|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
19-703 |
6.07e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 19 EAQILGAQNSELQAKTNETEKAFQTSQQKW---KEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQ 95
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 96 REKNEMEShiretALEEFRLQEEQWEAERRELqfivqeqdtavQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREER 175
Cdd:TIGR02168 341 ELEEKLEE-----LKEELESLEAELEELEAEL-----------EELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 176 LRKEFEATTLRVRKLEENIEAERAAHLESKFnsEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKH 255
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 256 NAQESFAKLNLLE-----KEYFSKNKKLNEDIEEQKKVIID-------------------LSKRLQY----NEKSCSELQ 307
Cdd:TIGR02168 483 ELAQLQARLDSLErlqenLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaaieaaLGGRLQAvvveNLNAAKKAI 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 308 EELVMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSGIHKDKDK-PPSFSVVLE-RLRRTL--TDYQNKLEDASNEL 383
Cdd:TIGR02168 563 AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfDPKLRKALSyLLGGVLvvDDLDNALELAKKLR 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 384 NSMNDV----------------KEKACNELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLK---- 443
Cdd:TIGR02168 643 PGYRIVtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkele 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 444 ------VELQNVLHCWEKEKAQAAQSESELQKLSQAFHKDAEEKLTFLHTLYQHLVAGCVLIKQPEGMLDKFswSELCAV 517
Cdd:TIGR02168 723 elsrqiSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL--KEELKA 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 518 LQENVDALIADLNRANEKIRHLEYICKNKSDTMRELQQTQEDTftkvaeqikaqescwHRQKKELELQyselflevqkra 597
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL---------------EEQIEELSED------------ 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 598 qkfQEIAEKNMEKLN-HIEKSHEQLVlensHFKKLLSQTQREQMSLLAACALMAGALYPLYSRSCALSTQRDFLQEQVNT 676
Cdd:TIGR02168 854 ---IESLAAEIEELEeLIEELESELE----ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
730 740 750
....*....|....*....|....*....|.
gi 1034664302 677 FEL----FKLEIRTLAQALSTVEEKKQEEAK 703
Cdd:TIGR02168 927 LELrlegLEVRIDNLQERLSEEYSLTLEEAE 957
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
71-337 |
1.01e-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: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 71 REYDLLMKEKSRLEKTL-----QEALEKHQREKNEMESHirETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKV 145
Cdd:COG1196 213 ERYRELKEELKELEAELlllklRELEAELEELEAELEEL--EAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 146 EKLETEHMDCSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLEGALQVE 225
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 226 KASQAEAVADLEIIKNEFKEVESA---YEREKHNAQESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKS 302
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAaaeLAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260 270
....*....|....*....|....*....|....*
gi 1034664302 303 CSELQEELVMAKKHQAFLVETCENNVKELESILDS 337
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
38-309 |
2.09e-09 |
|
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: 62.06 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 38 EKAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQREKNEMEshiRETALEEFRLQE 117
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME---RERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 118 EqweaeRRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQ-TSELEFSTQREERLRK--EFEATTLRVRKLEENI 194
Cdd:pfam17380 358 R-----KRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQElEAARKVKILEEERQRKiqQQKVEMEQIRAEQEEA 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 195 EAERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEA---VADLEIIKNEFKEVESAYEREKHNAQESFA-KLNLLEKE 270
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEerkRKKLELEKEKRDRKRAEEQRRKILEKELEErKQAMIEEE 512
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034664302 271 yfSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEE 309
Cdd:pfam17380 513 --RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
369-1161 |
3.63e-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: 61.23 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 369 LTDYQNKLEDASNELNSMNDVKEKACNELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVELQN 448
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 449 VLHCWEKEKAQAAQSESELQKLSQAFHKDAEEKltflhtlyqhlvagcvlikqpegmldkfswselcAVLQENVDALIAD 528
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKL----------------------------------EELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 529 LNRANEKIRHLEyickNKSDTMRELQQTQEDTFTKVAEQIKAQESCWHRQKKELElqyselflEVQKRAQKFQEIAEKNM 608
Cdd:TIGR02168 360 LEELEAELEELE----SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE--------RLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 609 EKLNHIEKSHEQLVLENShfKKLLSQTQREQMSLLAacalmagalyplysrscALSTQRDFLQEQVNTFELFKLEIRTLA 688
Cdd:TIGR02168 428 KKLEEAELKELQAELEEL--EEELEELQEELERLEE-----------------ALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 689 QALSTVEEKKQEEAKmkkktfkgliriFRKGVIAVLA-ANRLKILGQSCASLFTWMESFK--------EGIGMLVCTGEP 759
Cdd:TIGR02168 489 ARLDSLERLQENLEG------------FSEGVKALLKnQSGLSGILGVLSELISVDEGYEaaieaalgGRLQAVVVENLN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 760 QDKhkfpkhqkeqlrclQALSWLTSSDLLAAiisSMAELQDVIGKADPNSR---ICGHLLIGAAKNSFAKLMDKISLVME 836
Cdd:TIGR02168 557 AAK--------------KAIAFLKQNELGRV---TFLPLDSIKGTEIQGNDreiLKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 837 ciPLHSSRSITyvekDSLVQ--RLAHGLHKVNTLALKYG--LRGHVPITKSTASLQKQILGFTQrlhaaevERRSLRLEV 912
Cdd:TIGR02168 620 --YLLGGVLVV----DDLDNalELAKKLRPGYRIVTLDGdlVRPGGVITGGSAKTNSSILERRR-------EIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 913 TEFKRSVNEMKKELDKAQGLQMQL-NEFKQSKLITHE---KFESACEELNNALLREEQAQMLLNEQAQQLQELNYKLELH 988
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELeEELEQLRKELEElsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 989 SSEEADKNQTLGEAVKSLSEAKMELRRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESALRMAAKDKECVANHMRAVENT 1068
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 1069 LHKVRDQISLswSAASRNDFTLQLPKLHLETFAMEGLKGGPEvvacqAMIKSFMDVYQLASTRIMTLEKEMTSHRSHIAA 1148
Cdd:TIGR02168 847 IEELSEDIES--LAAEIEELEELIEELESELEALLNERASLE-----EALALLRSELEELSEELRELESKRSELRRELEE 919
|
810
....*....|...
gi 1034664302 1149 LKSELHTACLREN 1161
Cdd:TIGR02168 920 LREKLAQLELRLE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-338 |
4.34e-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: 61.23 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 23 LGAQNSELQAKTNETEKAfqtsQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQREKNEME 102
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKA----LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 103 SHIRETALEEFRLQEEQW-----EAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLR 177
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 178 KEFEATTLRVRKLEENIEAeraahleskfnseiiqlrirdLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNA 257
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIES---------------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 258 QESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSK---RLQYNEKSCSELQE-ELVMAKKHQAFLV---ETCENNVKE 330
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSlTLEEAEALENKIEddeEEARRRLKR 976
|
....*...
