|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-776 |
4.56e-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: 71.24 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 130 SQLLHNSSASELDVAEDLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEF---EKGEAIRQSLEYALAIAKKDARL 206
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVselEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 207 TVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDIlrthkdeyELLLKERGELESIL 286
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL--------EELEAELEELESRL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 287 QKQNSALQNLSKKMKDMELEhrdcsdlltrqvhkLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAhlKSKFNLEIT 366
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQ--------------IASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 367 QMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENA---YEREKQKAQENLEKVNRLEREYISTNK------------ 431
Cdd:TIGR02168 439 QAELEELEEELEELQEELERLEEALEELREELEEAEQAldaAERELAQLQARLDSLERLQENLEGFSEgvkallknqsgl 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 432 ---------QMNEKIEEKKEIIKDLSERLQ----ENEKIHRELQDKLATAKKHQVFVtetyennmielkLLLDSFAMSGQ 498
Cdd:TIGR02168 519 sgilgvlseLISVDEGYEAAIEAALGGRLQavvvENLNAAKKAIAFLKQNELGRVTF------------LPLDSIKGTEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 499 RTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLE------------DTSNELKK--------------------------- 539
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELAKklrpgyrivtldgdlvrpggvitggsa 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 540 ---MNALC-----ENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEK 611
Cdd:TIGR02168 667 ktnSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 612 VRAAESENEIQKLTraykKDMEEKLTFLHGLYQHLVAGCVLIKQPEGILDRFS-----WSELCAVLQENVDALILDLNRA 686
Cdd:TIGR02168 747 ERIAQLSKELTELE----AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKeelkaLREALDELRAELTLLNEEAANL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 687 NEKISHLEYICKSKSDTMKELQRSQED---DMSKMAEQM-KAQESC---------WQKQKKYLEQQYSDLLGEVHARAQE 753
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIeELEELIeeleseleaLLNERASLEEALALLRSELEELSEE 902
|
730 740
....*....|....*....|...
gi 2201826906 754 YKETAEKNKEKICVLEKRQEELA 776
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLA 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
145-469 |
3.81e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 145 EDLKRKLCQAKE--EKVDIIIKhnqELRDyeiQIVKLRSEFEKGE---AIRQSLE----YALAIAKKDARLTVRTVEEEL 215
Cdd:TIGR02169 173 EKALEELEEVEEniERLDLIID---EKRQ---QLERLRREREKAEryqALLKEKReyegYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 216 SDARNKLAELQVFNEKLQQRLVETEktfhiaqqkwkeqqQRLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQN 295
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIE--------------QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 296 LSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIK--------------QLEENFEAERAAHLKSKF 361
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAelkeeledlraeleEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 362 NLEITQMRIRELEGA---LQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKvnrLEREYISTNKQMNEKIE 438
Cdd:TIGR02169 393 KLEKLKREINELKREldrLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK---QEWKLEQLAADLSKYEQ 469
|
330 340 350
....*....|....*....|....*....|.
gi 2201826906 439 EKKEIIKDLSERLQENEKIHRELQDKLATAK 469
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
142-778 |
9.92e-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: 63.54 E-value: 9.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 142 DVAEDLKRKL--CQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEY-ALAIAKKDARLTVRTVEEELSDA 218
Cdd:TIGR02168 193 DILNELERQLksLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELkEAEEELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 219 RNKLAELQVFNEKLQQRL---------VETEKTFHIAQQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESILQKQ 289
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 290 ----NSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLE---ENFEAERAAHLKSKFN 362
Cdd:TIGR02168 353 leslEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrERLQQEIEELLKKLEE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 363 LEI--TQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENA---YEREKQKAQENLEKVNRLEREYISTNK------ 431
Cdd:TIGR02168 433 AELkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQAldaAERELAQLQARLDSLERLQENLEGFSEgvkall 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 432 ---------------QMNEKIEEKKEIIKDLSERLQ----ENEKIHRELQDKLATAKKHQVFVtetyennmielkLLLDS 492
Cdd:TIGR02168 513 knqsglsgilgvlseLISVDEGYEAAIEAALGGRLQavvvENLNAAKKAIAFLKQNELGRVTF------------LPLDS 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 493 FAMSGQRTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLE------------DTSNEL-KKMNALCENTTKELEISRdKMC 559
Cdd:TIGR02168 581 IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDNALELaKKLRPGYRIVTLDGDLVR-PGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 560 VLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQnvqqrweeekvRAAESENEIQKLTRAYKKDMEEKLTFL 639
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALA-----------ELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 640 HGLYQHLVAGCVLIKQpegildrfsWSELCAVLQENVDALILDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMskma 719
Cdd:TIGR02168 729 SALRKDLARLEAEVEQ---------LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK---- 795
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201826906 720 EQMKAQEScwqkQKKYLEQQYSDLLGEVHA---RAQEYKETAEKNKEKICVLEKRQEELALE 778
Cdd:TIGR02168 796 EELKALRE----ALDELRAELTLLNEEAANlreRLESLERRIAATERRLEDLEEQIEELSED 853
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
212-472 |
1.15e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 212 EEELSDARNKLAELQ-VFNEkLQQRL------VETEKTFHIAQQKWKEQQQRLASEKDDILRthkDEYELLLKERGELES 284
Cdd:COG1196 178 ERKLEATEENLERLEdILGE-LERQLeplerqAEKAERYRELKEELKELEAELLLLKLRELE---AELEELEAELEELEA 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 285 ILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLE 364
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 365 ITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEII 444
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250 260
....*....|....*....|....*...
gi 2201826906 445 KDLSERLQENEKIHRELQDKLATAKKHQ 472
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEE 441
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
523-1221 |
2.43e-09 |
|
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: 62.00 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 523 LTAYQNKLEDTSNELKKMNALCENTTKELEisrdkmcVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQN 602
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 603 VQQRWEEEKVRAAESENEIQKLTRAyKKDMEEKLTflhglyqhlvagcvlikqpegildrfSWSELCAVLQENVDALILD 682
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESK-LDELAEELA--------------------------ELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 683 LNRANEKISHLEyickSKSDTMKELQRSQEDDMSKMAEQMKAQescwQKQKKYLEQQYSDLlgevharaqeyKETAEKNK 762
Cdd:TIGR02168 360 LEELEAELEELE----SRLEELEEQLETLRSKVAQLELQIASL----NNEIERLEARLERL-----------EDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 763 EKICVLEKRQEELALENlyVKNTLTQIQKEHSSLLAACALLAGALYPLYGRSCAMSIQRDLLQDQVNiyeLVNQEIRTLV 842
Cdd:TIGR02168 421 QEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA---QLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 843 HILSGVEEEKEDDAKIKKHKFRG---------LIHV---FRRGVIAVLAANRLKVLAQSSSSLFSLINGFKE--GIGILV 908
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVdegYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQneLGRVTF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 909 CVGDSKgKHNMSRYNKEgircvEALNWFTSP-DLLTAVISSVTELQDVISKtdpkscLSGRLLVS---AARNSFSKLMDK 984
Cdd:TIGR02168 576 LPLDSI-KGTEIQGNDR-----EILKNIEGFlGVAKDLVKFDPKLRKALSY------LLGGVLVVddlDNALELAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 985 LNVImesVPLDSsrsvtyveknsliqrlahglHRINARALEAGSCDRRpiMKSIASLQKQIAEFTQRLHTVEVERCSLRR 1064
Cdd:TIGR02168 644 GYRI---VTLDG--------------------DLVRPGGVITGGSAKT--NSSILERRREIEELEEKIEELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1065 ELAEFKLNFSKMKQEADKAQSLKE----QLSLFKQSKLIAHKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLE 1140
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1141 LHSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVE 1220
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
.
gi 2201826906 1221 A 1221
Cdd:TIGR02168 859 A 859
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-492 |
2.98e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 149 RKLCQAKE--EKVDIIIkhnQELRDyeiQIVKLRSEFEKgeAiRQSLEYALAIAKKDARLTV---RTVEEELSDARNKLA 223
Cdd:COG1196 179 RKLEATEEnlERLEDIL---GELER---QLEPLERQAEK--A-ERYRELKEELKELEAELLLlklRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 224 ELQVFNEKLQQRLVETEKtfhiaqqKWKEQQQRLASEKDDILRTHKDEYELLlKERGELESILQKQNSALQNLSKKMKDM 303
Cdd:COG1196 250 ELEAELEELEAELAELEA-------ELEELRLELEELELELEEAQAEEYELL-AELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 304 ElehrdcsdlltrqvhkleysaEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVS 383
Cdd:COG1196 322 E---------------------EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 384 QAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQd 463
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE- 459
|
330 340
....*....|....*....|....*....
