPNVLMIGKDPLSGKS 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370459164 133 VEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ 180
Cdd:cd22228 106 MEEIKKMLLLVLGCAVQCERKEEFIERIKQLDIETQAAIVSHIQEVTH 153
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
834-1290 |
2.05e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 834 RLRAQSEAAeERMQVLESEGRQ-----HLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLRE 908
Cdd:COG1196 204 PLERQAEKA-ERYRELKEELKEleaelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 909 KESQHQRYQGLEQRLEaELQAAATSKEEALMELKTRALQLEEELFQLRQgpaglgpKKRAEPQLVETQNVRLIEVERSNA 988
Cdd:COG1196 283 LEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 989 MLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETR 1068
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1069 GQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQE------------VA 1136
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflegvkaAL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1137 LLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQ 1216
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALAR 594
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1217 LDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQK 1290
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
|
| HkD_SF |
cd22211 |
Hook domain-containing proteins superfamily; The Hook domain superfamily includes Hook adaptor ... |
56-180 |
3.68e-19 |
|
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: 85.41 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 56 LSDGALLLRVLGIIAPSSRGGPRmLRGLDGPAAWRV-W-NLNHLWGRLRDFYQEEL-QLLILSPPPDLQTLGFDPlSEEA 132
Cdd:cd22211 23 LSDGVVLAEILSQIDPSYFDSEW-LESRDSSDNWVLkLnNLKKLYRSLSKYYREVLgQQLSDLPLPDLSAIARDG-DEEE 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1370459164 133 VEQLegvLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ 180
Cdd:cd22211 101 IVKL---LELVLGAAVQCENKEEYIARIQQLDESTQAELMLIIQEVLE 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
717-1204 |
1.56e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 717 GESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREA 796
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 797 VEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEK 876
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 877 AvvRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLR 956
Cdd:COG1196 447 A--AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 957 QGPAGLGPKKRAEPQLVETQNVRLIEVERSNAmlVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEK 1036
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDD--EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1037 SVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHREL 1116
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1117 QGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGE----------R 1186
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpeppdL 762
|
490
....*....|....*...
gi 1370459164 1187 GELRGRLARLELERAQLE 1204
Cdd:COG1196 763 EELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
725-1323 |
3.58e-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: 91.27 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 725 AEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQawEQARLREAVEAAGQEL 804
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA--ELEELEEELEELQEEL 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 805 ESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEAL---------QAELE 875
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvDEGYE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 876 KAVVrgKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQL 955
Cdd:TIGR02168 537 AAIE--AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 956 RQGPAGLgpkkraepqlveTQNVRLIEvERSNAMLVAEKAALQGQLQHLEGQLGSLQGraqelLLQSQRAQEHSSRLQAE 1035
Cdd:TIGR02168 615 RKALSYL------------LGGVLVVD-DLDNALELAKKLRPGYRIVTLDGDLVRPGG-----VITGGSAKTNSSILERR 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1036 KSVLEIQGQ--ELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAH 1113
Cdd:TIGR02168 677 REIEELEEKieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1114 RELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRG----LEEELRRLQSEHDRAQMLLAELSRERGELQGERGEL 1189
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkaLREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1190 RGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRdH 1269
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR-R 915
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370459164 1270 LHREQREYLDQLNA--------LRREKQKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRL 1323
Cdd:TIGR02168 916 ELEELREKLAQLELrleglevrIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
725-1203 |
2.62e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.46 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 725 AEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQEL 804
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 805 ESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKEL 884
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 885 GDRLEHLQRELEQAALERQEFLREKESQHQRYQG------------------LEQRLEAELQAAATSKEEALM-----EL 941
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaalllaglrglagavaVLIGVEAAYEAALEAALAAALqnivvED 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 942 KTRALQLEEELFQLRQGPAGLGP----KKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQE 1017
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPldkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1018 LLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLV 1097
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1098 RHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQS-------EHDRAQM 1170
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllaieEYEELEE 795
|
490 500 510
....*....|....*....|....*....|...
gi 1370459164 1171 LLAELSRERGELQGERGELRGRLARLELERAQL 1203
Cdd:COG1196 796 RYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
728-1298 |
5.38e-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: 83.95 E-value: 5.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 728 EALREEVAQLRR-KAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELES 806
Cdd:TIGR02168 213 ERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 807 ASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGD 886
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 887 RLEHLQRELEQAALERQEFLREKESQHQRYQGLE---QRLEAELQAAATSKEEALMELKTRALQ--------LEEELFQL 955
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEarlERLEDRRERLQQEIEELLKKLEEAELKelqaeleeLEEELEEL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 956 RQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEG-------------QLGSLQGRAQELL--- 1019
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkallknqsGLSGILGVLSELIsvd 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1020 ----------LQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQ-------EETRGQQQALLRDHKALA 1082
Cdd:TIGR02168 533 egyeaaieaaLGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndreilKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1083 QL----------------------QRRQEAE------LEGLLVRHRDL---------------KANMRALELAHRELQGR 1119
Cdd:TIGR02168 613 KLrkalsyllggvlvvddldnaleLAKKLRPgyrivtLDGDLVRPGGVitggsaktnssilerRREIEELEEKIEELEEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1120 HEQLQAQRASVEAQEVALLAERERLMQDGHRQR----GLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLAR 1195
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1196 LELERAQLEMQSQQLRESNQQLDLsacRLTTQCELLTQLRSAQEEENRQL--LAEVQALSRENRELLERSLESRDHLHRE 1273
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKE---ELKALREALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEE 849
|
650 660
....*....|....*....|....*
gi 1370459164 1274 QREYLDQLNALRREKQKLVEKIMDQ 1298
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
871-1203 |
5.52e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.87 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 871 QAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAElqaaatskEEALMELKTRALQLEE 950
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL--------RKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 951 ELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSS 1030
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1031 RLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALE 1110
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1111 LAHRELQGRHEQLQAQRASVEAQEVALLAERERlmqdghrqrgLEEELRrlqsehDRAQMLLAELSRERGELQGERGELR 1190
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDN----------LQERLS------EEYSLTLEEAEALENKIEDDEEEAR 971
|
330
....*....|...
gi 1370459164 1191 GRLARLELERAQL 1203
Cdd:TIGR02168 972 RRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
882-1204 |
3.01e-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: 78.57 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 882 KELGDRLEHLQRELEQAaLERQEFLREKesqhQRYQGLEqrLEAELQAAATSKEEALMELKTralqLEEELFQLRQGPAG 961
Cdd:TIGR02169 194 DEKRQQLERLRREREKA-ERYQALLKEK----REYEGYE--LLKEKEALERQKEAIERQLAS----LEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 962 LGPKKRAEPQLVETQNVRLIEVERSNAMLVAEK-AALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLE 1040
Cdd:TIGR02169 263 LEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1041 IQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRH 1120
Cdd:TIGR02169 343 REIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1121 EQLQAQRASVEAQEVALLAERERLmqdGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELER 1200
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
....
gi 1370459164 1201 AQLE 1204
Cdd:TIGR02169 500 RASE 503
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
718-1303 |
3.12e-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: 78.19 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREaeaqawEQARLREAV 797
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEA------EIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 798 EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEgrqhleeaererreKEALQAELEKA 877
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE--------------LEDLRAELEEV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 878 VVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLeAELQAAATSKEEALMELKTRALQLEEELfqlrq 957
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALEI----- 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 958 gpaglgpkKRAEPQLVETQNVRlieversnAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKS 1037
Cdd:TIGR02169 451 --------KKQEWKLEQLAADL--------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1038 VLEIQGQELH---RKLEVLEEEVRAARQS------------QEETRGQQQALLRDHKA----------LAQLQRRQEAEL 1092
Cdd:TIGR02169 515 VLKASIQGVHgtvAQLGSVGERYATAIEVaagnrlnnvvveDDAVAKEAIELLKRRKAgratflplnkMRDERRDLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1093 EG---------------------------LLVRH----RDLKANMRALELA-----------------------HRELQG 1118
Cdd:TIGR02169 595 EDgvigfavdlvefdpkyepafkyvfgdtLVVEDieaaRRLMGKYRMVTLEgelfeksgamtggsraprggilfSRSEPA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1119 RHEQLQAQRASVEAQEVALLAERERL----------MQDGHRQ-RGLEEELRRLQSEHDRAQMLLAELSRERGELQGERG 1187
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIenrldelsqeLSDASRKiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1188 ELRGRLARLELERAQLEMQSQQLREsnQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQAL-SRENRELLERSL-- 1264
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEE--ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYle 832
|
650 660 670
....*....|....*....|....*....|....*....
gi 1370459164 1265 ESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1303
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
934-1280 |
3.14e-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: 78.19 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 934 KEEALMELKTRALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQg 1013
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLE- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1014 raQELLLQSQRAQEHSSRLQAEKSVLEiqgqELHRKLEVL-EEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAEL 1092
Cdd:TIGR02169 251 --EELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1093 EGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLmqdghrqrglEEELRRLQSEHDRAQMLL 1172
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----------DKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1173 AELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLD-------LSACRLTTQCELLTQLRSAQEEENRQL 1245
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEeekedkaLEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350
....*....|....*....|....*....|....*...
gi 1370459164 1246 LAEVQALSRENREL---LERSLESRDHLHREQREYLDQ 1280
Cdd:TIGR02169 475 KEEYDRVEKELSKLqreLAEAEAQARASEERVRGGRAV 512
|
|
| HkD_Hook |
cd22222 |
Hook domain found in Hook family of microtubule-binding proteins; The Hook family includes ... |
56-178 |
6.49e-14 |
|
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: 70.74 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 56 LSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAA-WR--VWNLNHLWGRLRDFYQEEL-QLLILSPPPDLQTLGfdplSEE 131
Cdd:cd22222 23 LSDGVAIAQVLNQIDPEYFSDSWLSKIKPDVGDnWRlkVSNLKKILKGIVDYYSEVLgQQISGFTMPDVNAIA----EKE 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1370459164 132 AVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEV 178
Cdd:cd22222 99 DPKELGRLLQLVLGCAVNCERKEEYIQAIMGLEESVQHVVMEAIQEL 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
920-1254 |
6.81e-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: 73.94 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 920 EQRLEAELQAAATSK-----EEALMELK-------------TRALQLEEELFQLRQGPAGLgpkkraepqLVETQNVRLI 981
Cdd:TIGR02168 172 ERRKETERKLERTREnldrlEDILNELErqlkslerqaekaERYKELKAELRELELALLVL---------RLEELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 982 EVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAAR 1061
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1062 QSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAER 1141
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1142 ERLMQD----GHRQRGLEEELRRLQSEHDRAQMllAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQL 1217
Cdd:TIGR02168 403 ERLEARlerlEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350
....*....|....*....|....*....|....*..
gi 1370459164 1218 DLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSR 1254
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
259-1011 |
7.16e-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: 73.94 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 259 QLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAG-RLPRLQEELR 337
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAeELAELEEKLE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 338 RCRERLQAAEAyksQLEEERVLSGVLEASKALLEEQLEAARercARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAE 417
Cdd:TIGR02168 348 ELKEELESLEA---ELEELEAELEELESRLEELEEQLETLR---SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 418 ENVELELELQR------SLEPPPGSPGEAPLAGAAPSLQDEVREAEAgRLRTLERENRELRGLLQVLQGQPGGQHPLLEA 491
Cdd:TIGR02168 422 EIEELLKKLEEaelkelQAELEELEEELEELQEELERLEEALEELRE-ELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 492 PREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQALDLA-PPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQ 570
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDS 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 571 ASDWSPQESGSPVETQEsPEKAGRRSSLQSPASVAPPQGPG--------TKIQAPQLLGGETEGREA---PQGELVpeAW 639
Cdd:TIGR02168 581 IKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYllggvlvvDDLDNALELAKKLRPGYRivtLDGDLV--RP 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 640 GLRQEGpehkpGPSEPSSVQLEEQegpnqgldlatgqAEAREHDQRLEGTvrdpawqkpqqksegalevqvwegpipGES 719
Cdd:TIGR02168 658 GGVITG-----GSAKTNSSILERR-------------REIEELEEKIEEL---------------------------EEK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 720 LASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEA 799
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 800 AGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVV 879
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 880 RGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEaELQAAATSKEEALMELKTRALQLEEELFQLRQGP 959
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE-ELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1370459164 960 AGLGPK-KRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSL 1011
Cdd:TIGR02168 932 EGLEVRiDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
726-1260 |
9.04e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 726 EQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELE 805
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 806 SASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELG 885
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 886 DRLEHLQRELEQAALE--RQEFLREKESQHQRYQ----------------------GLEQRLEAELQAAATSKEEAL-ME 940
Cdd:TIGR02169 476 EEYDRVEKELSKLQRElaEAEAQARASEERVRGGraveevlkasiqgvhgtvaqlgSVGERYATAIEVAAGNRLNNVvVE 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 941 LKTRALQLEEELFQLRQGPAGLGP--KKRAEPQLVE-------------------------------TQNVRLIE----- 982
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATFLPlnKMRDERRDLSilsedgvigfavdlvefdpkyepafkyvfgdTLVVEDIEaarrl 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 983 -------------VERSNAM---------LVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLE 1040
Cdd:TIGR02169 636 mgkyrmvtlegelFEKSGAMtggsraprgGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1041 IQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKAL--------AQLQRRQE---------AELEGLLVRHR--D 1101
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkeleARIEELEEdlhkleealNDLEARLSHSRipE 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1102 LKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQdghRQRGLEEELRRLQSEHDRAQMLLAELSRERGE 1181
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE---QRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 1182 LQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELL 1260
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
992-1221 |
9.79e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 71.72 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 992 AEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQ 1071
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1072 QALLRdhkalaQLQRRQEAELEGLLVRHRDLKANMRALELAH---RELQGRHEQLQAQRASVEAQEVALLAERERLMQDg 1148
Cdd:COG4942 107 AELLR------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKylaPARREQAEELRADLAELAALRAELEAERAELEAL- 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370459164 1149 hrQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSA 1221
Cdd:COG4942 180 --LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
998-1303 |
1.47e-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: 72.78 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 998 QGQLQHLEGQLGSLQGRAQELLLQSQRAQEHssrlqaeksvLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRD 1077
Cdd:TIGR02168 185 RENLDRLEDILNELERQLKSLERQAEKAERY----------KELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1078 HKALAqlqrRQEAELEGLLVRHRDLKANMRALElahRELQGRHEQLQAQRASVEAQEVALLAERERLMQDghrQRGLEEE 1157
Cdd:TIGR02168 255 LEELT----AELQELEEKLEELRLEVSELEEEI---EELQKELYALANEISRLEQQKQILRERLANLERQ---LEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1158 LRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELE-----------RAQLEMQSQQLRESNQQLDLSACRLTT 1226
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrleelEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1227 QCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1303
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
829-1206 |
3.33e-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: 71.64 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 829 EREGSRLRAQSEAAEERMQvlesegrqhlEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLRE 908
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLR----------ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 909 KESQHQRYQGLEQRLEaELQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLgpKKRAEPQLVETqnvrlieversna 988
Cdd:TIGR02169 732 EEKLKERLEELEEDLS-SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSRIPE------------- 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 989 mLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETR 1068
Cdd:TIGR02169 796 -IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1069 GQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDG 1148
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370459164 1149 HRQ---RGLEEELRRLQS-------EHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQ 1206
Cdd:TIGR02169 955 DVQaelQRVEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
728-1282 |
1.30e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 728 EALREEVAQLRRKAEAL------GDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQawEQARLREAVEAAG 801
Cdd:COG4913 238 ERAHEALEDAREQIELLepirelAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRA--ELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 802 QELESASQEREALVEALAAAG--------RERRQWEREGSRLRAQSEAAEERMQVLE----SEGRQHLEEAERERREKEA 869
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 870 LQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAAtskEEA-----LMELK-- 942
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDE---AELpfvgeLIEVRpe 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 943 -------------TRALQL--EEELFQ--------------LRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAmlvae 993
Cdd:COG4913 473 eerwrgaiervlgGFALTLlvPPEHYAaalrwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPF----- 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 994 KAALQGQLQHL--------EGQLgSLQGRA---QELLLQSQRAQEH-SSRLQAEKSVL----EIQGQELHRKLEVLEEEV 1057
Cdd:COG4913 548 RAWLEAELGRRfdyvcvdsPEEL-RRHPRAitrAGQVKGNGTRHEKdDRRRIRSRYVLgfdnRAKLAALEAELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1058 RAARQSQEETRGQQQALLRDHKALAQLQRRQEAEL--EGLLVRHRDLKANMRALELAHRELqgrhEQLQAQRASVEAQEV 1135
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL----AALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1136 ALLAERERLMQdghRQRGLEEELRRLQSEHDRAQMLLAELsrERGELQGERGELRGRLARLELERAQLEMQsQQLRESNQ 1215
Cdd:COG4913 703 ELEEELDELKG---EIGRLEKELEQAEEELDELQDRLEAA--EDLARLELRALLEERFAAALGDAVERELR-ENLEERID 776
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370459164 1216 QLDLSACRLTTQCE-LLTQLRSAQEEENRQLLAEVQALsRENRELLERsLEsRDHLHREQREYLDQLN 1282
Cdd:COG4913 777 ALRARLNRAEEELErAMRAFNREWPAETADLDADLESL-PEYLALLDR-LE-EDGLPEYEERFKELLN 841
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
747-1139 |
1.61e-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: 69.32 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 747 ELEAQARKLEAQNTEAARLsKELaqarraeaeahreaeaqaweQARLREA-VEAAGQELESASQEREALVEALAAAGRER 825
Cdd:TIGR02168 197 ELERQLKSLERQAEKAERY-KEL--------------------KAELRELeLALLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 826 RQWEREGSRLRAQSEAAEERMQVLESEgrqhleeAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEF 905
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEE-------IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 906 LREKEsqhqryqgleqrleaELQAAATSKEEALMELKTRALQLEEELFQLRQgpaglgpKKRAEPQLVETQNVRLIEVER 985
Cdd:TIGR02168 329 ESKLD---------------ELAEELAELEEKLEELKEELESLEAELEELEA-------ELEELESRLEELEEQLETLRS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 986 SNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELL--LQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQS 1063
Cdd:TIGR02168 387 KVAQLELQIASLNNEIERLEARLERLEDRRERLQqeIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1064 QEETRGQQQALLRDHKALAQLQRRQEAeLEGLLVRHRDLKANMRALELAHRELQGRHEQLqAQRASVEAQ-EVALLA 1139
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVL-SELISVDEGyEAAIEA 541
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
790-1243 |
2.57e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 790 QARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLEsegrqHLEEAERERREKEA 869
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 870 LQAELEkavvrgkELGDRLEHLQRELEqaalERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLE 949
Cdd:COG4717 137 LEAELA-------ELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 950 EELFQLRQGPAGL--------GPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQEL--L 1019
Cdd:COG4717 206 QRLAELEEELEEAqeeleeleEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVlgL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1020 LQSQRAQEHSSRLQAEKSVLEIQGQELHRKLE--VLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRR-QEAELEGLL 1096
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1097 VRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELS 1176
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 1177 RERGELQGERGELRGRLARLELER--AQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR 1243
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
256-805 |
1.65e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 256 LALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALS--GQAKRAELYREEAEALRERAGRLP--- 330
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEleLEEAQAEEYELLAELARLEQDIARlee 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 331 ----------RLQEELRRCRERLQAAEAYKSQLEEER-VLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLG 399
Cdd:COG1196 310 rrreleerleELEEELAELEEELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 400 EAHAELDSLRHQVDQLAEENVELELELQRSLEpppGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQ 479
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEE---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 480 gQPGGQHPLLEAPREDPVLPVLEEAPQtpvafdHSPQGLVQKARDGGPQA--LDLAPPALDSVLEASAECPQAPDSDPQE 557
Cdd:COG1196 467 -ELLEEAALLEAALAELLEELAEAAAR------LLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAA 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 558 AESPLQAAAMDPQASDWspqESGSPVETQESPEKAGRRSSLqspasvappqgPGTKIQAPQLLggetegREAPQGELVPE 637
Cdd:COG1196 540 LEAALAAALQNIVVEDD---EVAAAAIEYLKAAKAGRATFL-----------PLDKIRARAAL------AAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 638 AWGLRQEGPEHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKPQQKSEGALEVQvwegpipg 717
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL-------- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV 797
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
....*...