gi 1034664302 331 LESILDSF 338
Cdd:TIGR02168 977 LENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
81-425 |
4.37e-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: 61.23 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 81 SRLEKtlQEALEKHQREKNEMESHIRET--ALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDL 158
Cdd:TIGR02168 671 SILER--RREIEELEEKIEELEEKIAELekALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 159 LRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEI 238
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 239 IKNEFKEVESAYER---EKHNAQESFAKLNL---------------LEKEYFSKNkKLNEDIEEQKKVIIDLSKRLQYNE 300
Cdd:TIGR02168 829 LERRIAATERRLEDleeQIEELSEDIESLAAeieeleelieeleseLEALLNERA-SLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 301 KSCSELQEELVMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSGIHKDKDKPPSFSvvLERLRRTLTDYQNKLEDAS 380
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDD--EEEARRRLKRLENKIKELG 985
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034664302 381 N-ELNSMNDVKE----------------KACNELDSTKQKIDSHTKNikELQDKLADVNKEL 425
Cdd:TIGR02168 986 PvNLAAIEEYEElkerydfltaqkedltEAKETLEEAIEEIDREARE--RFKDTFDQVNENF 1045
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-398 |
5.62e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 41 FQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKtlqeaLEKHQREKNEMESHIRETALEEFRLQEEQW 120
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-----YQALLKEKREYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 121 EAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSElefstqREERLRKEFEATTLRVRKLEENI-----E 195
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIaekerE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 196 AERAAHLESKFNSEI--IQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLnlleKEYFS 273
Cdd:TIGR02169 317 LEDAEERLAKLEAEIdkLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 274 KNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKKHQAFLVETCENNVKELEsildsftvsgqwtsgihKDKD 353
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-----------------KQEW 455
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034664302 354 KppsfsvvLERLRRTLTDYQNKLEDASNELNSMNDVKEKACNELD 398
Cdd:TIGR02169 456 K-------LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-285 |
1.40e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 17 HLEAQiLGAQNSELQAKTNETEKAfQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQR 96
Cdd:COG1196 236 ELEAE-LEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 97 EKNEmeshiretaLEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEhmdcsdLLRRQTSELEFSTQREERL 176
Cdd:COG1196 314 LEER---------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE------LAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 177 RKEFEATTLRVRKLEENIEAE-RAAHLESKfnSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKH 255
Cdd:COG1196 379 EELEELAEELLEALRAAAELAaQLEELEEA--EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270
....*....|....*....|....*....|
gi 1034664302 256 NAQESFAKLNLLEKEYFSKNKKLNEDIEEQ 285
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-284 |
1.58e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 28 SELQAKTNETEK---AFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTL---QEALEkhqreknEM 101
Cdd:TIGR02169 712 SDASRKIGEIEKeieQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhklEEALN-------DL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 102 ESHIRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDcsdlLRRQTSELEfstQREERLRKEFE 181
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE----LQEQRIDLK---EQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 182 ATTLRVRKLEENIEAeraahleskfnseiIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESF 261
Cdd:TIGR02169 858 NLNGKKEELEEELEE--------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
250 260
....*....|....*....|...
gi 1034664302 262 AKLNLLEKEYFSKNKKLNEDIEE 284
Cdd:TIGR02169 924 AKLEALEEELSEIEDPKGEDEEI 946
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-320 |
2.98e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 39 KAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQREKNEMESHIRETALEEFRLQEE 118
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 119 QWEAERRELQfiVQEQDTAVQNMHKKVEKLETEhmdcsdlLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAER 198
Cdd:COG1196 315 EERLEELEEE--LAELEEELEELEEELEELEEE-------LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 199 AAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKL 278
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034664302 279 NEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKKHQAFL 320
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
72-314 |
4.41e-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: 57.76 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 72 EYDLLMKEKSRLEKTLQEALEKHQREKNEMEShiRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETE 151
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQE--LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 152 HMDCSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAE 231
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 232 AVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKK-LNEDIEEQKKVIIDLSKRLQYNEKSCSELQEEL 310
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREEL 470
|
....
gi 1034664302 311 VMAK 314
Cdd:TIGR02168 471 EEAE 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-470 |
4.64e-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: 54.68 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 213 LRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNeDIEEQKKVIIDL 292
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-RLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 293 SKRLQYNEKSCSELQEELVMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSGIHKD-KDKPPSFSVVLERLRRTLTD 371
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEElESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 372 YQNKLEDASNELNSMNDVKEKACNELDSTKQKIDSHTK-----NIKELQDKLADVNKELSHLHTKCADREALISTLKVEL 446
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260
....*....|....*....|....
gi 1034664302 447 QNVLHCWEKEKAQAAQSESELQKL 470
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSL 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
138-705 |
7.71e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 138 VQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLRK---EFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLR 214
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 215 IRDLEgalqvekasqaEAVADLEiiknEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNEdIEEQKKVIIDLSK 294
Cdd:PRK03918 275 IEELE-----------EKVKELK----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 295 RLQYNEKSCSELQEEL-VMAKKHQAFlvETCENNVKELESILDSFTVsgqwtsgihKDKDKPPSFSVVLERLRRTLTDYQ 373
Cdd:PRK03918 339 RLEELKKKLKELEKRLeELEERHELY--EEAKAKKEELERLKKRLTG---------LTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 374 NKLEDASNELNSMNDVKEKACNELDSTKQKI--------DSHTKNI-KELQDKLADVNKELSHLhtkcADREALISTLKV 444
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELlEEYTAELKRIEKELKEI----EEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 445 ELQNVLHCWE---KEKAQAAQSESELQKLSQAFHKDAEEKLTFLHTLYQHLVAgcvLIKQPEGMLDKFswselcavlqEN 521
Cdd:PRK03918 484 ELEKVLKKESeliKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK---LKGEIKSLKKEL----------EK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 522 VDALIADLNRANEKIRHLEyicKNKSDTMRELQQTQEDTFTKVAEQIKAQESCWhrqKKELELQYSELFLEV-QKRAQKF 600
Cdd:PRK03918 551 LEELKKKLAELEKKLDELE---EELAELLKELEELGFESVEELEERLKELEPFY---NEYLELKDAEKELEReEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 601 QEIAEKNMEKLNHIEKSHEQLVLENSHFKKLLSQTQ-----REQMSLLAACALMAGALYPLYSRSCALSTQRDFLQEQVN 675
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590
....*....|....*....|....*....|
gi 1034664302 676 TFELFKLEIRTLAQALSTVEEKKQEEAKMK 705
Cdd:PRK03918 705 EREKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
80-395 |
1.22e-06 |
|
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: 52.59 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 80 KSRLEKTLQEALEKHQreKNEMESHIRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLl 159
Cdd:pfam07888 33 QNRLEECLQERAELLQ--AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 160 rrqtseLEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEII 239
Cdd:pfam07888 110 ------SEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 240 KNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNE------DIEEQKKVIIDLSKRLQYNEKSCSELQEEL--- 310
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaENEALLEELRSLQERLNASERKVEGLGEELssm 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 311 ------VMAKKHQAFLvETCENNVKELESILDSFTVSGQWTS-------GIHKDKDKPPSFSVVLERLRRTLTDYQNKLE 377
Cdd:pfam07888 264 aaqrdrTQAELHQARL-QAAQLTLQLADASLALREGRARWAQeretlqqSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330
....*....|....*...
gi 1034664302 378 DASNELNsmndvKEKACN 395
Cdd:pfam07888 343 KLEVELG-----REKDCN 355
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
50-469 |
1.68e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 50 EECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEaLEKHQREKnemESHIRETALEEFRLQEEQWEAER-RELQ 128
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRE-LEERIEEL---KKEIEELEEKVKELKELKEKAEEyIKLS 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 129 FIVQEQDTAVQNMHKKVEKLETEhmdcSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEA-ERAAHLESKFN 207
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEE----INGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 208 seiiqlRIRDLEGALQVEKasqaeavadleiIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNE------- 280
Cdd:PRK03918 376 ------RLKKRLTGLTPEK------------LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgk 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 281 ---------------DIEEQKKVIIDLSKRLQYNEKSCSELQEELV-----MAKKHQAFLVETCENNVKELESILDSFTv 340
Cdd:PRK03918 438 cpvcgrelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRelekvLKKESELIKLKELAEQLKELEEKLKKYN- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 341 sgqwtsgihkdkdkppsfsvvLERLRRTLTDYQnKLEDASNELNSMNDVKEKACNELDSTKQKIDSHTKNIKELQDKLAD 420
Cdd:PRK03918 517 ---------------------LEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664302 421 VNKELSHLHTKCADR-EALISTLK------VELQNVLHCWEKEKAQAAQSESELQK 469
Cdd:PRK03918 575 LLKELEELGFESVEElEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDK 630
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
27-448 |
1.86e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 52.33 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 27 NSELQAKTNETEKAFQTSQQKWKE-ECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQR--------E 97
Cdd:TIGR04523 128 KLEKQKKENKKNIDKFLTEIKKKEkELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelllsnlK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 98 KNEMESHIRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLR 177
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 178 KEFEatTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNA 257
Cdd:TIGR04523 288 KQLN--QLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 258 QESFAKLNLLEKEyfskNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKKhqaflvetcENNVKELESILDS 337
Cdd:TIGR04523 366 EEKQNEIEKLKKE----NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ---------EKELLEKEIERLK 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 338 FTVSGQwTSGIHKDKDKPPSFSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEKACNELDSTKQKIDSHTKNIKELQDK 417
Cdd:TIGR04523 433 ETIIKN-NSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
410 420 430
....*....|....*....|....*....|.