gi 2201826906 464 KLATAKKHQVFVTETYENNMIELKLLLDS 492
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
196-425 |
4.98e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 196 ALAIAKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRThKDEYELL 275
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-EKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 276 LKERGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAA 355
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 356 hlkskfnLEITQMRIRELEGALQMEKVSQAEALSDLEmirKEFKEVENAYEREKQKAQENLEKVNRLERE 425
Cdd:COG4942 176 -------LEALLAELEEERAALEALKAERQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-466 |
6.17e-09 |
|
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: 60.84 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 162 IIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLE---YALAIAKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVE 238
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 239 TEKTFHIAQQKWKEQQQRLASEKDDILRthkdeyelLLKERGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQV 318
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAE--------AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 319 HKLEysaeqeeRLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEF 398
Cdd:TIGR02168 824 ERLE-------SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201826906 399 KEVEnayerekQKAQENLEKVNRLEREYISTNKQMNekieekkeiikDLSERLQENEKIHRELQDKLA 466
Cdd:TIGR02168 897 EELS-------EELRELESKRSELRRELEELREKLA-----------QLELRLEGLEVRIDNLQERLS 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-423 |
6.40e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 131 QLLHNSSASELDVAEDLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFekgEAIRQSLEyalaiakkDARLTVRT 210
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL---EELELELE--------EAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 211 VEEELSDARNKLAELQVFNEKLQQRLVETEKtfhiAQQKWKEQQQRLASEKDDIlrthKDEYELLLKERGELESILQKQN 290
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEEL----EEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 291 SALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRI 370
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2201826906 371 RELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLE 423
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
271-627 |
1.13e-08 |
|
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: 60.07 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 271 EYELLLKERGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFE 350
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 351 AERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTN 430
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 431 KQMNekieEKKEIIKDLSERLQENEKIHRELQDKLATAKKhqvfvtetyennmiELKLLLDSFAMSGQRtagtckdkdkp 510
Cdd:TIGR02168 838 RRLE----DLEEQIEELSEDIESLAAEIEELEELIEELES--------------ELEALLNERASLEEA----------- 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 511 sslsvLETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANAnkelnhlhtecadka 590
Cdd:TIGR02168 889 -----LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE--------------- 948
|
330 340 350
....*....|....*....|....*....|....*..
gi 2201826906 591 aligtLQMELQNVQQRWEEEKVRAAESENEIQKLTRA 627
Cdd:TIGR02168 949 -----YSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
119-780 |
1.82e-08 |
|
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: 59.30 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 119 EAKRLCSAKSGSQLLHNSSASELDVAE---DLKRKLCQAKEEKVDIIIK----HNQELRDYEIQIVKLRSEFEKGEaiRQ 191
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLE--RQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 192 SLEYALAIAKKDARLTvrTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRTHKDE 271
Cdd:TIGR02168 318 LEELEAQLEELESKLD--ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 272 yELLLKERGELESILQKQNSALQNLSK-----KMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLE 346
Cdd:TIGR02168 396 -ASLNNEIERLEARLERLEDRRERLQQeieelLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 347 ENFEAERAAHLKSKFNLEITQMRIRELEGALQMEK--VSQAEALSDLEMIRKEFKEVENAYEREKQKA-QENLEK--VNR 421
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSGILGVLSELISVDEGYEAAIEAAlGGRLQAvvVEN 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 422 LE--REYISTNKQMNE--------KIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQ---------VFVTETYENN 482
Cdd:TIGR02168 555 LNaaKKAIAFLKQNELgrvtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggVLVVDDLDNA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 483 MIELKLLL----------DSFAMSGQRTAGTCKDKDKPSSLSV-LETLRYTLTAYQNKLEDTSNELKKMNALCENTTKEL 551
Cdd:TIGR02168 635 LELAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 552 EISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKKD 631
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 632 MEE-------------KLTFLHGLYQHLVAGCVLIKQpegilDRFSWSELCAVLQENVDALILDLNRANEKISHLEYICK 698
Cdd:TIGR02168 795 KEElkalrealdelraELTLLNEEAANLRERLESLER-----RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 699 SKSDTMKELQ----------RSQEDDMSKMAEQMKAQESCWQKQKKYLEQ----------------------------QY 740
Cdd:TIGR02168 870 ELESELEALLnerasleealALLRSELEELSEELRELESKRSELRRELEElreklaqlelrleglevridnlqerlseEY 949
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 2201826906 741 SDLLGEVHARAQEYKETAEKNKEKICVLEKRQEELALENL 780
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-635 |
2.73e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 145 EDLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEyALAIAKKDARLTVRTVEEELSDARNKLAE 224
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 225 ---------------------------LQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRL--ASEKDDILRTHKDEYELL 275
Cdd:PRK03918 271 lkkeieeleekvkelkelkekaeeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeLEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 276 LKERGELESILQKQNSA------LQNLSKKMKDMELEhrdcsdlltRQVHKLEYSAEQEERLKKELEAATDRIKQLEENF 349
Cdd:PRK03918 351 EKRLEELEERHELYEEAkakkeeLERLKKRLTGLTPE---------KLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 350 EAERAAHLKSKFNLEITQMRIRELEGalQMEKVSQAEALSDLEMIRKEFKEVENAyEREKQKAQENLEKVNRLEREYIST 429
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 430 NKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQVFVT------ETYENNMIELKLLLDSFAMSGQRTAGT 503
Cdd:PRK03918 499 KELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKkeleklEELKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 504 CKDKDKPSSLSVLETLRYTLTAYQ--NKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNh 581
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS- 657
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2201826906 582 lHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLtRAYKKDMEEK 635
Cdd:PRK03918 658 -EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-KEELEEREKA 709
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
548-1229 |
8.63e-08 |
|
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: 56.99 E-value: 8.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 548 TKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLtRA 627
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-RE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 628 YKKDMEEKLTFLHGLYQHLVAgcvliKQPEGILDRFSWSELCAVLQENVDALILDLNRANEKISHLEyickSKSDTMKEL 707
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELES-----KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE----SRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 708 QRSQEDDMSKMAEQMKAQescwQKQKKYLEQQYSDLlgevharaqeyKETAEKNKEKICVLEKRQEELALENlyVKNTLT 787
Cdd:TIGR02168 381 LETLRSKVAQLELQIASL----NNEIERLEARLERL-----------EDRRERLQQEIEELLKKLEEAELKE--LQAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 788 QIQKEHSSLLAACALLAGALYPLYGRSCAMSIQRDLLQDQVNiyeLVNQEIRTLVHILSGVEEEKEDDAKIKKHKFRG-- 865
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA---QLQARLDSLERLQENLEGFSEGVKALLKNQSGLsg 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 866 -------LIHV---FRRGVIAVLAANRLKVLAQSSSSLFSLINGFKE--GIGILVCVGDS------KGKHNMSRYNKEGI 927
Cdd:TIGR02168 521 ilgvlseLISVdegYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQneLGRVTFLPLDSikgteiQGNDREILKNIEGF 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 928 RCVeALNWFTSPDLLTAVISSVteLQDVISKTDPKSCLSGRLLVSAARNSFSKLMDKLNVIMESVPLDSSRSVTYVEKNS 1007
Cdd:TIGR02168 601 LGV-AKDLVKFDPKLRKALSYL--LGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1008 LIQRLAHGLHRINARALEagscdrrpIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLK 1087
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAE--------LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1088 EQLSLFKQSKLIAHKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLEL-HSSEEADKNQV---LSETVKRLSEA 1163
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaLDELRAELTLLneeAANLRERLESL 829
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201826906 1164 KMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQ 1229
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
211-784 |
1.23e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 211 VEEELSDARNKLAELQVFNEKLqqrlVETEKTFHIAQQKWKEQQQRLASE-------KDDILRTHKDEYELLLKERGELE 283
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAM----ADIRRRESQSQEDLRNQLQNTVHEleaakclKEDMLEDSNTQIEQLRKMMLSHE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 284 SILQKQNSALQNLSKKMKDMELEHRDCSDL--------LTRQVHKLEYS-----------AEQEERLKKE--------LE 336
Cdd:pfam15921 184 GVLQEIRSILVDFEEASGKKIYEHDSMSTMhfrslgsaISKILRELDTEisylkgrifpvEDQLEALKSEsqnkiellLQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 337 AATDRIKQLEENFE------AERAAHLKSKFN-----LEITQMRIRElEGALQMEKVSQAEalSDLEMIRKEFKEVENAY 405
Cdd:pfam15921 264 QHQDRIEQLISEHEveitglTEKASSARSQANsiqsqLEIIQEQARN-QNSMYMRQLSDLE--STVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 406 ErekqkaqenlEKVNRLEREYISTNKQMNEKIEEKKEIIkdlserlQENEKIHRELQDKLATAKKHQVFVTETYENNmie 485
Cdd:pfam15921 341 E----------DKIEELEKQLVLANSELTEARTERDQFS-------QESGNLDDQLQKLLADLHKREKELSLEKEQN--- 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 486 lKLLLDsfamsgqrtagtckdKDKPSSLsvletlryTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDL 565
Cdd:pfam15921 401 -KRLWD---------------RDTGNSI--------TIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 566 KEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWE------EEKVRAAESEN-EIQKLTRAYKKDMEEkltf 638
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaslQEKERAIEATNaEITKLRSRVDLKLQE---- 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 639 lhglYQHLvagcvlikQPEGildrfswsELCAVLQENVDALILDLnranekishleyickSKSDTMKELQRSQEDDMSKM 718
Cdd:pfam15921 533 ----LQHL--------KNEG--------DHLRNVQTECEALKLQM---------------AEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201826906 719 AEQMKAQESCWQKQKKYLEQQYSDLLGEVharaQEYKETAEKNKEKICVLEKRQEELALENLYVKN 784
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLEL----QEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
147-470 |
1.45e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 147 LKRKLCQAKEEKVDIIIKH-NQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKK---DARLTVRTVEEELSDARNKL 222
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWNKElKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKeltNSESENSEKQRELEEKQNEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 223 AELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQrLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKD 302
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQNQEK-LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 303 MEL---EHRDCSDLLTRQVHKLEYSAEQE----ERLKKELEAATDRIKQLEENfeaerAAHLKSKF-NLEITQMRIRELE 374
Cdd:TIGR04523 452 KELiikNLDNTRESLETQLKVLSRSINKIkqnlEQKQKELKSKEKELKKLNEE-----KKELEEKVkDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 375 GALQMEKVSQAEALSDLE--MIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQ 452
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEdeLNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
330
....*....|....*...