gi 1370459164 798 EAAGQELE 805
Cdd:COG1196 752 ALEELPEP 759
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1014-1290 |
2.74e-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: 65.46 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1014 RAQELLLQSQRAQEHSSRLQAeksVLEiqgqELHRKLEVLEEEVRAA----RQSQEETRGQQQALLRDHKALAQLQRRQE 1089
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLED---ILN----ELERQLKSLERQAEKAerykELKAELRELELALLVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1090 AELEGLLVRHRDLKANMRALELAHRELqgRHEQLQAQRASVEAQEvallaereRLMQDGHRQRGLEEELRRLQSEHDRAQ 1169
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEEL--RLEVSELEEEIEELQK--------ELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1170 MLLAELSRERGELQGERGELRGRLARLELE----RAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQl 1245
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKleelKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ- 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1370459164 1246 LAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQK 1290
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1100-1295 |
4.16e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1100 RDLKANMRALELAHRELQGRHEQLQA-----------QRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRA 1168
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELlepirelaeryAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1169 QMLLAELSRERGELQGERGELRGRLARLELER-AQLEMQSQQLRESNQQLDLSACRLTTQCELLtQLRSAQEEEnrqlla 1247
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAAL-GLPLPASAE------ 380
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1370459164 1248 EVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
882-1295 |
5.38e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 882 KELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAElqaaatskEEALMELKTralqLEEELFQLRQGPAG 961
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEH--------EERREELET----LEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 962 LGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKA-------ALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQA 1034
Cdd:PRK02224 270 TEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1035 EKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQAL------LRDHKALAQLQR-RQEAELEGLLVRHRDLKANMR 1107
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELeeeieeLRERFGDAPVDLgNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1108 ALELAHRELQGRHEQLQAQRAS----------VEAQEVALLAE-RERLMQDGHRQRGLEEELRRLQSEHDRAQMLL---- 1172
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEdRERVEELEAELEDLEEEVEEVEERLERAEDLVeaed 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1173 -AELSRERGELQGER--------GELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR 1243
Cdd:PRK02224 510 rIERLEERREDLEELiaerretiEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1244 QL--LAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:PRK02224 590 SLerIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEF 643
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
722-1297 |
6.68e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 722 SGVAEQEalrEEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAG 801
Cdd:TIGR02169 163 AGVAEFD---RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 802 QELES--ASQEREALVEALAAAGRERRQWERE------GSRLRAQSE----AAEERMQVLESEGRQHLEEAERERREKEA 869
Cdd:TIGR02169 240 EAIERqlASLEEELEKLTEEISELEKRLEEIEqlleelNKKIKDLGEeeqlRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 870 LQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEaLMELKTRALQLE 949
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 950 EELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGraqelllQSQRAQEHS 1029
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA-------DLSKYEQEL 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1030 SRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRD----HKALAQLQRRQE-----------AELEG 1094
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvHGTVAQLGSVGEryataievaagNRLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1095 LLVRHRDLKAnmRALELAHRELQGRHEQLQAQRASVEAQEVALLA----------------------------------- 1139
Cdd:TIGR02169 552 VVVEDDAVAK--EAIELLKRRKAGRATFLPLNKMRDERRDLSILSedgvigfavdlvefdpkyepafkyvfgdtlvvedi 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1140 ------------------------------------------ERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSR 1177
Cdd:TIGR02169 630 eaarrlmgkyrmvtlegelfeksgamtggsraprggilfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQ 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1178 ERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLS-----------ACRLTTQCELLTQLRSAQEE----EN 1242
Cdd:TIGR02169 710 ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienvkselkelEARIEELEEDLHKLEEALNDlearLS 789
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1370459164 1243 RQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMD 1297
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
822-1295 |
1.57e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 822 GRERRQWEREGSRLR---AQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELgdrlEHLQRELEQA 898
Cdd:PRK03918 168 GEVIKEIKRRIERLEkfiKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 899 ALERQEFLREKESQHQRYQGLEQRLEaelqaaatSKEEALMELKTRALQLEEelfqlrqgpaglgpkkraepqlvetqnv 978
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIE--------ELKKEIEELEEKVKELKE---------------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 979 rLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEiqgqELHRKLEVLEEEVR 1058
Cdd:PRK03918 288 -LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1059 aarqsqeetrgqqqaLLRDHKALAQLQRRQEAELEGLLVrhRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEvall 1138
Cdd:PRK03918 363 ---------------LYEEAKAKKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEI---- 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1139 AERERLMQDGHRQRGLEEELRRLQSEHDRAQmLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLResnqqld 1218
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPVCGRELTEEHRKE-LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES------- 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1219 lsacRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREyLDQLNALRREKQKLVEKI 1295
Cdd:PRK03918 494 ----ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE-LEKLEELKKKLAELEKKL 565
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
789-1130 |
1.72e-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: 62.78 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 789 EQARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKE 868
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 869 ALQAELEKAVVRGKELGDRLEHLQRELEQ-AALERQEFLREKESQHQRYQGLEQRLEAELQAAatskEEALMELKTRALQ 947
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 948 LEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEG-------QLGSLQGRAQELLL 1020
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKerdeleaQLRELERKIEELEA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1021 QSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVrAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHR 1100
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP-EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLD 989
|
330 340 350
....*....|....*....|....*....|
gi 1370459164 1101 DLKANMRALELAHRELQGRHEQLQAQRASV 1130
Cdd:TIGR02169 990 ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
727-1295 |
1.79e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 727 QEALREEVAqlrRKAEAlGDELEAQARKLEAQNTEAARLSKELAQARRAE--AEAHREAEAQAWEQARLREAVEAA---- 800
Cdd:PTZ00121 1161 EDARKAEEA---RKAED-AKKAEAARKAEEVRKAEELRKAEDARKAEAARkaEEERKAEEARKAEDAKKAEAVKKAeeak 1236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 801 --GQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAv 878
Cdd:PTZ00121 1237 kdAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK- 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 879 vRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEA---ELQAAATSKEEAlmelKTRALQLEEELFQL 955
Cdd:PTZ00121 1316 -KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKEEA----KKKADAAKKKAEEK 1390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 956 RQGPAGlgpKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQlGSLQGRAQELLLQSQ---RAQEHSSRL 1032
Cdd:PTZ00121 1391 KKADEA---KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKADEAKKKAEeakKAEEAKKKA 1466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1033 QAEKSVLEIQGQ-ELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELegllvrhRDLKANMRALEL 1111
Cdd:PTZ00121 1467 EEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEA-------KKAEEAKKADEA 1539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1112 AHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLL--------------AELSR 1177
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeekkmkaeeakkAEEAK 1619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1178 ERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCE----LLTQLRSAQEEENRQllaeVQALS 1253
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkkKAEEAKKAEEDEKKA----AEALK 1695
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1370459164 1254 RENREllERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:PTZ00121 1696 KEAEE--AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
880-1285 |
2.39e-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: 62.29 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 880 RGKELGDRLEHLQRELEQA--ALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQ 957
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLreALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 958 GPAGLGPKKRAE-PQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQG-----------RAQELLLQSQRA 1025
Cdd:TIGR00618 293 APLAAHIKAVTQiEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeihirdaHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1026 QEHSSR-----LQAEKSVLEIQGQELHRKLEVLEEEvraarQSQEETRGQQQALLRDHKALAQLQrrQEAELEGLLVRHR 1100
Cdd:TIGR00618 373 QQHTLTqhihtLQQQKTTLTQKLQSLCKELDILQRE-----QATIDTRTSAFRDLQGQLAHAKKQ--QELQQRYAELCAA 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1101 DLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRL--QSEHDRAQMLLAELSre 1178
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLcgSCIHPNPARQDIDNP-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1179 rGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRE 1258
Cdd:TIGR00618 524 -GPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
|
410 420
....*....|....*....|....*..
gi 1370459164 1259 LLERSLESRDHLHREQREYLDQLNALR 1285
Cdd:TIGR00618 603 LSEAEDMLACEQHALLRKLQPEQDLQD 629
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
789-1295 |
3.57e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 789 EQARLREAVEAAGQELESASQEREALVEALAAAGRER---RQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERR 865
Cdd:PRK02224 228 QREQARETRDEADEVLEEHEERREELETLEAEIEDLRetiAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 866 EKEALQAELEkavvrgkELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLE------AELQAAATSKEEALM 939
Cdd:PRK02224 308 DAEAVEARRE-------ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEelreeaAELESELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 940 ELKTRALQLEEELFQLRQGPAGLGpkkraepqlvetqnVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGR---AQ 1016
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAP--------------VDLGNAEDFLEELREERDELREREAELEATLRTARERveeAE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1017 ELLLQSQ------------------RAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQ--EETRGQQQALLR 1076
Cdd:PRK02224 447 ALLEAGKcpecgqpvegsphvetieEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIErlEERREDLEELIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1077 DHKALAQLQRRQeaeLEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEE 1156
Cdd:PRK02224 527 ERRETIEEKRER---AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1157 ELRRLQSEHDRAQMlLAELSRERGELQGERGELRGRLARlELERAQLEmqsqQLRESNQQLDLSACRLTTQCELLTQLRS 1236
Cdd:PRK02224 604 AEDEIERLREKREA-LAELNDERRERLAEKRERKRELEA-EFDEARIE----EAREDKERAEEYLEQVEEKLDELREERD 677
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370459164 1237 AQEEENRQLLAEVQALS--RENRELLERSLESRDHLHREQREYLDQLNALRRE-KQKLVEKI 1295
Cdd:PRK02224 678 DLQAEIGAVENELEELEelRERREALENRVEALEALYDEAEELESMYGDLRAElRQRNVETL 739
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
902-1295 |
8.57e-09 |
|
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: 60.57 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 902 RQEFLREKESQHQRYQGLEQRLEAELQAAaTSKEEALMELKTR---ALQLEEELF-QLRQGPAGLGPKKRAEPQLVETQN 977
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKEL-EKKHQQLCEEKNAlqeQLQAETELCaEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 978 VRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEev 1057
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEE-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1058 RAARQSQEETRGQQQAllrdhKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVAL 1137
Cdd:pfam01576 160 RISEFTSNLAEEEEKA-----KSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1138 LAERERlmqdghrqrgLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRES---- 1213
Cdd:pfam01576 235 RAQLAK----------KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEleal 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1214 NQQLDLSACRLTTQCEL-------LTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRR 1286
Cdd:pfam01576 305 KTELEDTLDTTAAQQELrskreqeVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES 384
|
....*....
gi 1370459164 1287 EKQKLVEKI 1295
Cdd:pfam01576 385 ENAELQAEL 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
718-1277 |
1.60e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEalgdELEAQARKLEAQNTEAARLSKELAQarraeaeahreaeaqawEQARLREAV 797
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEERIEELKK-----------------EIEELEEKV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 798 EAAgQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESegrqhleeaererrekeaLQAELEKA 877
Cdd:PRK03918 283 KEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE------------------KEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 878 VVRGKELGDRLEHLQrELEQAALERQEFLREKESQHQRYQGLE-QRLEAELQAAATSKEE---ALMELKTRALQLEEELF 953
Cdd:PRK03918 344 KKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEieeEISKITARIGELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 954 QLRQGPAGLGPKKRAEPqlveTQNVRLIEVERSNAM--LVAEKAALQGQLQHLEGQLGSLQGRAQELllqsQRAQEHSSR 1031
Cdd:PRK03918 423 ELKKAIEELKKAKGKCP----VCGRELTEEHRKELLeeYTAELKRIEKELKEIEEKERKLRKELREL----EKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1032 LQAEKSVLEiQGQELHRKLEVLE-EEVRAARQSQEETRGQQQALLRDHKALaqlqrrqEAELEgllvRHRDLKANMRALE 1110
Cdd:PRK03918 495 LIKLKELAE-QLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSL-------KKELE----KLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1111 LAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQ--------RGLEEELRRLQSEHDRAQMLLAELSRERGEL 1182
Cdd:PRK03918 563 KKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1183 QgergELRGRLArlELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALS--RENRELL 1260
Cdd:PRK03918 643 E----ELRKELE--ELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREkaKKELEKL 716
|
570
....*....|....*..