gi 1034664302 418 LADVNKELSHLHTKCADREALISTLKVELQN 448
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISD 542
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-480 |
2.21e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 81 SRLEKTLQEaLEKHQREKNEMESHIRETALEEFRLQEEQWEAER-RELQFIVQEqdTAVQNMHKKVEKLETEHMDCSDLL 159
Cdd:TIGR02169 170 RKKEKALEE-LEEVEENIERLDLIIDEKRQQLERLRREREKAERyQALLKEKRE--YEGYELLKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 160 RRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAEraahleskfnSEIIQLRIRDLEGALQVEKASQAEAVAdleii 239
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL----------GEEEQLRVKEKIGELEAEIASLERSIA----- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 240 knefkevesAYEREKHNAQESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQynekscsELQEELvmakkhqaf 319
Cdd:TIGR02169 312 ---------EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------ELKEEL--------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 320 lvetcENNVKELESIldsftvsgqwtsgihkdkdkppsfSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEKACNELDS 399
Cdd:TIGR02169 367 -----EDLRAELEEV------------------------DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 400 TKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVELqnvlhcwEKEKAQAAQSESELQKLSQAFHKDAE 479
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL-------SKYEQELYDLKEEYDRVEKELSKLQR 490
|
.
gi 1034664302 480 E 480
Cdd:TIGR02169 491 E 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
81-706 |
2.44e-06 |
|
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: 52.28 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 81 SRLEKTLQEALEKHQREKNEMESHIRETALEEFRLQEEQWEAER--RELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDL 158
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKalEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 159 LRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEA---ERAAHLESKFNSEIIQLRIRDlegaLQVEKASQAEAVAD 235
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeEELKLLAKEEEELKSELLKLE----RRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 236 LEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKK 315
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 316 HQAflvetcENNVKELESILDSFTVSGQwtsgihKDKDKPPSFSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEKACN 395
Cdd:pfam02463 401 SEE------EKEAQLLLELARQLEDLLK------EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 396 ELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVELQNVLHCWEKEKAQAAQSESELQKLSQAFH 475
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 476 KDAE-EKLTFLHTLYQHLVAGCVLIKQPEGMLDKFSWSELCAVLQENVDALIADLNRANEKIRHLEYICKNKSDTMRELQ 554
Cdd:pfam02463 549 VIVEvSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 555 -QTQEDTFTKVAEQIKAQESCWHRQKKELELQYSELFLEVQKRAQKFQEIAEKNMEKLNHIEKSHEQLVLENSHFKKlLS 633
Cdd:pfam02463 629 lKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-QR 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034664302 634 QTQREQMSLLAACALMAGALYPLYSRScalSTQRDFLQEQVNTFELFKLEIRTlaQALSTVEEKKQEEAKMKK 706
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKI---NEELKLLKQKIDEEEEEEEKSRL--KKEEKEEEKSELSLKEKE 775
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
56-537 |
3.49e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 56 EHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQREKNEMESH--IRETALEEfrlQEEQWEAERRELQFIVQE 133
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggDRLEQLER---EIERLERELEERERRRAR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 134 QDTAVQNMH------------------KKVEKLETEHMDCSDLLRRQTSELEFSTQREERLRKEFEAttLRVRKLeeNIE 195
Cdd:COG4913 364 LEALLAALGlplpasaeefaalraeaaALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS--LERRKS--NIP 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 196 AeraahleskfnsEIIQLRiRDLEGALQVeKASQAEAVADLEIIKNEFKEVESAYEREKHNaqesfAKLNLL-EKEYFSK 274
Cdd:COG4913 440 A------------RLLALR-DALAEALGL-DEAELPFVGELIEVRPEEERWRGAIERVLGG-----FALTLLvPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 275 -------NK--------KLNEDIEEQKKVIID---LSKRLQYNEKSCSE-LQEELvmakkHQAFLVETCEnNVKELESIL 335
Cdd:COG4913 501 alrwvnrLHlrgrlvyeRVRTGLPDPERPRLDpdsLAGKLDFKPHPFRAwLEAEL-----GRRFDYVCVD-SPEELRRHP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 336 DSFTVSGQ----WTSGIHKDKDKPPSFSVV--------------LERLRRTLTDYQNKLEDASNELNSMNDVKE--KACN 395
Cdd:COG4913 575 RAITRAGQvkgnGTRHEKDDRRRIRSRYVLgfdnraklaaleaeLAELEEELAEAEERLEALEAELDALQERREalQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 396 ELDSTKQKIDSHTKNIKELQDKLADV---NKELSHLHTKCADREALISTLKVELQNVLHCWEKEKAQAAQSESELQKLSQ 472
Cdd:COG4913 655 EYSWDEIDVASAEREIAELEAELERLdasSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034664302 473 AFHKDAEEKLTFLHTLYQHLVAGCVLIKQPEGMLDKfswselcavLQENVDALIADLNRANEKIR 537
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERELREN---------LEERIDALRARLNRAEEELE 790
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
47-482 |
4.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 47 KWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKtLQEALEKHQREKNEMEShiRETALEEFRLQEEQWEAERRE 126
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE-LKKKLKELEKRLEELEE--RHELYEEAKAKKEELERLKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 127 LQFIVQEQdtaVQNMHKKVEKLETEHMDCSDLLRRQTSELEfstQREERLRKEFEA-------TTLRVRKLEENIEAE-- 197
Cdd:PRK03918 381 LTGLTPEK---LEKELEELEKAKEEIEEEISKITARIGELK---KEIKELKKAIEElkkakgkCPVCGRELTEEHRKEll 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 198 RAAHLE-SKFNSEIIQL--RIRDLEGAL-QVEKA-SQAEAVADLEIIKNEFKEVESayEREKHNAQESFAKLNLLE--KE 270
Cdd:PRK03918 455 EEYTAElKRIEKELKEIeeKERKLRKELrELEKVlKKESELIKLKELAEQLKELEE--KLKKYNLEELEKKAEEYEklKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 271 YFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKKHQAFL----VETCENNVKELESILDSFTvsgqwts 346
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNEYL------- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 347 gihKDKDKPPSfsvvLERLRRTLTDYQNKLEDASNELNSMNDVKEKACNELDSTKQKIDShtKNIKELQDKLADVNKELS 426
Cdd:PRK03918 606 ---ELKDAEKE----LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELA 676
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664302 427 HLHTKCADREALISTLKVELQNVLHcwEKEKAQAAQSESELQKLSQAFHKDAEEKL 482
Cdd:PRK03918 677 GLRAELEELEKRREEIKKTLEKLKE--ELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
178-460 |
4.53e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 178 KEFEATTLRvRKLEENIEAER---AAHLESkFNSEIIQLRIRDLEGALQ--------VEKASQAEAVADLEIIKNEFKEV 246
Cdd:PRK05771 7 KKVLIVTLK-SYKDEVLEALHelgVVHIED-LKEELSNERLRKLRSLLTklsealdkLRSYLPKLNPLREEKKKVSVKSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 247 ESAyerekhnAQESFAKLNLLEKEYFSKNKKLNEdIEEQKKVIIDLSKRLQYNEKSCSELQEELvmAKKH-QAFLVETCE 325
Cdd:PRK05771 85 EEL-------IKDVEEELEKIEKEIKELEEEISE-LENEIKELEQEIERLEPWGNFDLDLSLLL--GFKYvSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 326 NNVKELESILDSFTVsgqwtSGIHKDKDKPPSFSVVLerlrrtltdyQNKLEDASNELNSmNDVKEKACNELDSTKQKID 405
Cdd:PRK05771 155 DKLEELKLESDVENV-----EYISTDKGYVYVVVVVL----------KELSDEVEEELKK-LGFERLELEEEGTPSELIR 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1034664302 406 SHTKNIKELQDKLADVNKELSHLHTKCADreaLISTLKVELQNvlhcwEKEKAQA 460
Cdd:PRK05771 219 EIKEELEEIEKERESLLEELKELAKKYLE---ELLALYEYLEI-----ELERAEA 265
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-453 |
7.33e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 36 ETEKAFQTSQQKwKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQREKNEMESHIRETALEEFRL 115
Cdd:COG4717 75 ELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 116 QEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHmdcSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIE 195
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLAT---EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 196 AERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEF--------KEVESAYEREKHNAQESFAKLNLL 267
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 268 EKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKKHQAFLveTCENNVKELESILDSFTVSG--QWT 345
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDeeELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 346 SGIHKDKDKppsfsvvlERLRRTLTDYQNKLEDASNELNSMNDV--KEKACNELDSTKQKIDSHTKNIKELQDKLADVNK 423
Cdd:COG4717 389 AALEQAEEY--------QELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|..