gi 2201826906 453 ENEKIHRELQDKLATAKK 470
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKK 624
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
140-426 |
2.52e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 140 ELDVAEDLKRKLCQAKEEKvdiiikhNQELRDYEIQIVKLRSEFEKGEAIR---------QSLE---YALAIAKKDARlt 207
Cdd:PRK02224 406 DLGNAEDFLEELREERDEL-------REREAELEATLRTARERVEEAEALLeagkcpecgQPVEgspHVETIEEDRER-- 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 208 VRTVEEELSDARNKLAELQVFNEKLQQrLVETEKTFHIAQQKWKEQQQRLA---------SEKDDILRTHKDEYEL---- 274
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAerretieekRERAEELRERAAELEAeaee 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 275 --------------LLKERGELESILQKQNSALQNLsKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATD 340
Cdd:PRK02224 556 kreaaaeaeeeaeeAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRE 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 341 RIKQLEENFEAERAAHLKSKfnLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAyeREKQKAQENleKVN 420
Cdd:PRK02224 635 RKRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL--RERREALEN--RVE 708
|
....*.
gi 2201826906 421 RLEREY 426
Cdd:PRK02224 709 ALEALY 714
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
166-425 |
8.17e-07 |
|
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: 53.92 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 166 NQELRDYEIQIVKLRSEFEKgeaiRQSLEYALAIAKKDArltvrtvEEELSDARNKLAELQVFNEKLQQRLVETEKTFHI 245
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRR----IENRLDELSQELSDA-------SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 246 AQQK---WKEQQQRLASEKDDILRT-HKDEYELLLKERGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKL 321
Cdd:TIGR02169 749 LEQEienVKSELKELEARIEELEEDlHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 322 EYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEV 401
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260
....*....|....*....|....
gi 2201826906 402 ENAYEREKQKAQENLEKVNRLERE 425
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-1195 |
8.25e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 314 LTRQVHKLEYSAEQEER---LKKELEAA-----TDRIKQLEENFEAeraahlkskFNLEITQMRIRELEGALQMekvsqA 385
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykeLKAELRELelallVLRLEELREELEE---------LQEELKEAEEELEELTAEL-----Q 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 386 EALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEiikdLSERLQENEKIHRELQDKL 465
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----LEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 466 ATAKKhqvfVTETYENNMIELKLLLDSFAmsgqrtagtckdKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKMNALCE 545
Cdd:TIGR02168 340 AELEE----KLEELKEELESLEAELEELE------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 546 NTTKELEISRDKMCVLSQDLKEARDKLANANKELnhLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLT 625
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 626 RaykkdmeekltflhglyqhlvagcvlikqpegildrfswselcavlqenvdalilDLNRANEKIshleyicksksDTMK 705
Cdd:TIGR02168 482 R-------------------------------------------------------ELAQLQARL-----------DSLE 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 706 ELQRSQEDDMSKMAEQMKaqescWQKQKKYLEQQYSDLLgEVharAQEYKETAEKnkekicVLEKRQEELALENLYVKNT 785
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLK-----NQSGLSGILGVLSELI-SV---DEGYEAAIEA------ALGGRLQAVVVENLNAAKK 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 786 LTQIQKEHSSllaacallagalyplyGRsCAMSIQRDLLQDQVNIYEL-VNQEIRTLVHILSGVEEEKEddakikkhKFR 864
Cdd:TIGR02168 561 AIAFLKQNEL----------------GR-VTFLPLDSIKGTEIQGNDReILKNIEGFLGVAKDLVKFDP--------KLR 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 865 GLIHVFRRGVIAV---LAANRLKVLAQSSSSLFSLiNGFKEGIGILVCVGDSKGKHNMSRYNKEGIRCVEALNWFTSP-- 939
Cdd:TIGR02168 616 KALSYLLGGVLVVddlDNALELAKKLRPGYRIVTL-DGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKia 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 940 ---DLLTAVISSVTELQDVISKTDpKSCLSGRLLVSAARNSFSKLMDKLNVIMESVpldSSRSVTYVEKNSLIQRLAHGL 1016
Cdd:TIGR02168 695 eleKALAELRKELEELEEELEQLR-KELEELSRQISALRKDLARLEAEVEQLEERI---AQLSKELTELEAEIEELEERL 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1017 HRINARALEAgscdrrpiMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQeadKAQSLKEQLSLFKQS 1096
Cdd:TIGR02168 771 EEAEEELAEA--------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE---RLESLERRIAATERR 839
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1097 KLIAHKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNK-------LELHSSEEADKNQVLSETVKRLSEAKMELRR 1169
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasleeaLALLRSELEELSEELRELESKRSELRRELEE 919
|
890 900
....*....|....*....|....*.
gi 2201826906 1170 KDQSLRQLNRLLTQLEQDKRRLKESI 1195
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
258-487 |
1.30e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 258 ASEKDDILRTHKDEYELllkeRGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRqvhkLEYSAEQEERLKKELEA 337
Cdd:TIGR02169 670 RSEPAELQRLRERLEGL----KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE----IEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 338 ATDRIKQLEENFEAERAAhlKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLE 417
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSE--LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 418 KVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQVFVtETYENNMIELK 487
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-RDLESRLGDLK 888
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
213-463 |
1.42e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 213 EELSDARNKLAELQVFNEKLQQRLVETEKTFH-----IAQQKWKEQQQRLASEKDDI----LRTHKDEYELLLKERGELE 283
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKkeselIKLKELAEQLKELEEKLKKYnleeLEKKAEEYEKLKEKLIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 284 ---SILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEysaeqeERLKKELEAATDRIKQLEEnFEAERAAHLKSK 360
Cdd:PRK03918 539 geiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE------ELGFESVEELEERLKELEP-FYNEYLELKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 361 FNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQEnlEKVNRLEREYISTN---KQMNEKI 437
Cdd:PRK03918 612 KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--EEYLELSRELAGLRaelEELEKRR 689
|
250 260
....*....|....*....|....*.
gi 2201826906 438 EEKKEIIKDLSERLQENEKIHRELQD 463
Cdd:PRK03918 690 EEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
148-421 |
2.38e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 148 KRKLcQAKEEKVDIIikhNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAkkDARLTVRTVEEELSDARNKLAELQV 227
Cdd:COG4913 609 RAKL-AALEAELAEL---EEELAEAEERLEALEAELDALQERREALQRLAEYS--WDEIDVASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 228 FNEKLQQrlvetektfhiAQQKWKEQQQRLasekddilRTHKDEYELLLKERGELES----ILQKQNSALQNLSKKMKDM 303
Cdd:COG4913 683 SSDDLAA-----------LEEQLEELEAEL--------EELEEELDELKGEIGRLEKeleqAEEELDELQDRLEAAEDLA 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 304 ELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHlKSKFNLEITQMRIrELEGALQMEKVS 383
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADLDA-DLESLPEYLALL 821
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2201826906 384 QAEALSDLEMIRKEFKEVEN------------AYEREKQKAQENLEKVNR 421
Cdd:COG4913 822 DRLEEDGLPEYEERFKELLNensiefvadllsKLRRAIREIKERIDPLND 871
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-634 |
4.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 153 QAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAiakkDARLTVRTVEEELSDARNKLAElqvfnekL 232
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE----ELEEELEEAEEELEEAEAELAE-------A 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 233 QQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESiLQKQNSALQNLSKKMKDMELEHRDCSD 312
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 313 LLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDL- 391
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGl 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 392 -----EMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNE--------KIEEKKEIIKDLSERLQENEKIH 458
Cdd:COG1196 523 agavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 459 RELQDKLATAKKHQVFVTETYENNMIELKLLLDSFAMSGQRTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELK 538
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 539 KMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESE 618
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
490
....*....|....*.
gi 2201826906 619 NEIQKLTRAYKKDMEE 634
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-627 |
6.29e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 383 SQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKeiikDLSERLQENEKIHRELQ 462
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 463 DKLATAKKhqvfvtetyennmiELKLLLDSFAMSGQRTAGTC--KDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKM 540
Cdd:COG4942 97 AELEAQKE--------------ELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 541 NALcentTKELEISRDKMCVLSQDLKEARDKLANANKElnhlhtecadKAALIGTLQMELQNVQQRWEEEKVRAAESENE 620
Cdd:COG4942 163 AAL----RAELEAERAELEALLAELEEERAALEALKAE----------RQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*..
gi 2201826906 621 IQKLTRA 627
Cdd:COG4942 229 IARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
320-636 |
1.12e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 320 KLEYSAEQEERLK---KELEAatdRIKQLEEnfEAERAAH---LKSKFN---LEITQMRIRELEGALQMEKVSQAEALSD 390
Cdd:COG1196 180 KLEATEENLERLEdilGELER---QLEPLER--QAEKAERyreLKEELKeleAELLLLKLRELEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 391 LEMIRKEFKEVENAYEREKQKAQENLEKVNRL-EREYISTNK--QMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLAT 467
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAqAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 468 AKKHQVFVTETYENNMIELKLLLDSFAMSGQRTAGTCKDKDkpSSLSVLETLRYTLTAYQNKLEDTSNELKKMNALCENT 547
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 548 TKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIgtLQMELQNVQQRWEEEKVRAAESENEIQKLTRA 627
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEAALLEAALAELLEELAEAA 490
|
....*....