gi 1370459164 1261 ERSLESRDHLHREQREY 1277
Cdd:PRK03918 717 EKALERVEELREKVKKY 733
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
732-1186 |
2.43e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 732 EEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQarraeAEAHReaeaqawEQARLREAVEAAGQELESASQER 811
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE-----LREEL-------EKLEKLLQLLPLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 812 EALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQhleEAERERREKEALQAELEKAVVRGKELGDRLEHL 891
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQ---LSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 892 QRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLeEELFQLRQGPAGLGPKKRAEPQ 971
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI-AGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 972 LVETQNVRLIEVERSNAMLvaEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRK-- 1049
Cdd:COG4717 298 ASLGKEAEELQALPALEEL--EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAal 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1050 ---LEVLEEEVRAARQSQEETRGQQQALLRDHKalAQLQRRQEAELEGLLVRHRD-LKANMRALELAHRELQGRHEQLQA 1125
Cdd:COG4717 376 laeAGVEDEEELRAALEQAEEYQELKEELEELE--EQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459164 1126 QRASVEaQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGER 1186
Cdd:COG4717 454 ELAELE-AELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
718-1264 |
3.21e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAeaeahreaeaqaweqarlREAV 797
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD------------------AEAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 798 EAAGQELESASQE-REALVEALAAAGRERRQWER---EGSRLRAQSEAAEERMQVLESEgrqhLEEAERERREKEALQAE 873
Cdd:PRK02224 313 EARREELEDRDEElRDRLEECRVAAQAHNEEAESlreDADDLEERAEELREEAAELESE----LEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 874 LEKAVvrgKELGDRLEHLQRELEQAALERQEFLREKESQHQRyqglEQRLEAELQAAATSKEEAlmelktralqleEELF 953
Cdd:PRK02224 389 LEEEI---EELRERFGDAPVDLGNAEDFLEELREERDELRER----EAELEATLRTARERVEEA------------EALL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 954 QLRQGPAGLGPKKRAE-PQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEgQLGSLQGRAQELLLQSQRAQEHSSRL 1032
Cdd:PRK02224 450 EAGKCPECGQPVEGSPhVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1033 QAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLlvrhRDLKANMRALELA 1112
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIADA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1113 HRELQGRHEQLqAQRASVEAQevallaERERLMQDGHRQRGLEEE-----LRRLQSEHDRAQMLLAELSRERGELQGERG 1187
Cdd:PRK02224 605 EDEIERLREKR-EALAELNDE------RRERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERD 677
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1188 ELRGRLARLELERAQLEmqsqQLRESNQQLDLSACRLTTQCELLTQLrsaqEEENRQLLAEvqaLSRENRELLERSL 1264
Cdd:PRK02224 678 DLQAEIGAVENELEELE----ELRERREALENRVEALEALYDEAEEL----ESMYGDLRAE---LRQRNVETLERML 743
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
944-1291 |
3.31e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.82 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 944 RALQLEEELFqlrqgpaglgpkkRAEPQLVETQNvRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQG--RAQElllQ 1021
Cdd:PRK04863 287 EALELRRELY-------------TSRRQLAAEQY-RLVEMARELAELNEAESDLEQDYQAASDHLNLVQTalRQQE---K 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1022 SQRAQ----EHSSRLQAEKSVLEiqgqELHRKLEVLEEEVRAARQSQEETRGQ----QQALLRDHKALAQLQRRQEAele 1093
Cdd:PRK04863 350 IERYQadleELEERLEEQNEVVE----EADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQA--- 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1094 glLVRHRDLKANMralELAHRELQGRHEQLQAQRASVeAQEVALLAERERLMQDGHRQ--------RGLEEELRRLQSeH 1165
Cdd:PRK04863 423 --LERAKQLCGLP---DLTADNAEDWLEEFQAKEQEA-TEELLSLEQKLSVAQAAHSQfeqayqlvRKIAGEVSRSEA-W 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1166 DRAQMLLAELSRERGELQgERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSacrlTTQCELLTQLRSAQEeenrql 1245
Cdd:PRK04863 496 DVARELLRRLREQRHLAE-QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKN----LDDEDELEQLQEELE------ 564
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1370459164 1246 lAEVQALSRENRELLERSLESRDHLhreqreylDQLNALRREKQKL 1291
Cdd:PRK04863 565 -ARLESLSESVSEARERRMALRQQL--------EQLQARIQRLAAR 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1049-1267 |
3.43e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1049 KLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRA 1128
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1129 SVEAQevalLAERERLMQDGHRQRGLEEELRRLQ-SEHDRAQMLLAELSRER----GELQGERGELRGRLARLELERAQL 1203
Cdd:COG4942 101 AQKEE----LAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARreqaEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1204 EMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1267
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-1298 |
3.44e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 728 EALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAqarraeaeahreaeaqawEQARLREAVEAAGQELESA 807
Cdd:PRK03918 175 KRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP------------------ELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 808 SQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLEsEGRQHLEEAERERREKEALQAELEKAVVRGKELGDR 887
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 888 LEHLQRELEqaalERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEAlmELKTRALQLEEELFQLRQGPAGLGPKKR 967
Cdd:PRK03918 316 LSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 968 AEpqlvetqnvRLIEVERsnamlvaEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQEHSSRLQAEKSVLEIQGQEL- 1046
Cdd:PRK03918 390 EK---------ELEELEK-------AKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGKCPVCGRELt 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1047 -HRKLEVLEEEVRAARQSQEEtrgqqqaLLRDHKALAQLqRRQEAELEGLLVRHRDLKANMRALELAhRELQGRHEQLQA 1125
Cdd:PRK03918 447 eEHRKELLEEYTAELKRIEKE-------LKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQL-KELEEKLKKYNL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1126 QRASVEAQEVALLaeRERLMQDGHRQRGLEEELRRLQSEHDRaqmlLAELSRERGELQGERGELRGRLARL------ELE 1199
Cdd:PRK03918 518 EELEKKAEEYEKL--KEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELgfesveELE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1200 RAQLEMQS------------QQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESR 1267
Cdd:PRK03918 592 ERLKELEPfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
570 580 590
....*....|....*....|....*....|.
gi 1370459164 1268 DHLHREQREYLDQLNALRREKQKLVEKIMDQ 1298
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1023-1211 |
3.63e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1023 QRAQEHSSRL-QAEKSVLEIQgqelhRKLEVLEEeVRAARQSQEETRgQQQALLRDHKALAQLQRRQ------EAELEGL 1095
Cdd:COG4913 228 DALVEHFDDLeRAHEALEDAR-----EQIELLEP-IRELAERYAAAR-ERLAELEYLRAALRLWFAQrrlellEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1096 LVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQR-----GLEEELRRLQSE------ 1164
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERerrraRLEALLAALGLPlpasae 380
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1370459164 1165 -----HDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLR 1211
Cdd:COG4913 381 efaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
878-1262 |
4.47e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.60 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 878 VVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQaaatskeealmELKTRALQLEEELFQLRQ 957
Cdd:pfam07888 26 VPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRR-----------ELESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 958 GPAGLGPKKRAEPQLVEtqnvrliEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKS 1037
Cdd:pfam07888 95 KHEELEEKYKELSASSE-------ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1038 VLEIQGQELHRKLEVLEEEVRA-------ARQSQEETRGQQQALLRDHKALAQL---QRRQEAELEGLLVRHRDLK---- 1103
Cdd:pfam07888 168 EEEAERKQLQAKLQQTEEELRSlskefqeLRNSLAQRDTQVLQLQDTITTLTQKlttAHRKEAENEALLEELRSLQerln 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1104 ANMRALELAHREL-----QGRHEQLQAQRASVEAQEVAL-LAERERLMQDGHRQRGLEEE--LRRLQSEHDRAQMLLAEL 1175
Cdd:pfam07888 248 ASERKVEGLGEELssmaaQRDRTQAELHQARLQAAQLTLqLADASLALREGRARWAQEREtlQQSAEADKDRIEKLSAEL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1176 SRERGELQGERgelrgrlarleLERAQLEMQSQQLRESNQQLDLSACRLTTqcELLTQLRSAQEEEnRQLLAEVQALSRE 1255
Cdd:pfam07888 328 QRLEERLQEER-----------MEREKLEVELGREKDCNRVQLSESRRELQ--ELKASLRVAQKEK-EQLQAEKQELLEY 393
|
....*..
gi 1370459164 1256 NRELLER 1262
Cdd:pfam07888 394 IRQLEQR 400
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
886-1280 |
5.01e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 886 DRLEHLQR--ELEQAALERQEFLREKESQHQR-------YQGLEQRLEAELQAAatskeEALMELKTRALQLEEELFQLR 956
Cdd:COG3096 279 ERRELSERalELRRELFGARRQLAEEQYRLVEmareleeLSARESDLEQDYQAA-----SDHLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 957 QGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAqellLQSQRAQEhssRLQAEK 1036
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRA----IQYQQAVQ---ALEKAR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1037 SVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALlrdhkALAQLQRRQEAELEGLLVRHRDLKANMRALELAhREL 1116
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKL-----SVADAARRQFEKAYELVCKIAGEVERSQAWQTA-REL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1117 --QGRHEQLQAQRASVEAQEvalLAERERLMqdgHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLA 1194
Cdd:COG3096 501 lrRYRSQQALAQRLQQLRAQ---LAELEQRL---RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1195 RLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRsaqeEENRQLLAEVQALSRENRELLERSLE---SRDHLh 1271
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLR----EQSGEALADSQEVTAAMQQLLEREREatvERDEL- 649
|
....*....
gi 1370459164 1272 REQREYLDQ 1280
Cdd:COG3096 650 AARKQALES 658
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
726-1295 |
9.09e-08 |
|
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: 57.29 E-value: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 726 EQEALREEVAQLRRKAEALGD---------ELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREA 796
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEqlkkqqllkQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIH 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 797 VEAAGQ--ELESASQEREALVEALAAAGRERR---QWEREGSRLRAQSEAAEERmqvlesegRQHLEEAERERREKEALQ 871
Cdd:TIGR00618 314 TELQSKmrSRAKLLMKRAAHVKQQSSIEEQRRllqTLHSQEIHIRDAHEVATSI--------REISCQQHTLTQHIHTLQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 872 AELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQ-HQRYQGLEQRLEAELQAAATSKEEALMELKTRALQlee 950
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ--- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 951 ELFQlrqgpaglgpKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQS------QR 1024
Cdd:TIGR00618 463 ESAQ----------SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltrrmQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1025 AQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLvRHRDLKA 1104
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS-EAEDMLA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1105 nmralELAHRELQGRHEQLQAQRASVEAQ---------EVALLAERERLMQDGHRQRGLEEELRRLQSEHDRaQMLLAEL 1175
Cdd:TIGR00618 612 -----CEQHALLRKLQPEQDLQDVRLHLQqcsqelalkLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKM 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1176 SRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQ-LRSAQEEENRQLLAEVQALSR 1254
Cdd:TIGR00618 686 QSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFN 765
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1370459164 1255 ENRELL--ERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:TIGR00618 766 NNEEVTaaLQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEI 808
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
833-1300 |
9.12e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 833 SRLRAQSEAAEERMQVLEsEGRQHLEEAERERREKEALQAELEKAVVRGKELgdRLEHLQRELEQAALERQEFLREKESQ 912
Cdd:COG4913 238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 913 HQRYQGLEQRLEA--------------ELQAAATSKEEALMELKTRALQLEEEL----FQLRQGPAGLGPKKRAEPQLVE 974
Cdd:COG4913 315 EARLDALREELDEleaqirgnggdrleQLEREIERLERELEERERRRARLEALLaalgLPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 975 TQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGR---------------AQEL------------LLQSQRAQE 1027
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRksniparllalrdalAEALgldeaelpfvgeLIEVRPEEE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1028 ----------HSSRL------QAEKSVLEIQgQELHRKLEVLEEEVRAARQSQEETRGQQQALLR-----DHKALA---- 1082
Cdd:COG4913 475 rwrgaiervlGGFALtllvppEHYAAALRWV-NRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGkldfkPHPFRAwlea 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1083 QLQRRQ-------EAEL---------EGLL----VRHR----------------------DLKANMRALELAHRELQGRH 1120
Cdd:COG4913 554 ELGRRFdyvcvdsPEELrrhpraitrAGQVkgngTRHEkddrrrirsryvlgfdnraklaALEAELAELEEELAEAEERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1121 EQLQAQRASVEAQEVALLAERERLMQDgHRQRGLEEELRRLQSEHDR---AQMLLAELSRERGELQGERGELRGRLARLE 1197
Cdd:COG4913 634 EALEAELDALQERREALQRLAEYSWDE-IDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELK 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1198 LERAQLEMQSQQLRESNQQLDlsacrlttqcELLTQLRSAQEEENRQLLAEV--QALSRENRELLERSLESRdhlhreqr 1275
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQ----------DRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEER-------- 774
|
570 580
....*....|....*....|....*
gi 1370459164 1276 eyLDQLNALRREKQKLVEKIMDQYR 1300
Cdd:COG4913 775 --IDALRARLNRAEEELERAMRAFN 797
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-1295 |
1.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 728 EALREEVAQLRRKAEALGDELEAQA---RKLEAQNTEAARLSKELAQARRAEAeahreaeaqawEQARLREAVEAAGQEL 804
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTEnieELIKEKEKELEEVLREINEISSELP-----------ELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 805 ESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLEsEGRQHLEEAERERREKEALQAELEKAVVRGKEL 884
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 885 GDRLEHLQRELEqaalERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEAlmELKTRALQLEEELFQLRQGPAGLGP 964
Cdd:PRK03918 313 EKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEKRLEELEERH--ELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 965 KKRAEpqlvetqnvRLIEVERsnamlvaEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQEHSSRLQAEKSVLEIQGQ 1044
Cdd:PRK03918 387 EKLEK---------ELEELEK-------AKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGKCPVCGR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1045 EL--HRKLEVLEEEVRAARQSQEEtrgqqqaLLRDHKALAQLqRRQEAELEGLLVRHRDLKANMRALELAhRELQGRHEQ 1122
Cdd:PRK03918 444 ELteEHRKELLEEYTAELKRIEKE-------LKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQL-KELEEKLKK 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1123 LQAQRASVEAQEVALLAER--------ERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGE------------- 1181
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKliklkgeiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfesveeleerl 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1182 ------------LQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDlsacRLTTQCELLTQLRSaqEEENRQLLAEV 1249
Cdd:PRK03918 595 kelepfyneyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKYS--EEEYEELREEY 668
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1370459164 1250 QALSRE---NRELLERSLESRDHLHREQREYLDQLNAlRREKQKLVEKI 1295
Cdd:PRK03918 669 LELSRElagLRAELEELEKRREEIKKTLEKLKEELEE-REKAKKELEKL 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
911-1136 |
1.43e-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: 55.54 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 911 SQHQRYQGLEQRLEaELQAAATSKEEALMELKTRALQLEEELFQLRQgpaglgpKKRAEPQLVETQNVRLIEVERSNAML 990
Cdd:COG4942 17 AQADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 991 VAEKAALQGQLQHLEGQLGSLQGRAQ--------ELLLQSQRAQEHSSRLQAEKSVLEI---QGQELHRKLEVLEEEVRA 1059
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1060 ARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVA 1136
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
291-1129 |
1.50e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 291 LEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQ-EELRRCRERLQAAEAYKSQLEEErvlsgvLEASKAL 369
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRlEELREELEELQEELKEAEEELEE------LTAELQE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 370 LEEQLEAAR----ERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEpppgSPGEapLAGA 445
Cdd:TIGR02168 265 LEEKLEELRlevsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES----KLDE--LAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 446 APSLQDEVREAEAgRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEApqtpvafdhspqglvqkardg 525
Cdd:TIGR02168 339 LAELEEKLEELKE-ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA--------------------- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 526 gpqALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQASDWSPQESGSpVETQESPEKAGRRSSLQSPASVA 605
Cdd:TIGR02168 397 ---SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL-EELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 606 PPQGPGTKIQAPQLLGGETEGREAPQGELVPEAWGLRQ--EGPEHKPGPSEPSSVQLEEQEGPNQGLDLATGqaearEHD 683
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALG-----GRL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 684 QRLEGTVRDPAWQK---PQQKSEGA---LEVQVWEGPIPGESLASGVAEQEALREEVAQLRRKAEALGDELEAQ-ARKLE 756
Cdd:TIGR02168 548 QAVVVENLNAAKKAiafLKQNELGRvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlGGVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 757 AQN-TEAARLSKELAQARR-----------------AEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEAL 818
Cdd:TIGR02168 628 VDDlDNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKEL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 819 AAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKavvrgkelgdrlehLQRELEQA 898
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE--------------LEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 899 ALERQEFLREKESQHQRYQGLEQRLEAeLQAAATSKEEALMELKTRALQLEEELFQLRQgpaglgpkkraepqlvetqnv 978
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLER--------------------- 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 979 RLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVR 1058
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370459164 1059 AARQSQEETRGQQQAL-LRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRAS 1129
Cdd:TIGR02168 912 ELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1085-1303 |
2.00e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1085 QRRQEAELegllvRHRDLKANMRALELAHRELQGRHEQLQAQ----------RASVEAQEVALLA--------ERERLMQ 1146
Cdd:TIGR02168 172 ERRKETER-----KLERTRENLDRLEDILNELERQLKSLERQaekaerykelKAELRELELALLVlrleelreELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1147 D----GHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSAC 1222
Cdd:TIGR02168 247 ElkeaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1223 RLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLhREQREYLDQLNALRREKQKLVEKIMDQYRVL 1302
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-EELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
.
