|
Name |
Accession |
Description |
Interval |
E-value |
| SMYLE_N |
pfam18615 |
Short myomegalin-like EB1 binding proteins, N-terminal domain; This N-terminal region is found ... |
1-376 |
0e+00 |
|
Short myomegalin-like EB1 binding proteins, N-terminal domain; This N-terminal region is found in SMYLE (for short myomegalin-like EB1 binding protein). It includes the SMYLE homology (SmyH) domain found in the first 100 residues at the N terminus. This conserved SmyH domain is required and sufficient for PKA scaffolding protein AKAP9, and the pericentrosomal protein CDK5RAP2 binding.
Pssm-ID: 465822 Cd Length: 387 Bit Score: 678.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 1 MKEICRICARELCGNQRRWIFHTASKLNLQVLLSHVLGKDVPRDGKAEFACSKCAFMLDRIYRFDTVIARIEALSIERLQ 80
Cdd:pfam18615 1 MKEACRICARELCGNQRRWIFHPAAKLNLQVLLSHALGRELTRDGRGEFACSKCAFMLDRMYRFDTVIARVEALSIERLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 81 KLLLEKDRLKFCIASMYRKNN-DDSGAEIKAGNGTVDMSVLPDARYSALLQEDFAYSGFECWVENEDQIQEPHSCHGSEG 159
Cdd:pfam18615 81 KLLLEKDRLRQCIAGLYRKNNsEESGPEDKVGDGTVDLSGLPDARYSALLQEDLAYSGYESWAEHEEQALDHHHCHASEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 160 PGNRPRRCRGCAALRVADSDYEAICKVPRKVARSISCGPSSRWSTSICTEEPALSEVGPPDLASTKVPPDGESMEEETPG 239
Cdd:pfam18615 161 PGSRPRRCRGCAALRVADSDYEAVCKVPRKVARSISCGPSTRYSASTGNEEPSVSELGPATLGNTKSPCEGESMEEGSPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 240 SSVESLDASVQ-ASPPQQKDEETERSAKELGKCDCCSDD--QAPQHGCNHKLELALSMIKGLDYKPIQSPRGSRLPIPVK 316
Cdd:pfam18615 241 SSVESLDTTVDvVQPPQQKDEESDKGEKDDRKCDQSSEEktTASSSLSSSGLELALSLLRGCEYRPVQSPRGSRLPVLVK 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392289 317 SSLPGAKPGPSMTDGV-------SSGFLNRSLKPLYKTPVSYPLELSDLQELWDDLCEDYLPLRVQP 376
Cdd:pfam18615 321 SSLSPGGLSYPLLDGSpgaglvcSTSFLSALREPFPQTPLDLQLELSELEELWLDLYVEYPPLRLQQ 387
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
451-1020 |
4.90e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 451 ETLKsRERETEELYQVIEgqndtmAKLREMLHQSQLGQLHSsegtspAQQQVALLDLQSALfcSQLEIQKLQRVVRQKER 530
Cdd:COG1196 203 EPLE-RQAEKAERYRELK------EELKELEAELLLLKLRE------LEAELEELEAELEE--LEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 531 QLADAKQcvqfveaAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKE 610
Cdd:COG1196 268 ELEELRL-------ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 611 QLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSAL---EEKEKELRQLRLAVRERDHDLERLR 687
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALraaAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 688 DVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCK 767
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 768 ---LGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTR-EQESQAAAEKLVQALMER------- 836
Cdd:COG1196 501 adyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEdDEVAAAAIEYLKAAKAGRatflpld 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 837 ----------NSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLG 906
Cdd:COG1196 581 kiraraalaaALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 907 DLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAA-DMESLTRNIQIKEDLIKDLQMQLVDPE 985
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAeEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590
....*....|....*....|....*....|....*
gi 2056392289 986 DIPAMERLTQEVLLLREKVASVESQGQEISGNRRQ 1020
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
453-1095 |
2.76e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 453 LKSRERETEELYQVIEGQNDTMAKLREMLH--QSQLGQLHSseGTSPAQQQVAllDLQSALFCSQLEIQKLQRVVRQKER 530
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQelEEKLEELRL--EVSELEEEIE--ELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 531 QLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAE--------------------KYN 590
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrleeleeqletlrsKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 591 EIRTQEQNIQ--------HLNHSLSHKEQLLQEFRELLQYRDNSDktLEANEMLLEKLRQRIHDKAVALERAIdekfSAL 662
Cdd:TIGR02168 390 QLELQIASLNneierleaRLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLE----EAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 663 EEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKfSRWQKEQESI 742
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD-EGYEAAIEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 743 IQQLQTSLHDRNKEVEDLSATLLCKLGPGQSEIAEElcqrlqrkermlqDLLSDRNKQVLEHEM--EIQGLLQSVSTREq 820
Cdd:TIGR02168 543 LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPL-------------DSIKGTEIQGNDREIlkNIEGFLGVAKDLV- 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 821 ESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE-VTPTGRLGKQTDQGSMQIPSRdDSTSLTAKEDVS 899
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDlVRPGGVITGGSAKTNSSILER-RREIEELEEKIE 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 900 IPRSTLGDLDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQ 978
Cdd:TIGR02168 688 ELEEKIAELEKaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 979 MQLvdpedipamERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAhpE 1058
Cdd:TIGR02168 768 ERL---------EEAEEELAEAEAEIEELEAQIEQLK-EELKALREALDELRAELTLLNEEAANLRERLESLERRIA--A 835
|
650 660 670
....*....|....*....|....*....|....*..
gi 2056392289 1059 SSERDRTLQVELEGAQVLRSRLEEVLGRSLERLNRLE 1095
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-832 |
1.18e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.33 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 562 ELRKALQQLQEE---------LQNKSQQLRAWEaeKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDnsdKTLEA 632
Cdd:TIGR02169 195 EKRQQLERLRRErekaeryqaLLKEKREYEGYE--LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE---KRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 633 NEMLLEKLRQRIHDKAVALERAIDEKfsaLEEKEKELRQLRLAVRERDHDLERLrdvlssnEATMQSMESLLRAKGLEVE 712
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEK---IGELEAEIASLERSIAEKERELEDA-------EERLAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 713 QLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQtSLHDRNKEVEDLSATLLCKLGPGQSEIAEelcqrLQRKERMLQD 792
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELE-EVDKEFAETRDELKDYREKLEKLKREINE-----LKRELDRLQE 413
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2056392289 793 LLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQA 832
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
527-842 |
2.05e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 527 QKERQLADAKQCVQFVEAAAHESEQQkeaswkhnqelRKALQQLQEELQNKSQQLRAWEAEKYNEI----------RTQE 596
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEELSRQIsalrkdlarlEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 597 QNIQHLNHSLSHK-EQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDkavaLERAIDEKFSALEEKEKELRQLRLA 675
Cdd:TIGR02168 743 EQLEERIAQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 676 VRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQlqtsLHDRNK 755
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA----LALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 756 EVEDLSATLLcklgpgqsEIAEELcQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALME 835
Cdd:TIGR02168 895 ELEELSEELR--------ELESKR-SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
....*..
gi 2056392289 836 RNSELQA 842
Cdd:TIGR02168 966 DEEEARR 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
372-1101 |
2.52e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 372 LRVQPMTEELLKQQK-LNSH-------ETTITQQSVSDSHL----AELQEKIQQTEATNKILQEKLNEMSYELKCAQESS 439
Cdd:TIGR02168 274 LEVSELEEEIEELQKeLYALaneisrlEQQKQILRERLANLerqlEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 440 QKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREML--HQSQLGQLhSSEGTSPAQQQVALLDLQSALFCSQLE 517
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERL-EARLERLEDRRERLQQEIEELLKKLEE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 518 --IQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELR----------KALQQLQEELQNKSQQLRAWE 585
Cdd:TIGR02168 433 aeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAErelaqlqarlDSLERLQENLEGFSEGVKALL 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 586 AEKyneiRTQEQNIQHLNHSLSHKEQLLQE----FRELLQY--RDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKF 659
Cdd:TIGR02168 513 KNQ----SGLSGILGVLSELISVDEGYEAAieaaLGGRLQAvvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQG 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 660 SALEEKEKELRQLRLA--VRERDHDLERLRDVLSSNEATMQSMESLLR-AKGLEVEQLSTTCQNLQWLKEEMETKFSRwq 736
Cdd:TIGR02168 589 NDREILKNIEGFLGVAkdLVKFDPKLRKALSYLLGGVLVVDDLDNALElAKKLRPGYRIVTLDGDLVRPGGVITGGSA-- 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 737 kEQESIIQQlqtslhdRNKEVEDLSATLlcKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVS 816
Cdd:TIGR02168 667 -KTNSSILE-------RRREIEELEEKI--EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 817 TREQESQAAAEKLVQAlmerNSELQALRQYLGGRDSLMSQAPISNQQAEVTptgrlgKQTDQGSMQipsrddstslTAKE 896
Cdd:TIGR02168 737 RLEAEVEQLEERIAQL----SKELTELEAEIEELEERLEEAEEELAEAEAE------IEELEAQIE----------QLKE 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 897 DVSIPRSTLgdldtvAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKD 976
Cdd:TIGR02168 797 ELKALREAL------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 977 LQMQLVDPEDIpaMERLTQEVLLLREKVASVESQGQEISGNR---RQQLLLMLEGLVDERSRLNEALQAERQLYSSLvkf 1053
Cdd:TIGR02168 871 LESELEALLNE--RASLEEALALLRSELEELSEELRELESKRselRRELEELREKLAQLELRLEGLEVRIDNLQERL--- 945
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 2056392289 1054 hahpesSERdrtLQVELEGAQVLRSRLEEVLGRSLERLNRLET-LAAIG 1101
Cdd:TIGR02168 946 ------SEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENkIKELG 985
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
391-1006 |
3.58e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 391 ETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEmsyelkcAQESSQKQDGTIQNLKETLKSRERETEELyqviegq 470
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYE-------LLAELARLEQDIARLEERRRELEERLEEL------- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 471 ndtmaklremlhqsqlgqlhssegtspaqqqvalldlqsalfcsQLEIQKLQRVVRQKERQLADAkqcvqfvEAAAHESE 550
Cdd:COG1196 322 --------------------------------------------EEELAELEEELEELEEELEEL-------EEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 551 QQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTL 630
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 631 EANEMLLEKLRQRihdkavalERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAkgle 710
Cdd:COG1196 431 AELEEEEEEEEEA--------LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE---- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 711 veqlsttcqnlqwLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVED-LSATLLCKLGPGQSEIAEELCQRLQRKERM 789
Cdd:COG1196 499 -------------AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAaYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 790 LQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEkLVQALMERNSELQALRQYLGGRDSLmSQAPISNQQAEVTPT 869
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-VASDLREADARYYVLGDTLLGRTLV-AARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 870 GRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSmmAVQ 949
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE--EEL 721
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392289 950 EEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMERLTQEVLLLREKVAS 1006
Cdd:COG1196 722 EEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
383-765 |
8.59e-10 |
|
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: 63.12 E-value: 8.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 383 KQQKLNSHETTITQQSVSDSH-LAELQEKIQQTEATNKILQEKLNEMS-YELKCAQESSQKQDGTIQNLKETLKSRERET 460
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKiKKQLSEKQKELEQNNKKIKELEKQLNqLKSEISDLNNQKEQDWNKELKSELKNQEKKL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 461 EELYQVIEGQNDTMAKLREmlhqsQLGQLHSSegtspaqqqvaLLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQ 540
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNE-----QISQLKKE-----------LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 541 FVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQ---LRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFR 617
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEierLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 618 ELLQYRDNSDKTLEANemlLEKLRQRIHDKAVALERAIDEKfSALEEKEKELRQLRLAVRERDHDLE----RLRDVLSSN 693
Cdd:TIGR04523 468 TQLKVLSRSINKIKQN---LEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKIEKLEsekkEKESKISDL 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392289 694 EATMQSMESLLRAKGLEVEQLSTTcQNLQWLKEEmETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLL 765
Cdd:TIGR04523 544 EDELNKDDFELKKENLEKEIDEKN-KEIEELKQT-QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-687 |
1.57e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.39 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 369 YLPLRVQPMTEELLKQQKLnsHETTITQQSVSDSHLAELQEKIQQteatnkiLQEKLNEMSYELKCAQESSQKQDGTIQN 448
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRE--LSSLQSELRRIENRLDELSQELSD-------ASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 449 LKETLKSRERETEELYQVIEGQNDTMAKLREMLH--QSQLGQLHSSEGTSPAQQQVALL---------------DLQSAL 511
Cdd:TIGR02169 742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHklEEALNDLEARLSHSRIPEIQAELskleeevsriearlrEIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 512 FCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAekynE 591
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA----Q 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 592 IRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLE----------ANEMLLEKLRQRIHDKAVALE-------RA 654
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipEEELSLEDVQAELQRVEEEIRalepvnmLA 977
|
330 340 350
....*....|....*....|....*....|....*....