gi 2201826906 628 YKKDMEEKL 636
Cdd:COG1196 491 ARLLLLLEA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1004-1267 |
1.95e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1004 EKNSLIQRLAHGLHRINARALEAGScDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKA 1083
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1084 QSLKEQLSLFKQSKLIAHKRFESACEELNNALH-WEHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSE 1162
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1163 AKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQTLLSWTAATRNDF 1242
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260
....*....|....*....|....*
gi 2201826906 1243 TLQLPKLHLETFAVEGLKGGPEVVA 1267
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
142-353 |
3.00e-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: 48.80 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 142 DVAEDLKRKLCQAKEEKvDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYA-----LAIAKKDARLTVRTVEEELS 216
Cdd:COG3096 893 DRLEELREELDAAQEAQ-AFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAkeqqrRLKQQIFALSEVVQRRPHFS 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 217 --DARNKLAELQVFNEKLQQRLVETEktfhiaqqkwkeqQQRlaSEKDDILRTHKDEYELLLKERGELESILQKQNSALQ 294
Cdd:COG3096 972 yeDAVGLLGENSDLNEKLRARLEQAE-------------EAR--REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQ 1036
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201826906 295 NLSKKMKDMEL------------EHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAER 353
Cdd:COG3096 1037 ELEQELEELGVqadaeaeerariRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
170-601 |
3.17e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.89 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 170 RDYEIQIVKLRSE---FEKGEAIRQSLEYALAIAKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIA 246
Cdd:TIGR00606 366 RDSLIQSLATRLEldgFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 247 QQKWKEQQQRLASEKDDILRTHKDEYELLLKE----RGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLE 322
Cdd:TIGR00606 446 KEILEKKQEELKFVIKELQQLEGSSDRILELDqelrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 323 YSAEQEERLKKELEAATDRIKQLEenfeaeraahlkskfnleitqmRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVE 402
Cdd:TIGR00606 526 QLNHHTTTRTQMEMLTKDKMDKDE----------------------QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKS 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 403 NayerEKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERL------QENEKIHRELQDKLATAKKHQVFV- 475
Cdd:TIGR00606 584 K----EINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKQRAMLa 659
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 476 --TETYENNMIELKLLLDSFAMSGQRTAGTCKDKDKpsslsVLETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEI 553
Cdd:TIGR00606 660 gaTAVYSQFITQLTDENQSCCPVCQRVFQTEAELQE-----FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2201826906 554 SRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQ 601
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE 782
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
102-616 |
4.10e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 102 YMIDIMNLSSPVSHVD---HEAKRLCSaksgsqllhnssaselDVAEDLKRKLCQAKEEKVDIIIKHNQ---ELRDYEIQ 175
Cdd:pfam15921 315 YMRQLSDLESTVSQLRselREAKRMYE----------------DKIEELEKQLVLANSELTEARTERDQfsqESGNLDDQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 176 IVKLRSEFEKGE---AIRQSLEYALAIAKKDARLTVRTVEEELSDaRNklaeLQVfneklqQRLVETEKTFHIAQQKWKE 252
Cdd:pfam15921 379 LQKLLADLHKREkelSLEKEQNKRLWDRDTGNSITIDHLRRELDD-RN----MEV------QRLEALLKAMKSECQGQME 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 253 QQQRLASEKDDILrthkdeyELLLKERGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTR-------------QVH 319
Cdd:pfam15921 448 RQMAAIQGKNESL-------EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASlqekeraieatnaEIT 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 320 KLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIREL----------EGALQMEKVSQAEALS 389
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtAGAMQVEKAQLEKEIN 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 390 DLEMIRKEFKEVEnayEREKQKAQENLEKVNRLEREYIstnKQMNEKieekkeiikdlSERLQENEKIHRE---LQDKLA 466
Cdd:pfam15921 601 DRRLELQEFKILK---DKKDAKIRELEARVSDLELEKV---KLVNAG-----------SERLRAVKDIKQErdqLLNEVK 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 467 TAKKHQVFVTETYEnnmielkLLLDSFAMSGQRTAGTCKdkdkpsslsvleTLRYTLTAYQNKLEDTSNELKKMNA---- 542
Cdd:pfam15921 664 TSRNELNSLSEDYE-------VLKRNFRNKSEEMETTTN------------KLKMQLKSAQSELEQTRNTLKSMEGsdgh 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 543 ---LCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTL---------QMELQNVQQRWEEE 610
Cdd:pfam15921 725 amkVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVateknkmagELEVLRSQERRLKE 804
|
....*.
gi 2201826906 611 KVRAAE 616
Cdd:pfam15921 805 KVANME 810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1038-1229 |
6.43e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1038 IASLQKQIAEFTQRLHTVEVERCSLRRELAEFKlnfSKMKQEADKAQSLKEQLSLFKQSKLIAHKRFESACEELNNALHW 1117
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1118 EHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHD 1197
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190
....*....|....*....|....*....|..
gi 2201826906 1198 AESALCMAAKDRELIINQMKSVEATLHTVRDQ 1229
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
229-450 |
7.75e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 229 NEKLQQRL--VETEKTFHIAQQKWK---EQQQRLASEKDDILRTHKDEYELLLKERG-------------ELESILQKQN 290
Cdd:pfam17380 268 NEFLNQLLhiVQHQKAVSERQQQEKfekMEQERLRQEKEEKAREVERRRKLEEAEKArqaemdrqaaiyaEQERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 291 SALQNLSKKMKDMELEHRDCSDLLT-----RQVHKLEYSAEQE-ERLKKELEAA--------------------TDRIKQ 344
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEEIAMeisrmRELERLQMERQQKnERVRQELEAArkvkileeerqrkiqqqkveMEQIRA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 345 LEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALsdlemiRKEFKEVENAYEREKQKAQENLEKVnrLER 424
Cdd:pfam17380 428 EQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEE------RKRKKLELEKEKRDRKRAEEQRRKI--LEK 499
|
250 260
....*....|....*....|....*.
gi 2201826906 425 EYISTNKQMNEKIEEKKEIIKDLSER 450
Cdd:pfam17380 500 ELEERKQAMIEEERKRKLLEKEMEER 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
522-760 |
1.11e-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: 46.30 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 522 TLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQ 601
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 602 NVQQRWEEEKVRAAESeneiqkLTRAYKKDMEEKLTFLhglyqhlvagcVLIKQPEGILDRFSW-SELCAVLQENVDALI 680
Cdd:COG4942 94 ELRAELEAQKEELAEL------LRALYRLGRQPPLALL-----------LSPEDFLDAVRRLQYlKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 681 LDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMSKMAEQMKAQESCWQKQKKY------LEQQYSDLLGEVHARAQEY 754
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaeLQQEAEELEALIARLEAEA 236
|
....*.
gi 2201826906 755 KETAEK 760
Cdd:COG4942 237 AAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
85-631 |
1.41e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 85 FIVEDDVHSTELLDLKSYMIDiMNLSSPVSHVDHEAKRLCSAKSGSQllhNSSASELDVAEDLK---RKLCQAKEEKVDI 161
Cdd:pfam05483 261 FLLEESRDKANQLEEKTKLQD-ENLKELIEKKDHLTKELEDIKMSLQ---RSMSTQKALEEDLQiatKTICQLTEEKEAQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 162 IIKHNQELRDYEIQIVKLrsefekgEAIRQSLEYALaiakkdarltvRTVEEELSDARNklaELQVFNEKLQQRLVETEK 241
Cdd:pfam05483 337 MEELNKAKAAHSFVVTEF-------EATTCSLEELL-----------RTEQQRLEKNED---QLKIITMELQKKSSELEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 242 TFHIAQQKWKEQQQrlasekddiLRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKL 321
Cdd:pfam05483 396 MTKFKNNKEVELEE---------LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 322 EYSAEQEERLKKELEAATDRIKQLEEN-----FEAERAAHLKSKFNLE-------ITQMRIRELEGALQMEKVSQAEA-- 387
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEASDMTLElkkhqedIINCKKQEERMLKQIENLEEKEMnl 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 388 LSDLEMIRKEFKEVENAYEREKQKAQENLEKVnrlEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQ--DKL 465
Cdd:pfam05483 547 RDELESVREEFIQKGDEVKCKLDKSEENARSI---EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKalKKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 466 ATAKKHQVFVtetYENNMIELKLLLDSFAMSGQRTAGTCKDKDKPSSLSVlETLRYTLTAYQNKLEDTSNELKKMNALCE 545
Cdd:pfam05483 624 GSAENKQLNA---YEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE-EKLLEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 546 NTTKEleisrdkMCVLSQDLKEARDKLANA-NKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKL 624
Cdd:pfam05483 700 HKIAE-------MVALMEKHKHQYDKIIEErDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
....*..