gi 1034664302 424 ELSHLHT--KCADREALISTLKVELQNVLHCW 453
Cdd:COG4717 461 ELEQLEEdgELAELLQELEELKAELRELAEEW 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
885-1056 |
7.96e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 885 ASLQKQILGFTQRLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQGlqmQLNEFKQSKLITHEKFESACEELNNALLRE 964
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA---EEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 965 EQAQM----LLNEQA---QQLQELNYKLELHSSEEADKNQTLGEAVKSLSEAKMELRRKDQSLRQLNRHLTQLEQDKRRL 1037
Cdd:COG1196 319 EELEEelaeLEEELEeleEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170
....*....|....*....
gi 1034664302 1038 EENIHDAESALRMAAKDKE 1056
Cdd:COG1196 399 AAQLEELEEAEEALLERLE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-1048 |
2.62e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 364 RLRRTLTDYQnKLEDASNELnsmndvkEKACNELDSTKQKidshTKNIKELQDKLADVNKELSHLHTKCADREalISTLK 443
Cdd:TIGR02168 180 KLERTRENLD-RLEDILNEL-------ERQLKSLERQAEK----AERYKELKAELRELELALLVLRLEELREE--LEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 444 VELQNVLHCWEKEKAQAAQSESELQKLSQAFHKDAEEKLTFLHTLYQHLVagcvLIKQPEGMLdkfswselcAVLQENVD 523
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN----EISRLEQQK---------QILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 524 ALIADLNRANEKIRHLEyickNKSDTMRE---LQQTQEDTFTKVAEQIKAQESCWHRQKKELELQYSELFLEVQKRAQKF 600
Cdd:TIGR02168 313 NLERQLEELEAQLEELE----SKLDELAEelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 601 QEI---AEKNMEKLNHIEKSHEQLvleNSHFKKLLSQTQREQMSLLAAcalmagALYPLYSRSCALSTQRDFLQEQVNTF 677
Cdd:TIGR02168 389 AQLelqIASLNNEIERLEARLERL---EDRRERLQQEIEELLKKLEEA------ELKELQAELEELEEELEELQEELERL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 678 ELFKLEIRTLAQALSTVEEKKQEEAKMKKKTFKGLIRIFR------KGVIAVLA-ANRLKILGQSCASLFTWMESFK--- 747
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsEGVKALLKnQSGLSGILGVLSELISVDEGYEaai 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 748 -----EGIGMLVCTGEPQDKhkfpkhqkeqlrclQALSWLTSSDLLAAiisSMAELQDVIGKADPNSR---ICGHLLIGA 819
Cdd:TIGR02168 540 eaalgGRLQAVVVENLNAAK--------------KAIAFLKQNELGRV---TFLPLDSIKGTEIQGNDreiLKNIEGFLG 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 820 AKNSFAKLMDKISLVMEciPLHSSRSITyvekDSLVQ--RLAHGLHKVNTLALKYG---------LRGHVPITKSTASLQ 888
Cdd:TIGR02168 603 VAKDLVKFDPKLRKALS--YLLGGVLVV----DDLDNalELAKKLRPGYRIVTLDGdlvrpggviTGGSAKTNSSILERR 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 889 KQILGFTQRLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQ----GLQMQLNEFKQSKLITHEKFESACEELNNALLRE 964
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 965 EQAQMLLNEQAQQLQELNYKLELHSSEEADKNQ----------TLGEAVKSLSEAKMELRRKDQSLRQ-----------L 1023
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkeelkALREALDELRAELTLLNEEAANLRErleslerriaaT 836
|
730 740
....*....|....*....|....*
gi 1034664302 1024 NRHLTQLEQDKRRLEENIHDAESAL 1048
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
29-467 |
3.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 29 ELQAKTNETEKAfqTSQQKWKEECRRFEHDLEERDNmiqncNREYDLLMKEKSRLEKTLQEALEKHQREKNEMESHIRET 108
Cdd:PTZ00121 1448 EAKKKAEEAKKA--EEAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 109 A--LEEFRLQEEQWEA-------ERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLRKE 179
Cdd:PTZ00121 1521 AkkADEAKKAEEAKKAdeakkaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 180 FEATTL----RVRKLEE-NIEAE--RAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYER 252
Cdd:PTZ00121 1601 YEEEKKmkaeEAKKAEEaKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 253 EKHNAQESFAKLNLLEK-EYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQ-EELVMAKKHQAFLVETCENN--- 327
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEaEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKkEAEEDKKKAEEAKKDEEEKKkia 1760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 328 --VKELESILDSFTVSGQWTSGIHKDKDKPPSFSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEKACNELDSTKQKID 405
Cdd:PTZ00121 1761 hlKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKN 1840
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034664302 406 SHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVELQNVLHCWEKEKAQAAQSESEL 467
Cdd:PTZ00121 1841 MQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
909-1154 |
5.86e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 909 RLE--VTEFKRSVNEMKKELDKAQGLQMQLNEFKQSKL-ITHEKFESACEELNNALLREEQAQMLLNEQAQQLQELNYKL 985
Cdd:TIGR02168 190 RLEdiLNELERQLKSLERQAEKAERYKELKAELRELELaLLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 986 ELHSSEEADKNQTLGEAVKSLSEAKMELRRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESALRMAAKDkecvanhmrav 1065
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE----------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 1066 entLHKVRDQISLswSAASRNDFTLQLPKLHLETFAMEGLKGGPEvvacqamiksfmDVYQLASTRIMTLEKEMTSHRSH 1145
Cdd:TIGR02168 339 ---LAELEEKLEE--LKEELESLEAELEELEAELEELESRLEELE------------EQLETLRSKVAQLELQIASLNNE 401
|
....*....