gi 2056392289 655 IDE------KFSALEEKEKELRQLRLAVRERDHDLERLR 687
Cdd:TIGR02169 978 IQEyeevlkRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
369-1001 |
8.52e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.13 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 369 YLPLRVQPMTEEL--LKQQKLNSHETTITQQsvsdshlaelQEKIQQTEATNKILQEKLNEMSyelkcaqESSQKQDGTI 446
Cdd:pfam15921 235 YLKGRIFPVEDQLeaLKSESQNKIELLLQQH----------QDRIEQLISEHEVEITGLTEKA-------SSARSQANSI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 447 QNLKETLKSRERETEELYqviegqndtMAKLREMlhQSQLGQLHSS--EGTSPAQQQVALLDLQSALFCSQLEIQKLQRv 524
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMY---------MRQLSDL--ESTVSQLRSElrEAKRMYEDKIEELEKQLVLANSELTEARTER- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 525 vRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL--------------RKALQQLQEELQNKSQQLRAWEAEKYN 590
Cdd:pfam15921 366 -DQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQG 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 591 EIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALEraidEKFSALEEKEKELR 670
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ----EKERAIEATNAEIT 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 671 QLRLAVRERDHDLERLR---DVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQesiiQQLQ 747
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK----AQLE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 748 TSLHDRNKEVEDLSatLLCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAE 827
Cdd:pfam15921 597 KEINDRRLELQEFK--ILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 828 KLvqALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIpsrddstSLTAKEDVSIPRSTLGD 907
Cdd:pfam15921 675 DY--EVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV-------AMGMQKQITAKRGQIDA 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 908 LDT-VAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPED 986
Cdd:pfam15921 746 LQSkIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
650
....*....|....*
gi 2056392289 987 IpaMERLTQEVLLLR 1001
Cdd:pfam15921 826 I--IQRQEQESVRLK 838
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
419-1096 |
1.80e-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: 58.93 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 419 KILQEKLNEMS-YELKCAQESSQKQdgtIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSp 497
Cdd:TIGR02169 214 QALLKEKREYEgYELLKEKEALERQ---KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 498 AQQQVALLDLQSalfcsqlEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK 577
Cdd:TIGR02169 290 LRVKEKIGELEA-------EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 578 SQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQ---RIHDKAVALERA 654
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAaiaGIEAKINELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 655 IDEKFSALEEKEKELRQLRlavrerdHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqwlkEEMETKFSR 734
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLA-------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS----EERVRGGRA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 735 WQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLGP-------GQSEIAEELCQRLQRKE--RM----LQDLLSDRNKQV 801
Cdd:TIGR02169 512 VEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNrlnnvvvEDDAVAKEAIELLKRRKagRAtflpLNKMRDERRDLS 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 802 LEHEMEIQGLLQSVSTREQESQAAAEKLVQ--ALMERnseLQALRQYLGG------------RDSLMSQAPISNQQAEVT 867
Cdd:TIGR02169 592 ILSEDGVIGFAVDLVEFDPKYEPAFKYVFGdtLVVED---IEAARRLMGKyrmvtlegelfeKSGAMTGGSRAPRGGILF 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 868 PTgRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMA 947
Cdd:TIGR02169 669 SR-SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 948 VQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMER---LTQEVLLLREKVASVESQGQEISG--NRRQQL 1022
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipeIQAELSKLEEEVSRIEARLREIEQklNRLTLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 1023 LLMLEGLVDERSRLNEALQAERQ--------LYSSLVKFHAHPESSE-RDRTLQVELEGAQVLRSRLEEVLGRSLERLNR 1093
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKsiekeienLNGKKEELEEELEELEaALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
...
gi 2056392289 1094 LET 1096
Cdd:TIGR02169 908 LEA 910
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
453-954 |
8.20e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 453 LKSRERETEELYQVIEGQND-----TMAKLREMLHQS---QLGQLHSSEGTSPAQQQVALLDLQSAL---FCSQLEIQKL 521
Cdd:COG4717 14 FRDRTIEFSPGLNVIYGPNEagkstLLAFIRAMLLERlekEADELFKPQGRKPELNLKELKELEEELkeaEEKEEEYAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 522 QRVVRQKERQLADAKQcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEaEKYNEIRTQEQNIQH 601
Cdd:COG4717 94 QEELEELEEELEELEA-----ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE-ERLEELRELEEELEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 602 LNHSLSHKEQLLQEfrellQYRDNSDKTLEANEMLLEKLrQRIHDKAVALERAIDEKFSALEEKEKELRQLRlAVRERDH 681
Cdd:COG4717 168 LEAELAELQEELEE-----LLEQLSLATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQLE-NELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 682 DLERLRDVLSSNEATmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEvEDLS 761
Cdd:COG4717 241 LEERLKEARLLLLIA--AALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-EELE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 762 ATLLCKL-------GPGQSEIAEELCQRLQRKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQAL 833
Cdd:COG4717 318 EEELEELlaalglpPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 834 MERNSELQALRQYLGgrdslmSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTS--LTAKEDVSIPRSTLGDLDTV 911
Cdd:COG4717 398 QELKEELEELEEQLE------ELLGELEELLEALDEEELEEELEELEEELEELEEELEelREELAELEAELEQLEEDGEL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2056392289 912 AGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQ 954
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
404-618 |
2.26e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 404 LAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLhQ 483
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL-A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 484 SQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLeIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL 563
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2056392289 564 RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRE 618
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
521-1012 |
2.51e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 521 LQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRaweaEKYNEIRTQEQNIQ 600
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR----EQAELNRLKKKYLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 601 HLNHSLSHKEQLL-----------QEFRELLQYRDNSDKTLEANEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKEL 669
Cdd:pfam05557 87 ALNKKLNEKESQLadarevisclkNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 670 RQLRLAVRERDHDLERLRD----VLSSNE--ATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEE---METKFSRWQKEQE 740
Cdd:pfam05557 166 AEAEQRIKELEFEIQSQEQdseiVKNSKSelARIPELEKELERLREHNKHLNENIENKLLLKEEvedLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 741 SII------QQLQTSLHDRNKEVEDLSATLlcklgPGQSEIAEELCQrLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQS 814
Cdd:pfam05557 246 EAAtlelekEKLEQELQSWVKLAQDTGLNL-----RSPEDLSRRIEQ-LQQREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 815 VS----------TREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQ---------------------- 862
Cdd:pfam05557 320 LAqylkkiedlnKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQllerieeaedmtqkmqahneem 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 863 -----QAEVTPTG-RLGKQTDQGSMQIPSRDDST--SLTAKEDVSIPRStlgDLDTVAGLEKELSNAKEELEL-MAKKER 933
Cdd:pfam05557 400 eaqlsVAEEELGGyKQQAQTLERELQALRQQESLadPSYSKEEVDSLRR---KLETLELERQRLREQKNELEMeLERRCL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 934 ESQMELS---ALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIP--AMERLTQEVLLLREKVASVE 1008
Cdd:pfam05557 477 QGDYDPKktkVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPetTSTMNFKEVLDLRKELESAE 556
|
....