gi 2201826906 625 TRAYKKD 631
Cdd:pfam05483 773 KMEAKEN 779
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
77-693 |
1.45e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 77 FEASQLEAFIVEDDVHSTELLDLKSYMIDIMNLSSPVSHVDHEAKRL-CSAKSGSQLLHNSSASEL----DVAEDLKRKL 151
Cdd:TIGR01612 1984 FENQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELNKLsCDSQNYDTILELSKQDKIkekiDNYEKEKEKF 2063
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 152 -----CQAKEEKVDIIIKHNQELRDYEIQIVKLRSEF-EKGEAIRQSleyalaiaKKDARLTVRTVEEELSDARNKLAEL 225
Cdd:TIGR01612 2064 gidfdVKAMEEKFDNDIKDIEKFENNYKHSEKDNHDFsEEKDNIIQS--------KKKLKELTEAFNTEIKIIEDKIIEK 2135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 226 QVFNEKLQQ-----------RLVETEKT-------FHIAQQKWKEQQQRLASEKDDILRTHKDEYEL---LLKERGELES 284
Cdd:TIGR01612 2136 NDLIDKLIEmrkecllfsyaTLVETLKSkvinhseFITSAAKFSKDFFEFIEDISDSLNDDIDALQIkynLNQTKKHMIS 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 285 ILQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHK-----LEYSAEQEERLKKELEAATDRIKQLEEN---FEAERAAH 356
Cdd:TIGR01612 2216 ILADATKDHNNLIEKEKEATKIINNLTELFTIDFNNadadiLHNNKIQIIYFNSELHKSIESIKKLYKKinaFKLLNISH 2295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 357 LKSKFNlEITqmriRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYERE-KQKAQENLEKVNRLEREYISTNKQMNE 435
Cdd:TIGR01612 2296 INEKYF-DIS----KEFDNIIQLQKHKLTENLNDLKEIDQYISDKKNIFLHAlNENTNFNFNALKEIYDDIINRENKADE 2370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 436 KIEEKKEIIKDLSERLQENEKIHRELQDKLatakkhqVFVTeTYENNMIELKLLLdsfamsgqrtagtcKDKDKPSSLSV 515
Cdd:TIGR01612 2371 IENINNKENENIMQYIDTITKLTEKIQDIL-------IFVT-TYENDNNIIKQHI--------------QDNDENDVSKI 2428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 516 LETLRYTLTAYQ---NKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLK------EARDKLANANKELNHLHTEC 586
Cdd:TIGR01612 2429 KDNLKKTIQSFQeilNKIDEIKAQFYGGNNINNIIITISQNANDVKNHFSKDLTieneliQIQKRLEDIKNAAHEIRSEQ 2508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 587 ADK--AALIGTLQMELQNVQQR-WEEEKVRAAESENEIQKLtRAYKKDMEEKLTFLHGlYQHLVAGCV--------LIKQ 655
Cdd:TIGR01612 2509 ITKytNAIHNHIEEQFKKIENNsNKDEVYKINEIDNIIEKI-INYNKEPEVKLHAIID-NKNEFASIIpdiknliaLIES 2586
|
650 660 670
....*....|....*....|....*....|....*...
gi 2201826906 656 PEGILDRFSWsELCAVLQENVDALILDLNRANEKISHL 693
Cdd:TIGR01612 2587 EYGNNNNISY-KVAIKHEEDANNIILDLNKSQNILNHL 2623
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
200-417 |
1.53e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 44.28 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 200 AKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTfhIAQQKWKEQQQRLASEKddilrthkdEYELLLKER 279
Cdd:pfam05010 9 ALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKT--IAQMIEEKQKQKELEHA---------EIQKVLEEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 280 GELESILQKQNSALQNLSKKMKdmelehrdcsdlltRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERaAHLKS 359
Cdd:pfam05010 78 DQALADLNSVEKSFSDLFKRYE--------------KQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALK-AHAEE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201826906 360 KF---NLEITQMRIRelegalqmekvSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLE 417
Cdd:pfam05010 143 KLdqaNEEIAQVRSK-----------AKAETAALQASLRKEQMKVQSLERQLEQKTKENEE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
153-607 |
1.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 153 QAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAiaKKDARLTVRTVEEELSDARNKLAELQVFNEKL 232
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE--KLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 233 QQRLvetektfhiaqQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDMELEhrdcsd 312
Cdd:COG4717 152 EERL-----------EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE------ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 313 lLTRQVHKLEYSAEQEERLKKELEAATD--RIKQLEENFEAERAAHLKSKFNLEITQmRIRELEGALQMekVSQAEALSD 390
Cdd:COG4717 215 -LEEAQEELEELEEELEQLENELEAAALeeRLKEARLLLLIAAALLALLGLGGSLLS-LILTIAGVLFL--VLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 391 LEMIRKEFKEVENAYEREKQKAQENLEkvnrlEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKK 470
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 471 HQvfvtetyenNMIELKLLLDSfamsgqrtAGTCKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKMNALCENTTK- 549
Cdd:COG4717 366 EE---------LEQEIAALLAE--------AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEe 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2201826906 550 ----ELEISRDKMCVLSQDLKEARDKLANANKELNHLHT--ECADKAALIGTLQMELQNVQQRW 607
Cdd:COG4717 429 eleeELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELRELAEEW 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1029-1239 |
1.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1029 CDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLR--RELAEFKLNFSKMKQEADKAQSLKEQLSLFKQSKLIAhkRFES 1106
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1107 ACEELNNALHwehQAQVLLNEQAQQLQELNNKLELHsseeadKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQ 1186
Cdd:COG4913 296 ELEELRAELA---RLEAELERLEARLDALREELDEL------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2201826906 1187 DKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQTLLSWTAATR 1239
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
119-621 |
1.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 119 EAKRLCSAKSGSQLLHNSSASELDVAEDLKRKlcQAKEEKVDIIIKHNQELRDYEiQIVKLRSEFEKGEAIRQSLEYAla 198
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADELKKA--AAAKKKADEAKKKAEEKKKAD-EAKKKAEEAKKADEAKKKAEEA-- 1456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 199 iaKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFH----IAQQKWKEQQQRLASEKDDILRTHKDEYEl 274
Cdd:PTZ00121 1457 --KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeakkAAEAKKKADEAKKAEEAKKADEAKKAEEA- 1533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 275 llKERGELESILQKQNSalQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERA 354
Cdd:PTZ00121 1534 --KKADEAKKAEEKKKA--DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 355 AHLKSKFNLEITQMRIR---ELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNK 431
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKkaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK 1689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 432 ----------------QMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKK--HQVFVTETYENNMIELKLLLDSF 493
Cdd:PTZ00121 1690 aaealkkeaeeakkaeELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAKKDEEEKKKIAHLKKEEEKK 1769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 494 AMSGQRTAGTC-----KDKDKPSSLSVLETLRYTLTAYQNKLEDTsnelkKMNALCENTTKELEISRDKMCVLSQDL--- 565
Cdd:PTZ00121 1770 AEEIRKEKEAVieeelDEEDEKRRMEVDKKIKDIFDNFANIIEGG-----KEGNLVINDSKEMEDSAIKEVADSKNMqle 1844
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2201826906 566 --KEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEI 621
Cdd:PTZ00121 1845 eaDAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-690 |
1.87e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 156 EEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQS-LEYALAIAKKD------ARLTVRTVEEELSDARNKLAELQVF 228
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPIRELaERYAAARERLAeleylrAALRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 229 NEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLS-------KKMK 301
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 302 DMELEHRDCSDLLTRQVHKLE---YSAEQEER-LKKELEAATDRIKQLEENfeaeraahlKSKFNLEITQMRiRELEGAL 377
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEealAEAEAALRdLRRELRELEAEIASLERR---------KSNIPARLLALR-DALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 378 qmeKVSQAEA--LSDLEMIRKEFKEVENAYER-----------EKQKAQENLEKVNRLE-REYISTNKQMNEKIEEKKEI 443
Cdd:COG4913 454 ---GLDEAELpfVGELIEVRPEEERWRGAIERvlggfaltllvPPEHYAAALRWVNRLHlRGRLVYERVRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 444 IKD--LSERLQENEKIHRE-LQDKLATA------------KKHQVFVTETyenNMIelkllldsfamSGQRTAGTCKDKD 508
Cdd:COG4913 531 LDPdsLAGKLDFKPHPFRAwLEAELGRRfdyvcvdspeelRRHPRAITRA---GQV-----------KGNGTRHEKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 509 KPSSLSVL--------ETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISR--DKMCVLSQDLKEARDKLANANKE 578
Cdd:COG4913 597 RIRSRYVLgfdnraklAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 579 LNHLHTECADKAAL---IGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAyKKDMEEKLTFLHGLYQHLVAGCvLIKQ 655
Cdd:COG4913 677 LERLDASSDDLAALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-LDELQDRLEAAEDLARLELRAL-LEER 754
|
570 580 590
....*....|....*....|....*....|....*
gi 2201826906 656 PEGILDRFSWSELCAVLQENVDALILDLNRANEKI 690
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
142-346 |
2.41e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 142 DVAEDLKRKLCQAKEEKVDIIiKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAI-----AKKDARLTVRTVEEELS 216
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFVQ-QHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTqrdakQQAFALTEVVQRRAHFS 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 217 --DARNKLAELQVFNEKLQQRLVEtektfhiaqqkwKEQQQRLASEKddiLRTHKDEYELLLKERGELESILQKQNSALQ 294
Cdd:PRK04863 973 yeDAAEMLAKNSDLNEKLRQRLEQ------------AEQERTRAREQ---LRQAQAQLAQYNQVLASLKSSYDAKRQMLQ 1037
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2201826906 295 NLSKKMKDMELehRDCSDLLTRqvhkleySAEQEERLKKELEAATDRIKQLE 346
Cdd:PRK04863 1038 ELKQELQDLGV--PADSGAEER-------ARARRDELHARLSANRSRRNQLE 1080
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1036-1193 |
2.53e-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: 45.14 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1036 KSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLKEQLSLFKQS-------KLIAHKRFESAC 1108
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1109 EELNNALHWE----HQAQVLLNEQAQQLQELNNKLELH----SSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRL 1180
Cdd:COG4942 149 REQAEELRADlaelAALRAELEAERAELEALLAELEEEraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
170
....*....|...