gi 1370459164 1303 E 1303
Cdd:TIGR02168 406 E 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
789-1323 |
2.23e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 789 EQARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREgsRLRAQSEAAEERMQVLESEGRQHLEEAERERREKE 868
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 869 ALQAELEKAVvrgkelGDRLEHLQRELEQAALErqefLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQL 948
Cdd:COG4913 327 ELEAQIRGNG------GDRLEQLEREIERLERE----LEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 949 EEELFQLRQgpaglgpkKRAEpqlvetqnvrlieversnamLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEH 1028
Cdd:COG4913 397 EEELEALEE--------ALAE--------------------AEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1029 -SSRLQAEKSVLEIQGqELhrkLEVLEEEVR---AArqsqeET--RGQQQALLRDHKALAQL-----QRRQEAELEGLLV 1097
Cdd:COG4913 449 lAEALGLDEAELPFVG-EL---IEVRPEEERwrgAI-----ERvlGGFALTLLVPPEHYAAAlrwvnRLHLRGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1098 RHRDLKANMRALE---LAHR------ELQGRHEQLQAQRAS---VEAQEvALLAERERLMQDGHRQRG------------ 1153
Cdd:COG4913 520 RTGLPDPERPRLDpdsLAGKldfkphPFRAWLEAELGRRFDyvcVDSPE-ELRRHPRAITRAGQVKGNgtrhekddrrri 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1154 ----------------LEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRG---------RLARLELERAQLEMQSQ 1208
Cdd:COG4913 599 rsryvlgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1209 QLRESNQQLDlsacrlttqcELLTQLRSAQEEENrQLLAEVQALSRENRELLERslesRDHLHREQREYLDQLNALRREK 1288
Cdd:COG4913 679 RLDASSDDLA----------ALEEQLEELEAELE-ELEEELDELKGEIGRLEKE----LEQAEEELDELQDRLEAAEDLA 743
|
570 580 590
....*....|....*....|....*....|....*
gi 1370459164 1289 QKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRL 1323
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEERIDAL 778
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
870-1263 |
3.48e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 870 LQAELEKAVVRGKELGDRLEHLQRELE-------------QAALERQEFLREKESQH---QRYQG----LEQRLEAELQA 929
Cdd:PRK04863 291 LRRELYTSRRQLAAEQYRLVEMARELAelneaesdleqdyQAASDHLNLVQTALRQQekiERYQAdleeLEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 930 AATSKEEaLMELKTRALQLEEELFQLRQgpaglgpkkraepQLVETQnvrlieversNAMLVAEKAALQGQ--LQHLEgq 1007
Cdd:PRK04863 371 VEEADEQ-QEENEARAEAAEEEVDELKS-------------QLADYQ----------QALDVQQTRAIQYQqaVQALE-- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1008 lgslqgRAQELLLQSQRAQEHSSRLQAEksvLEIQGQELHRKLEVLEEEVRAArqsqeetrgqqQALLRDHKALAQLQR- 1086
Cdd:PRK04863 425 ------RAKQLCGLPDLTADNAEDWLEE---FQAKEQEATEELLSLEQKLSVA-----------QAAHSQFEQAYQLVRk 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1087 ------RQEA-----ELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQrasveaqevallaerERLMQDGHRQRGL- 1154
Cdd:PRK04863 485 iagevsRSEAwdvarELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA---------------ERLLAEFCKRLGKn 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1155 ---EEELRRLQSEHdraQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDlsacRLTTQC--- 1228
Cdd:PRK04863 550 lddEDELEQLQEEL---EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALA----RLREQSgee 622
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1370459164 1229 ------------ELLTQLRSAQEEENrQLLAEVQALSRENRELLERS 1263
Cdd:PRK04863 623 fedsqdvteymqQLLERERELTVERD-ELAARKQALDEEIERLSQPG 668
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
731-1162 |
3.86e-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: 55.34 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 731 REEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELaqarraeaeahreaeaqaweqARLREAVEAAGQELESASQE 810
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMAREL---------------------EELSARESDLEQDYQAASDH 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 811 REALVEALAAAGR-ERRQWEregsrLRAQSEAAEERMQVLESEGRQHleeaererrekEALQAELEKAVVRGKELGDRLE 889
Cdd:COG3096 336 LNLVQTALRQQEKiERYQED-----LEELTERLEEQEEVVEEAAEQL-----------AEAEARLEAAEEEVDSLKSQLA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 890 HLQRELE----------QA--ALERQEFLREKESQHQryQGLEQRLeAELQAAATSKEEALMELKTR------ALQLEEE 951
Cdd:COG3096 400 DYQQALDvqqtraiqyqQAvqALEKARALCGLPDLTP--ENAEDYL-AAFRAKEQQATEEVLELEQKlsvadaARRQFEK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 952 LFQLRQGPAGLGPKKRAEPQLVEtqnvrLIEVERSNAMLVAEKAALQGQLQHLEgQLGSLQGRAQELLlqSQRAQEHSSR 1031
Cdd:COG3096 477 AYELVCKIAGEVERSQAWQTARE-----LLRRYRSQQALAQRLQQLRAQLAELE-QRLRQQQNAERLL--EEFCQRIGQQ 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1032 LQAEKsVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQ---RRQEAELEGLlvrhrdlkANMRA 1108
Cdd:COG3096 549 LDAAE-ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERL--------REQSG 619
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1109 LELAHRelqgrhEQLQAQRASVEAQEVALLAERERLMQdghRQRGLEEELRRLQ 1162
Cdd:COG3096 620 EALADS------QEVTAAMQQLLEREREATVERDELAA---RKQALESQIERLS 664
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1007-1218 |
4.84e-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: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1007 QLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQqqallrdhkaLAQLQR 1086
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----------LAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1087 RQEAELEGLLVRHRDLKANMRALELAHRE-----LQGRHEQLQAQRASVEAQEVAlLAERERLMQDGHRQRGLEEELRRL 1161
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQYLKYLA-PARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1162 QSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLD 1218
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-480 |
5.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 255 HLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQAL-----SGQAKRAELYREEAEALRERAGRL 329
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAeaelaEAEEALLEAEAELAEAEEELEELA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 330 PRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLR 409
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459164 410 HQVDQLAEENVELELELQRSLEpppgsPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQG 480
Cdd:COG1196 466 AELLEEAALLEAALAELLEELA-----EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIG 531
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
834-1201 |
7.66e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 834 RLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGdrlehlQRELEQAALERQEFLREKESQH 913
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA------KKALEYYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 914 QRYQGLEQRLEAELQAAATSKEEALMELKtRALQLEEELFQLRQgpaglgpKKRAEpqlvETQNVRLIEVERSNAMLvaE 993
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRDEQEEIESSK-QEIEKEEEKLAQVL-------KENKE----EEKEKKLQEEELKLLAK--E 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 994 KAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQA 1073
Cdd:pfam02463 295 EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1074 LLRDHKALAQLQRRQEAELE-GLLVRHRDLKANMRALELAHRElqgrhEQLQAQRASVEAQEVALLAERERLMQDGHRQR 1152
Cdd:pfam02463 375 LLAKKKLESERLSSAAKLKEeELELKSEEEKEAQLLLELARQL-----EDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1370459164 1153 GLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERA 1201
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1032-1298 |
1.01e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1032 LQAEKSVLEIQGQElhrKLEVLEEEvraaRQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALEL 1111
Cdd:pfam17380 278 VQHQKAVSERQQQE---KFEKMEQE----RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1112 AHRELQGRHEQLQAQRASVEAQEVALLAERERLM----QDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERG 1187
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEISRMRELERLQmerqQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1188 ELRGR-LARLELERAQlEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEvqalsrENRELLERSLES 1266
Cdd:pfam17380 431 EARQReVRRLEEERAR-EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEE------QRRKILEKELEE 503
|
250 260 270
....*....|....*....|....*....|..
gi 1370459164 1267 RDHLHREQreyldqlnalrREKQKLVEKIMDQ 1298
Cdd:pfam17380 504 RKQAMIEE-----------ERKRKLLEKEMEE 524
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1138-1295 |
1.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1138 LAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLEL--ERAQLEMQSQQLRESNQ 1215
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1216 QLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
823-1268 |
1.53e-06 |
|
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: 52.80 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 823 RERRQWEREGSRLRAQSEAAEERMQ----VLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELE-Q 897
Cdd:pfam05483 233 KEINDKEKQVSLLLIQITEKENKMKdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMStQ 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 898 AALERQ---------EFLREKESQHQ---RYQGLEQRLEAELQAAATSKEEALmelKTRALQLEEELFQLRQGPAGLGPK 965
Cdd:pfam05483 313 KALEEDlqiatkticQLTEEKEAQMEelnKAKAAHSFVVTEFEATTCSLEELL---RTEQQRLEKNEDQLKIITMELQKK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 966 KRAEPQLVETQNVRLIEVERSNAMLvAEKAALQGQLQHLEGQLGSLQGRAQEL--LLQSQRAQEHSsrLQAEKSVLEIQG 1043
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELifLLQAREKEIHD--LEIQLTAIKTSE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1044 QELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQ--------LQRRQEAELEGLLVRHRDLKA--NMRALELAH 1113
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtleLKKHQEDIINCKKQEERMLKQieNLEEKEMNL 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1114 R-ELQGRHEQLQAQRASV-----EAQEVALLAERERLMQDgHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQ---- 1183
Cdd:pfam05483 547 RdELESVREEFIQKGDEVkckldKSEENARSIEYEVLKKE-KQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgs 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1184 GERGELRG---RLARLELERA-------------QLEMQSQQLRESNQQLDLSACRLTTqcELLTQLRSAQEEENRQLLA 1247
Cdd:pfam05483 626 AENKQLNAyeiKVNKLELELAsakqkfeeiidnyQKEIEDKKISEEKLLEEVEKAKAIA--DEAVKLQKEIDKRCQHKIA 703
|
490 500
....*....|....*....|.
gi 1370459164 1248 EVQALSRENRELLERSLESRD 1268
Cdd:pfam05483 704 EMVALMEKHKHQYDKIIEERD 724
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-481 |
1.73e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 283 DSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEE---LRRCRERLQAAEAYKSQLEEErvl 359
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDAS--- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 360 SGVLEAskalLEEQLEAARERCARLHETQREnllLRTRLGEAHAELDSLRHQVDQlaeenveleleLQRSLEPPPGSPGE 439
Cdd:COG4913 684 SDDLAA----LEEQLEELEAELEELEEELDE---LKGEIGRLEKELEQAEEELDE-----------LQDRLEAAEDLARL 745
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1370459164 440 APLAGAAPSLQDEVREAEAGRLR-TLERENRELRGLLQVLQGQ 481
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELReNLEERIDALRARLNRAEEE 788
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
718-1226 |
1.95e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQN-TEAARLSKELAQARRaeaeahreaeaqawEQARLREA 796
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNnRDIAGIKDKLAKIRE--------------ARDRQLAV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 797 VEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAA--EERMQVLESEGRQHLEEAERERREKEALQAEL 874
Cdd:pfam12128 413 AEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAtpELLLQLENFDERIERAREEQEAANAEVERLQS 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 875 EKAVVRGKElGDRLEHLQRElEQAALERQEFLREKESQHQRYQGleqRLEAELQAAATSKEEALMELKTRALQLEEEL-- 952
Cdd:pfam12128 493 ELRQARKRR-DQASEALRQA-SRRLEERQSALDELELQLFPQAG---TLLHFLRKEAPDWEQSIGKVISPELLHRTDLdp 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 953 ----FQLRQGPAGLGPKKRAEP-------QLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQgRAQELLLQ 1021
Cdd:pfam12128 568 evwdGSVGGELNLYGVKLDLKRidvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS-REETFART 646
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1022 S-QRAQEHSSRLQAEKSvleiqgQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAEL-------- 1092
Cdd:pfam12128 647 AlKNARLDLRRLFDEKQ------SEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREArtekqayw 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1093 ---------------EGLLVRHRDLKANMRALEL-AHRELQGRheQLQAQRASVEAQEVALLAER-ERLMQDGHRQRGLE 1155
Cdd:pfam12128 721 qvvegaldaqlallkAAIAARRSGAKAELKALETwYKRDLASL--GVDPDVIAKLKREIRTLERKiERIAVRRQEVLRYF 798
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370459164 1156 EELR-RLQSEHDRAQMLLAELSRERGELQGERG----ELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTT 1226
Cdd:pfam12128 799 DWYQeTWLQRRPRLATQLSNIERAISELQQQLArliaDTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT 874
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
726-1307 |
2.45e-06 |
|
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: 52.43 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 726 EQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEaeahreaeaqaweQARLREAVEAAGQELE 805
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQL-------------RSELREAKRMYEDKIE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 806 SASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEgrqhleeaererrekealqAELEKAvvRGKELG 885
Cdd:pfam15921 346 ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKE-------------------LSLEKE--QNKRLW 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 886 DR-------LEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAaatsKEEALMELKTRALQLEEELFQLRQG 958
Cdd:pfam15921 405 DRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQG----KNESLEKVSSLTAQLESTKEMLRKV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 959 PAGLGPKKraepqlvetqnVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQ---EHSSRLQAE 1035
Cdd:pfam15921 481 VEELTAKK-----------MTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1036 KSVLEIQGQELHRKLEVLEEEVRAARQsqeetrgqqqaLLRDHKALAQLQRRQEAELEGLLvrhRDLKANMRALELAHRE 1115
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMTQ-----------LVGQHGRTAGAMQVEKAQLEKEI---NDRRLELQEFKILKDK 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1116 LQGRHEQLQAQRASVEAQEVALL---AERERLMQDghrqrgLEEELRRLQSEHDRAQMLLAELSRERGEL------QGER 1186
Cdd:pfam15921 616 KDAKIRELEARVSDLELEKVKLVnagSERLRAVKD------IKQERDQLLNEVKTSRNELNSLSEDYEVLkrnfrnKSEE 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1187 GELRGRLARLELERAQLEM-QSQQLRESNQQLDLSACRLTTQCELLTQLRSAQ---EEENRQLLAEVQALSRENRELL-- 1260
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELeQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQidaLQSKIQFLEEAMTNANKEKHFLke 769
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1370459164 1261 ERSLESRD--HLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPVPL 1307
Cdd:pfam15921 770 EKNKLSQElsTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
726-1218 |
2.46e-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: 52.28 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 726 EQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELE 805
Cdd:TIGR00618 373 QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 806 SASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELG 885
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 886 DRLEHLQRELEQAALERQefLREKESQHQRYQGLEQRLEAELQAAaTSKEEALMELKTRALQLEEELFQLRQGPAglgpk 965
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQ--LTSERKQRASLKEQMQEIQQSFSIL-TQCDNRSKEDIPNLQNITVRLQDLTEKLS----- 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 966 kRAEPQLVETQNVRLIEVERSNAMLvaEKAALQGQLQHLEGQ-LGSLQGRAQELLLQSQRAQEHSSRLQAEKSvleiqGQ 1044
Cdd:TIGR00618 605 -EAEDMLACEQHALLRKLQPEQDLQ--DVRLHLQQCSQELALkLTALHALQLTLTQERVREHALSIRVLPKEL-----LA 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1045 ELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQgrHEQLQ 1124
Cdd:TIGR00618 677 SRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM--HQART 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1125 AQRASVEAQEVA---LLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGE-----------LQGERGELR 1190
Cdd:TIGR00618 755 VLKARTEAHFNNneeVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdedilnlqcetLVQEEEQFL 834
|
490 500
....*....|....*....|....*...
gi 1370459164 1191 GRLARLELERAQLEMQSQQLRESNQQLD 1218
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
983-1183 |
2.87e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 983 VERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ--RAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAA 1060
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1061 RQSQEETRGQQQALLRD------HKALAQLQRRQEAELEGLLVRH---RDLKANMRALE-LAHRELQGRHEQLQAQRASV 1130
Cdd:COG3206 246 RAQLGSGPDALPELLQSpviqqlRAQLAELEAELAELSARYTPNHpdvIALRAQIAALRaQLQQEAQRILASLEAELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1370459164 1131 EAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQ 1183
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| HOOK_N |
pfam19047 |
HOOK domain; This domain is found at the N-terminus of HOOK proteins. |
56-178 |
3.06e-06 |
|
HOOK domain; This domain is found at the N-terminus of HOOK proteins.