gi 2056392289 1009 SQGQ 1012
Cdd:pfam05557 557 LKNQ 560
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
403-705 |
3.05e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.97 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 403 HLAELQEKIQQTEATNKILQEKLNEMSYEL-KCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDtmakLREML 481
Cdd:TIGR00618 557 QRASLKEQMQEIQQSFSILTQCDNRSKEDIpNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL----QDVRL 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 482 HQSQLGQLHSSEGTSPAQQQVALL---DLQSALFCSQLEIQKLQRVVRQ------KERQLADAKQCVQFVEAAAHESEQQ 552
Cdd:TIGR00618 633 HLQQCSQELALKLTALHALQLTLTqerVREHALSIRVLPKELLASRQLAlqkmqsEKEQLTYWKEMLAQCQTLLRELETH 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 553 KEASWKHNQELRKALQQLQEELQNK----SQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDK 628
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAARedalNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNR 792
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392289 629 TLEANEMLLEKLRQRIHDKAVALEraiDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLR 705
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
420-857 |
5.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 420 ILQEKLNEMSYEL-KCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMlhQSQLGQLhssegtspa 498
Cdd:COG4717 46 MLLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEEL--------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 499 QQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKeaswkhnQELRKALQQLQEELQNKS 578
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE-------AELAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 579 QQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEK 658
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 659 FSALEEKEKELRQLRLAVRErdHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqWLKEEMETKFSRWQKE 738
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLA--LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL-GLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 739 QESIIQQLQTSLHDRNKEV-----EDLSATLLCKLGPGQSEIAEELCQRLQRKERmLQDLLSDRNKQVLEHEMEIQGLLQ 813
Cdd:COG4717 345 RIEELQELLREAEELEEELqleelEQEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2056392289 814 SVStrEQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQA 857
Cdd:COG4717 424 ALD--EEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
386-856 |
5.86e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 386 KLNSHETTITQqsvSDSHLAELQEKIQQTEATNKILQEKLNEmsYELKcaQESSQKQDGTIQNLKETLKSRERETEELYQ 465
Cdd:PRK02224 207 RLNGLESELAE---LDEEIERYEEQREQARETRDEADEVLEE--HEER--REELETLEAEIEDLRETIAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 466 VIEGQNDTMAKLREMLHqsqlGQLHSSEGTSPAQQqvALLDLQSALfcsQLEIQKLQRVVRQKERQLADAKQCVQFVEAA 545
Cdd:PRK02224 280 EVRDLRERLEELEEERD----DLLAEAGLDDADAE--AVEARREEL---EDRDEELRDRLEECRVAAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 546 AHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAE------KYNEIRTQEQNIQHLNHSL-SHKEQLLQEFRE 618
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelreRFGDAPVDLGNAEDFLEELrEERDELREREAE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 619 LLQYRDNSDKTLEANEMLLEKLR-----QRIHDKAVAleRAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDV---- 689
Cdd:PRK02224 431 LEATLRTARERVEEAEALLEAGKcpecgQPVEGSPHV--ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLveae 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 690 --LSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQK---EQESIIQQLQTSLHDRNKEVEDLSATL 764
Cdd:PRK02224 509 drIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREaaaEAEEEAEEAREEVAELNSKLAELKERI 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 765 --LCKLGPGQSEIAE--ELCQRLQRKERMLQDL-------LSDRNKQVLEHEMEIQGllqsvsTREQESQAAAEKLVQAL 833
Cdd:PRK02224 589 esLERIRTLLAAIADaeDEIERLREKREALAELnderrerLAEKRERKRELEAEFDE------ARIEEAREDKERAEEYL 662
|
490 500
....*....|....*....|...
gi 2056392289 834 MERNSELQALRQylgGRDSLMSQ 856
Cdd:PRK02224 663 EQVEEKLDELRE---ERDDLQAE 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
515-805 |
7.93e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 515 QLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWE-AEKYNEIR 593
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 594 TQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLr 673
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL- 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 674 lavRERDHDLERLRDVLSsneatmqsmesllrakglevEQLSTTCQNLQWLKEEMETKFSRwQKEQESIIQQLQtslhDR 753
Cdd:TIGR02169 881 ---ESRLGDLKKERDELE--------------------AQLRELERKIEELEAQIEKKRKR-LSELKAKLEALE----EE 932
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2056392289 754 NKEVEDLSATLLCKlgPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHE 805
Cdd:TIGR02169 933 LSEIEDPKGEDEEI--PEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
558-841 |
2.88e-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: 51.90 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 558 KHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQ---------------------HLNHSLSHKEQLLQEF 616
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKaleyyqlkekleleeeyllylDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 617 RELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEAT 696
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 697 MQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHD----RNKEVEDLSATLLCKLGPGQ 772
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLeserLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392289 773 SEiaeelcQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQ 841
Cdd:pfam02463 406 EA------QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
421-981 |
3.53e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 51.27 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 421 LQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEGTSPAQQ 500
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 501 QVALLDlQSALFCSQLEIQKLQRVVRQKERQLADAKQC-VQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK-- 577
Cdd:pfam15921 156 AAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEis 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 578 ---------SQQLRAWEAEKYNEI--------------------------------RTQEQNIQ---------------- 600
Cdd:pfam15921 235 ylkgrifpvEDQLEALKSESQNKIelllqqhqdrieqliseheveitgltekassaRSQANSIQsqleiiqeqarnqnsm 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 601 ---HLNHSLSHKEQLLQEFRELLQYRDNSDKTLE-----ANEMLLEKLRQR--IHDKAVALERAIDEKFSALEEKEKELR 670
Cdd:pfam15921 315 ymrQLSDLESTVSQLRSELREAKRMYEDKIEELEkqlvlANSELTEARTERdqFSQESGNLDDQLQKLLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 671 qlrlavRERDHDlERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQW-LKEEMETKFSRWQKEQE------SII 743
Cdd:pfam15921 395 ------LEKEQN-KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSeCQGQMERQMAAIQGKNEslekvsSLT 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 744 QQLQTSLHDRNKEVEDLSATllcKLGPGQSE-IAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGL--LQSVSTREQ 820
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAK---KMTLESSErTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELqhLKNEGDHLR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 821 ESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTpTGRLGKQTDQGSMQIpsrDDSTSLTAKEDVSI 900
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVE-KAQLEKEINDRRLEL---QEFKILKDKKDAKI 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 901 P--RSTLGDLDtvagLEK-ELSNAKEElelMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIK----EDL 973
Cdd:pfam15921 621 RelEARVSDLE----LEKvKLVNAGSE---RLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKseemETT 693
|
....*...
gi 2056392289 974 IKDLQMQL 981
Cdd:pfam15921 694 TNKLKMQL 701
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
628-1082 |
3.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 628 KTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAK 707
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 708 GLEVEqlsttcqnLQWLKEEMETKFSRWQKEQESI--IQQLQTSLHDRNKEVEDLSATLLCKLGPGQSEIAEELcQRLQR 785
Cdd:COG4717 129 PLYQE--------LEALEAELAELPERLEELEERLeeLRELEEELEELEAELAELQEELEELLEQLSLATEEEL-QDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 786 KERMLQDLLSDRNKQVLEHEMEIQGLlqsvstREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE 865
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEEL------EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 866 VTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRSTLGDLDtvaglEKELSNAKEELELMAKKERESQMELSAlqsm 945
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE-----EEELEELLAALGLPPDLSPEELLELLD---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 946 mavQEEELQVQAADMESLTRNIQIK--EDLIKDL--QMQLVDPEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQQ 1021
Cdd:COG4717 345 ---RIEELQELLREAEELEEELQLEelEQEIAALlaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392289 1022 L-LLMLEGLVDERSRLNEALQAER----QLYSSLVKFHAHPESSERDRTLQVELEGAQVLRSRLEE 1082
Cdd:COG4717 422 LeALDEEELEEELEELEEELEELEeeleELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
494-701 |
4.27e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 494 GTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEE 573
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 574 LQNKSQQLRAWEAEKYNEIRTQEQNIQH-------LNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQrihd 646
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2056392289 647 kavALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSME 701
Cdd:COG4942 168 ---ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
637-1114 |
4.74e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 637 LEKLRQRIHDKAVALERAIDEKFSALEEKEKE------------LRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLL 704
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQieekeekdlherLNGLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 705 ---RAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEqesiIQQLQTSLHDRNKEVEDLSATllCKLGPGQSEIAEELCQ 781
Cdd:PRK02224 244 eehEERREELETLEAEIEDLRETIAETEREREELAEE----VRDLRERLEELEEERDDLLAE--AGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 782 RLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISN 861
Cdd:PRK02224 318 ELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELR 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 862 QQAEVTPTgRLGKQTDQGSMQIPSRDDS----TSLTAK---------------------------EDVSIPRSTLGDLDT 910
Cdd:PRK02224 398 ERFGDAPV-DLGNAEDFLEELREERDELrereAELEATlrtarerveeaealleagkcpecgqpvEGSPHVETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 911 VAGLEKELSNAKEELELMAKK--------ERESQME-----LSALQSMMAVQEEELQVQAADMESLTRNIQikedlikDL 977
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERleraedlvEAEDRIErleerREDLEELIAERRETIEEKRERAEELRERAA-------EL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 978 QMQLVDPEDipAMERLTQEVLLLREKVASVESQGQEISgNRRQQL------LLMLEGLVDERSRLNEALQA------ERQ 1045
Cdd:PRK02224 550 EAEAEEKRE--AAAEAEEEAEEAREEVAELNSKLAELK-ERIESLerirtlLAAIADAEDEIERLREKREAlaelndERR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 1046 LYSSlvkfhahpESSERDRTLQVE-----LEGAQVLRSRLEEVLGRSLERLNRL-----ETLAAIGG-----GELESVRI 1110
Cdd:PRK02224 627 ERLA--------EKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELreerdDLQAEIGAvenelEELEELRE 698
|
....
gi 2056392289 1111 HHKH 1114
Cdd:PRK02224 699 RREA 702
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
400-588 |
1.00e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 400 SDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAK-LR 478
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 479 EMLHQ----SQLGQLHSSEGTSPAQQQVALLD-LQSAlfcSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQK 553
Cdd:COG3883 94 ALYRSggsvSYLDVLLGSESFSDFLDRLSALSkIADA---DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190
....*....|....*....|....*....|....*
gi 2056392289 554 EASWKHNQELRKALQQLQEELQNKSQQLRAWEAEK 588
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
514-690 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 514 SQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEEL-QNKSQQLRAWEAekynEI 592
Cdd:COG4913 272 AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLER----EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 593 RTQEQNIQHLNHSLSHKEQLLQEF--------RELLQYRDNSDKTLEAnemlLEKLRQRIHDKAVALERAIDEKFSALEE 664
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALglplpasaEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE 423
|
170 180
....*....|....*....|....*.
gi 2056392289 665 KEKELRQLRLAVRERDHDLERLRDVL 690
Cdd:COG4913 424 LEAEIASLERRKSNIPARLLALRDAL 449
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
379-845 |
1.18e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 379 EELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEmsyelkcaQESSQKQDGTIQNLKETLKSRER 458
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE--------QLKKQQLLKQLRARIEELRAQEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 459 ETEELYQVIEGQNDtmaKLREMLHQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQC 538
Cdd:TIGR00618 278 VLEETQERINRARK---AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 539 VQFveAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYN--------EIRTQEQNIQHLNHSLSHKE 610
Cdd:TIGR00618 355 IHI--RDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIlqreqatiDTRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 611 QLLQEFRELLQ--YRDNSDKTLEANEMLLEKLRQRIHDKAVALERAidekfSALEEKEKELRQLRLAVRERDHDLER-LR 687
Cdd:TIGR00618 433 QELQQRYAELCaaAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK-----EQIHLQETRKKAVVLARLLELQEEPCpLC 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 688 DVLSSNEATMQSM------ESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDLS 761
Cdd:TIGR00618 508 GSCIHPNPARQDIdnpgplTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 762 ATL-----LCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNK-QVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALME 835
Cdd:TIGR00618 588 NLQnitvrLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrLHLQQCSQELALKLTALHALQLTLTQERVREHALSI 667
|
490
....*....|
gi 2056392289 836 RNSELQALRQ 845
Cdd:TIGR00618 668 RVLPKELLAS 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
609-863 |
1.19e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 609 KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIhdkaVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRD 688
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 689 VLSSNEATMQSMESLLRAK-GLEVEQLSTTCQNLQWLKEemetkFSRWQKEQESIIQQLQTSLHDRNKEVEDLSATLlck 767
Cdd:COG4942 105 ELAELLRALYRLGRQPPLAlLLSPEDFLDAVRRLQYLKY-----LAPARREQAEELRADLAELAALRAELEAERAEL--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 768 lgpgqseiaEELCQRLQRKERMLQDLLSDRNKqvlehemeiqgLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYL 847
Cdd:COG4942 177 ---------EALLAELEEERAALEALKAERQK-----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*.