gi 2201826906 1181 LTQLEQDKRRLKE 1193
Cdd:COG4942 229 IARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1022-1195 |
2.67e-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: 45.14 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1022 RALEAGSCDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQE-ADKAQSLKEQL-SLFKQSKLI 1099
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAElEAQKEELAELLrALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1100 AHKRFESAcEELNNALHWEHQAQVLLNEQAQQLQELNNKLElhssEEADKNQVLSETVKRLSEAKMELRRKDQSLRQL-- 1177
Cdd:COG4942 121 PLALLLSP-EDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEEERAALEALka 195
|
170 180
....*....|....*....|
gi 2201826906 1178 --NRLLTQLEQDKRRLKESI 1195
Cdd:COG4942 196 erQKLLARLEKELAELAAEL 215
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
195-463 |
2.67e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 45.71 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 195 YALAIAKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIaQQKWKEQQQRLASEKDDILRTHKDEYEL 274
Cdd:pfam15818 74 CALEEEKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQL-HLLAKEDHHKQLNEIEKYYATITGQFGL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 275 LLKERGELESILQ--------------KQNSALQNLSKKMKDMelehrdCSDLLTRQV---HKLEysaeqEERLkkELEA 337
Cdd:pfam15818 153 VKENHGKLEQNVQeaiqlnkrlsalnkKQESEICSLKKELKKV------TSDLIKSKVtcqYKMG-----EENI--NLTI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 338 ATDRIKQLEENFEAERAahLKSKFNLEITQMR---------IRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYERE 408
Cdd:pfam15818 220 KEQKFQELQERLNMELE--LNKKINEEITHIQeekqdiiisFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQ 297
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2201826906 409 KQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQD 463
Cdd:pfam15818 298 REKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
150-578 |
3.61e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 150 KLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKKDarltVRTVEEELSDARNKLAELQVF- 228
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE----KLNIQKNIDKIKNKLLKLELLl 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 229 ---------NEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRTHKdeyelllkergELESILQKQNSALQNLSKK 299
Cdd:TIGR04523 204 snlkkkiqkNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT-----------QLNQLKDEQNKIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 300 MKDMELEHRDCSDlLTRQVHKLEysaEQEERLKKELEAatDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQM 379
Cdd:TIGR04523 273 QKELEQNNKKIKE-LEKQLNQLK---SEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 380 EKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREyistnkqmnekieekkeiIKDLSERLQENEKIHR 459
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ------------------INDLESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 460 ELQDKLATAKKHQVFVTETYENnmielkllLDSFAMSGQRTAGTCKDKDKPSSLSVLETLRYTlTAYQNKLEDTSNELKK 539
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIER--------LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR-ESLETQLKVLSRSINK 479
|
410 420 430
....*....|....*....|....*....|....*....
gi 2201826906 540 MNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKE 578
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1077-1223 |
4.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1077 KQEADKA---QSLKEQLSLFKQSKLIAHKRF------------ESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLEL 1141
Cdd:COG1196 206 ERQAEKAeryRELKEELKELEAELLLLKLREleaeleeleaelEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1142 HSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEA 1221
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
..
gi 2201826906 1222 TL 1223
Cdd:COG1196 366 AL 367
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
259-636 |
4.65e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 259 SEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDMElEHRDCSDLLTRQVHKLEYSAEQEERLKKELEaa 338
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELE-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 339 tDRIKQLEENFEaeraahlkskfNLEITQMRIRELEGalqmekvsQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEK 418
Cdd:PRK03918 266 -ERIEELKKEIE-----------ELEEKVKELKELKE--------KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 419 VNRLereyISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQVFVTETYENNMIELKLLLDSfamsgq 498
Cdd:PRK03918 326 IEER----IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEE------ 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 499 rtagtckdkdkpsslsvLETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDK--LANAN 576
Cdd:PRK03918 396 -----------------LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEYT 458
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 577 KELNHLHTECADKAALIGTLQMELQNVqqrweeEKVRAAESENEIQKLTRAYKKDMEEKL 636
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELREL------EKVLKKESELIKLKELAEQLKELEEKL 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
145-490 |
7.45e-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: 44.19 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 145 EDLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAiAKKDARLTVRTVEEELSDARNKLAE 224
Cdd:pfam02463 197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ-EEIESSKQEIEKEEEKLAQVLKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 225 LqvfnEKLQQRLVETEKTFHIAQQKWKEQQQRLAsekddilrthKDEYELLLKERGELESILQKQNSALQNLSKKMKDme 304
Cdd:pfam02463 276 E----EEKEKKLQEEELKLLAKEEEELKSELLKL----------ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE-- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 305 lehrdcsdlltRQVHKLEYSAEQEERLKKELEAAtdRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQ 384
Cdd:pfam02463 340 -----------LEKELKELEIKREAEEEEEEELE--KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 385 AEALSDLEMIRKEFKEVENAYER----EKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQeNEKIHRE 460
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELeileEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ-LVKLQEQ 485
|
330 340 350
....*....|....*....|....*....|
gi 2201826906 461 LQDKLATAKKHQVFVTETYENNMIELKLLL 490
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLAL 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
167-306 |
7.62e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 167 QELRDYEIQIVKLRSEFEKGEAIRQSLEYALAiaKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIA 246
Cdd:COG3206 219 QQLSELESQLAEARAELAEAEARLAALRAQLG--SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL 296
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201826906 247 QQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDM-ELE 306
Cdd:COG3206 297 RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELrRLE 357
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
250-367 |
1.03e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 250 WKEQQQR-LASEKDDILRTHKDEYELLLKERGELESI---LQKQNSALQNLSKKMKDMELEHRDC-SDLLTRQVHKLEYS 324
Cdd:smart00787 137 WRMKLLEgLKEGLDENLEGLKEDYKLLMKELELLNSIkpkLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKLKKL 216
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2201826906 325 AEQEERLKKELEAATDRIKQLEENFEAERAahLKSKFNLEITQ 367
Cdd:smart00787 217 LQEIMIKVKKLEELEEELQELESKIEDLTN--KKSELNTEIAE 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
100-630 |
1.15e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 100 KSYMIDIMNLSSPVSHVDHEAKRLCSAKSGSQLLHNSSASELDVAEDLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKL 179
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 180 RSEF-----EKGEAIRQSLEYALAIAKKDarltVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQ 254
Cdd:TIGR04523 294 KSEIsdlnnQKEQDWNKELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 255 QRLASEKDDIlRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDMELEHrdcsDLLTRQVHKLEysaEQEERLKKE 334
Cdd:TIGR04523 370 NEIEKLKKEN-QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK----ELLEKEIERLK---ETIIKNNSE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 335 LEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQE 414
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 415 NLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKihRELQDKLATAKKHQvfvtETYENNMIELKLLLDSfa 494
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQ----KSLKKKQEEKQELIDQ-- 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 495 msgqrtagtcKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLAN 574
Cdd:TIGR04523 594 ----------KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2201826906 575 ANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRaaesENEIQKLTRAYKK 630
Cdd:TIGR04523 664 IIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIR----IKDLPKLEEKYKE 715
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
230-585 |
1.17e-03 |
|
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: 43.35 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 230 EKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDiLRTHKDEYElllKERGELESILQKQNSALQNLSKKMKDMELEHRD 309
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKER-YKRDREQWE---RQRRELESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 310 CSDL---LTRQVHKL-EYSAEQEERLKK-----------------ELEAATDRIKQLEENFEAERAAHLKSKFNLEITQM 368
Cdd:pfam07888 106 LSASseeLSEEKDALlAQRAAHEARIREleediktltqrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 369 RIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENlekvNRLEREYISTNKQMNEKIEEKKEIIKDLS 448
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN----EALLEELRSLQERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 449 ERLQENEKIHRELqdklatakkHQVFVtetyENNMIELKLLLDSFAMSGQRtAGTCKDKdkpsslsvlETLRYTLTAYQN 528
Cdd:pfam07888 262 SMAAQRDRTQAEL---------HQARL----QAAQLTLQLADASLALREGR-ARWAQER---------ETLQQSAEADKD 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2201826906 529 KLEDTSNELKKMNAL-----CENTTKELEISRDKMCVLSQ------DLKEARDKLANANKELNHLHTE 585
Cdd:pfam07888 319 RIEKLSAELQRLEERlqeerMEREKLEVELGREKDCNRVQlsesrrELQELKASLRVAQKEKEQLQAE 386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
202-420 |
1.30e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 202 KDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLAsekddilrthkdeyelllkergE 281
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----------------------E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 282 LESILQKQNSALQNLSKKMKDME--LEHRDCSDLLTRqVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAahlks 359
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDvlLGSESFSDFLDR-LSALSKIADADADLLEELKADKAELEAKKAELEAKLA----- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2201826906 360 kfNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVN 420
Cdd:COG3883 158 --ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-432 |
1.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 225 LQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDdilrtHKDEYELLLKERGELESILQKQNSALQNLSKKMKDME 304
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEE-----KEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 305 lehrdcsdlltrQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEA-ERAAHLKSKFNLEITQMRiRELEGALQMEKVS 383
Cdd:COG4717 123 ------------KLLQLLPLYQELEALEAELAELPERLEELEERLEElRELEEELEELEAELAELQ-EELEELLEQLSLA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2201826906 384 QAEALSDL----EMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQ 432
Cdd:COG4717 190 TEEELQDLaeelEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
185-621 |
1.64e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 185 KGEAIRQSLEY--ALAIAKKDARLTVRTVEEElsdaRNKLAELQVFNEKLQQRLVETEKTFH----IAQQKWK--EQQQR 256
Cdd:pfam05557 15 QNEKKQMELEHkrARIELEKKASALKRQLDRE----SDRNQELQKRIRLLEKREAEAEEALReqaeLNRLKKKylEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 257 LASEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDMELEHrdcsDLLTRQVHKLEYSAEQEERLKKELE 336
Cdd:pfam05557 91 KLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERL----DLLKAKASEAEQLRQNLEKQQSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 337 AATDRIKQLEenfeaeraahlkskfnleitqMRIRELEGALQMEKVSQAEALSDLEMIR-KEFKEVENAYEREKQKAQEN 415
Cdd:pfam05557 167 EAEQRIKELE---------------------FEIQSQEQDSEIVKNSKSELARIPELEKeLERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 416 L-EKVNRLEREYISTNKQMNEKIEEKKeiikdlserlqENEKIHRELQD--KLATAKKHQVFVTETYENNMIElkLLLDS 492
Cdd:pfam05557 226 LkEEVEDLKRKLEREEKYREEAATLEL-----------EKEKLEQELQSwvKLAQDTGLNLRSPEDLSRRIEQ--LQQRE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 493 FAMSGQRTAGTCKDKDKPSSLSVLETlryTLTAYQNKLEDTSNELKKMNALCENTTKELEIsrdkmcvLSQDLKEARDKL 572
Cdd:pfam05557 293 IVLKEENSSLTSSARQLEKARRELEQ---ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLL-------LTKERDGYRAIL 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2201826906 573 ANANKELNHLHTECADKAALIGTLQMeLQNVQQRWEEEKVRAAESENEI 621
Cdd:pfam05557 363 ESYDKELTMSNYSPQLLERIEEAEDM-TQKMQAHNEEMEAQLSVAEEEL 410
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1066-1223 |
2.18e-03 |
|
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: 42.74 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1066 LAEFKLNFSKMKQEADKAQSLKEQLS-LFKQSKLIAHKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLELH-- 1142
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAeLRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1143 -----SSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMK 1217
Cdd:TIGR02168 275 evselEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
....*.