Pssm-ID: 465958 Cd Length: 151 Bit Score: 48.56 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 56 LSDGALLLRVLGIIAPSSRGGPRMLRGLDGPAA-WR--VWNLNHLWGRLRDFYQEELQLLILSPP-PDLQTLG--FDPls 129
Cdd:pfam19047 25 LTDGVAMAQVLHQIDPSWFTEAWLSRIKEDVGDnWRlkVSNLKKILQSVVDYYQDVLGQQISDFLlPDVNLIGehSDP-- 102
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1370459164 130 eeavEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEV 178
Cdd:pfam19047 103 ----AELGRLLQLILGCAVNCEKKQEYIQQIMTLEESVQHVVMTAIQEL 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
886-1279 |
5.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 886 DRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEA-LMELKTRALQLEEELFQLRQGPaglgp 964
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdVASAEREIAELEAELERLDASS----- 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 965 kkraepqlvetqnvrlieversnamlvaekaalqGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQ 1044
Cdd:COG4913 685 ----------------------------------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1045 ELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRdlkanmRALELAHRELQGR-HEQL 1123
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE------EELERAMRAFNREwPAET 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1124 QAQRASVEAQEvALLAERERLMQDG-HRQRGLEEELRRLQSEHDRAQmLLAELSRERGELQGERGELRGRLARLEL---E 1199
Cdd:COG4913 805 ADLDADLESLP-EYLALLDRLEEDGlPEYEERFKELLNENSIEFVAD-LLSKLRRAIREIKERIDPLNDSLKRIPFgpgR 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1200 RAQLEMQSQQLRESNqqldlsacrlttqcELLTQLRSAQeeENRQLLAEVQALSRENR--ELLERsLESRDHLH--REQR 1275
Cdd:COG4913 883 YLRLEARPRPDPEVR--------------EFRQELRAVT--SGASLFDEELSEARFAAlkRLIER-LRSEEEESdrRWRA 945
|
....
gi 1370459164 1276 EYLD 1279
Cdd:COG4913 946 RVLD 949
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1312 |
6.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 678 EAR--EHDQRLEGTVRDPAWQKPQQKSEGALEVQVWEGPIPGESL---------ASGVAEQEALREEV--AQLRRKAEAL 744
Cdd:PTZ00121 1216 EARkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmahfarrqAAIKAEEARKADELkkAEEKKKADEA 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 745 GDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV----EAAGQELES------ASQEREAL 814
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkaeaEAAADEAEAaeekaeAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 815 VEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKavvRGKELGDRLEHLQRE 894
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK---KKAEEAKKADEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 895 LEQAalerqeflreKESQHQRYQGLEQRLEAELQAAATSKEEAlMELKTRALQLEEELFQLRQGPAGlgpKKRAEpqlve 974
Cdd:PTZ00121 1453 AEEA----------KKAEEAKKKAEEAKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAEA---KKKAD----- 1513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 975 tqnvrliEVERsnamlvAEKAAlqgqlqhlegqlgslqgRAQELllqsQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLE 1054
Cdd:PTZ00121 1514 -------EAKK------AEEAK-----------------KADEA----KKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1055 -EEVRAARQSQEETRGQQQAlLRDHKALAQLQRRQEAELEGLLVRHRDLKAnmralELAHRELQGRHEQLQAQRASVEAQ 1133
Cdd:PTZ00121 1560 aEEKKKAEEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKA-----EEAKKAEEAKIKAEELKKAEEEKK 1633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1134 EVALLAERErlmqdghrqrglEEELRR---LQSEHDRAQMLLAELSRERGELQGERGELRgrlaRLELERAQLEMQSQQL 1210
Cdd:PTZ00121 1634 KVEQLKKKE------------AEEKKKaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAK----KAEEDEKKAAEALKKE 1697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1211 RESNQQLDLSACRLTTQCELLTQLRSAqEEENRQLLAEVQALSRENR---ELLERSLESRDHLHREQREYLDQLNALRRE 1287
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
650 660
....*....|....*....|....*
gi 1370459164 1288 KQKLVEKIMDQYRVLEPVPLPRTKK 1312
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1021-1242 |
8.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1021 QSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQE--ETRGQQQALLRDHKALAQLQRRQEAELEGLLVR 1098
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1099 HRDLKANMRALELAHRELQGrHEQLQAQRASVEAQEVALLAERERLmQDGHRQ-RGLEEELRRLQSE-HDRAQMLLAELS 1176
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARY-TPNHPDvIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370459164 1177 RERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTqceLLTQLRSAQEEEN 1242
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES---LLQRLEEARLAEA 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1123-1345 |
8.70e-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: 49.76 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1123 LQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQ 1202
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1203 LEMQSQQLRESNQQLDLSACRLTTQCEL---------------------LTQLRSAQEEENRQLLAEVQALsrenRELLE 1261
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLalllspedfldavrrlqylkyLAPARREQAEELRADLAELAAL----RAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1262 RSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRLMRPRREGGPPGGLRLGAD 1341
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....
gi 1370459164 1342 GAGS 1345
Cdd:COG4942 251 LKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
901-1287 |
9.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 901 ERQEFLREKESQHQRYQGLEQRLEAELQAAAtSKEEALMELKTRALQLEEELFQLRQgpaglgpkKRAEPQlvetQNVRL 980
Cdd:COG4717 54 EADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEA--------ELEELR----EELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 981 IEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsqraqehsSRLQAEKSVLEIQGQELHRKLEvleeevRAA 1060
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELE------ELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1061 RQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQgRHEQLQAQRASVEAQEVALLAE 1140
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAALLALL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1141 RERLMQDGHRQRGLEEELRRLQSehdrAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLR----ESNQQ 1216
Cdd:COG4717 263 GLGGSLLSLILTIAGVLFLVLGL----LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEE 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 1217 LDLSACRLTTQCELLTQLRSAQEE--------ENRQLLAEVQALSREnrellerSLESRDHLHREQREYLDQLNALRRE 1287
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEElqleeleqEIAALLAEAGVEDEE-------ELRAALEQAEEYQELKEELEELEEQ 410
|
|
| HkD_Hook1 |
cd22225 |
Hook domain found in protein Hook 1 (Hook1) and similar proteins; Hook1 is a ... |
89-178 |
1.26e-05 |
|
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: 46.77 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 89 WR--VWNLNHLWGRLRDFYQEELQLLILSPP-PDLQTLG--FDPLseeaveQLEGVLRLLLGASVQCEHRELFIRHIQGL 163
Cdd:cd22225 58 WRikMSNLKKILQGIVDYYHEFLDQQISEFLlPDLNRIAehSDPV------ELGRLLQLILGCAVNCEKKQEHIQNIMTL 131
|
90
....*....|....*
gi 1370459164 164 SLEVQSELAAAIQEV 178
Cdd:cd22225 132 EESVQHVVMTAIQEL 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1121-1289 |
1.45e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1121 EQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLA--ELSRERGELQGERGELRGRLARLEL 1198
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1199 ERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1278
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|.
gi 1370459164 1279 DQLNALRREKQ 1289
Cdd:COG4717 234 NELEAAALEER 244
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
487-666 |
1.54e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 487 PLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQAlDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAA 566
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR-RLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 567 MDPQASDWSPQ-ESGSPVETQESPEKAGRRSSLQSPASVAP---------PQGPGTKIQAPQLLGGETEGREAPQGElvP 636
Cdd:PHA03247 2818 LPPAASPAGPLpPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRS--T 2895
|
170 180 190
....*....|....*....|....*....|
gi 1370459164 637 EAWGLRQEGPEHKPGPSEPSSVQLEEQEGP 666
Cdd:PHA03247 2896 ESFALPPDQPERPPQPQAPPPPQPQPQPPP 2925
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
940-1287 |
1.72e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.57 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 940 ELKTRALQLEEELFQLRQgpaglgpkkraepQLVETQNvRLIEVERSNAMLVAEKAALQGQLQHLEGQLgslqgraqELL 1019
Cdd:COG3096 282 ELSERALELRRELFGARR-------------QLAEEQY-RLVEMARELEELSARESDLEQDYQAASDHL--------NLV 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1020 LQSQRAQEHSSRLQAE----KSVLEIQGQ---ELHRKLEVLEEEVRAARQSQEETRGQ----QQALLRDH-KALAQLQRR 1087
Cdd:COG3096 340 QTALRQQEKIERYQEDleelTERLEEQEEvveEAAEQLAEAEARLEAAEEEVDSLKSQladyQQALDVQQtRAIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1088 QeaelegllvRHRDLKANMRALELAHRELQGRHEQLQAQRASVEaQEVALLAERERLMQDGHRQ--------RGLEEELR 1159
Cdd:COG3096 420 Q---------ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT-EEVLELEQKLSVADAARRQfekayelvCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1160 RLQSeHDRAQMLLAELsRERGELQGERGELRGRLARLEleraQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQE 1239
Cdd:COG3096 490 RSQA-WQTARELLRRY-RSQQALAQRLQQLRAQLAELE----QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1370459164 1240 EENRQLLAEvqalsrenrelLERSLESRDHLHREqreyLDQLNALRRE 1287
Cdd:COG3096 564 AQLEELEEQ-----------AAEAVEQRSELRQQ----LEQLRARIKE 596
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1031-1295 |
1.83e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1031 RLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEaELEGLLVRHRDLKANMRALE 1110
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQ-LLKQLRARIEELRAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1111 LAHRELQGRHEQL-----QAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGE 1185
Cdd:TIGR00618 281 ETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1186 RGELRGRLARLELERAQLE--MQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERS 1263
Cdd:TIGR00618 361 HEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYA 440
|
250 260 270
....*....|....*....|....*....|..
gi 1370459164 1264 LESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:TIGR00618 441 ELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-414 |
1.84e-05 |
|
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: 49.67 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 166 EVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPS 245
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 246 RAPAEGPSHHLALQ---------LANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYR 316
Cdd:TIGR02168 775 EELAEAEAEIEELEaqieqlkeeLKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 317 EEAEALRERagrlprLQEELRRCRERLQAAEAYKSQLEEERVLsgvLEASKALLEEQLEAARERcarLHETQRENLLLRT 396
Cdd:TIGR02168 855 ESLAAEIEE------LEELIEELESELEALLNERASLEEALAL---LRSELEELSEELRELESK---RSELRRELEELRE 922
|
250
....*....|....*...
gi 1370459164 397 RLGEAHAELDSLRHQVDQ 414
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDN 940
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1048-1329 |
1.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1048 RKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRR--QEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQA 1125
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1126 QRASVEAQEvALLAERERLMQDGHRQRGL--EEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLEleraqL 1203
Cdd:COG4717 161 LEEELEELE-AELAELQEELEELLEQLSLatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE-----N 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1204 EMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAqeEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNA 1283
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAAALLALLGLGGSL--LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370459164 1284 LRREKQKLVEKIMDQYRVLEPVPLPRTKKGSWLADKVKRLMRPRRE 1329
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
724-1120 |
2.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 724 VAEQEALREEVAQLRRKAEAL---GDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQA-RLREAVEA 799
Cdd:COG4717 131 YQELEALEAELAELPERLEELeerLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeELQQRLAE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 800 AGQELESASQEREALVealaaagRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVV 879
Cdd:COG4717 211 LEEELEEAQEELEELE-------EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 880 ------RGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQ-GLEQRLEAELQAAATSKEEALMELKTRALQLEEEL 952
Cdd:COG4717 284 gllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 953 FQLRQgpaglgpkKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQehssrl 1032
Cdd:COG4717 364 QLEEL--------EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE------ 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1033 qaeksvLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQE--AELEGLLVRHRDLKANMRALE 1110
Cdd:COG4717 430 ------LEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEElkAELRELAEEWAALKLALELLE 503
|
410
....*....|
gi 1370459164 1111 LAHRELQGRH 1120
Cdd:COG4717 504 EAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-404 |
2.46e-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: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 262 NAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSG--------------QAKRAELyREEAEALRERAG 327
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasaEREIAEL-EAELERLDASSD 685
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 328 RLPRLQEELRRCRERLQAAEAYKSQLEEERvlsGVLEASKALLEEQLEAARERCARLHETQRE--NLLLRTRLGEAHAE 404
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEI---GRLEKELEQAEEELDELQDRLEAAEDLARLelRALLEERFAAALGD 761
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
833-1287 |
2.48e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 833 SRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKES- 911
Cdd:pfam05557 58 RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEl 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 912 ------QHQRYQGLEQR---LEAELQAAATsKEEALMELKTRALQLEEELFQLRQGPAGLG--PKKRAEPQLVETQNVRL 980
Cdd:pfam05557 138 qerldlLKAKASEAEQLrqnLEKQQSSLAE-AEQRIKELEFEIQSQEQDSEIVKNSKSELAriPELEKELERLREHNKHL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 981 IEVERSNAML-----------------VAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSR----------LQ 1033
Cdd:pfam05557 217 NENIENKLLLkeevedlkrklereekyREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRieqlqqreivLK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1034 AEKSVLEIQGQELHRKLEVLEEEVRAARQSQEEtrgqQQALLRDHKALAQ-LQRR-----QEAELEGLLVRHRDLKANM- 1106
Cdd:pfam05557 297 EENSSLTSSARQLEKARRELEQELAQYLKKIED----LNKKLKRHKALVRrLQRRvllltKERDGYRAILESYDKELTMs 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1107 ---RALELAHRELQGRHEQLQAQRASVEAQEVALLAErerlmQDGHRQRG--LEEELRRLQSEHDRAQMLLA-----ELS 1176
Cdd:pfam05557 373 nysPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEE-----LGGYKQQAqtLERELQALRQQESLADPSYSkeevdSLR 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1177 RERGELQGERGELRGRLARLELERAQLEMQsqqlresnQQLDLSACR-LTTQCELLTQLRSAQEEENRQLLAEVQALSRE 1255
Cdd:pfam05557 448 RKLETLELERQRLREQKNELEMELERRCLQ--------GDYDPKKTKvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRL 519
|
490 500 510
....*....|....*....|....*....|...
gi 1370459164 1256 NReLLERSLESRDHLHREQREYLDQ-LNALRRE 1287
Cdd:pfam05557 520 LK-KLEDDLEQVLRLPETTSTMNFKeVLDLRKE 551
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
964-1291 |
2.84e-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: 49.07 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 964 PKKRAEPQLV-----ETQNVRLIEVERSNAMLVAEKA----ALQGQLQHLEGQLGSLQGRAQELLLQSQRA--------- 1025
Cdd:pfam12128 214 PKSRLNRQQVehwirDIQAIAGIMKIRPEFTKLQQEFntleSAELRLSHLHFGYKSDETLIASRQEERQETsaelnqllr 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1026 ------QEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLqrrQEAELEGLLVRH 1099
Cdd:pfam12128 294 tlddqwKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELEN---LEERLKALTGKH 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1100 RDLKANMRALELA-----HRELQGRHEQLQAQRasvEAQEVALLAERERLmqdghrqRGLEEELRrlqSEHDRAqmlLAE 1174
Cdd:pfam12128 371 QDVTAKYNRRRSKikeqnNRDIAGIKDKLAKIR---EARDRQLAVAEDDL-------QALESELR---EQLEAG---KLE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1175 LSRERGELQGERGELRGRLARLELERAQLEMQSQQLresnqqldlsacrlttqcELLTQLRSAQEEENrqllAEVQALSR 1254
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRLNQATATPELLLQLENFD------------------ERIERAREEQEAAN----AEVERLQS 492
|
330 340 350
....*....|....*....|....*....|....*..
gi 1370459164 1255 ENRELLERSLESRDHLHREQREYLDQLNALRREKQKL 1291
Cdd:pfam12128 493 ELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
256-427 |
2.85e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 256 LALQLANAKAQLRRLRQELEEKAELlldsQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEE 335
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 336 LRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENL-LLRTRLGEAHAELDSLRHQVDQ 414
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLaELEEELEEAQEELEELEEELEQ 231
|
170
....*....|...