gi 2056392289 848 GGRDSLMSQAPISNQQ 863
Cdd:COG4942 237 AAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
498-710 |
1.21e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 498 AQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNK 577
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 578 SQQLRAWEAEKY--------------NEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQR 643
Cdd:COG4942 103 KEELAELLRALYrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392289 644 IHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLE 710
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-992 |
1.33e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 383 KQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNE--MSYELKCAQESSQKQDGTIQNLKETLKSRERET 460
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 461 EELYQVIEGQNDTMAKLREMLHQSQLG--QLHSSEGTSPAQQQValldlqsalfcsQLEIQKLQRVVRQKERQLADAKQC 538
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKSRHsdELTSLLGYFPNKKQL------------EDWLHSKSKEINQTRDRLAKLNKE 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 539 VQFVEAAAH------ESEQQKEASWKHN-------QELRKALQQLQEELQNKSQQLRAWEAEK------YNEIRTQEQNI 599
Cdd:TIGR00606 600 LASLEQNKNhinnelESKEEQLSSYEDKlfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATavysqfITQLTDENQSC 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 600 QHLNHSLSHKEQLLQEFRELLQYRDNSDKT-LEANEMLLEKLRQRIHDKAVALERaideKFSALEEKEKELRQLRLAVRE 678
Cdd:TIGR00606 680 CPVCQRVFQTEAELQEFISDLQSKLRLAPDkLKSTESELKKKEKRRDEMLGLAPG----RQSIIDLKEKEIPELRNKLQK 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 679 RDHDLERLRDVLSSNEATMQS-MESLLRAKGLEVEqlSTTCQNLQWLKEEMETKFSRWQKEQESIiqQLQTSLHDRNKEV 757
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTiMPEEESAKVCLTD--VTIMERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEK 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 758 EDlsatllcklgpgqseiAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQ---SVSTREQESQAAAEKLVqalm 834
Cdd:TIGR00606 832 QE----------------KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEEQLV---- 891
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 835 ERNSELQALRQylggrdslmsqaPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVSIPRStlgDLDTVAGL 914
Cdd:TIGR00606 892 ELSTEVQSLIR------------EIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE---KVKNIHGY 956
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 915 EKELSNAKEELELMAKKERESqmELSALQSMMAVQEEELQVQAADMESLTRNI---QIKEDLIKDLQMQLVDPEDIPAME 991
Cdd:TIGR00606 957 MKDIENKIQDGKDDYLKQKET--ELNTVNAQLEECEKHQEKINEDMRLMRQDIdtqKIQERWLQDNLTLRKRENELKEVE 1034
|
.
gi 2056392289 992 R 992
Cdd:TIGR00606 1035 E 1035
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-690 |
1.97e-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: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 358 LQELWDDLCEDYLPLRVQpMTEELLKQQKLNSHEttitqqSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQE 437
Cdd:TIGR02168 745 LEERIAQLSKELTELEAE-IEELEERLEEAEEEL------AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 438 SSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREmlhqsqlgqlhssegtspaqqqvALLDLQSALFCSQLE 517
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-----------------------EIEELEELIEELESE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 518 IQKLQRVVRQKERQLADAKqcvqfvEAAAHESEQQKEASwKHNQELRKALQQLQEELqNKSQqlraweaEKYNEIrtqEQ 597
Cdd:TIGR02168 875 LEALLNERASLEEALALLR------SELEELSEELRELE-SKRSELRRELEELREKL-AQLE-------LRLEGL---EV 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 598 NIQHLNHSLSHKEQLLQEFrellqyrdnsdktLEANEMLLEKLRQRIHDKAVALERAIDE----KFSALEEKEkELRQLR 673
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEE-------------AEALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYE-ELKERY 1002
|
330
....*....|....*..
gi 2056392289 674 LAVRERDHDLERLRDVL 690
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETL 1019
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
369-766 |
2.54e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.28 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 369 YLPLRVQPMTEELLKQQKLNS------------HETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQ 436
Cdd:pfam10174 71 HLQLTIQALQDELRAQRDLNQllqqdfttspvdGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 437 ESSQKQDGTIQNLKETLKSR------ERETEELYQVIEGQNDTMAKLREMLHQSQLGQLHSSEG----TSPAQQQVALLD 506
Cdd:pfam10174 151 QTLGARDESIKKLLEMLQSKglpkksGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREElhrrNQLQPDPAKTKA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 507 LQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEA 586
Cdd:pfam10174 231 LQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 587 E---KYNEIRTQEQNIQHLNHSLSHKEQ---LLQEFRELLQYRdnsdktLEANEMLLEKLRQRIHDKAvaleraiDEKfS 660
Cdd:pfam10174 311 KletLTNQNSDCKQHIEVLKESLTAKEQraaILQTEVDALRLR------LEEKESFLNKKTKQLQDLT-------EEK-S 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 661 ALEEKEKELRQLrLAVRER-----DHDLERLRDVLSSNEATMQSMESllRAKGLEVEQlSTTCQNLQWLKE---EMETKF 732
Cdd:pfam10174 377 TLAGEIRDLKDM-LDVKERkinvlQKKIENLQEQLRDKDKQLAGLKE--RVKSLQTDS-SNTDTALTTLEEalsEKERII 452
|
410 420 430
....*....|....*....|....*....|....
gi 2056392289 733 SRWQKEQESIIQQLQTSLHDRNKEVEDLSATLLC 766
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKENKDLKEKVSA 486
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
522-717 |
2.92e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 522 QRVVRQKERQLADAKQCVQFVEAAA-HESE---QQKEASWKHN--QELRKALQQLQEELQNKSQQLRAWE--AEKYNEIR 593
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAeLEAEaeeKREAAAEAEEeaEEAREEVAELNSKLAELKERIESLEriRTLLAAIA 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 594 TQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEA--NEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKELRQ 671
Cdd:PRK02224 603 DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAefDEARIEEARED-KERAEEYLEQVEEKLDELREERDDLQA 681
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2056392289 672 LRLAVRERDHDLERLRDVLSSNEATMQSMESLLRakglEVEQLSTT 717
Cdd:PRK02224 682 EIGAVENELEELEELRERREALENRVEALEALYD----EAEELESM 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
457-845 |
3.48e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 457 ERETEELYQVIEGQ---NDTMAKLREMLHQSQLgqlhssEGTSPAQQqvALLDLQSALFCSQleiqklQRVVRQKERQLA 533
Cdd:pfam17380 286 ERQQQEKFEKMEQErlrQEKEEKAREVERRRKL------EEAEKARQ--AEMDRQAAIYAEQ------ERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 534 DAKQcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAwEAEKYNEIRTQEQNIQhlnhslshkEQLL 613
Cdd:pfam17380 352 RIRQ-----EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKILEEERQ---------RKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 614 QEFRELLQYRDNSDktlEANEMLLEKLRqrihdkavaleraidekfsalEEKEKELRQLRLAVRERDHDLERLRDVLSSN 693
Cdd:pfam17380 417 QQKVEMEQIRAEQE---EARQREVRRLE---------------------EERAREMERVRLEEQERQQQVERLRQQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 694 EATMQSMESLLRAKGLEVEqlsttcQNLQWLKEEMETKfSRWQKEQESIIQQLQTSLHDRnkevedlsatllcklgpgQS 773
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEE------QRRKILEKELEER-KQAMIEEERKRKLLEKEMEER------------------QK 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392289 774 EIAEELCQRLQRKERmlqdllsdRNKQVLEHEMEIQgllqsvstrEQESQAAAEKLVQALMERNSELqaLRQ 845
Cdd:pfam17380 528 AIYEEERRREAEEER--------RKQQEMEERRRIQ---------EQMRKATEERSRLEAMEREREM--MRQ 580
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
395-1023 |
4.69e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 395 TQQSVSDSHLAELQEKIQQTEATNKIlQEKLNEMSYELKCAQESSQKQDGTIQNLKEtlksRERETEELYQVIEGQNDTM 474
Cdd:TIGR00606 197 TQGQKVQEHQMELKYLKQYKEKACEI-RDQITSKEAQLESSREIVKSYENELDPLKN----RLKEIEHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 475 AKL--REMLHQSQLGQLHssegtspaqqqvalLDLQSALFCSQLEIQKL----QRVVRQKERQLADAKQCVQFVEAAAHE 548
Cdd:TIGR00606 272 KALksRKKQMEKDNSELE--------------LKMEKVFQGTDEQLNDLyhnhQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 549 SEQQKeaswkhnQELRKALQQLQEELQNKSQQLRAWEAEKY-NEIRTQEQNIQHLNHSlshkEQLLQEFRELLQYRDNSD 627
Cdd:TIGR00606 338 LNQEK-------TELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFS----ERQIKNFHTLVIERQEDE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 628 --------KTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERD---HDLERLRDVLSSNEAT 696
Cdd:TIGR00606 407 aktaaqlcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEgssDRILELDQELRKAERE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 697 MQSME--SLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQL-----QTSLHDRNKEVEDLSATLLCKLG 769
Cdd:TIGR00606 487 LSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEmltkdKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 770 P--GQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQAL--MERNSELQALRQ 845
Cdd:TIGR00606 567 GyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsQDEESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 846 YLggRDSLMSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEDVS-IPRSTLGDLDTVAGLEKELSNAKEE 924
Cdd:TIGR00606 647 EI--EKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISdLQSKLRLAPDKLKSTESELKKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 925 LELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPE----DIPAMERLTQEVLLL 1000
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltDVTIMERFQMELKDV 804
|
650 660
....*....|....*....|...