gi 2201826906 1218 SVEATL 1223
Cdd:TIGR02168 355 SLEAEL 360
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
203-400 |
2.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 203 DARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEKTFH----IAQQKWKEQQQRLASEKddiLRTHKDEYELLLKE 278
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalqrLAEYSWDEIDVASAERE---IAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 279 RGELESiLQKQnsaLQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQ-LEENFEAERAAHL 357
Cdd:COG4913 684 SDDLAA-LEEQ---LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLeLRALLEERFAAAL 759
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2201826906 358 KSKFNLEITqmriRELEGALQMEKVSQAEALSDLEMIRKEFKE 400
Cdd:COG4913 760 GDAVERELR----ENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1038-1223 |
2.47e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1038 IASLQKQIAEFTQRLHTVEVERCSLRRELAEFKlNFSKMKQEADKAQSLKEQLSLFKQSKLIAHKRFESACEELNNALHW 1117
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKG 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1118 EhqaQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKM----ELRRKDQSLRQLNRLLTQL---EQDKRR 1190
Cdd:PRK03918 540 E---IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFesveELEERLKELEPFYNEYLELkdaEKELER 616
|
170 180 190
....*....|....*....|....*....|...
gi 2201826906 1191 LKESIHDAESALCMAAKDRELIINQMKSVEATL 1223
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
137-482 |
2.51e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 137 SASELDVAEDLKRKLCQAKEEKVDII-IKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKKDARLTVRTVEEEL 215
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVqEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 216 SDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQN 295
Cdd:pfam02463 782 KTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEE 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 296 LSKKMKdmELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEG 375
Cdd:pfam02463 862 EITKEE--LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 376 ALQMEKVSQAEALSDLEMIRKEFKEVENAYErekqkaqeNLEKVN-RLEREYISTNKQMNEKIEEKkeiikdlsERLQEN 454
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKE--------ELGKVNlMAIEEFEEKEERYNKDELEK--------ERLEEE 1003
|
330 340
....*....|....*....|....*...
gi 2201826906 455 EKIHRELQDKLATAKKHQVFVTETYENN 482
Cdd:pfam02463 1004 KKKLIRAIIEETCQRLKEFLELFVSINK 1031
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
211-414 |
2.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 211 VEEELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDIlrthkDEYELLLKERgelESILQKQN 290
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI-----AEAEAEIEER---REELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 291 SALQNLSKKMKDME--LEHRDCSDLLTRqVHKLEYSAEQE-------ERLKKELEAATDRIKQLEENFEAERAAHLKSKF 361
Cdd:COG3883 93 RALYRSGGSVSYLDvlLGSESFSDFLDR-LSALSKIADADadlleelKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2201826906 362 NLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQE 414
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
193-394 |
2.78e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 193 LEYALAIAKKDARLTVRTVEEELSDARNKL----AELQVFNEK-------------------LQQRLVETEKTFHIAQQK 249
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELeeaeAALEEFRQKnglvdlseeaklllqqlseLESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 250 WKEQQQRLASEK--------DDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDME--LEHRDCSDLLTRQVh 319
Cdd:COG3206 242 LAALRAQLGSGPdalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRaqLQQEAQRILASLEA- 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2201826906 320 KLEYSAEQEERLKKELEAATDRIKQLEENfEAERAAhLKSkfNLEITQMRIRELEGALQMEKVSQAEALSDLEMI 394
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPEL-EAELRR-LER--EVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
169-422 |
3.18e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 169 LRDYEIQIVKLRSEFEKGEAIRqslEYALAiAKKDARLTVRTVEEElsdaRNKLAELQVFNEKLQQRLVETEK---TFHI 245
Cdd:PRK02224 208 LNGLESELAELDEEIERYEEQR---EQARE-TRDEADEVLEEHEER----REELETLEAEIEDLRETIAETERereELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 246 AQQKWKEQQQRLASEKDDILrthkDEYELllkERGELESILQKQnsalQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSA 325
Cdd:PRK02224 280 EVRDLRERLEELEEERDDLL----AEAGL---DDADAEAVEARR----EELEDRDEELRDRLEECRVAAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 326 EQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEV---E 402
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELrerE 428
|
250 260
....*....|....*....|
gi 2201826906 403 NAYEREKQKAQENLEKVNRL 422
Cdd:PRK02224 429 AELEATLRTARERVEEAEAL 448
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
227-416 |
3.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 227 VFNEKLQQRLVETEKTfhiAQQKWKEQQQRLASEKDDILRTHKDEYellLKERGELESILQKQNSALQNLSKKMKDMELE 306
Cdd:PRK12704 24 VRKKIAEAKIKEAEEE---AKRILEEAKKEAEAIKKEALLEAKEEI---HKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 307 HRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQL--EENFEAERAAHLKSKfnlEITQMRIRelegalQMEKVSQ 384
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELieEQLQELERISGLTAE---EAKEILLE------KVEEEAR 168
|
170 180 190
....*....|....*....|....*....|..
gi 2201826906 385 AEALSdleMIRKEFKEvenAYEREKQKAQENL 416
Cdd:PRK12704 169 HEAAV---LIKEIEEE---AKEEADKKAKEIL 194
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-635 |
3.68e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 138 ASELDVAEDLKRKLCQAKE-EKVdiiiKHNQELRDYE---IQIVKLRSEFEKGEAIRQSLEYALAIAKKDARLTVRTVEE 213
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKaEEE----RNNEEIRKFEearMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 214 ELSDARNKLAELQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRL------ASEKDDILRTHKDEYELLLKERGELEsilQ 287
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAeaakaeAEAAADEAEAAEEKAEAAEKKKEEAK---K 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 288 KQNSALQNLSKKMKDMELEHRDCSD-LLTRQVHKLEYSAEQEERLKK---ELEAATDRIKQLEENFEAE----RAAHLKS 359
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDkKKADELKKAAAAKKKADEAKKkaeEKKKADEAKKKAEEAKKADeakkKAEEAKK 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 360 KFNLEITQMRIRELEGALQM--EKVSQAEALSDLEMIRKEFKEVENAYE-----------REKQKAQENLEKVNRLEREY 426
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEakkkadeakkaEEAKKADEAKKAEEAKKADE 1538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 427 ISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQVFVTETYENNMIELKLLLDSFAMSGQRTAGTCKD 506
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 507 KDKPSSLSVLETLRYTLTAYQNKLEDtsnELKKmnalCENTTKELEISRDKMCVLSQDLKEARDKLANANKElnhlhTEC 586
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAE---EKKK----AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA-----EED 1686
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2201826906 587 ADKAALIGTLQME----LQNVQQRWEEEK-----VRAAESENEIqKLTRAYKKDMEEK 635
Cdd:PTZ00121 1687 EKKAAEALKKEAEeakkAEELKKKEAEEKkkaeeLKKAEEENKI-KAEEAKKEAEEDK 1743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1021-1192 |
3.99e-03 |
|
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: 41.59 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1021 ARALEAGSCDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELaefklnfSKMKQEADKAQSLKEQLSLFKQSKLIA 1100
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-------KDYREKLEKLKREINELKRELDRLQEE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1101 HKRFESACEELNNALHWEHQAQVLLNEQAQQLQElnnklelhssEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRL 1180
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELEEEKEDKAL----------EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
170
....*....|..