gi 1370459164 415 LAEENVELELELQ 427
Cdd:COG4717 232 LENELEAAALEER 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
919-1129 |
4.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 919 LEQRLEAELQAAATSK---EEALMELKTRALQLEEEL--FQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAE 993
Cdd:COG3206 162 LEQNLELRREEARKALeflEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 994 KAALQGQLQHLEGQLGSLQG-------RAQELLLQSQRAQEhSSRLQAEKSVLeiqgQELHRKLEVLEEEVRA-ARQSQE 1065
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspviqqlRAQLAELEAELAEL-SARYTPNHPDV----IALRAQIAALRAQLQQeAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 1066 ETRGQQQALLRDHKALAQLQRRQEAELEGL---LVRHRDLKANMRALELAHRELQGRHEQLQAQRAS 1129
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1024-1295 |
5.61e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1024 RAQEHSSRLQAEKSVLEIQGQELHRKLE--VLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRD 1101
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRAriELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1102 LKANMRALELAHRElqgrHEQLQAqrasvEAQEVallaererlmqdghrQRGLEEELRRLQSEHDRAQMLLAELSRERGE 1181
Cdd:pfam05557 81 KKKYLEALNKKLNE----KESQLA-----DAREV---------------ISCLKNELSELRRQIQRAELELQSTNSELEE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1182 LQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENR--QLLAEVQAL------- 1252
Cdd:pfam05557 137 LQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLrehnkhl 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1370459164 1253 --SRENRELLERSLES-RDHLHREQrEYLDQLNALRREKQKLVEKI 1295
Cdd:pfam05557 217 neNIENKLLLKEEVEDlKRKLEREE-KYREEAATLELEKEKLEQEL 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
257-411 |
6.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 257 ALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAK---RAELYREEAEaLRERAGRLPRLQ 333
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeqlEREIERLERE-LEERERRRARLE 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 334 EELRRCRERLQA-AEAYKSQLEEervlsgvLEASKALLEEQLEAARERCARLHETQREnllLRTRLGEAHAELDSLRHQ 411
Cdd:COG4913 366 ALLAALGLPLPAsAEEFAALRAE-------AAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERR 434
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
871-1219 |
7.80e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 871 QAELEKAVVRGKELGDRLEHLQRELEqaALERQ----------EFLREKESQHQryqgleqrleaELQAAATSKEEALME 940
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEIS--DLNNQkeqdwnkelkSELKNQEKKLE-----------EIQNQISQNNKIISQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 941 LKTRALQLEEELFQLRQgpaglgPKKRAEPQLVETQN-VRLIEVER-----SNAMLVAEKAALQGQLQH-------LEGQ 1007
Cdd:TIGR04523 340 LNEQISQLKKELTNSES------ENSEKQRELEEKQNeIEKLKKENqsykqEIKNLESQINDLESKIQNqeklnqqKDEQ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1008 LGSLQGRAQEL-----LLQSQRAQEHS--SRLQAEKSVLEIQGQELHR-------KLEVLEEEVRAARQSQEETrgqQQA 1073
Cdd:TIGR04523 414 IKKLQQEKELLekeieRLKETIIKNNSeiKDLTNQDSVKELIIKNLDNtresletQLKVLSRSINKIKQNLEQK---QKE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1074 LlrdhkalaqlqRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEaQEVALLAERERLMQDGHRQRG 1153
Cdd:TIGR04523 491 L-----------KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE-SKISDLEDELNKDDFELKKEN 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370459164 1154 LEEELRRLQSE----HDRAQMLLA---ELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDL 1219
Cdd:TIGR04523 559 LEKEIDEKNKEieelKQTQKSLKKkqeEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSS 631
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
628-1167 |
9.41e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 628 EAPQGELVPEAWGLRQEGPEHKPgpSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKPQQKSEGAlE 707
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA-E 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 708 VQVWEGPIPGESL---ASGVAEQEALREEVAQLRRKAEALgdeleaqaRKLEAQNTEAARLSKELAQARRAEAEAHREAE 784
Cdd:PTZ00121 1371 KKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADEL--------KKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 785 AQAWEQARLREAVEAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERER 864
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 865 REKEALQAELEKAvvrgkelGDRLEHLQRELEQAALERQEFLREKESQHQryqgLEQRLEAElqaaatskeealmELKTR 944
Cdd:PTZ00121 1523 KADEAKKAEEAKK-------ADEAKKAEEKKKADELKKAEELKKAEEKKK----AEEAKKAE-------------EDKNM 1578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 945 ALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsqR 1024
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEEL-----K 1653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1025 AQEHSSRLQAEksvleiqgqELHRKLEVLEEEVRAARQSQEETRGQQQALLR---DHKALAQLQRRQEAEL-EGLLVRHR 1100
Cdd:PTZ00121 1654 KAEEENKIKAA---------EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeEAKKAEELKKKEAEEKkKAEELKKA 1724
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1101 DLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHR-------QRGLEEELRRLQSEHDR 1167
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRkekeaviEEELDEEDEKRRMEVDK 1798
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
429-689 |
9.80e-05 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 46.98 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 429 SLEPPPGSPGEAPLAGAAPSLQDEVREAeAGRLR------TLERENRELRGLLQVLQGQPGGQHPLLEA------PREDP 496
Cdd:PHA03378 693 TMQPPPRAPTPMRPPAAPPGRAQRPAAA-TGRARppaaapGRARPPAAAPGRARPPAAAPGRARPPAAApgrarpPAAAP 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 497 VLPVLEEAPQTPVAFDHSPQG--LVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESP---LQAAAMDPQA 571
Cdd:PHA03378 772 GAPTPQPPPQAPPAPQQRPRGapTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRGRPslkKPAALERQAA 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 572 SDWSPQ-ESGSPVETQESP---EKAGRRSSLQSPASVAPPQGPGTKIQAPQLLGGETEG-REAPQGELVPEAWGLRQEGP 646
Cdd:PHA03378 852 AGPTPSpGSGTSDKIVQAPvfyPPVLQPIQVMRQLGSVRAAAASTVTQAPTEYTGERRGvGPMHPTDIPPSKRAKTDAYV 931
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1370459164 647 EHKPGPSEPSSVQLEEQEGPNQGLDLATGQAEAREHDQRLEGT 689
Cdd:PHA03378 932 ESQPPHGGQSHSFSVIWENVSQGQQQTLECGGTTKQERAMLGT 974
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
992-1261 |
1.13e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 992 AEKAALQGQLQHLEGQLgslqgraqelllQSQRAQEHSSRLQAEKSVLEIQG-QELHRKLEVLEEEVRAARQsqEETRGQ 1070
Cdd:PRK04863 837 AELRQLNRRRVELERAL------------ADHESQEQQQRSQLEQAKEGLSAlNRLLPRLNLLADETLADRV--EEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1071 QQALLRDHKALAQLQRRQEaELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQ-RASVE----------AQEVALLA 1139
Cdd:PRK04863 903 LDEAEEAKRFVQQHGNALA-QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQaFALTEvvqrrahfsyEDAAEMLA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1140 E--------RERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLR 1211
Cdd:PRK04863 982 KnsdlneklRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARAR 1061
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1212 ESNQQLDLSACRltTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLE 1261
Cdd:PRK04863 1062 RDELHARLSANR--SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
761-1148 |
1.16e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 761 EAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEALaaagRERRQWEREGSRLRAQSE 840
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAL----RQQEKIERYQADLEELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 841 AAEERMQVLEsegrqhleeaeRERREKEALQAELEKAVVRGKELGDRLEHLQRELE----------QA--ALERQEFLRE 908
Cdd:PRK04863 363 RLEEQNEVVE-----------EADEQQEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiqyqQAvqALERAKQLCG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 909 KESQHQryQGLEQRLEaELQAAATSKEEALMELKTR------ALQLEEELFQLRQGPAGLGPKKRAEPQLVEtqnvrLIE 982
Cdd:PRK04863 432 LPDLTA--DNAEDWLE-EFQAKEQEATEELLSLEQKlsvaqaAHSQFEQAYQLVRKIAGEVSRSEAWDVARE-----LLR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 983 VERSNAMLVAEKAALQGQLQHLEGQLgSLQGRAQELLLQSQraQEHSSRLQAEkSVLEIQGQELHRKLEVLEEEVRAARQ 1062
Cdd:PRK04863 504 RLREQRHLAEQLQQLRMRLSELEQRL-RQQQRAERLLAEFC--KRLGKNLDDE-DELEQLQEELEARLESLSESVSEARE 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1063 SQEETRGQQQALLRDHKALAQL----QRRQEAeLEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALL 1138
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAARapawLAAQDA-LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALD 658
|
410
....*....|
gi 1370459164 1139 AERERLMQDG 1148
Cdd:PRK04863 659 EEIERLSQPG 668
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
979-1291 |
1.60e-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: 46.04 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 979 RLIEVERSNAMLVAEKAALQGQL----QHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLE 1054
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQRekekERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1055 EEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQ-----------L 1123
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQteeelrslskeF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1124 QAQRASVEAQEVALLAERERLMQDGHR-----QRGLE-----EELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRL 1193
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKlttahRKEAEneallEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAEL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1194 ARLELERAQLemqSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHRE 1273
Cdd:pfam07888 275 HQARLQAAQL---TLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGRE 351
|
330
....*....|....*...
gi 1370459164 1274 QREYLDQLNALRREKQKL 1291
Cdd:pfam07888 352 KDCNRVQLSESRRELQEL 369
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-471 |
1.63e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 130 EEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQ--PGAGVVLALSGPDPGELAPAELEMLSR 207
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEaaARLLLLLEAEADYEGFLEGVKAALLLA 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 208 SLMGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAE 287
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 288 VQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEE-ERVLSGVLEAS 366
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGsRRELLAALLEA 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 367 KALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGspgEAPLAGAA 446
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE---LLEEEALE 754
|
330 340
....*....|....*....|....*
gi 1370459164 447 PSLQDEVREAEAGRLRTLERENREL 471
Cdd:COG1196 755 ELPEPPDLEELERELERLEREIEAL 779
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
216-620 |
1.69e-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: 46.39 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 216 LARERDLGAQRLA--------ELLLEREPLCLRPEAPSRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAE 287
Cdd:COG1020 904 VAREDAPGDKRLVayvvpeagAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 288 VQGLEAEIRRLRQEAQALSGQAKRAE----------LYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEER 357
Cdd:COG1020 984 AEEEEEEAALALLLLLVVVVGDDDFFffggglglllLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPL 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 358 VLSGVLEASKALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSP 437
Cdd:COG1020 1064 AAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVA 1143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 438 GEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQG 517
Cdd:COG1020 1144 LAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 518 LVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDPQEAESPLQAAAMDPQASDWSPQESGSPVETQESPEKAGRRSS 597
Cdd:COG1020 1224 LAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLAL 1303
|
410 420
....*....|....*....|...
gi 1370459164 598 LQSPASVAPPQGPGTKIQAPQLL 620
Cdd:COG1020 1304 LLLLALALALLLLLLLLLALLLL 1326
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
286-398 |
2.21e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 286 AEVQGLEAEIRRLRQEAQALSgqakraelyREEAEALRERAGrlpRLQEELRRCRERLQAAEAyksQLEEERVLSGVLEA 365
Cdd:COG0542 411 EELDELERRLEQLEIEKEALK---------KEQDEASFERLA---ELRDELAELEEELEALKA---RWEAEKELIEEIQE 475
|
90 100 110
....*....|....*....|....*....|...
gi 1370459164 366 SKALLEEQLEAARERCARLHETQRENLLLRTRL 398
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
659-1275 |
2.53e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.94 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 659 QLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQKpQQKSEGALEVQVWEgpipgesLASGVAEQEALREEVAQLR 738
Cdd:pfam01576 111 QLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISE-------FTSNLAEEEEKAKSLSKLK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 739 RKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEahreaeaqawEQARLREAVEAAGQELESASQEREALVEAL 818
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQE----------QIAELQAQIAELRAQLAKKEEELQAALARL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 819 AAAGRERRQWEREGSRLRAQ-SEAAEErmqvLESEgrqhleeaererrekealQAELEKAVVRGKELGDRLEHLQRELEQ 897
Cdd:pfam01576 253 EEETAQKNNALKKIRELEAQiSELQED----LESE------------------RAARNKAEKQRRDLGEELEALKTELED 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 898 A--ALERQEFLREKesQHQRYQGLEQRLEAElqaaATSKEEALMELKTRALQLEEELfqlrqgpaglgpkkraepqlvet 975
Cdd:pfam01576 311 TldTTAAQQELRSK--REQEVTELKKALEEE----TRSHEAQLQEMRQKHTQALEEL----------------------- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 976 qNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEE 1055
Cdd:pfam01576 362 -TEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1056 EVRAARQSQEETRGQQQALLRDHKAL-AQLQRRQEAeLEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQ- 1133
Cdd:pfam01576 441 ELESVSSLLNEAEGKNIKLSKDVSSLeSQLQDTQEL-LQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQl 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1134 ---EVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQL 1210
Cdd:pfam01576 520 stlQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL 599
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370459164 1211 RESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSREnrelLERSLESRDHLHREQR 1275
Cdd:pfam01576 600 EKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARA----LEEALEAKEELERTNK 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1045-1305 |
2.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1045 ELHRKLEVLEEEVRAARQSQEEtrgqqqalLRDHKALAQLQRRQEAELEGllvRHRDLKANMRALELAHRELQGRHEQLQ 1124
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKE--------LEELKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1125 AQRASV-EAQEVALLAERERLMQDGHRQ--RGLEEELRRLQSEHDRAQMLLAELS---RERGELQGERGELRGRLARLEl 1198
Cdd:PRK03918 280 EKVKELkELKEKAEEYIKLSEFYEEYLDelREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELE- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1199 ERAQLEMQSQQLRESNQQL-----DLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLE-------- 1265
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLkkrltGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkc 438
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1370459164 1266 -------SRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLEPV 1305
Cdd:PRK03918 439 pvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1016-1204 |
2.73e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1016 QELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGL 1095
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1096 lvrhrdlkANMRALELAHRELqgrhEQLQAQRASVEAQEVALLAERERlmqdghrqrgLEEELRRLQSEHDRAQmllAEL 1175
Cdd:COG1579 86 --------RNNKEYEALQKEI----ESLKRRISDLEDEILELMERIEE----------LEEELAELEAELAELE---AEL 140
|
170 180
....*....|....*....|....*....
gi 1370459164 1176 SRERGELQGERGELRGRLARLELERAQLE 1204
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELA 169
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
726-1303 |
3.11e-04 |
|
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: 45.73 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 726 EQEALREEVA---QLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV----- 797
Cdd:pfam02463 154 RRLEIEEEAAgsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldylk 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 798 -------------EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERER 864
Cdd:pfam02463 234 lneeridllqellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 865 REKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTR 944
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 945 ALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVErsnaMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQR 1024
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE----EEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1025 aqehSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKA 1104
Cdd:pfam02463 470 ----SEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1105 NMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERE---RLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGE 1181
Cdd:pfam02463 546 STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipkLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1182 LQGERGELRGRLARLELERAQLEMQSQqlreSNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVqALSRENRELLE 1261
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGV----SLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL-AKEEILRRQLE 700
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1370459164 1262 RSLESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1303
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLK 742
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
892-1151 |
3.40e-04 |
|
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: 45.02 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 892 QRELEQAALERQefLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLGPKKRAEpQ 971
Cdd:pfam05667 223 EEEWNSQGLASR--LTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGS-R 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 972 LVETQNVRLIEVERSNAMLVAEKAALQGQLQ-HLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKL 1050
Cdd:pfam05667 300 FTHTEKLQFTNEAPAATSSPPTKVETEEELQqQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1051 EVLEEEVRAARQSQE---ETRGQQQALLRDHKALAQ----LQRRQEAELEGLLVRHRDLK--ANMRALELAHR--ELQGR 1119
Cdd:pfam05667 380 EELEKQYKVKKKTLDllpDAEENIAKLQALVDASAQrlveLAGQWEKHRVPLIEEYRALKeaKSNKEDESQRKleEIKEL 459
|
250 260 270
....*....|....*....|....*....|....*
gi 1370459164 1120 HEQLQ---AQRASVEAQEVALLAERERLMQDGHRQ 1151
Cdd:pfam05667 460 REKIKevaEEAKQKEELYKQLVAEYERLPKDVSRS 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1128-1303 |
3.88e-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: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1128 ASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQS 1207
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1208 QQLRESNQQLdlsacrlttQCELLTQLRSAQEEENRQLLAEVqaLSRENRELLERSLESRDHLHREQREYLDQLNALRRE 1287
Cdd:COG4942 93 AELRAELEAQ---------KEELAELLRALYRLGRQPPLALL--LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170
....*....|....*.
gi 1370459164 1288 KQKLVEKIMDQYRVLE 1303
Cdd:COG4942 162 LAALRAELEAERAELE 177
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
870-1214 |
4.35e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.67 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 870 LQAELEKAVVRGKELGDRLEHLQRELEQAALErqefLREKESQHQRyqgLEQRLEAELQAAATSKEE------ALMELKT 943
Cdd:pfam19220 81 AEGELEELVARLAKLEAALREAEAAKEELRIE----LRDKTAQAEA---LERQLAAETEQNRALEEEnkalreEAQAAEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 944 RALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ 1023
Cdd:pfam19220 154 ALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1024 RAQEhssRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLK 1103
Cdd:pfam19220 234 EAVE---AHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1104 ANMRALELAHRELQGRHEQLQAQRASVEAQevallaererlmqdghrqrgLEEELRRLQSEHDRAQMLLAELSRERGELQ 1183
Cdd:pfam19220 311 QQFQEMQRARAELEERAEMLTKALAAKDAA--------------------LERAEERIASLSDRIAELTKRFEVERAALE 370
|
330 340 350
....*....|....*....|....*....|.
gi 1370459164 1184 GERGELRGRLARLELERAQLEMQSQQLRESN 1214
Cdd:pfam19220 371 QANRRLKEELQRERAERALAQGALEIARESR 401
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
887-1300 |
4.35e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 887 RLEHLQRELEQAALERQEFLREKESQHQRYQGLEQR--LEAELQAAATSKEEALMELKTRALQLEEelFQLRQGPAGLGP 964
Cdd:PRK10246 217 QVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLdeLQQEASRRQQALQQALAAEEKAQPQLAA--LSLAQPARQLRP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 965 ----------KKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQ-----RAQ-EH 1028
Cdd:PRK10246 295 hweriqeqsaALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNelagwRAQfSQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1029 SSRLQAEKSVLEIQGQELHRKLEVL--------EEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAelegllvrhr 1100
Cdd:PRK10246 375 QTSDREQLRQWQQQLTHAEQKLNALpaitltltADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQ---------- 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1101 dlkaNMRALELAHRELQGRHEQLQAQRASV-----EAQEVALLAERERLMQDghrqrgLEEELRRLQS----------EH 1165
Cdd:PRK10246 445 ----LQVAIQNVTQEQTQRNAALNEMRQRYkektqQLADVKTICEQEARIKD------LEAQRAQLQAgqpcplcgstSH 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1166 DRAQMLLAElsrergelqgERGELRGRLARLELERAQLEMQSQQLResnqqldlsacrltTQCELLTQLRSAQEEENRQL 1245
Cdd:PRK10246 515 PAVEAYQAL----------EPGVNQSRLDALEKEVKKLGEEGAALR--------------GQLDALTKQLQRDESEAQSL 570
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459164 1246 LAEVQALSRENRELLER---SLESRDHLH---REQREYLDQLNALrREKQKLVEKIMDQYR 1300
Cdd:PRK10246 571 RQEEQALTQQWQAVCASlniTLQPQDDIQpwlDAQEEHERQLRLL-SQRHELQGQIAAHNQ 630
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1000-1221 |
4.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1000 QLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEetrgQQQALLRDHK 1079
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1080 ALAQLQRRQEAELEGLLVRH--RDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQdghRQRGLEEE 1157
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA---LKAELEAA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1158 LRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSA 1221
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
992-1296 |
5.01e-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: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 992 AEKAALQGQLQHLEGQLGSLQG---RAQELLLQSQRAQEHSSRLQAEKSVLEiqGQELHRKLEVLEEEVRAARQSQEETR 1068
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAqeqQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQEAQAFIQ 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1069 GQQQALlrdhkalaqlqrrqeAELEGLLvrhrdlkANMRALELAHRELQGRHEQLQAQRASVEAQEVALlaerERLMQdg 1148
Cdd:COG3096 914 QHGKAL---------------AQLEPLV-------AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL----SEVVQ-- 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1149 hrqrgleeelRRLQSEHDRAQMLLAELSrergelqgergELRGRLarleleRAQLEMQSQQLRESNQQLDLSACRLTTQC 1228
Cdd:COG3096 966 ----------RRPHFSYEDAVGLLGENS-----------DLNEKL------RARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 1229 ELLTQLRSAQEEENRQLLA---EVQALS-RENRELLERSLESRDHLH------REQREYLD-QLNALRREKQKLVEKIM 1296
Cdd:COG3096 1019 QVLASLKSSRDAKQQTLQEleqELEELGvQADAEAEERARIRRDELHeelsqnRSRRSQLEkQLTRCEAEMDSLQKRLR 1097
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
880-1248 |
5.09e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 880 RGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAElQAAATSKEEALMELKTRALQLEEELFQLRQGP 959
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE-EAARQKLQLEKVTTEAKIKKLEEDILLLEDQN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 960 AGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVL 1039
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1040 EIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKAL-AQLQRRQEaelegllvrhrDLKANMRALELAHRELQG 1118
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELeAQISELQE-----------DLESERAARNKAEKQRRD 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1119 RHEQLQAQRASVE------AQEVALLAERERlmQDGHRQRGLEEELRR----LQSEHDRAQMLLAELSRERGELQGERGE 1188
Cdd:pfam01576 297 LGEELEALKTELEdtldttAAQQELRSKREQ--EVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLEQAKRNKAN 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1189 LRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLtQLRSAQEEENRQLLAE 1248
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQEL-QARLSESERQRAELAE 433
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1109-1221 |
5.80e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.88 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1109 LELAHRELQGRHEQLQAQRASVEAQEVALLAE---RERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAE--LSRErgELQ 1183
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLARLEAElgaEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKgaVSQQ--ELD 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 1370459164 1184 GERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSA 1221
Cdd:COG1566 152 EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQA 189
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
823-1173 |
6.08e-04 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 44.41 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 823 RERRQWEREgsRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALER 902
Cdd:COG3447 291 AERRRQRLR--ERELALRAALELLALGLLLAALDDALLLLNARGLLLLALSLAALLLLRLALLLLLLALDALLLLLADDD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 903 QEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQgpaglgpkkRAEPQLVETQNVRLIE 982
Cdd:COG3447 369 RGELRGDLLRRRGATRLGAVVARLLRRSGGRGEEVVVLLVIAQVEEALELALRER---------REERLLERLALALELL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 983 VERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQ 1062
Cdd:COG3447 440 AITAALLAAALLLALADLLLLLLAEAAQLLARALLLGLDRLLADAALAALAALADLLGALLSAGLRRRGGRRLGARLIRS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1063 SQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERE 1142
Cdd:COG3447 520 LLSRVLAELGAVELLLALIADLTEVALGAEALERLLERLLLALLGLGLAVAALLATLGLLLALLAALALSGAAALLALGA 599
|
330 340 350
....*....|....*....|....*....|.