gi 1034664302 1146 IAALKSELH 1154
Cdd:TIGR02168 402 IERLEARLE 410
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
26-474 |
6.12e-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: 47.42 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 26 QNSELQAKTNETEKAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREY-------DLLMKEKSRLEKTLQEAL-EKHQRE 97
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELtearterDQFSQESGNLDDQLQKLLaDLHKRE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 98 KN---EMESHIR--------ETALEEFR--LQEEQWEAER---------RELQFIVQEQDTAVQNMHKKVEK---LETEH 152
Cdd:pfam15921 391 KElslEKEQNKRlwdrdtgnSITIDHLRreLDDRNMEVQRleallkamkSECQGQMERQMAAIQGKNESLEKvssLTAQL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 153 MDCSDLLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERA--AHLESKFNSEIIQLR--------IRDLEGAL 222
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAeiTKLRSRVDLKLQELQhlknegdhLRNVQTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 223 QVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNE-DIEEQKKviidlSKRLQYNEK 301
Cdd:pfam15921 551 EALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfKILKDKK-----DAKIRELEA 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 302 SCSELQEELVMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSGIHKD--------KDKPPSFSVVLERLRRTLTDYQ 373
Cdd:pfam15921 626 RVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDyevlkrnfRNKSEEMETTTNKLKMQLKSAQ 705
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 374 NKLEDASNELNSMNDVKEKAC-------NELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVEL 446
Cdd:pfam15921 706 SELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
490 500 510
....*....|....*....|....*....|....*
gi 1034664302 447 QN------VLHCWEKE-KAQAAQSESELQKLSQAF 474
Cdd:pfam15921 786 NKmageleVLRSQERRlKEKVANMEVALDKASLQF 820
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
26-469 |
1.68e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 26 QNSELQAKTNETEKAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQRE----KNEM 101
Cdd:pfam12128 277 RQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQlpswQSEL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 102 ESHIRETALEEFRLQEEQWEAERRElQFIVQEQDTAVQNMHKKVEKL----ETEHMDCSDLLRRQTSElefstqreerLR 177
Cdd:pfam12128 357 ENLEERLKALTGKHQDVTAKYNRRR-SKIKEQNNRDIAGIKDKLAKIrearDRQLAVAEDDLQALESE----------LR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 178 KEFEATTLRVRKLEENIEaERAAHL-----------ESKFNSEIIQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEV 246
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLK-SRLGELklrlnqatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQA 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 247 ESAYEREKHNAQESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSC-SELQEELVMAKKHQAFLVETCE 325
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHrTDLDPEVWDGSVGGELNLYGVK 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 326 NNVK------------ELESILDSFTVSGQWTSGIHKDKDKPPS-FSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEK 392
Cdd:pfam12128 585 LDLKridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVqANGELEKASREETFARTALKNARLDLRRLFDEKQS 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 393 ---ACNE-LDSTK-------QKIDSHTK-NIKELQDKLADVNKELSHLHT-KCADREALISTLKVELQNVLHCWEKEKAQ 459
Cdd:pfam12128 665 ekdKKNKaLAERKdsanerlNSLEAQLKqLDKKHQAWLEEQKEQKREARTeKQAYWQVVEGALDAQLALLKAAIAARRSG 744
|
490
....*....|
gi 1034664302 460 AAQSESELQK 469
Cdd:pfam12128 745 AKAELKALET 754
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
85-309 |
2.06e-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: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 85 KTLQEALEKHQREKNEMESHIRETaleefrlqeeqwEAERRELQFIVQEQDTAVQNMHKKVEKLETEhmdcsdlLRRQTS 164
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAAL------------KKEEKALLKQLAALERRIAALARRIRALEQE-------LAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 165 ELEFSTQREERLRKEFEATTLRVRKLEENIE-AERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAvADLEIIKNEF 243
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKEELAELLRALYrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA-EELRADLAEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034664302 244 KEVESAYEREKhnaqesfAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEE 309
Cdd:COG4942 163 AALRAELEAER-------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
27-315 |
2.22e-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: 45.40 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 27 NSELQAKTNETEKaFQTSQQKWKEECRRFEHDLEERDNMIQNcnreydllmkeKSRLEKTLQEALEKHQREKNEMESHIr 106
Cdd:TIGR04523 362 QRELEEKQNEIEK-LKKENQSYKQEIKNLESQINDLESKIQN-----------QEKLNQQKDEQIKKLQQEKELLEKEI- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 107 etalEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLRKEFEATTLR 186
Cdd:TIGR04523 429 ----ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 187 VRKLEENIeaeraahleSKFNSEIIQLRIRdlEGALQVEKASQAEAVADLE--IIKNEFKEVESAYEREKHNAQESFAKL 264
Cdd:TIGR04523 505 KKELEEKV---------KDLTKKISSLKEK--IEKLESEKKEKESKISDLEdeLNKDDFELKKENLEKEIDEKNKEIEEL 573
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034664302 265 NLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKK 315
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
19-420 |
2.69e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 19 EAQILGAQNSELQAKTNETEKAFQTSQQKWKEECRRFEHDLEERDNMIQNCNreydllmkeksrLEKTLQEALEKHQREK 98
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG------------LDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 99 NEMESHIRETaLEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREERLRK 178
Cdd:PRK02224 320 EDRDEELRDR-LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 179 EFEATTLRVRKLEENIEA---------ERAAHLESKFNSeiIQLRIR----------------DLEGALQVEKASQ---- 229
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEElreerdelrEREAELEATLRT--ARERVEeaealleagkcpecgqPVEGSPHVETIEEdrer 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 230 -AEAVADLEIIKNEFKEVESAYEREKhNAQESFAKLNLLEKeyfsKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQE 308
Cdd:PRK02224 477 vEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEE----RREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 309 EL-----VMAKKHQAflVETCENNVKELESILDSFTVSgqwtsgihkdkdkppsfsvvLERLRRtLTDYQNKLEDASNEL 383
Cdd:PRK02224 552 EAeekreAAAEAEEE--AEEAREEVAELNSKLAELKER--------------------IESLER-IRTLLAAIADAEDEI 608
|
410 420 430
....*....|....*....|....*....|....*...
gi 1034664302 384 NSMNDvKEKACNEL-DSTKQKIDSHTKNIKELQDKLAD 420
Cdd:PRK02224 609 ERLRE-KREALAELnDERRERLAEKRERKRELEAEFDE 645
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
921-1091 |
2.96e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 921 EMKKELD--KAQGLQMQLNEFKQSKLITHEKFESACEELNNALLREEQAQMLLNEQAQQLQELNYKLELHSSEEADKNQT 998
Cdd:COG1196 217 ELKEELKelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 999 LGEAVKSLSEAKMELRRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESALRMAAKDKECVANHMRAVENTLHKV---RDQ 1075
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAeaeLAE 376
|
170
....*....|....*.
gi 1034664302 1076 ISLSWSAASRNDFTLQ 1091
Cdd:COG1196 377 AEEELEELAEELLEAL 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
76-310 |
3.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 76 LMKEKSRLEKTLQEALEkHQREKNEMESHIRET-----ALEEFRLQEEQWEAERRELQFIVQEQDTA-VQNMHKKVEKLE 149
Cdd:COG4913 216 YMLEEPDTFEAADALVE-HFDDLERAHEALEDAreqieLLEPIRELAERYAAARERLAELEYLRAALrLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 150 TEhmdcsdlLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLESkfnseiIQLRIRDLEGALQVEKASQ 229
Cdd:COG4913 295 AE-------LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 230 AEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEyfsknkkLNEDIEEQKKVIIDLSKRLQynekscsELQEE 309
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA-------LEEALAEAEAALRDLRRELR-------ELEAE 427
|
.
gi 1034664302 310 L 310
Cdd:COG4913 428 I 428
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
14-471 |
3.73e-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: 44.71 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 14 VNVHLEAQIlgAQNSELQAKTNETE---KAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLM---------KEKS 81
Cdd:pfam05483 132 VSLKLEEEI--QENKDLIKENNATRhlcNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMIlafeelrvqAENA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 82 RLEK--TLQEALEKHQREKNEMESHI--RETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVeKLETEHMDCS- 156
Cdd:pfam05483 210 RLEMhfKLKEDHEKIQHLEEEYKKEIndKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKT-KLQDENLKELi 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 157 ---DLLRRQTSELEFSTQR----EERLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIR----DLEGALQVE 225
Cdd:pfam05483 289 ekkDHLTKELEDIKMSLQRsmstQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEattcSLEELLRTE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 226 KASQAEAVADLEIIKNEFKEVESAYE---REKHNAQESFAKLN--LLEKE-YFSKNKKLNEDIEEQKKVIIDLSKRLQYN 299
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEemtKFKNNKEVELEELKkiLAEDEkLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 300 EKSCSELQEELVMAKKHQAFLVETCENNVKELES---------------ILDSFTVSGQWTSGIHKDKDKPPSFSVVLER 364
Cdd:pfam05483 449 EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklknieltahcdklLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 365 LRRTLTDYQNKLEDASNELNSMNDVKEKACNELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADreaLISTLKV 444
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN---LKKQIEN 605
|
490 500
....*....|....*....|....*..