gi 2056392289 1001 REKVASVESQGQEISGNRRQQLL 1023
Cdd:TIGR00606 805 ERKIAQQAAKLQGSDLDRTVQQV 827
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
380-662 |
4.98e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 380 ELLKQQKLNSHETTITQQSVSDShLAELQeKIQQTEATNKILQEKLNEMSYELKCAQESsqkqdgtIQNLKETLKSRERE 459
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQT-LALLD-KIDRQKEETEQLKQQLAQAPAKLRQAQAE-------LEALKDDNDEETRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 460 TEElyqviegqNDTMAKLREMLHQ--SQLGQLHSSEGTSPAQ---QQVALLDLQSALFCSQLEIQKL------------- 521
Cdd:PRK11281 117 TLS--------TLSLRQLESRLAQtlDQLQNAQNDLAEYNSQlvsLQTQPERAQAALYANSQRLQQIrnllkggkvggka 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 522 ----QRVVRQKERQLADAKQCVQFVEAAAHE------SEQQKEASWKHNQeLRKALQQLQEELQNKsqqlRAWEAEK-YN 590
Cdd:PRK11281 189 lrpsQRVLLQAEQALLNAQNDLQRKSLEGNTqlqdllQKQRDYLTARIQR-LEHQLQLLQEAINSK----RLTLSEKtVQ 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392289 591 EIRTQEQNIQHLNHSLSHKEqlLQEFRELLQYRDNSdkTLEANEMLLEKLRQR-IHDKAVALERAIDEKFSAL 662
Cdd:PRK11281 264 EAQSQDEAARIQANPLVAQE--LEINLQLSQRLLKA--TEKLNTLTQQNLRVKnWLDRLTQSERNIKEQISVL 332
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
652-1024 |
6.88e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 652 ERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDvlssneatmqSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETK 731
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----------EREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 732 FSRWQKEQESI---IQQLQTSLHDRNKEVEDLSATLlcklgpgqSEIAEELcqrlqrkERMLQDLLSDRNKQVLEHEMEI 808
Cdd:TIGR02169 239 KEAIERQLASLeeeLEKLTEEISELEKRLEEIEQLL--------EELNKKI-------KDLGEEEQLRVKEKIGELEAEI 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 809 QGLLQSVSTREQESQAAAEKLVQALMERNSEL-------QALRQYLGGRDSLMSQapISNQQAEvtptgRLGKQTDQGSM 881
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieeleREIEEERKRRDKLTEE--YAELKEE-----LEDLRAELEEV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 882 qipsrdDSTSLTAKEDVSIPRSTLGDL-DTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADM 960
Cdd:TIGR02169 377 ------DKEFAETRDELKDYREKLEKLkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392289 961 ESLTRNI-QIKEDLIKDLQMQLVDPEDIPAME-RLTQEVLLLREKVASVESQGQEISGNRRQQLLL 1024
Cdd:TIGR02169 451 KKQEWKLeQLAADLSKYEQELYDLKEEYDRVEkELSKLQRELAEAEAQARASEERVRGGRAVEEVL 516
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
519-740 |
6.97e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 46.29 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 519 QKLQRVVRQKERQLADAKqcvqfvEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEkyneirTQEQN 598
Cdd:pfam09787 14 QKAARILQSKEKLIASLK------EGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTE------LQELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 599 IQHLNHSLSHKEQLlQEFRELLQYRDNSDKTLEANemlLEKLRQRIHdkavaleraidekfSALEEKEKELRQLRLAVRE 678
Cdd:pfam09787 82 AQQQEEAESSREQL-QELEEQLATERSARREAEAE---LERLQEELR--------------YLEEELRRSKATLQSRIKD 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392289 679 RDHDLERLRDVL---SSNEATMQSMESLLR-------AKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQE 740
Cdd:pfam09787 144 REAEIEKLRNQLtskSQSSSSQSELENRLHqltetliQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGS 215
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
406-801 |
7.23e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 406 ELQEKIQQTEATNKILQEKL----------NEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMA 475
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKqeiknlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 476 KLREMLHQSQLGQLHSSEGTSPAQQQVALLdlqsalfcsQLEIQKLQRVVRQKERQLAdakqcvqfveaaahESEQQKEA 555
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVL---------SRSINKIKQNLEQKQKELK--------------SKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 556 SWKHNQELR---KALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSH---KEQLLQEFRELLQYRDNSDKT 629
Cdd:TIGR04523 501 LNEEKKELEekvKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlEKEIDEKNKEIEELKQTQKSL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 630 LEANEMLLEKLRQRiHDKAVALERAIDEKFSALEEKEKELRQLRLAVRErdhdlerlrdvLSSNEATMQSMESLLRAkgl 709
Cdd:TIGR04523 581 KKKQEEKQELIDQK-EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK-----------LSSIIKNIKSKKNKLKQ--- 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 710 EVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQT-----SLHDRNKEVEDLSATLLCKLGPGQSEIAEELcQRLQ 784
Cdd:TIGR04523 646 EVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwlkelSLHYKKYITRMIRIKDLPKLEEKYKEIEKEL-KKLD 724
|
410
....*....|....*..
gi 2056392289 785 RKERMLQDLLSDRNKQV 801
Cdd:TIGR04523 725 EFSKELENIIKNFNKKF 741
|
|
| zf-AD |
pfam07776 |
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical ... |
4-74 |
9.67e-05 |
|
Zinc-finger associated domain (zf-AD); The zf-AD domain, also known as ZAD, forms an atypical treble-cleft-like zinc co-ordinating fold. The zf-AD domain is thought to be involved in mediating dimer formation, but does not bind to DNA.
Pssm-ID: 462262 Cd Length: 75 Bit Score: 41.67 E-value: 9.67e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392289 4 ICRICARELcgNQRRWIFHTASK-LNLQVLLSHVLGKDVPR-DGKAEFACSKCAFMLDRIYRFDTVIARIEAL 74
Cdd:pfam07776 1 VCRLCLDES--DELIPIFDPSDSeKTLAEILEDCTGIELDPnDLLPKQICERCLSKLQEFYSFRERCLESQEL 71
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
390-856 |
1.19e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 390 HETTITQQSVSDSH-------LAELQEKIQQTEATNKILQEKLNEMSyelkcAQESSQKQDgtIQNLKETLKSRERETEE 462
Cdd:pfam10174 270 REEEIKQMEVYKSHskfmknkIDQLKQELSKKESELLALQTKLETLT-----NQNSDCKQH--IEVLKESLTAKEQRAAI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 463 LYQVIEGQNDTMAKLREMLH--QSQLGQLHSSEGTspaqQQVALLDLQSALFCS-------QLEIQKLQRVVRQKERQLA 533
Cdd:pfam10174 343 LQTEVDALRLRLEEKESFLNkkTKQLQDLTEEKST----LAGEIRDLKDMLDVKerkinvlQKKIENLQEQLRDKDKQLA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 534 DAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLL 613
Cdd:pfam10174 419 GLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 614 QEFRELLQ-------YRDNSDKTLEAN-------EMLLEKLRQRIHDKAVAlERAIDEKFSALEEKEKELRQLRLAVRER 679
Cdd:pfam10174 499 IDLKEHASslassglKKDSKLKSLEIAveqkkeeCSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQEVARYKEESGKA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 680 DHDLERLRDVL-------SSNEATMQSMESLLRAKGLEveqLSTTCQNLQWLKEEMETKfsrwqkeqesIIQQLQTSLHD 752
Cdd:pfam10174 578 QAEVERLLGILrevenekNDKDKKIAELESLTLRQMKE---QNKKVANIKHGQQEMKKK----------GAQLLEEARRR 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 753 RNKEVEDLSATLLCKLGPGQSEIAEEL----------CQRLQRKERMLQDLLSDRNKQVLEH-EMEIQGLLQSVStrEQE 821
Cdd:pfam10174 645 EDNLADNSQQLQLEELMGALEKTRQELdatkarlsstQQSLAEKDGHLTNLRAERRKQLEEIlEMKQEALLAAIS--EKD 722
|
490 500 510
....*....|....*....|....*....|....*.
gi 2056392289 822 SQAAAEKLVQALMERNS-ELQALRQYlggRDSLMSQ 856
Cdd:pfam10174 723 ANIALLELSSSKKKKTQeEVMALKRE---KDRLVHQ 755
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
406-742 |
1.24e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.25 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 406 ELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLREMlHQSQ 485
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAA-HSFV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 486 LGQLHSS-----EGTSPAQQQVALLDLQSALFCSQL-----EIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQqkea 555
Cdd:pfam05483 351 VTEFEATtcsleELLRTEQQRLEKNEDQLKIITMELqkkssELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 556 swkhnqelrkaLQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEFRELLQYR--DNSDKTLEAN 633
Cdd:pfam05483 427 -----------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEklKNIELTAHCD 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 634 EMLLE--KLRQRIHDKAVAL-------------ERAIDEKFSALEEKEKELRQLRLAVRER-DHDLERLRDVLSSNEATM 697
Cdd:pfam05483 496 KLLLEnkELTQEASDMTLELkkhqediinckkqEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENA 575
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2056392289 698 QSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESI 742
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
550-699 |
1.35e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.13 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 550 EQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKY------NEIRTQEQNIQHLNHslsHKEQLLQEFRELLQYR 623
Cdd:pfam13851 46 EKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQslknlkARLKVLEKELKDLKW---EHEVLEQRFEKVERER 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 624 DNsdkTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDL----ERLRDVLSSNEATMQS 699
Cdd:pfam13851 123 DE---LYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQLNEVLAAANLDPDALqavtEKLEDVLESKNQLIKD 199
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
561-1116 |
1.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 561 QELRKALQQLQEELQNKSQQLRAWE-----AEKYNEIRTQEQNIQHLNHSLSH--KEQLLQEFRELLQYRDNSDKTLEAN 633
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEpirelAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 634 EMLLEKLRQRIHDKAVALERAIDE-KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVE 712
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 713 QLSTTCQNLQwlkEEMETKFSRWQKEqesiIQQLQTSLHDRNKEVEDLSATLLCkLGPGQSEIAEELCQRLQRKERMLQ- 791
Cdd:COG4913 391 ALLEALEEEL---EALEEALAEAEAA----LRDLRRELRELEAEIASLERRKSN-IPARLLALRDALAEALGLDEAELPf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 792 --DLLsdrnkQVLEHEME----IQGLLQSVSTR-----EQESQAAA--------EKLV-QALMERNSELQA--------- 842
Cdd:COG4913 463 vgELI-----EVRPEEERwrgaIERVLGGFALTllvppEHYAAALRwvnrlhlrGRLVyERVRTGLPDPERprldpdsla 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 843 -------------LRQYLGGRDSLM---SQAPISNQQAEVTPTGrLGKQtdqgsmqipsrddSTSLTAKEDVSIPRST-- 904
Cdd:COG4913 538 gkldfkphpfrawLEAELGRRFDYVcvdSPEELRRHPRAITRAG-QVKG-------------NGTRHEKDDRRRIRSRyv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 905 LGD--LDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAA--DMESLTRNIQIKEDLIKDLQmq 980