gi 1370459164 1143 RLMQDGHRQRGLEEELRRLQSEHDRAQMLLA 1173
Cdd:COG3447 600 ALLLAAAILGLAAALLALLRLLGERARLLET 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-958 |
6.20e-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: 43.98 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 719 SLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAVE 798
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 799 AAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEKAV 878
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 879 VRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQG 958
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
259-441 |
6.58e-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: 43.98 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 259 QLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALsgQAKRAELYREEAEALRE--RAGRLPRLQ--- 333
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL--RAELEAQKEELAELLRAlyRLGRQPPLAlll 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 334 ------EELRR-------CRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARL--HETQRENLL--LRT 396
Cdd:COG4942 127 spedflDAVRRlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALeaLKAERQKLLarLEK 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1370459164 397 RLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAP 441
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1143-1304 |
6.64e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1143 RLMQDGHRQRGLEEELRRLQSEhdraqmlLAELSRERGELQGERGELRGRLARLELERAQLEmqsQQLRESNQQL----- 1217
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDE-------LAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLgnvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1218 --DLSAcrLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRREKQKLVEKI 1295
Cdd:COG1579 88 nkEYEA--LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*....
gi 1370459164 1296 MDQYRVLEP 1304
Cdd:COG1579 166 EELAAKIPP 174
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
927-1143 |
7.64e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 927 LQAAATSKEEALMELKTRALQLEEELFQLRQGPAglgpkkRAEPQLVETQNvRLIEVERSNAMLVAEKAALQ----GQLQ 1002
Cdd:PRK11637 52 IQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAIS------QASRKLRETQN-TLNQLNKQIDELNASIAKLEqqqaAQER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1003 HLEGQLGSL--QGRAQ--ELLLQSQRAQEhSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDH 1078
Cdd:PRK11637 125 LLAAQLDAAfrQGEHTglQLILSGEESQR-GERILAYFGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQ 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370459164 1079 KALAQL--QRRQE-----AELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERER 1143
Cdd:PRK11637 204 QAQQQKleQARNErkktlTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQK 275
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
900-1221 |
7.73e-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: 43.96 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 900 LERQEFLREKESQHQRYQGLEQRLEAElqaaatsKEEALMEL-KTRALQLEEELFQL---RQGPAGLGPKKRAEPQLVET 975
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQE-------KEEKAREVeRRRKLEEAEKARQAemdRQAAIYAEQERMAMEREREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 976 QNVRLIEVERSNAMLVAEKAALQ-GQLQHLEgqlgslqgraqELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLE 1054
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEiSRMRELE-----------RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1055 EEVRAARQSQEETRGQQQALLRDHKALA-QLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQAQRASVEAQ 1133
Cdd:pfam17380 420 VEMEQIRAEQEEARQREVRRLEEERAREmERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1134 EvalLAERERLMQDGHRQRGL-------------EEELRRLQSEHDRAQMLLAELSRERGELQgERGELRGRLARLELER 1200
Cdd:pfam17380 500 E---LEERKQAMIEEERKRKLlekemeerqkaiyEEERRREAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMERER 575
|
330 340
....*....|....*....|.
gi 1370459164 1201 aqlEMQSQQLRESNQQLDLSA 1221
Cdd:pfam17380 576 ---EMMRQIVESEKARAEYEA 593
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1027-1298 |
8.72e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.97 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1027 EHSSRLQAEKSVLEIQGQELHRklevLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGllvrhrdLKANM 1106
Cdd:pfam07111 56 EGSQALSQQAELISRQLQELRR----LEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1107 RALELAHREL-QGRHEQLQ-AQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRE----RG 1180
Cdd:pfam07111 125 AGAEMVRKNLeEGSQRELEeIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEaellRK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1181 ELQGERGELRGRLARL--------------------ELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEE 1240
Cdd:pfam07111 205 QLSKTQEELEAQVTLVeslrkyvgeqvppevhsqtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370459164 1241 ENRQLLAEVQAL----SRENRELLERSLES----RDHLHREQREYLDQLNALRREKQKLVEKIMDQ 1298
Cdd:pfam07111 285 ELTRKIQPSDSLepefPKKCRSLLNRWREKvfalMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQ 350
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1066-1258 |
1.48e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 41.43 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1066 ETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQLQaqrasveaqevallaERERLM 1145
Cdd:pfam15619 22 ELQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLIARHNEEVRVLRERLRRLQ---------------EKERDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1146 QDGHRQRglEEELRRLQSEHDRaqmlLAELSRERGelQGERGELRGRLARLELEraqLEMQSQQLRESNQQLDLSACrlT 1225
Cdd:pfam15619 87 ERKLKEK--EAELLRLRDQLKR----LEKLSEDKN--LAEREELQKKLEQLEAK---LEDKDEKIQDLERKLELENK--S 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1370459164 1226 TQCELLTQLRSAQE--EENRQLLAEVQALSRENRE 1258
Cdd:pfam15619 154 FRRQLAAEKKKHKEaqEEVKILQEEIERLQQKLKE 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1121-1293 |
1.73e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1121 EQLQAQRASVEAQEVALLA--ERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLeL 1198
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL-L 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1199 ERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYL 1278
Cdd:COG3206 261 QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLE 340
|
170
....*....|....*
gi 1370459164 1279 DQLNALRREKQKLVE 1293
Cdd:COG3206 341 ARLAELPELEAELRR 355
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
130-504 |
1.89e-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: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 130 EEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSLEVQSELAAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSL 209
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 210 MGTLSKLARERDLGAQRLAELLLEREPLCLRpeapsRAPAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQ 289
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEE-----LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 290 GLEAEIRRLRQEAQALSGQAKRA--ELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASK 367
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALleRLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 368 ALLEEQLEAARERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAP 447
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370459164 448 SLQDEVREAEAGRLRTLERENRELRGLLQVLQGQPGGQHPLLEAPREDPVLPVLEEA 504
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
828-1286 |
1.93e-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: 42.94 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 828 WEREGSRLRAQSEAAEERMQVLESEGRQHLEEAERERREKEALQAELEkAVVRGKELGDRLEHLQRELEQAALERQEFLR 907
Cdd:COG3321 868 FQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAA-AAALALAAAALAALLALVALAAAAAALLALA 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 908 EKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLGPKKRAEPQLVETQNVRLIEVERSN 987
Cdd:COG3321 947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 988 AMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEET 1067
Cdd:COG3321 1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1068 RGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLkANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQD 1147
Cdd:COG3321 1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALA-AAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAAL 1185
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1148 GHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLELERAQLEMQSQQLRESNQQLDLSACRLTTQ 1227
Cdd:COG3321 1186 AAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALL 1265
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 1228 CELLTQLRSAQEEENRQLLAEVQALSRENRELLERSLESRDHLHREQREYLDQLNALRR 1286
Cdd:COG3321 1266 AAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAA 1324
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
891-1303 |
2.03e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 891 LQRELEQAALERQEF--LREKESQHQryQGLEQRLEA---ELQAAATSKEEALMELKTRALQLE----------EELFQL 955
Cdd:pfam15921 115 LQTKLQEMQMERDAMadIRRRESQSQ--EDLRNQLQNtvhELEAAKCLKEDMLEDSNTQIEQLRkmmlshegvlQEIRSI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 956 RQGPAGLGPKKRAEPQLVETQNVRLIEVERSNAM--LVAEKAALQGQLQHLEGQLGSLQGRAQ---ELLLQSQraQEHSS 1030
Cdd:pfam15921 193 LVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILreLDTEISYLKGRIFPVEDQLEALKSESQnkiELLLQQH--QDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1031 RLQAEKSVlEIQGqelhrklevLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLvrhrdlkanmrale 1110
Cdd:pfam15921 271 QLISEHEV-EITG---------LTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTV-------------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1111 lahrelqgrhEQLQAQrasveaqevalLAERERLMQDghRQRGLEEELRRLQSEhdraqmlLAELSRERGELQGERGELR 1190
Cdd:pfam15921 327 ----------SQLRSE-----------LREAKRMYED--KIEELEKQLVLANSE-------LTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1191 GRLARLELERAQLEMQSQQLRESNQQLdlsACRLTTQCELLTQLRSAQEEEN---RQLLAEVQALSRENRELLER---SL 1264
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRL---WDRDTGNSITIDHLRRELDDRNmevQRLEALLKAMKSECQGQMERqmaAI 453
|
410 420 430
....*....|....*....|....*....|....*....
gi 1370459164 1265 ESRDHLHREQREYLDQLNALRREKQKLVEKIMDQYRVLE 1303
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
252-481 |
2.18e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 252 PSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEA-LRERAGRLP 330
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAeLAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 331 RLQEELRRCRERL--QAAEAYKSQLEEERVL----SGVLEASKAL--LEEQLEAARERCARLHETQRENLLLRTRLGEAH 402
Cdd:COG4942 94 ELRAELEAQKEELaeLLRALYRLGRQPPLALllspEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459164 403 AELDSLRHQVDQLAEENVELELELQRSLEpppgspgeaplagaapSLQDEVREAEAgRLRTLERENRELRGLLQVLQGQ 481
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLA----------------RLEKELAELAA-ELAELQQEAEELEALIARLEAE 235
|
|
| HkD_Hook3 |
cd22226 |
Hook domain found in protein Hook 3 (Hook3) and similar proteins; Hook3 is an adaptor protein ... |
89-178 |
2.22e-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: 40.34 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 89 WR--VWNLNHLWGRLRDFYQEEL-QLLILSPPPDLQTLGfdplSEEAVEQLEGVLRLLLGASVQCEHRELFIRHIQGLSL 165
Cdd:cd22226 62 WRlkISNLKKILKGILDYNHEILgQQINDFTLPDVNLIG----EHSDAAELGRMLQLILGCAVNCEQKQEYIQTIMMMEE 137
|
90
....*....|...
gi 1370459164 166 EVQSELAAAIQEV 178
Cdd:cd22226 138 SVQHVVMTAIQEL 150
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
684-1112 |
2.30e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 684 QRLEGTVRdpawqKPQQKSEGALEVQVWEGPIPGESLASgVAEQEALREEVAQLRRKaeaLGDELEAQARKLEAQNTEAA 763
Cdd:pfam15921 429 QRLEALLK-----AMKSECQGQMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLRK---VVEELTAKKMTLESSERTVS 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 764 RLSKELAQARRAEAEAHReaeaqawEQARLREAVEAAGQELESASQErealvealaaaGRERRQWEREGSRLRAQSEAAE 843
Cdd:pfam15921 500 DLTASLQEKERAIEATNA-------EITKLRSRVDLKLQELQHLKNE-----------GDHLRNVQTECEALKLQMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 844 ERMQVLESEGRQHLEEAERERREKEALQaeLEKAvvrgkelgdrleHLQRELEQAALERQEFLREKESQHQRYQGLEQR- 922
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQ--VEKA------------QLEKEINDRRLELQEFKILKDKKDAKIRELEARv 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 923 --LEAE---LQAAATSKEEALMELKTRALQLEEELFQLRQGPAGLgpkkrAEPQLVETQNVR--LIEVERSNAMLVAEKA 995
Cdd:pfam15921 628 sdLELEkvkLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL-----SEDYEVLKRNFRnkSEEMETTTNKLKMQLK 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 996 ALQGQLQHLEGQLGSLQGraqelllQSQRAQEHSSRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALL 1075
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEG-------SDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
410 420 430
....*....|....*....|....*....|....*..
gi 1370459164 1076 RDHKALAQLQRRQEAELEGLLVRHRDLKANMRALELA 1112
Cdd:pfam15921 776 QELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVA 812
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1114-1217 |
2.73e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1114 RELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRL 1193
Cdd:PRK09039 46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
|
90 100
....*....|....*....|....*...
gi 1370459164 1194 ARLELE----RAQLEMQSQQLRESNQQL 1217
Cdd:PRK09039 126 DSEKQVsaraLAQVELLNQQIAALRRQL 153
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
887-1285 |
2.75e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 887 RLEHLQRELEQAAlERQEFLREKESQHQR-YQGLEQRLEAELQAA-ATSKEEALMELKTRALQLEEELFQLRQGPAGLGP 964
Cdd:COG3096 786 RLEELRAERDELA-EQYAKASFDVQKLQRlHQAFSQFVGGHLAVAfAPDPEAELAALRQRRSELERELAQHRAQEQQLRQ 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 965 KKRAEPQLVETQNvRLIeverSNAMLVAEkAALQGQLQHLEGQLGSLQGRAQELllqsQRAQEHSSRLQAEKSVLEIQGQ 1044
Cdd:COG3096 865 QLDQLKEQLQLLN-KLL----PQANLLAD-ETLADRLEELREELDAAQEAQAFI----QQHGKALAQLEPLVAVLQSDPE 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1045 ELhrklEVLEEEVRAARQSQEETRgqQQALlrdhkALAQLQRRQEA----ELEGLLVRHRD----LKANMRALELAHREL 1116
Cdd:COG3096 935 QF----EQLQADYLQAKEQQRRLK--QQIF-----ALSEVVQRRPHfsyeDAVGLLGENSDlnekLRARLEQAEEARREA 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1117 QGRHEQLQAQRASVEaQEVALLAERERLMQDGHRQrgLEEELRRL---------QSEHDRAQMLLAELSRERGElqgeRG 1187
Cdd:COG3096 1004 REQLRQAQAQYSQYN-QVLASLKSSRDAKQQTLQE--LEQELEELgvqadaeaeERARIRRDELHEELSQNRSR----RS 1076
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1188 ELRGRLARLELERAQLEmqsQQLRESNQqlDLSACRlttqcellTQLRSAQEEENRqllaeVQALSRENRelLERSLESR 1267
Cdd:COG3096 1077 QLEKQLTRCEAEMDSLQ---KRLRKAER--DYKQER--------EQVVQAKAGWCA-----VLRLARDND--VERRLHRR 1136
|
410 420
....*....|....*....|..