gi 1034664302 445 ELQNVLHCWEKEKAQAAQSESELQKLS 471
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLN 632
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
355-573 |
3.78e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 355 PPSFSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEKACNELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCAD 434
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 435 REALISTLKVELQNVLhcwekEKAQAAQSESELQ-KLSQAFHKDAEEKLTFLHTLYQHLVAgcvLIKQPEGMLDKFswSE 513
Cdd:COG4942 95 LRAELEAQKEELAELL-----RALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAEL--AA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 514 LCAVLQENVDALIADLNRANEKIRHLEYICKNKSDTMRELQQTQEDTFTKVAEQIKAQES 573
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
16-425 |
3.88e-04 |
|
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: 44.73 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 16 VHLEAQILGAQNSELQAKT------NETEKAFQTSQQKWKEECRRFE------HDLEERDNMIQNCNREydllMKEKSRL 83
Cdd:pfam05557 5 IESKARLSQLQNEKKQMELehkrarIELEKKASALKRQLDRESDRNQelqkriRLLEKREAEAEEALRE----QAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 84 EKTLQEALEKHQREKNEMESHIRETALE-EFRLQEEQWEAERRELQFIVQ------------EQDTAVQNMHKKVEKLET 150
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISClKNELSELRRQIQRAELELQSTnseleelqerldLLKAKASEAEQLRQNLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 151 EHMDCSDlLRRQTSELEFSTQREER---LRKEFEATTLRVRKLEENIEA--ERAAHL-ESKFNSEIIQLRIRDLEGALQV 224
Cdd:pfam05557 161 QQSSLAE-AEQRIKELEFEIQSQEQdseIVKNSKSELARIPELEKELERlrEHNKHLnENIENKLLLKEEVEDLKRKLER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 225 EKASQAEAVA---DLEIIKNEFKEVESAYEREKHNAQESFA-----------KLNLLEKEYFSKN---------KKLNED 281
Cdd:pfam05557 240 EEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDlsrrieqlqqrEIVLKEENSSLTSsarqlekarRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 282 IEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSG---IHKDKDKPPSF 358
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLLERIEEAedmTQKMQAHNEEM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 359 SVVLERLRRTLTDYQNKLEDASNELNSMNdvKEKACNELDSTKQKIDSHTKNIKELQ---DKLADVNKEL 425
Cdd:pfam05557 400 EAQLSVAEEELGGYKQQAQTLERELQALR--QQESLADPSYSKEEVDSLRRKLETLElerQRLREQKNEL 467
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-236 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 17 HLEAQILGAQNSELQAKTNETEKAFQtsQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKTLQEALEKHQR 96
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEE--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 97 EKNEMESHIRETALEEFRLQ--EEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHmdcsDLLRRQTSELEFSTQREE 174
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEelEEAEEALLERLERLEEELEELEEALAELEEEEEEEE----EALEEAAEEEAELEEEEE 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034664302 175 RLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLEGALQVEKASQAEAVADL 236
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
15-426 |
5.44e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 15 NVHLEAQILGAQNSELQAKTNETEkafqtSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEKSRLEKtLQEALEKH 94
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELE-----EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 95 QREKNEMESHIRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEK-------LETEHMdcSDLLRRQTSELE 167
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHR--KELLEEYTAELK 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 168 fstqreeRLRKEFEATTLRVRKLEEnieaeRAAHLESKFNSEIIQLRIRDLegALQVEKASQAEAVADLEIIKNEFKEVE 247
Cdd:PRK03918 463 -------RIEKELKEIEEKERKLRK-----ELRELEKVLKKESELIKLKEL--AEQLKELEEKLKKYNLEELEKKAEEYE 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 248 SAYErekhnaqesfaKLNLLEKEYFSKNKKLNEdIEEQKKVIIDLSKRLQYNEKSCSELQEELvmaKKHQAFLVETCENN 327
Cdd:PRK03918 529 KLKE-----------KLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEEELAELLKEL---EELGFESVEELEER 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 328 VKELESILDSFtvsgqwtsgihkdkdkppsfsvvlerlrrtltdyqNKLEDASNELNSMNDVKEKACNELDSTKQKIDSH 407
Cdd:PRK03918 594 LKELEPFYNEY-----------------------------------LELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
410
....*....|....*....
gi 1034664302 408 TKNIKELQDKLADVNKELS 426
Cdd:PRK03918 639 EKRLEELRKELEELEKKYS 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
365-641 |
6.27e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 365 LRRTLTDYQNKLEDASNELNSMNDVK-------EKACNELDSTKQKIDShTKNIKElqDKLADVNKELSHLHTKCADREA 437
Cdd:pfam15921 108 LRQSVIDLQTKLQEMQMERDAMADIRrresqsqEDLRNQLQNTVHELEA-AKCLKE--DMLEDSNTQIEQLRKMMLSHEG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 438 LIStlkvELQNVLHCWEKEKAQAAQSESELQKLS-QAFHKDAEEKLTFLHTLYQHLVAGCVLIKQPEGMLDKFSWSELCA 516
Cdd:pfam15921 185 VLQ----EIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKIEL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 517 VLQENVDALIADLNRANEKIRHLeyicKNKSDTMRELQQTQEDTFTKVAEQIKAQESCWHRQKKELELQYSELFLEVQKR 596
Cdd:pfam15921 261 LLQQHQDRIEQLISEHEVEITGL----TEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREA 336
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034664302 597 AQKFQEiaeknmeklnHIEKSHEQLVLENSHFKKllSQTQREQMS 641
Cdd:pfam15921 337 KRMYED----------KIEELEKQLVLANSELTE--ARTERDQFS 369
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
14-472 |
7.12e-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: 43.94 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 14 VNVHLEAQILGAQNSELQAKTNETEKAFqtsqqKWKEECRRFEHDLEERDNMIQNCNREYDLLM---KEKSRLEKTLQEA 90
Cdd:pfam05483 188 LNNNIEKMILAFEELRVQAENARLEMHF-----KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLiqiTEKENKMKDLTFL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 91 LEKHQREKNEME--SHIRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEF 168
Cdd:pfam05483 263 LEESRDKANQLEekTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 169 STQREERLRKEFEATTLRV--------RKLEENIEAERAAHLESKFNSEIIQlRIRDLEGALQVEKASQAEAVADLEIIK 240
Cdd:pfam05483 343 AKAAHSFVVTEFEATTCSLeellrteqQRLEKNEDQLKIITMELQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 241 NEFKEVESAYEREKHNAQESFAKLNLLEKE-----------------YFSKNKKLNEDIEEQKKVIIDLS----KRLQYN 299
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQELIFLLQAREKEihdleiqltaiktseehYLKEVEDLKTELEKEKLKNIELTahcdKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 300 EKSCSELQEELVMAKKHQaflvETCENNVKELESILDsftvsgQWTSGIHKDKDKPPSFSVVLERLRRTLTDYQNKLEDA 379
Cdd:pfam05483 502 KELTQEASDMTLELKKHQ----EDIINCKKQEERMLK------QIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 380 SNELNSMN----------DVKEKACNELdstKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVELQNV 449
Cdd:pfam05483 572 EENARSIEyevlkkekqmKILENKCNNL---KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
|
490 500
....*....|....*....|...