Cdd:COG4913 604 LGFdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAELEAELERLD-- 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 981 lvdpEDIPAMERLTQEVLLLREKVASVESQGQEISGNRRQqlllmlegLVDERSRLNEALQAERQLYSSLVKFHAHPESS 1060
Cdd:COG4913 682 ----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGR--------LEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392289 1061 ERDRTLQVELEGAQV--LRSRLEEVLGRSLERLNRLETlaaigggELESVRIHHKHAY 1116
Cdd:COG4913 750 LLEERFAAALGDAVEreLRENLEERIDALRARLNRAEE-------ELERAMRAFNREW 800
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
337-709 |
3.19e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.74 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 337 LNRSLKPLYKTPVSYPLELSDLQELWDdlcEDYLPLRVQpmteelLKQQKLnSHETTITQQSVsdsHLAELQEKIQQTEA 416
Cdd:pfam07111 286 LTRKIQPSDSLEPEFPKKCRSLLNRWR---EKVFALMVQ------LKAQDL-EHRDSVKQLRG---QVAELQEQVTSQSQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 417 TNKILQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERET----EELYQVIEGQNDTMAKLREMLHQSQ------- 485
Cdd:pfam07111 353 EQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTasaeEQLKFVVNAMSSTQIWLETTMTRVEqavarip 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 486 ---------LGQLHSSEGTSPAQQQVALLDLQS-----------ALFCSQLEIQKLQRVVRQKERQLAdAKQCVQFVEAA 545
Cdd:pfam07111 433 slsnrlsyaVRKVHTIKGLMARKVALAQLRQEScpppppappvdADLSLELEQLREERNRLDAELQLS-AHLIQQEVGRA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 546 AHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAW---------EAEKYNEIRTQEQNI--QHLNHSLSHKEQLLQ 614
Cdd:pfam07111 512 REQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVArqgqqesteEAASLRQELTQQQEIygQALQEKVAEVETRLR 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 615 EfrellQYRDNSDKTLEAnemlleklrQRIHDKAVALERAIDEKFSALEEKEKELRqlRLAVRERDHDLERLRDVLSSNE 694
Cdd:pfam07111 592 E-----QLSDTKRRLNEA---------RREQAKAVVSLRQIQHRATQEKERNQELR--RLQDEARKEEGQRLARRVQELE 655
|
410
....*....|....*
gi 2056392289 695 ATMQSMESLLRAKGL 709
Cdd:pfam07111 656 RDKNLMLATLQQEGL 670
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
540-831 |
5.17e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 540 QFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNksqqlraweAEK----YNEIRTQEqnIQHLNHSLSHKEQLLQE 615
Cdd:PLN02939 103 QRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQN---------AEKnillLNQARLQA--LEDLEKILTEKEALQGK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 616 FREL---LQYRDNSDKT-------LEANEMLLEKLRQRIHDKAV---ALERAIDEKFSALEEKEKELRQLRLAVR----- 677
Cdd:PLN02939 172 INILemrLSETDARIKLaaqekihVEILEEQLEKLRNELLIRGAtegLCVHSLSKELDVLKEENMLLKDDIQFLKaelie 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 678 -----ERDHDLERLRDVLssnEATMQSMESLLRAKGLEVEQLSTTCQNLQWLK-EEMETKFSRWQKEQESIIQQLQTSlH 751
Cdd:PLN02939 252 vaeteERVFKLEKERSLL---DASLRELESKFIVAQEDVSKLSPLQYDCWWEKvENLQDLLDRATNQVEKAALVLDQN-Q 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 752 DRNKEVEDLSATLlckLGPGQSEIAEELCQRLQRKERMLQDLLsdrnkQVLEHEMEIQGLLQSVSTreQESQAAAEKLVQ 831
Cdd:PLN02939 328 DLRDKVDKLEASL---KEANVSKFSSYKVELLQQKLKLLEERL-----QASDHEIHSYIQLYQESI--KEFQDTLSKLKE 397
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
496-679 |
5.62e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 496 SPAQQQVALLDLQSALfcsqLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEaswkhnqELRKALQQLQEELQ 575
Cdd:COG1579 1 AMPEDLRALLDLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 576 NKSQQLRAWEaEKYNEIRTQEQnIQHLNHSLSH----KEQLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIhdkaVAL 651
Cdd:COG1579 70 EVEARIKKYE-EQLGNVRNNKE-YEALQKEIESlkrrISDLEDEILELMERIEELEEELAELEAELAELEAEL----EEK 143
|
170 180
....*....|....*....|....*...
gi 2056392289 652 ERAIDEKFSALEEKEKELRQLRLAVRER 679
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAK 171
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
395-593 |
6.22e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 395 TQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELK--CAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQND 472
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 473 TMAKLREmlhqsqlgQLHSSEGTSPAQQQVALLDLQSalfcsqlEIQKLQRVVRQKERQLADAKQcvQFVEAAAHESEQQ 552
Cdd:COG3206 292 DVIALRA--------QIAALRAQLQQEAQRILASLEA-------ELEALQAREASLQAQLAQLEA--RLAELPELEAELR 354
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2056392289 553 KeaswkHNQELrKALQQLQEELQNKSQQLRAWEAEKYNEIR 593
Cdd:COG3206 355 R-----LEREV-EVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
901-1109 |
6.49e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 901 PRSTLGDLDTVAGLEKELSNAKEELELmAKKERESQMELSALQSMMAVQEEELQVQAADMESLT-----RNIQIKEDLIK 975
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALED-AREQIELLEPIRELAERYAAARERLAELEYLRAALRlwfaqRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 976 DLQMQLVDPEDipAMERLTQEVLLLREKVASVESQGQEISGNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLvkfHA 1055
Cdd:COG4913 299 ELRAELARLEA--ELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL---GL 373
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392289 1056 HPESSERD-----RTLQVELEGAQVLRSRLEEVLGRSLERLNRLETLAAIGGGELESVR 1109
Cdd:COG4913 374 PLPASAEEfaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
397-963 |
6.80e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 397 QSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQEssqkqdgtiqnLKETLKSRERETEELYQVIEgqndtmAK 476
Cdd:pfam01576 21 QQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEE-----------MRARLAARKQELEEILHELE------SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 477 LREMLHQSQlgQLHSSEgtSPAQQQVALLDlqsalfcSQLEIQKLQRVVRQKERQLADAKqcVQFVEAAAHESEQQkeas 556
Cdd:pfam01576 84 LEEEEERSQ--QLQNEK--KKMQQHIQDLE-------EQLDEEEAARQKLQLEKVTTEAK--IKKLEEDILLLEDQ---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 557 wkhNQELRKALQQLQEELQNKSQQLrAWEAEKyneirtqeqnIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEML 636
Cdd:pfam01576 147 ---NSKLSKERKLLEERISEFTSNL-AEEEEK----------AKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 637 LEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRE----RDHDLERLRDVLSSNEATMQSMESLLRAKGLEVE 712
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqKNNALKKIRELEAQISELQEDLESERAARNKAEK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 713 QLSTTCQNLQWLKEEMETKFS--------RWQKEQEsiIQQLQTSLHDRNKEVEdlsaTLLCKLGPGQSEIAEELCQRLQ 784
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTLDttaaqqelRSKREQE--VTELKKALEEETRSHE----AQLQEMRQKHTQALEELTEQLE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 785 RKERMLQDLlsDRNKQVLEHE-MEIQGLLQSVSTREQESQAAAEKL---VQALMERNSELQALRQYLGGRDSLMsQAPIS 860
Cdd:pfam01576 367 QAKRNKANL--EKAKQALESEnAELQAELRTLQQAKQDSEHKRKKLegqLQELQARLSESERQRAELAEKLSKL-QSELE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 861 N-----QQAEvTPTGRLGKQTDQGSMQIpsrDDSTSLTAKEDvsipRSTLGDLDTVAGLEKELSNAKEELELMAKKERES 935
Cdd:pfam01576 444 SvssllNEAE-GKNIKLSKDVSSLESQL---QDTQELLQEET----RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
570 580
....*....|....*....|....*...
gi 2056392289 936 QMELSALQSMMAVQEEELQVQAADMESL 963
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEAL 543
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
571-845 |
8.27e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 571 QEELQNKSQQLRAWEaEKYNEIRTQEQNIQHLNHSLSHKEQLLQEfrellQYRDNSDKTLEANEMlleklRQRIHDKAVA 650
Cdd:pfam01576 4 EEEMQAKEEELQKVK-ERQQKAESELKELEKKHQQLCEEKNALQE-----QLQAETELCAEAEEM-----RARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 651 LERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMEsllrakgLEVEQLSTTCQNLQ---WLKEE 727
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ-------LEKVTTEAKIKKLEediLLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 728 METKFSRWQKEQESIIQQLQTSLHDRNKEVEDLSatllcKLGPGQSEIAEELCQRLQRKERMLQDL----------LSDR 797
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLS-----KLKNKHEAMISDLEERLKKEEKGRQELekakrklegeSTDL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2056392289 798 NKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQ 845
Cdd:pfam01576 221 QEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
531-847 |
9.16e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 531 QLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQlraweaekyneIRTQEQNIQHLNHSLSHKE 610
Cdd:PRK11281 25 AFARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDK-----------IDRQKEETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 611 QLLQEF-RELLQYRDNSDKTLEANemlLEKLRQRihdkavALERAIDEKFSALEEKEKELRQLR-LAVRERDHdLERLRD 688
Cdd:PRK11281 94 AKLRQAqAELEALKDDNDEETRET---LSTLSLR------QLESRLAQTLDQLQNAQNDLAEYNsQLVSLQTQ-PERAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 689 VLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLqwlkeemetkfsrWQKEQESIiqQLQTSLhdRNKEVEdlSATLLCKL 768
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALL--NAQNDL--QRKSLE--GNTQLQDL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392289 769 GPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMeiqgllQSVSTREQESQAAAEKLVQALMERNSELQalrQYL 847
Cdd:PRK11281 225 LQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTV------QEAQSQDEAARIQANPLVAQELEINLQLS---QRL 294
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
610-840 |
1.08e-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: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 610 EQLLQEFRELLQYRDNSDKTLEANEML--LEKLRQRIHDKAVALE--RAIDEKFS------ALEEKEKELRQLRLAVRER 679
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLepIRELAERYAAARERLAelEYLRAALRlwfaqrRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 680 DHDLERLRDVLSSNEATMQSMESLLRAKGLE-VEQLSttcQNLQWLKEEMETKFSRWQkEQESIIQQLQTSLHDRNKEVE 758
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDrLEQLE---REIERLERELEERERRRA-RLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 759 DLSATLlcklgPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNS 838
Cdd:COG4913 384 ALRAEA-----AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEA 458
|
..