gi 1370459164 1268 DHLH---REQREYLDQ-LNALR 1285
Cdd:COG3096 1137 ELAYlsaDELRSMSDKaLGALR 1158
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
896-1255 |
2.85e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 896 EQAALERQEFLREKESQHQRYQGLEQRLEAELQAA----ATSKEEALMELKTRALQLEEELFQLRQGPAGLgpkkraepq 971
Cdd:pfam15964 345 EEANFEKTKALIQCEQLKSELERQKERLEKELASQqekrAQEKEALRKEMKKEREELGATMLALSQNVAQL--------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 972 lvETQnvrLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSV-----LEIQGQEL 1046
Cdd:pfam15964 416 --EAQ---VEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTktgrqLEIKDQEI 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1047 HR-KLEVLEEEVRAARQSQEETRGQQQALlrdhkALAQLQRRQEAELEglLVR------HRDLKANMRALELA----HRE 1115
Cdd:pfam15964 491 EKlGLELSESKQRLEQAQQDAARAREECL-----KLTELLGESEHQLH--LTRlekesiQQSFSNEAKAQALQaqqrEQE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1116 LQGRHEQLQAQRASVEAQEVALLAERERLMqdghrqRGLEEEL----RRLQSEHDRAQMLLAELSRERGELQGERGELRG 1191
Cdd:pfam15964 564 LTQKMQQMEAQHDKTVNEQYSLLTSQNTFI------AKLKEECctlaKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQK 637
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370459164 1192 RLARLELERAQLEMQSQQLRESNQQLDlSACRLTTQceLLTQLRSAQeeenRQLLAEVQALSRE 1255
Cdd:pfam15964 638 RNEELEEQCVQHGRMHERMKQRLRQLD-KHCQATAQ--QLVQLLSKQ----NQLFKERQNLTEE 694
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
888-1217 |
3.07e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 888 LEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEaELQAAA----TSKEE--ALMELKTRALQLEEELFQLRQGPAG 961
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNE-ELTSLAeeaqALKDEmdILRESSDKVKKLEATVETYKKKLED 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 962 LGPKKRAEPQLVET------QNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAE 1035
Cdd:pfam05622 147 LGDLRRQVKLLEERnaeymqRTLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1036 KsvleiqgqelhrklEVLEEEVRAARQSQEETRgqqqallrdhkaLAQLQRRQEAELEGLLVRHRDLKANMRAlELAHRE 1115
Cdd:pfam05622 227 K--------------ERLIIERDTLRETNEELR------------CAQLQQAELSQADALLSPSSDPGDNLAA-EIMPAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1116 LQGRHEQLQAQ----RASVEAQEVALLAERERLMQDGHRQR-GLEEELRRlqsehdrAQMLLAELSRERGELQGERGELR 1190
Cdd:pfam05622 280 IREKLIRLQHEnkmlRLGQEGSYRERLTELQQLLEDANRRKnELETQNRL-------ANQRILELQQQVEELQKALQEQG 352
|
330 340
....*....|....*....|....*..
gi 1370459164 1191 GRLARLELERAQLEMQSQQLRESNQQL 1217
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSEL 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
965-1302 |
3.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 965 KKRAEPQLVETQNV--RLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELllqsqraQEHSSRLQAeksvLEIQ 1042
Cdd:PRK03918 178 IERLEKFIKRTENIeeLIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-------EELKEEIEE----LEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1043 GQELHRKLEVLEEEVRAARQSQEETRGQQQALlrdhkalaQLQRRQEAELEGLLVRHRDLKANMRALELAHRELQGRHEQ 1122
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEEL--------EEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1123 LQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEH---DRAQMLLAELSRERGELQG-ERGELRGRLARLEL 1198
Cdd:PRK03918 319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELERLKKRLTGlTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1199 ERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEvqalsrENRELLERSLESRDHLHREQREYL 1278
Cdd:PRK03918 399 AKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE------HRKELLEEYTAELKRIEKELKEIE 472
|
330 340
....*....|....*....|....
gi 1370459164 1279 DQLNALRREKQKLVEKIMDQYRVL 1302
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELI 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1049-1281 |
3.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1049 KLEVLEEEVRAARQSQEETRGQQQALLRDHKAlaQLQRRQEAELEGLLvrhrdlkanmRALELAHRELQGRHEQLQAQRA 1128
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKA--QIEEKEEKDLHERL----------NGLESELAELDEEIERYEEQRE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1129 SVEAQEvallaERERLMQDGHRQRglEEELRRLQSEHDRAQMLLAELSRERGELQGERGELRGRLARLE----------- 1197
Cdd:PRK02224 231 QARETR-----DEADEVLEEHEER--REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaeag 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1198 ----------LERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRSAQEEENRQLlaevqalsRENRELLERSLESR 1267
Cdd:PRK02224 304 lddadaeaveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL--------REEAAELESELEEA 375
|
250
....*....|....
gi 1370459164 1268 DHLHREQREYLDQL 1281
Cdd:PRK02224 376 REAVEDRREEIEEL 389
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1111-1275 |
4.16e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1111 LAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDGHRQRGLEEELRRLQSEHDRAQMLLAelsrERGELQGERGElr 1190
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLV----QKEEQLDARAE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1191 grlaRLELERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTQLRsaQEEENRQLLAEVQALSRENRELLERSLESRDHL 1270
Cdd:PRK12705 99 ----KLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT--PEQARKLLLKLLDAELEEEKAQRVKKIEEEADL 172
|
....*
gi 1370459164 1271 HREQR 1275
Cdd:PRK12705 173 EAERK 177
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
887-958 |
4.72e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 4.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370459164 887 RLEHLQRELEQAALERQEFLREKESQHQRYQ----GLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQG 958
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEekkeKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
283-377 |
5.12e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 283 DSQAEVQGLEAEIRRLRQE----AQALSGQAKRAELYREEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERV 358
Cdd:PRK11448 139 DPENLLHALQQEVLTLKQQlelqAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKR 218
|
90 100
....*....|....*....|....*....
gi 1370459164 359 LSGVLEASK----------ALLEEQLEAA 377
Cdd:PRK11448 219 KEITDQAAKrlelseeetrILIDQQLRKA 247
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1044-1258 |
5.41e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.82 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1044 QELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQ-------LQRRQEAELEGLLVRHRDLKANMRALE----LA 1112
Cdd:pfam19220 51 LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVArlakleaALREAEAAKEELRIELRDKTAQAEALErqlaAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1113 HRELQGRHEQLQAQRASVEAQEvALLAERERLMQDGHRQRGL-EEELRRLQSEHDRAQMLLAELSRERGELQGERGELRG 1191
Cdd:pfam19220 131 TEQNRALEEENKALREEAQAAE-KALQRAEGELATARERLALlEQENRRLQALSEEQAAELAELTRRLAELETQLDATRA 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459164 1192 RLARLEL----ERAQLEMQSQQLRESNQQLDLSACRLTTQCELLTqlrsAQEEENRQLLAEVQALSRENRE 1258
Cdd:pfam19220 210 RLRALEGqlaaEQAERERAEAQLEEAVEAHRAERASLRMKLEALT----ARAAATEQLLAEARNQLRDRDE 276
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
172-571 |
6.01e-03 |
|
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: 41.38 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 172 AAAIQEVTQPGAGVVLALSGPDPGELAPAELEMLSRSL----MGTLSKLARERDLGAQRLAELLLEREPLCLRPEAPSRA 247
Cdd:COG1020 901 AVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALllppYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAA 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 248 PAEGPSHHLALQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLR------------QEAQALSGQAKRAELY 315
Cdd:COG1020 981 APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLlllllllflaaaAAAAAAAAAAAAAAAA 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 316 REEAEALRERAGRLPRLQEELRRCRERLQAAEAYKSQLEEERVLSGVLEASKALLEEQLEAARERCARLHETQRENLLLR 395
Cdd:COG1020 1061 APLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRL 1140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 396 TRLGEAHAELDSLRHQVDQLAEENVELELELQRSLEPPPGSPGEAPLAGAAPSLQDEVREAEAGRLRTLERENRELRGLL 475
Cdd:COG1020 1141 LVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 476 QVLQGQPGGQHPLLEAPREDPVLPVLEEAPQTPVAFDHSPQGLVQKARDGGPQALDLAPPALDSVLEASAECPQAPDSDP 555
Cdd:COG1020 1221 LLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLL 1300
|
410
....*....|....*.
gi 1370459164 556 QEAESPLQAAAMDPQA 571
Cdd:COG1020 1301 LALLLLLALALALLLL 1316
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
881-1260 |
6.61e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 881 GKELGDRLEHLQRELEQAALERQEfLREKESQHQRYQGLEQrleaeLQAAATSKEEALMELKTRALQLEEELFQLRQGPa 960
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRL-LNQEKTELLVEQGRLQ-----LQADRHQEHIRARDSLIQSLATRLELDGFERGP- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 961 glgpkkraepqlvetqnvrLIEVERSNAMLVaekaalqgQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKSVLe 1040
Cdd:TIGR00606 387 -------------------FSERQIKNFHTL--------VIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGL- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1041 iqGQELHRKLEVLEEEVRAAR----QSQEETRGQQQALLRDH---KALAQLQRRQE-AELEGLLVRHRDLKANMRALELA 1112
Cdd:TIGR00606 439 --GRTIELKKEILEKKQEELKfvikELQQLEGSSDRILELDQelrKAERELSKAEKnSLTETLKKEVKSLQNEKADLDRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1113 HRELQGRHEQLQAQRASVEAQEvalLAERERLMQDghrqrgleEELRRLQSEHDRAQMLLA-------ELSRERGELQGE 1185
Cdd:TIGR00606 517 LRKLDQEMEQLNHHTTTRTQME---MLTKDKMDKD--------EQIRKIKSRHSDELTSLLgyfpnkkQLEDWLHSKSKE 585
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370459164 1186 RGELRGRLARLELERAQLEMQSQQLResNQQLDLSACRLTTQCELLTQLRSAQEEENRQLLAEVQALSRENRELL 1260
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLEQNKNHIN--NELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAML 658
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
283-409 |
6.62e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 283 DSQAEVQGLEAEIR-RLRQEAQALSGQAKRAELYREEAEALRERAgrlprlqEELRrcrerlQAAEAYKSQLEEERVLSG 361
Cdd:PRK02224 314 ARREELEDRDEELRdRLEECRVAAQAHNEEAESLREDADDLEERA-------EELR------EEAAELESELEEAREAVE 380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1370459164 362 VLEASKALLEEQLEAARERCARLhETQRENL-----LLRTRLGEAHAELDSLR 409
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDA-PVDLGNAedfleELREERDELREREAELE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
298-964 |
6.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 298 LRQEAQALSGQAKRAELYREeaealreragrlprLQEELRRCRERLQAAEaYKSQLEEERVLSGVLEASKALLEEQLEAA 377
Cdd:COG1196 198 LERQLEPLERQAEKAERYRE--------------LKEELKELEAELLLLK-LRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 378 RERCARLHETQRENLLLRTRLGEAHAELDSLRHQVDQLAEENVELELELQRslepppgspgeapLAGAAPSLQDEVREAE 457
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-------------LEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 458 AgRLRTLERENRELRGLLQVLQGQpggqhplleapredpvlpvLEEApqtpvafdhspqglvQKARDGGPQALDLAPPAL 537
Cdd:COG1196 330 E-ELEELEEELEELEEELEEAEEE-------------------LEEA---------------EAELAEAEEALLEAEAEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 538 DSVLEASAECPQApDSDPQEAESPLQAAAMDPQASDWSPQESGSPVETQESPEKAGRRSSLQSPASVAPPQgpGTKIQAP 617
Cdd:COG1196 375 AEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL--EEAAEEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 618 QLLGGETEGREAPQGELVPEAWGLRQEGpehkpgpsepssVQLEEQEGPNQGLDLATGQAEAREHDQRLEGTVRDPAWQK 697
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAAL------------AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 698 PQQKSEGALEVQVWEGPIPGESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEA 777
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 778 EAHREAEAQAWEQARLREAVEAAGQELESASQEREALVEALAAAGRERRQwEREGSRLRAQSEAAEERMQVLESEGRQHL 857
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV-TLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 858 EEAERERREKEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEA 937
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
650 660
....*....|....*....|....*..
gi 1370459164 938 LMELKtralQLEEELFQLRQGPAGLGP 964
Cdd:COG1196 759 PPDLE----ELERELERLEREIEALGP 781
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
720-1297 |
6.78e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 720 LASGVAEQEALREEVA-QLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREA-- 796
Cdd:TIGR00606 413 LCADLQSKERLKQEQAdEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAek 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 797 ---VEAAGQELESASQEREALVEALAAAGRERRQWEREgSRLRAQSEA-------AEERMQVLESEGRQHLEEAERERRE 866
Cdd:TIGR00606 493 nslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMltkdkmdKDEQIRKIKSRHSDELTSLLGYFPN 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 867 KEALQAELEKAVVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLeaeLQAAATSKEEALMElktral 946
Cdd:TIGR00606 572 KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVCGSQDEESDLE------ 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 947 QLEEELFQLRQGPAGLGPKKRAEPQLVEtqnvRLIEVERSNAMLVAEKAALQGQLQHLEGQLgslqgraQELLLQSQRAQ 1026
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGATAVYSQFIT----QLTDENQSCCPVCQRVFQTEAELQEFISDL-------QSKLRLAPDKL 711
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1027 EhssRLQAEKSVLEIQGQELHRKLEVLEEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEGLLVRHRDLK--- 1103
Cdd:TIGR00606 712 K---STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcl 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1104 ---ANMRALELAHRELQGRHEQLQAQRASVEAQEVALLAERERLMQDghrqrgleEELRRLQSEHDRAQMLLAELSRERG 1180
Cdd:TIGR00606 789 tdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ--------HELDTVVSKIELNRKLIQDQQEQIQ 860
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1181 ELQGERGELRGrlarlelERAQLEMQSQQlresnqqldlsacrlttqcelltqlRSAQEEENRQLLAEVQALSRENRELL 1260
Cdd:TIGR00606 861 HLKSKTNELKS-------EKLQIGTNLQR-------------------------RQQFEEQLVELSTEVQSLIREIKDAK 908
|
570 580 590
....*....|....*....|....*....|....*..
gi 1370459164 1261 ERSLESRDHLHREQREYLDQLNALRREKQKLVEKIMD 1297
Cdd:TIGR00606 909 EQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
258-414 |
7.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 258 LQLANAKAQLRRLRQELEEKAELLLDSQAEVQGLEAEIRRLRQEAQALSGQAKRAELYREEAEALRERA-GRLPRL--QE 334
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeEQLGNVrnNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 335 ELRRCRERLQAAEAYKSQLEEE-RVLSGVLEASKALLEEQLEAARERCARLHETQREnllLRTRLGEAHAELDSLRHQVD 413
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAERE 166
|
.
gi 1370459164 414 Q 414
Cdd:COG1579 167 E 167
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
872-1255 |
7.77e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 40.94 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 872 AELEKAVVRGKELG----DRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAatskeEALMELKTRALQ 947
Cdd:PRK10246 533 DALEKEVKKLGEEGaalrGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQ-----DDIQPWLDAQEE 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 948 LEEELFQLRQgpaglgpKKRAEPQLVETQNvrliEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQE 1027
Cdd:PRK10246 608 HERQLRLLSQ-------RHELQGQIAAHNQ----QIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQS 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1028 HSSRlQAEKSVLEIQGQELHRKLEVL----EEEVRAARQSQEETRGQQQALLRDHKALAQLQRRQEAELEgllvrhrdlk 1103
Cdd:PRK10246 677 WQQR-QNELTALQNRIQQLTPLLETLpqsdDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQ---------- 745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1104 anmralelahrelqgRHEQLQAQ-----RASVEAQEVALLAErerLMQDGHRQRgLEEELRRLQSEHDRAQMLLAELSRE 1178
Cdd:PRK10246 746 ---------------RLQKAQAQfdtalQASVFDDQQAFLAA---LLDEETLTQ-LEQLKQNLENQRQQAQTLVTQTAQA 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1179 RGELQGERGELRGRLARLELERAQLEMQSQQLRESNqqldlsacrlTTQCELLTQLRsaQEEENRQ----LLAEVQALSR 1254
Cdd:PRK10246 807 LAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENT----------TRQGEIRQQLK--QDADNRQqqqaLMQQIAQATQ 874
|
.
gi 1370459164 1255 E 1255
Cdd:PRK10246 875 Q 875
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
718-1058 |
7.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 718 ESLASGVAEQEALREEVAQLRRKAEALGDELEAQARKLEAQNTEAARLSKELAQARRAEAEAHREAEAQAWEQARLREAV 797
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 798 EAAGQELESASQEREALVEALAAAGRERRQWEREGSRLRAQSEAAEERMQVLESEGRQhlEEAERERREKEALQAELEKA 877
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA--LEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 878 VVRGKELGDRLEHLQRELEQAALERQEFLREKESQHQRYQGLEQRLEAELQAAATSKEEALMELKTRALQLEEELFQLRQ 957
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 958 GPAGLGPKKRAEPQLVETQNVRLIEVERSNAMLVAEKAALQGQLQHLEGQLGSLQGRAQELLLQSQRAQEHSSRLQAEKS 1037
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|.
gi 1370459164 1038 VLEIQGQELHRKLEVLEEEVR 1058
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVAD 369
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1074-1172 |
9.42e-03 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 40.37 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459164 1074 LLRDHKAL--AQLQRR-QEAELEGLLvrhrdlkanmrALELAHRELQGRHEQLQAQRASVeAQEVALL----AERERLMQ 1146
Cdd:COG0172 6 LIRENPEAvkEALAKRgFDLDVDELL-----------ELDEERRELQTEVEELRAERNAL-SKEIGKAkkkgEEAEALIA 73
|
90 100 110
....*....|....*....|....*....|
gi 1370459164 1147 D----GHRQRGLEEELRRLQSEHDRAQMLL 1172
Cdd:COG0172 74 EvkelKEEIKELEEELKELEEELDELLLSI 103
|
|
| |