gi 1034664302 450 LHCWEkEKAQAAQSESELQKLSQ 472
Cdd:pfam05483 649 KQKFE-EIIDNYQKEIEDKKISE 670
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
10-710 |
7.36e-04 |
|
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: 43.88 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 10 KTKVVNVHLEAQILgAQNSELQAKTNETEKAFQTSQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKeksrLEKTLQe 89
Cdd:TIGR00606 199 GQKVQEHQMELKYL-KQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIK- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 90 ALEKHQREKNEMESHIRETALEEFRLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEhmdcSDLLRRQTSELEFS 169
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKE----RRLLNQEKTELLVE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 170 TQR--------------------EERLRKEFE--------------ATTLRVRKLEEniEAERAAHLESKFNSEI----- 210
Cdd:TIGR00606 349 QGRlqlqadrhqehirardsliqSLATRLELDgfergpfserqiknFHTLVIERQED--EAKTAAQLCADLQSKErlkqe 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 211 ----IQLRIRDLEGALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQE---SFAKLNLLEKEYFSKNKKLNEDIE 283
Cdd:TIGR00606 427 qadeIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQElrkAERELSKAEKNSLTETLKKEVKSL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 284 EQKKVIIDLSKRL------QYNEKSCSELQEELVMAKKHQAF--LVETCENNVKELESILDSFTVSGQWTSGIHKD---- 351
Cdd:TIGR00606 507 QNEKADLDRKLRKldqemeQLNHHTTTRTQMEMLTKDKMDKDeqIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKskei 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 352 ---KDKPPSFSVVLERLRRTLTDYQNKLEDASNELNSMNDVKEKACN------ELDSTKQKIDSHTKNIKELQDKLADVN 422
Cdd:TIGR00606 587 nqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGsqdeesDLERLKEEIEKSSKQRAMLAGATAVYS 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 423 KELSHLHTK---CADREALISTLKVELQNVLHCWEKEKAQAAQSESELQKLSQAFHKDAEEKLTFLHTLYQHLVAGCVLI 499
Cdd:TIGR00606 667 QFITQLTDEnqsCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 500 KQPEGMLDKFSWSelCAVLQENVDALIADLNRANEKIRHLEyICKNKSDTMRELQQTQEDTFTKVAEQIKAQESCwhrqk 579
Cdd:TIGR00606 747 PELRNKLQKVNRD--IQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQGS----- 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 580 kELELQYSELFLEVQKRAQKFQEIAEKNMEKLNHIEKSHEQLvlenSHFKKLLSQTQREQMSL---LAACALMAGALYPL 656
Cdd:TIGR00606 819 -DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI----QHLKSKTNELKSEKLQIgtnLQRRQQFEEQLVEL 893
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1034664302 657 YSRSCALSTQRDFLQEQVNTFELFKLEIRTLAQALSTVEEKKQEEAKMKKKTFK 710
Cdd:TIGR00606 894 STEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
897-1056 |
7.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 897 RLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQ----GLQMQLNEFKQSKLITHEKFESACEELNNALLREEQAQMLLN 972
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEaelaELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 973 EQAQQLQELNYKLELHSSEEADKNQTLGEAVKSLSEAKMELRRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESALRMAA 1052
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
....
gi 1034664302 1053 KDKE 1056
Cdd:COG1196 386 EELL 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
71-636 |
8.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 8.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 71 REYDLLMKEKSRLEKTLQEALEKHQREKNEMESHIRETALEEfrlqeeqwEAERRELQFIVQEQDTAVQNMHKKVEKLET 150
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAE--------EAKKKAEDARKAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 151 EHMDCSDLLRR--QTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAHLESKFNSEiiqlRIRDLEGALQVEKAS 228
Cdd:PTZ00121 1149 EDAKRVEIARKaeDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE----EERKAEEARKAEDAK 1224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 229 QAEAVADLEIIKnefKEVESAYEREKHNAQESFAKLNLLEKEYFSKN---------------------KKLNEDIEEQKK 287
Cdd:PTZ00121 1225 KAEAVKKAEEAK---KDAEEAKKAEEERNNEEIRKFEEARMAHFARRqaaikaeearkadelkkaeekKKADEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 288 VIIDLSKRLQYNEKSCSELQEELVMAKKHQAFLVETCENNVKELESildSFTVSGQWTSGIHKDKDKPPSFSVVLERLRR 367
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA---AKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 368 TLTDYQNKLEDA--SNELNSMNDVKEKACNELdstkQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVE 445
Cdd:PTZ00121 1379 KADAAKKKAEEKkkADEAKKKAEEDKKKADEL----KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 446 lqnvlhcwEKEKAQAAQSESELQKLSQAFHKDAEEKLTFLHtlyqhlvagcvLIKQPEGMLDKFSWSELCAVLQENVDal 525
Cdd:PTZ00121 1455 --------EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADE-----------AKKKAEEAKKKADEAKKAAEAKKKAD-- 1513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 526 iaDLNRANEkirhleyicKNKSDTMRELQQTQEDTFTKVAEQIKAQESCwhRQKKELELQYSELFLEVQKRAQKFQEIAE 605
Cdd:PTZ00121 1514 --EAKKAEE---------AKKADEAKKAEEAKKADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
570 580 590
....*....|....*....|....*....|.
gi 1034664302 606 KNMEKLNHIEKSHEQLVLENSHFKKLLSQTQ 636
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
891-1056 |
1.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 891 ILGFT--QRLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQGLQMQLnefkqsklithekfeSACEELNNALLREEQAQ 968
Cdd:COG4913 603 VLGFDnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL---------------QRLAEYSWDEIDVASAE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 969 MLLNEQAQQLQELnyklelhsseEADkNQTLGEAVKSLSEAKMELRRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESAL 1048
Cdd:COG4913 668 REIAELEAELERL----------DAS-SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
....*...
gi 1034664302 1049 RMAAKDKE 1056
Cdd:COG4913 737 EAAEDLAR 744
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
885-1041 |
1.40e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 885 ASLQKQILGFTQRLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQGLQMQLNEFKQSKLITHEkfesaceelnnallrE 964
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE---------------I 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034664302 965 EQAQMLLNEQAQQLQELNYKLELHSSEEADKNQTLGEAVKSLSEAKMELrrkDQSLRQLNRHLTQLEQDKRRLEENI 1041
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKI 172
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
882-1048 |
1.65e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 882 KSTASLQKQILGFTQRLhaaeverRSLRLEVTEFKRSVNEMKKE----LDKAQgLQMQLNEfkqskliTHEKFESACEEL 957
Cdd:PRK11281 80 EETEQLKQQLAQAPAKL-------RQAQAELEALKDDNDEETREtlstLSLRQ-LESRLAQ-------TLDQLQNAQNDL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 958 N--NALL-----REEQAQMLLNEQAQQLQELNykLELHSSEEADKN-----QTLGEAVKSLSEAKMELRRKD-------Q 1018
Cdd:PRK11281 145 AeyNSQLvslqtQPERAQAALYANSQRLQQIR--NLLKGGKVGGKAlrpsqRVLLQAEQALLNAQNDLQRKSlegntqlQ 222
|
170 180 190
....*....|....*....|....*....|
gi 1034664302 1019 SLRQLNRHLTQLEQDkrRLEENIHDAESAL 1048
Cdd:PRK11281 223 DLLQKQRDYLTARIQ--RLEHQLQLLQEAI 250
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
880-1053 |
1.78e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 880 ITKSTASLQKQILGFTQRLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQG-LQMQLNEFKQSKLITHEKFESACEELN 958
Cdd:COG4942 53 LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEeLAELLRALYRLGRQPPLALLLSPEDFL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 959 ---------NALLREEQAQML-LNEQAQQLQELNYKLELHSSEEADKNQTLGEAVKSLSEAKME----LRRKDQSLRQLN 1024
Cdd:COG4942 133 davrrlqylKYLAPARREQAEeLRADLAELAALRAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELA 212
|
170 180
....*....|....*....|....*....
gi 1034664302 1025 RHLTQLEQDKRRLEENIHDAESALRMAAK 1053
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
901-1077 |
1.89e-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: 42.75 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 901 AEVERRSLRLEvtEFKRSVNEMKKELDKAQGLqmqLNEFKQSKLITHEKFESACEELNNALLREEQAQMLLNEQAQQLQE 980
Cdd:TIGR02169 674 AELQRLRERLE--GLKRELSSLQSELRRIENR---LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 981 LNYKLELHSSEEADKNQTLGEAVKSLSEAKMEL-----RRKDQSLRQLNRHLTQLEQDKRRLEENIHDAESALRMAAKDK 1055
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180
....*....|....*....|..