gi 2056392289 839 EL 840
Cdd:COG4913 459 EL 460
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
384-694 |
1.12e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 384 QQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEK-LNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEE 462
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 463 LYQVIEGQNDTMAKLREMLHQSQLGQLHS-----SEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQ 537
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLAllglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 538 CVQFVEAAAHESEQQK-----EASWKHNQELRKALQQLQEELQNKSqqlrawEAEKYNEIRTQEQNIQHLNHS--LSHKE 610
Cdd:COG4717 312 ALEELEEEELEELLAAlglppDLSPEELLELLDRIEELQELLREAE------ELEEELQLEELEQEIAALLAEagVEDEE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 611 QLLQEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLE-RLRDV 689
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEaELEQL 465
|
....*
gi 2056392289 690 LSSNE 694
Cdd:COG4717 466 EEDGE 470
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
523-967 |
1.21e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 523 RVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELrKALQQLQEELQNKSQQLRAWEAEKYNE---IRTQEQNI 599
Cdd:TIGR00606 169 KALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMEL-KYLKQYKEKACEIRDQITSKEAQLESSreiVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 600 QHLNHSLSHKEQLLQEFRELlqyrDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKElrqlrlAVRER 679
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKL----DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQR------TVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 680 DHDLERLRDVLSSNEATMQsmesLLRAKGLEVEQLSTTCQnlqwLKEEMETKFSRwqkEQESIIQQLQTSL------HDR 753
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERR----LLNQEKTELLVEQGRLQ----LQADRHQEHIR---ARDSLIQSLATRLeldgfeRGP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 754 NKEVE-DLSATLLCKLGPGQSEIAEELCQRLQRKERMLQ---DLLSDRNK---QVLEHEMEI----QGLLQSVSTREQES 822
Cdd:TIGR00606 387 FSERQiKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQeqaDEIRDEKKglgRTIELKKEIlekkQEELKFVIKELQQL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 823 QAAAEKLV---QALMERNSELQALRQYLGGRDSLMSQAPISNQQAEVTPTGR-LGKQTDQGSMQIPSRDDSTSLTAKEDV 898
Cdd:TIGR00606 467 EGSSDRILeldQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRkLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 899 SIPR-------------STLGDLDTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTR 965
Cdd:TIGR00606 547 KDEQirkiksrhsdeltSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
..
gi 2056392289 966 NI 967
Cdd:TIGR00606 627 KL 628
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
389-1099 |
1.22e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 389 SHETTI-TQQSVSDSHLAELQEKIQQTEATnkiLQEKLNEMSYELKCAQESSQKQDGTIQNLKETLKSRERETEELYQvi 467
Cdd:pfam12128 269 SDETLIaSRQEERQETSAELNQLLRTLDDQ---WKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAA-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 468 egqndtmaklremLHQSQLGQLHSSegtspaqqqvalLDLQSALFCSQLEiqKLQRVVRQKERQLADAK-QCVQFVEAAA 546
Cdd:pfam12128 344 -------------ADQEQLPSWQSE------------LENLEERLKALTG--KHQDVTAKYNRRRSKIKeQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 547 HESEQQKEASWKHNQELRKALQQLQEEL--QNKSQQLRAWEAEKYNEIRTQEQNIQhLNHSLSHKEQLLQefrellqyrd 624
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELreQLEAGKLEFNEEEYRLKSRLGELKLR-LNQATATPELLLQ---------- 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 625 nsdktLEANEMLLEKLRQrihdkavALERAidekFSALEEKEKELRQLRLAvreRDHDLERLRD----VLSSNEATMQSM 700
Cdd:pfam12128 466 -----LENFDERIERARE-------EQEAA----NAEVERLQSELRQARKR---RDQASEALRQasrrLEERQSALDELE 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 701 ESLLRAKGLEVEQLSTTCQNlqwlkeemetkfsrWQKEQESIIQQLQTSLHDRNKEVEDLSATLLCKLG----------- 769
Cdd:pfam12128 527 LQLFPQAGTLLHFLRKEAPD--------------WEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYgvkldlkridv 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 770 PGQSEIAEELCQRLQRKERMLQDlLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLgg 849
Cdd:pfam12128 593 PEWAASEEELRERLDKAEEALQS-AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK-- 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 850 rdslmSQAPISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKEdvsiprSTLGDLDTVAGLEKELSNAKEEL-ELM 928
Cdd:pfam12128 670 -----NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE------ARTEKQAYWQVVEGALDAQLALLkAAI 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 929 AKKERESQMELSALQSMMAvqeEELQVQAADMESLTRNIQIKEDLIKDLQMQLVDPEDIPAMERLTQEVLLLR-----EK 1003
Cdd:pfam12128 739 AARRSGAKAELKALETWYK---RDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRrprlaTQ 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 1004 VASVESQGQEISGN----------RRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAHPESSERDRTLQVELEGA 1073
Cdd:pfam12128 816 LSNIERAISELQQQlarliadtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQL 895
|
730 740
....*....|....*....|....*.
gi 2056392289 1074 QVLRSRLEEVLGRSLERLNRLETLAA 1099
Cdd:pfam12128 896 EDLKLKRDYLSESVKKYVEHFKNVIA 921
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
382-847 |
1.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 382 LKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMSYELKCAQESSQKQD--GTIQNLKETLKSRERE 459
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 460 TEELYQVIEGQNDTMAKLREMlhQSQLGQLhssegtspaQQQVAlldlqsalfcsqleiQKLQRVVRQKERQLADAKQCV 539
Cdd:COG4717 148 LEELEERLEELRELEEELEEL--EAELAEL---------QEELE---------------ELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 540 QFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEF--- 616
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 617 -------RELLQYRDNSDKTLEANEMLLEKLRQRIHDKAV-----ALERAIDEKFSALEEKEKELRQLRLAVRERDHDLE 684
Cdd:COG4717 282 vlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELeellaALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 685 RLRdvlssNEATMQSMESLLRAKGLEVEqlsttcqnlqwlkEEMETKFSRWQKEQE--SIIQQLQTSLHDRNKEVEDLSA 762
Cdd:COG4717 362 ELQ-----LEELEQEIAALLAEAGVEDE-------------EELRAALEQAEEYQElkEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 763 TLlcklgpGQSEIAEELcQRLQRKERMLQDLLSDRNKQVLEHEMEIQGLLQS--VSTREQESQAAAEKLvQALMERNSEL 840
Cdd:COG4717 424 AL------DEEELEEEL-EELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAEL-RELAEEWAAL 495
|
....*..
gi 2056392289 841 QALRQYL 847
Cdd:COG4717 496 KLALELL 502
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
577-1061 |
1.24e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 577 KSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEfrELLQYRDnsdktleanemllekLRQRIHDKAVALERAID 656
Cdd:pfam10174 43 KERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQD--ELRAQRD---------------LNQLLQQDFTTSPVDGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 657 EKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQ 736
Cdd:pfam10174 106 DKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 737 K--EQESIIQQLQTSLHDRNKEVEDLSATLLCKL-GPGQSEIAEELCQRLQRKERMLQDLlsDRNKQVLEHEMEI---QG 810
Cdd:pfam10174 186 RiaEAEMQLGHLEVLLDQKEKENIHLREELHRRNqLQPDPAKTKALQTVIEMKDTKISSL--ERNIRDLEDEVQMlktNG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 811 LLQSVSTREQESQAAA------------EKLVQALMERNSELQALRQYLggrDSLMSQAPISNQQAEVTptgrlgkqtdq 878
Cdd:pfam10174 264 LLHTEDREEEIKQMEVykshskfmknkiDQLKQELSKKESELLALQTKL---ETLTNQNSDCKQHIEVL----------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 879 gsmqipsrddSTSLTAKEDVSIPRSTLGDLDTVAGLEKE--LSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQ 956
Cdd:pfam10174 330 ----------KESLTAKEQRAAILQTEVDALRLRLEEKEsfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 957 AADMESLTRNIQIKE-------DLIKDLQMQ--------------LVDPEDIpaMERLT-QEVLLLREKVASVESQGQEI 1014
Cdd:pfam10174 400 QKKIENLQEQLRDKDkqlaglkERVKSLQTDssntdtalttleeaLSEKERI--IERLKeQREREDRERLEELESLKKEN 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2056392289 1015 SgNRRQQLLLMLEGLVDERSRLNEALQAERQLYSSLVKFHAHPESSE 1061
Cdd:pfam10174 478 K-DLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE 523
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
501-775 |
1.45e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 501 QVALLDLQSALFCSQLEIQKLQRVVRQKER-QLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEE--LQNK 577
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKkaTESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 578 SQQLRAWEAEK---------YNEIRTQEQNIQHLNHSLSHKEQLLQEFRE-LLQYRDNSDKTLEANEML--LEKLRQRIH 645
Cdd:COG5185 315 EEQLAAAEAEQeleeskretETGIQNLTAEIEQGQESLTENLEAIKEEIEnIVGEVELSKSSEELDSFKdtIESTKESLD 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 646 DKAVALERAIDEKFSAL-----------EEKEKELRQLR----------------LAVRERDHDLERLRDVLSSNEATMQ 698
Cdd:COG5185 395 EIPQNQRGYAQEILATLedtlkaadrqiEELQRQIEQATssneevskllneliseLNKVMREADEESQSRLEEAYDEINR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 699 SMESLLRAKGLEVEQLSttcQNLQWLKEEMETKFSRWQKEQESIIQ---QLQTSLHDRNKEVEDLSATLLCKLGPGQSEI 775
Cdd:COG5185 475 SVRSKKEDLNEELTQIE---SRVSTLKATLEKLRAKLERQLEGVRSkldQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
542-779 |
1.45e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 542 VEAAAHESEQQKEASwkhnQELRKALQQLQEELqNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHK-----EQLLQEF 616
Cdd:PRK03918 520 LEKKAEEYEKLKEKL----IKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 617 RELLQYRD------NSDKTLEANEMLLEKLRqrihDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHdlERLRDVL 690
Cdd:PRK03918 595 KELEPFYNeylelkDAEKELEREEKELKKLE----EELDKAFEELAETEKRLEELRKELEELEKKYSEEEY--EELREEY 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 691 SSNEATMQSMESllRAKGLEvEQLSTTCQNLQWLKEEMEtKFSRWQKEQESIIQQLQtSLHDRNKEVEDLSATL----LC 766
Cdd:PRK03918 669 LELSRELAGLRA--ELEELE-KRREEIKKTLEKLKEELE-EREKAKKELEKLEKALE-RVEELREKVKKYKALLkeraLS 743
|
250
....*....|...