gi 2201826906 1181 LTQLEQDKRRLK 1192
Cdd:TIGR02169 485 LSKLQRELAEAE 496
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
145-463 |
4.14e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 145 EDLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKKDARLTVRTVEEELSDARNKLAE 224
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 225 LQVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLASEKDDILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDM- 303
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLt 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 304 -ELEHRDCSDLLTRQVHK--LEYSAEQEE------RLKKELEAATDRIKQLEENFEAERAAHLKSKFN-----------L 363
Cdd:TIGR00618 694 yWKEMLAQCQTLLRELEThiEEYDREFNEienassSLGSDLAAREDALNQSLKELMHQARTVLKARTEahfnnneevtaA 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 364 EITQMRIRELEGALQMEKVSQAEALSDL----EMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEE 439
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLktleAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
330 340
....*....|....*....|....
gi 2201826906 440 KKEIIKDLSERLQENEKIHRELQD 463
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
162-361 |
4.23e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 162 IIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKKDARLTVRTVEEELSDARNKLAELQVFNEKLQQRLVETEK 241
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 242 TfhiaQQKWKEQQQRLASEKDDILRTHKDeyelLLKERGELESILQKQNSALQNLSKKMKDMELEhrdcsdlltrqvhkL 321
Cdd:COG4942 158 D----LAELAALRAELEAERAELEALLAE----LEEERAALEALKAERQKLLARLEKELAELAAE--------------L 215
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2201826906 322 EYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKF 361
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
168-359 |
4.78e-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: 40.29 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 168 ELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKKDarltVRTVEEELSDARNKLAELQVFNEKLQQRLvetektfhiaq 247
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARI----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 248 QKWKEQQQRLASEKddilrthkdEYELLLKErgelesiLQKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQ 327
Cdd:COG1579 76 KKYEEQLGNVRNNK---------EYEALQKE-------IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE 139
|
170 180 190
....*....|....*....|....*....|..
gi 2201826906 328 EERLKKELEAATDRIKQLEENFEAERAAHLKS 359
Cdd:COG1579 140 LEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
144-306 |
5.63e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 144 AEDLKRKLCQAKEEKVDIII------KHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYAL----AIAKKDARLTVRTVEE 213
Cdd:TIGR01612 1564 AEKSEQKIKEIKKEKFRIEDdaakndKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLketeSIEKKISSFSIDSQDT 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 214 ELSDARNKLAELQVFNEKL--QQRLVETEKTfhiaqqKWKEQQQRLASEKDDIlRTHKDEYELLLKE---------RGEL 282
Cdd:TIGR01612 1644 ELKENGDNLNSLQEFLESLkdQKKNIEDKKK------ELDELDSEIEKIEIDV-DQHKKNYEIGIIEkikeiaianKEEI 1716
|
170 180
....*....|....*....|....
gi 2201826906 283 ESILQKQNSALQNLSKKMKDMELE 306
Cdd:TIGR01612 1717 ESIKELIEPTIENLISSFNTNDLE 1740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
263-470 |
6.30e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 263 DILRTHKDEYELLLKERGELESILQKQNSALQNLSKKMKDMELEhrdcSDLLTRQVHKLEysaEQEERLKKELEAATDRI 342
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALE---QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 343 KQLEENFEAERAA-----------HLKSKFNLEITQMRIRELEGALQ-MEKVSQA--EALSDLEMIRKEFKEVENAYERE 408
Cdd:COG4942 93 AELRAELEAQKEElaellralyrlGRQPPLALLLSPEDFLDAVRRLQyLKYLAPArrEQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2201826906 409 KQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKK 470
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
276-635 |
6.46e-03 |
|
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: 40.65 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 276 LKERGELesiLQKQNSALQNLSKKmkdmELEHRDCSDLLTRQVHKLEysaEQEERLKKELEAATDRIKQLEENFEAERAA 355
Cdd:pfam07888 40 LQERAEL---LQAQEAANRQREKE----KERYKRDREQWERQRRELE---SRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 356 H--LKSKFNL-----EITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVeNAYEREKQKAQENLE-KVNRLEREYI 427
Cdd:pfam07888 110 SeeLSEEKDAllaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA-GAQRKEEEAERKQLQaKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 428 STNKQMNEKIEEKKEIIkdlSERLQENEKIHReLQDKLATAKKHQVfvtetyennmiELKLLLDSfamsgqrtagtckdk 507
Cdd:pfam07888 189 SLSKEFQELRNSLAQRD---TQVLQLQDTITT-LTQKLTTAHRKEA-----------ENEALLEE--------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 508 dkpsslsvLETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANkelnhlhteca 587
Cdd:pfam07888 239 --------LRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR----------- 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2201826906 588 dkaaliGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKKDMEEK 635
Cdd:pfam07888 300 ------ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
146-794 |
8.41e-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: 40.80 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 146 DLKRKLCQAKEEKVDIIIKHNQELRDYEIQIVKLRSEFEKGEAIRQSLEYALAIAKKDARltVRTVEEELSDARNKLAEL 225
Cdd:TIGR00606 443 ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKE--VKSLQNEKADLDRKLRKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 226 QVFNEKLQQRLVETEKTFHIAQQKWKEQQQRLasekdDILRTHKDEYELLLKE---RGELESILQKQNSALQNLSKKMKD 302
Cdd:TIGR00606 521 DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR-----KIKSRHSDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 303 MELEHRDCSDLLTRQVHKLEYSAEQEERLKKEL------EAATDRIKQLEENFEAERA--AHLKSKFNLE---ITQMRIR 371
Cdd:TIGR00606 596 LNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSKqrAMLAGATAVYsqfITQLTDE 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 372 ELEGALQMEKVSQAEA-----LSDLE-MIR---KEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKE 442
Cdd:TIGR00606 676 NQSCCPVCQRVFQTEAelqefISDLQsKLRlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 443 IIKDLSE---RLQENEKIHRELQDKLATAKKHQVFVT-------ETYENNMIELKLLLDSFAMSGQRTAGTCKDKDKPSS 512
Cdd:TIGR00606 756 VNRDIQRlknDIEEQETLLGTIMPEEESAKVCLTDVTimerfqmELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 513 lsvlETLRyTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAAL 592
Cdd:TIGR00606 836 ----HELD-TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 593 IGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKKDMEEKLTFLHGLYQHLVAGC-VLIKQPEGILDRFSWS-ELCA 670
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKdDYLKQKETELNTVNAQlEECE 990
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 671 VLQENVDALI------LDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMSKMAE-QMKAQESCWQKQKKYLE------ 737
Cdd:TIGR00606 991 KHQEKINEDMrlmrqdIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQmQVLQMKQEHQKLEENIDlikrnh 1070
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201826906 738 -------QQYSD--LLGEVHARAQEYKETAEKNKEKICVLEKRQEELALENLYVKNTLTQIQKEHS 794
Cdd:TIGR00606 1071 vlalgrqKGYEKeiKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-1229 |
8.54e-03 |
|
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: 40.82 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 405 YEREKQKAQENLEKVnrleREYISTNKQMnekieekkeiikdLSERLQENEKihreLQDKLATAKKHQVFVTETYEnnmI 484
Cdd:TIGR02169 168 FDRKKEKALEELEEV----EENIERLDLI-------------IDEKRQQLER----LRREREKAERYQALLKEKRE---Y 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 485 ELKLLLDSF-AMSGQRTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNEL-KKMNALCENTTKELeisRDKMCVLS 562
Cdd:TIGR02169 224 EGYELLKEKeALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRV---KEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 563 QDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKK---DMEEKLTFL 639
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 640 HGLYQHLVAgcvLIKQPEGILDRFSwselcaVLQENVDALILDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMSKMA 719
Cdd:TIGR02169 381 AETRDELKD---YREKLEKLKREIN------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 720 EQMKAQESCWQKQKKYlEQQYSDLlgevharaqeyketaeknKEKICVLEKRQEELALENLYVKNTLTQIQKEHSsllaa 799
Cdd:TIGR02169 452 KQEWKLEQLAADLSKY-EQELYDL------------------KEEYDRVEKELSKLQRELAEAEAQARASEERVR----- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 800 callagalyplYGRScamsiQRDLLQDQVN-IYELVNQEIR------TLVHILSG-----VEEEKEDDAK--IKKHKFRg 865
Cdd:TIGR02169 508 -----------GGRA-----VEEVLKASIQgVHGTVAQLGSvgeryaTAIEVAAGnrlnnVVVEDDAVAKeaIELLKRR- 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 866 lihvfRRGVIAVLAANRLKVLAQSSSSLfsLINGFkegIGILVcvgdskgkhNMSRYNKEgircVEALNWFTSPDllTAV 945
Cdd:TIGR02169 571 -----KAGRATFLPLNKMRDERRDLSIL--SEDGV---IGFAV---------DLVEFDPK----YEPAFKYVFGD--TLV 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 946 ISSVTELQDVISK----------TDPKSCLSGRLLVSAARNSFSKlMDKLNVIMESVPLDSSRSvtyvEKNSLIQRLAHG 1015
Cdd:TIGR02169 626 VEDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGILFSR-SEPAELQRLRERLEGLKR----ELSSLQSELRRI 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1016 LHRINA--RALEAGSCDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFK-----LNFSKMKQEADKAQsLKE 1088
Cdd:TIGR02169 701 ENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKselkeLEARIEELEEDLHK-LEE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2201826906 1089 QLSLFKQSKLIA---------------HKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLELHSSEEADKnqvL 1153
Cdd:TIGR02169 780 ALNDLEARLSHSripeiqaelskleeeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE---I 856
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2201826906 1154 SETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQ 1229
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| |