gi 1034664302 1056 ECVANHMRAVENTLHKVRDQIS 1077
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIK 850
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
178-469 |
1.91e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 178 KEFEATTLRVRKLEENIEAERAAHLESKFNSEIIQLRIRDLE------------GALQVEKASQAEAVADLEIIKNEFKE 245
Cdd:pfam05701 70 EELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEqgiadeasvaakAQLEVAKARHAAAVAELKSVKEELES 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 246 VESAY-----ERE--KHNAQESFAKLNLLEKEYFSKNKKLNE-------------DIEEQK--------KVIIDLSKRLQ 297
Cdd:pfam05701 150 LRKEYaslvsERDiaIKRAEEAVSASKEIEKTVEELTIELIAtkeslesahaahlEAEEHRigaalareQDKLNWEKELK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 298 YNEKSCSELQEELVMAKKHQAFLvETCENNVKELESILDSFTVS--GQWTSGIHKDKDKPPSFSVVLERLRRTLTDYQNK 375
Cdd:pfam05701 230 QAEEELQRLNQQLLSAKDLKSKL-ETASALLLDLKAELAAYMESklKEEADGEGNEKKTSTSIQAALASAKKELEEVKAN 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 376 LEDASNELNSMNDV---------KEKAcnELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHTKCADREALISTLKVEL 446
Cdd:pfam05701 309 IEKAKDEVNCLRVAaaslrseleKEKA--ELASLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQL 386
|
330 340
....*....|....*....|...
gi 1034664302 447 QNVLHCWEKEKAQAAQSESELQK 469
Cdd:pfam05701 387 QQAAQEAEEAKSLAQAAREELRK 409
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
220-473 |
2.48e-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: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 220 GALQVEKASQAEAVADLEIIKNEFKEVESAYEREKHNAQESFAKLNLLEKEYfsknKKLNEDIEEQKKVIIDLSKRLQYN 299
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEY----NELQAELEALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 300 EKSCSELQEELvmakKHQAFLVETCENNVKELESILDSftvsgqwtsgihkdkdkpPSFSVVLERL--RRTLTDYQNKLe 377
Cdd:COG3883 78 EAEIEERREEL----GERARALYRSGGSVSYLDVLLGS------------------ESFSDFLDRLsaLSKIADADADL- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 378 dasneLNSMNDVKEKACNELDSTKQKIDSHTKNIKELQDKLADVNKELshlhtkcADREALISTLKVELQNVLHCWEKEK 457
Cdd:COG3883 135 -----LEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ-------AEQEALLAQLSAEEAAAEAQLAELE 202
|
250
....*....|....*.
gi 1034664302 458 AQAAQSESELQKLSQA 473
Cdd:COG3883 203 AELAAAEAAAAAAAAA 218
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
235-424 |
3.12e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 235 DLEIIKNEFKEVESAYEREkhnAQESFAKLNLLEKEYF------SKNKKLNedieeqkKVIIDLSKRLQYNEKSCSELQE 308
Cdd:TIGR01612 1545 DSEIIIKEIKDAHKKFILE---AEKSEQKIKEIKKEKFrieddaAKNDKSN-------KAAIDIQLSLENFENKFLKISD 1614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 309 elvMAKKHQAFLVETcennvKELESILDSFTVSGQWTSgIHKDKDKPPSFSVVLERLRrtltDYQNKLEDASNELNSMNd 388
Cdd:TIGR01612 1615 ---IKKKINDCLKET-----ESIEKKISSFSIDSQDTE-LKENGDNLNSLQEFLESLK----DQKKNIEDKKKELDELD- 1680
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034664302 389 vkekacNELDSTKQKIDSHTKN----IKELQDKLADVNKE 424
Cdd:TIGR01612 1681 ------SEIEKIEIDVDQHKKNyeigIIEKIKEIAIANKE 1714
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
132-315 |
3.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 132 QEQDTAVQNMHKKVEKLETEhmdcsdlLRRQTSELEFSTQREERLRKEFEATTLRVRKLEENIEAERAAhLESKfnSEII 211
Cdd:COG3883 19 QAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE-IEER--REEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 212 QLRIRDL------EGALQV--------EKASQAEAV-----ADLEIIkNEFKEVESAYEREKHNAQESFAKLNLLEKEYF 272
Cdd:COG3883 89 GERARALyrsggsVSYLDVllgsesfsDFLDRLSALskiadADADLL-EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034664302 273 SKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEELVMAKK 315
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
885-1077 |
4.74e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 885 ASLQKQILGFTQRLHAAEVERRSLRLEVTEFKRSVNEMKKELDKAQGlQMQLNEFKQSKLITHEkfesacEELNNAL--L 962
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEI------AELRAELeaQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 963 REEQAQMLLneQAQQLQELNYKLELHSSEEADKNQTLGEAVKSLSEAkmelrRKDQsLRQLNRHLTQLEQDKRRLEENIH 1042
Cdd:COG4942 103 KEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA-----RREQ-AEELRADLAELAALRAELEAERA 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1034664302 1043 DAESALRMAAKDKECVANHMRAVENTLHKVRDQIS 1077
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
906-1040 |
7.10e-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: 40.77 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 906 RSLRLEVTEFKRSVNEMKKELDKAQ----GLQMQLNEFKQSKLITHEKFESACEELNNALLREEQAQMLLNEQAQQLQEL 981
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQqeinEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034664302 982 NYKLE-LHSSEEADKNQTLGEAVKS----LSEAKMELRRKDQSLRQLNRHLTQLEQDKRRLEEN 1040
Cdd:TIGR04523 294 KSEISdLNNQKEQDWNKELKSELKNqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
28-430 |
9.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 28 SELQAKTNETEKafqtsQQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEksrlektlqeaLEKHQREKNEMESHIRE 107
Cdd:PRK01156 332 SVLQKDYNDYIK-----KKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKK-----------IEEYSKNIERMSAFISE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 108 TALEEFrLQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDcsdlLRRQTSELE-----------FSTQREERL 176
Cdd:PRK01156 396 ILKIQE-IDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE----LSRNMEMLNgqsvcpvcgttLGEEKSNHI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 177 RKEFEATTLR----VRKLEENIEA--ERAAHLEsKFNSEIIQLRIRDLEGALQVEKASQAEaVADLEIIKNEFKEVESAY 250
Cdd:PRK01156 471 INHYNEKKSRleekIREIEIEVKDidEKIVDLK-KRKEYLESEEINKSINEYNKIESARAD-LEDIKIKINELKDKHDKY 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 251 EREKH--------------------NAQESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIIDLSKRLQYNEKSCSELQEEl 310
Cdd:PRK01156 549 EEIKNrykslkledldskrtswlnaLAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 311 VMAKKHQAFLVETCENNVKELESILDSFTVSGQWTSGIHKDKdkppsfsvvlerlrRTLTDYQNKLEDASNELNSMNDvk 390
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDL--------------KEITSRINDIEDNLKKSRKALD-- 691
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1034664302 391 eKACNELDSTKQKIDSHTKNIKELQDKLADVNKELSHLHT 430
Cdd:PRK01156 692 -DAKANRARLESTIEILRTRINELSDRINDINETLESMKK 730
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
45-291 |
9.73e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 45 QQKWKEECRRFEHDLEERDNMIQNCNREYDLLMKEK----SRLEKTLQEAlEKHQREKNEMESHIRET-------ALEEF 113
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARlqalEDLEKILTEK-EALQGKINILEMRLSETdariklaAQEKI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 114 R--LQEEQWEAERRELQFIVQEQDTAVQNMHKKVEKLETEHMDCSDLLRRQTSELEFSTQREER---LRKEFEATTLRVR 188
Cdd:PLN02939 195 HveILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERvfkLEKERSLLDASLR 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034664302 189 KLE-------------------------ENIEA--ERAA-HLEskfNSEIIQLRIRDLEGALQVEKASQAEAVAD----- 235
Cdd:PLN02939 275 ELEskfivaqedvsklsplqydcwwekvENLQDllDRATnQVE---KAALVLDQNQDLRDKVDKLEASLKEANVSkfssy 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034664302 236 -LEIIKNEFKEVESAYEREKHnaqESFAKLNLLEKEYFSKNKKLNEDIEEQKKVIID 291
Cdd:PLN02939 352 kVELLQQKLKLLEERLQASDH---EIHSYIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| |