gi 2056392289 767 KLGPGQSEIAEEL 779
Cdd:PRK03918 744 KVGEIASEIFEEL 756
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
634-845 |
1.74e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 634 EMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRlavreRDHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQ 713
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 714 LSTTCQNLQWLKEEMETKFSRWQkeQESIIQQLQTSLHDRNKEVEDLSATLlcklGPGQSEIaeelcQRLQRKERMLQDL 793
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELL--QSPVIQQLRAQLAELEAELAELSARY----TPNHPDV-----IALRAQIAALRAQ 306
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2056392289 794 LSDRNKQVLEhemEIQGLLQSVSTREQESQAAAEKL---VQALMERNSELQALRQ 845
Cdd:COG3206 307 LQQEAQRILA---SLEAELEALQAREASLQAQLAQLearLAELPELEAELRRLER 358
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
772-1081 |
2.14e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 772 QSEIAEELcQRLQRKERMLQ-DLLSDRNKQVLEHEMEIQGLLQSVSTREQESQAAAEKLVQALMERNSELQALRQYLGGR 850
Cdd:TIGR02168 208 QAEKAERY-KELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 851 DSLMSQapISNQQAEVTPTGRLGKQTDQGSMQIPSRDDSTSLTAKedvsipRSTLGDLDTVAGLEKELSNAKEELELMAK 930
Cdd:TIGR02168 287 QKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELE------SKLDELAEELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 931 KERESQMELSALQSMMAVQEEELQVQAAD-------MESLTRNIQIKEDLIKDLQMQLvdpedipamERLTQEVLLLREK 1003
Cdd:TIGR02168 359 ELEELEAELEELESRLEELEEQLETLRSKvaqlelqIASLNNEIERLEARLERLEDRR---------ERLQQEIEELLKK 429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392289 1004 VASVESQGQEISGNRRQQlllMLEGLVDERSRLNEALQAERQLYSslVKFHAHPESSERDRTLQVELEGAQVLRSRLE 1081
Cdd:TIGR02168 430 LEEAELKELQAELEELEE---ELEELQEELERLEEALEELREELE--EAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
548-1021 |
3.14e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 548 ESE-QQKEASWKHNQEL----RKALQQLQeeLQNKSQQLRAWEAEKYNEIRTQEQN-IQHL--------NHSLSHKEQLL 613
Cdd:pfam05483 98 EAElKQKENKLQENRKIieaqRKAIQELQ--FENEKVSLKLEEEIQENKDLIKENNaTRHLcnllketcARSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 614 QEFRELLQYRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQlrlAVRERDHDLERLRDVLSSN 693
Cdd:pfam05483 176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 694 EATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQTSLHDRNKEVEDL--SATLLCKLGPG 771
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiATKTICQLTEE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 772 QSEIAEELCQ----------RLQRKERMLQDLLSDRNKQVLEHEMEiqglLQSVSTREQESQAAAEKLVQALMERNSELQ 841
Cdd:pfam05483 333 KEAQMEELNKakaahsfvvtEFEATTCSLEELLRTEQQRLEKNEDQ----LKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 842 ALRQYLGGRDSLMSQapisNQQAEVTPTGRLGKQTDQGSMqIPSRDDSTsltakEDVSIprstlgDLDTVAGLEKELSNA 921
Cdd:pfam05483 409 ELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFL-LQAREKEI-----HDLEI------QLTAIKTSEEHYLKE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 922 KEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQikEDLIKDLQMQlvdpedipamERLTQEVLLLR 1001
Cdd:pfam05483 473 VEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ--EDIINCKKQE----------ERMLKQIENLE 540
|
490 500
....*....|....*....|
gi 2056392289 1002 EKVASVESQGQEISGNRRQQ 1021
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQK 560
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
498-1091 |
3.44e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 498 AQQQVALLDLQSALFcSQLEIQKLQRVVRQKERQLADAkqcvqfvEAAAHESEQQKEAswkHNQELRKALQQLQeelQNK 577
Cdd:COG4913 271 LAELEYLRAALRLWF-AQRRLELLEAELEELRAELARL-------EAELERLEARLDA---LREELDELEAQIR---GNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 578 SQQLRAWEAEkyneirtqeqnIQHLNHSLSHKEQLLQEFRELLQyrdNSDKTLEANEMLLEKLRQRIHDKAVALERAIDE 657
Cdd:COG4913 337 GDRLEQLERE-----------IERLERELEERERRRARLEALLA---ALGLPLPASAEEFAALRAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 658 KFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSMESLLRakglevEQLSTTCQNLQWLKE--EMETKFSRW 735
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA------EALGLDEAELPFVGEliEVRPEEERW 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 736 QKEQE---------------------SIIQQLQTSLH---------DRNKEVEDLSA-TLLCKL----GPGQSEIAEELC 780
Cdd:COG4913 477 RGAIErvlggfaltllvppehyaaalRWVNRLHLRGRlvyervrtgLPDPERPRLDPdSLAGKLdfkpHPFRAWLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 781 QR-----------LQRKER--MLQDLLSDRNKQvleHEMEIQGLLQSV-----STREQ-----ESQAAAEKLVQALMERN 837
Cdd:COG4913 557 RRfdyvcvdspeeLRRHPRaiTRAGQVKGNGTR---HEKDDRRRIRSRyvlgfDNRAKlaaleAELAELEEELAEAEERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 838 SELQALRQYLGGRDSLMSQapISNQQAEvtptgrlgkqtdqgsmqipsrddstsltakedvsiprstlgDLDtVAGLEKE 917
Cdd:COG4913 634 EALEAELDALQERREALQR--LAEYSWD-----------------------------------------EID-VASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 918 LSNAKEELELMakkeRESQMELSALQSMMAVQEEELQVQAADMESLTRNI-----QIK--EDLIKDLQMQLVDPEDIPAm 990
Cdd:COG4913 670 IAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIgrlekELEqaEEELDELQDRLEAAEDLAR- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 991 erlTQEVLLLREKVAsvesqgQEISGNRRQQlllMLEGLVDERSRLNEAL-QAERQLYSSLVKFHAHPESSERDrtLQVE 1069
Cdd:COG4913 745 ---LELRALLEERFA------AALGDAVERE---LRENLEERIDALRARLnRAEEELERAMRAFNREWPAETAD--LDAD 810
|
650 660
....*....|....*....|..
gi 2056392289 1070 LEGAQVLRSRLEEVLGRSLERL 1091
Cdd:COG4913 811 LESLPEYLALLDRLEEDGLPEY 832
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
354-587 |
3.64e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 354 ELSDLQELWDDLcEDYLPLRVQPMTEELLKQQKLNSHETTITQqsvsdSHLAELQEKIQQTEATNKILQEKLNEMSYELK 433
Cdd:TIGR02169 252 ELEKLTEEISEL-EKRLEEIEQLLEELNKKIKDLGEEEQLRVK-----EKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 434 CAQESSQKQDGTIQNLKETLKSRERETEELYQVIEGQNDTMAKLRemlhqSQLGQLHSSEGTS---PAQQQVALLDLQSA 510
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR-----AELEEVDKEFAETrdeLKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 511 LFCSQLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKE--------ASWKHNQ--------------------E 562
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkaleikkQEWKLEQlaadlskyeqelydlkeeydR 480
|
250 260
....*....|....*....|....*
gi 2056392289 563 LRKALQQLQEELQNKSQQLRAWEAE 587
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEER 505
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
515-1046 |
4.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 515 QLEIQKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQlQEELQNKSQQLRAWEAEKYNEIRT 594
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARIEELRAQEAV 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 595 QEQNIQHLNHSlSHKEQLLQEFRELLQYRDNSDK---TLEANEMLLEKLRQriHDKAVALERAIDEKFSALEekEKELRQ 671
Cdd:TIGR00618 279 LEETQERINRA-RKAAPLAAHIKAVTQIEQQAQRihtELQSKMRSRAKLLM--KRAAHVKQQSSIEEQRRLL--QTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 672 LRLAVRERDHDLERlRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQlqtsLH 751
Cdd:TIGR00618 354 EIHIRDAHEVATSI-REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL----AH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 752 DRNKEVEDLSATLLCKLGPG---QSEIAEE-LCQRLQRKERMLQDLLSDRnKQVLEHEMEIQGLLQSVSTREQESQAAAE 827
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITctaQCEKLEKiHLQESAQSLKEREQQLQTK-EQIHLQETRKKAVVLARLLELQEEPCPLC 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 828 KlvqALMERNSELQALRQyLGGRDSLMSQ---APISNQQAEVTPTGRLGKQTDQG---SMQIPSRDDSTSLTAKEDVSIP 901
Cdd:TIGR00618 508 G---SCIHPNPARQDIDN-PGPLTRRMQRgeqTYAQLETSEEDVYHQLTSERKQRaslKEQMQEIQQSFSILTQCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 902 RSTLGDLDTVAGLEKELsnaKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMEsltrnIQIKEDLIKDLQMQL 981
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLT---EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE-----LALKLTALHALQLTL 655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2056392289 982 VDPEDIPAMERLTQEVLLLREKVASVESQGQeisgNRRQQLLLMLEGLVDERSRLNEALQAERQL 1046
Cdd:TIGR00618 656 TQERVREHALSIRVLPKELLASRQLALQKMQ----SEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
519-668 |
5.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 519 QKLQRVVRQKERQL-ADAKQCVQFVEAAAHE--SEQQKEASWKHN--QELRKALQQLQEELQNKSQQLRaweaEKYNEIR 593
Cdd:PRK12704 38 EEAKRILEEAKKEAeAIKKEALLEAKEEIHKlrNEFEKELRERRNelQKLEKRLLQKEENLDRKLELLE----KREEELE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392289 594 TQEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTL---EANEMLLEKLRQRIHDKAVALERAIDEKfsALEEKEKE 668
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLtaeEAKEILLEKVEEEARHEAAVLIKEIEEE--AKEEADKK 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
379-747 |
5.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 379 EELLKQQKLNSHETTITQQSVSDSHLAELQEKIQQTEATNKILQEKLNEMS--------YELKCAQESSQKQDGTIQNLK 450
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeleaelaeLQEELEELLEQLSLATEEELQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 451 ETLKSRERETEELYQVIEGQNDTMAKLREmlHQSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKER 530
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 531 QLADAKQCVQFVEAAAHESEQQKEASwkhNQELRKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKE 610
Cdd:COG4717 274 TIAGVLFLVLGLLALLFLLLAREKAS---LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 611 QLLQEFRELLQYRDnsdktLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVL 690
Cdd:COG4717 351 ELLREAEELEEELQ-----LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392289 691 S--SNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMET--KFSRWQKEQESIIQQLQ 747
Cdd:COG4717 426 DeeELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELR 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
660-865 |
5.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 660 SALEEKEKELRQLRlavrerdHDLERLRDVLSSNEATMQSMESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEq 739
Cdd:COG4942 20 DAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 740 esiIQQLQTSLHDRNKEVEDLSATL--LCKLGPGQSEIAEELCQRLQRKERMLQDLLSDRNKQVleheMEIQGLLQSVST 817
Cdd:COG4942 92 ---IAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA----EELRADLAELAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2056392289 818 REQESQAAAEKLVQALMERNSELQALRQYLGGRDSLMSQAPISNQQAE 865
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
419-829 |
5.75e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 419 KILQEKLNEMSYELKCAQESSQ-------KQDGTIQNLKETLKSRE---RETEELYQVIEGQndtmaklremlhqsqlgq 488
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKslsklknKHEAMISDLEERLKKEEkgrQELEKAKRKLEGE------------------ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 489 lhssegTSPAQQQVALLdlqsalfcsQLEIQKLQRVVRQKERQLADAkqcvqfvEAAAHESEQQKEASWKHNQELRKALQ 568
Cdd:pfam01576 217 ------STDLQEQIAEL---------QAQIAELRAQLAKKEEELQAA-------LARLEEETAQKNNALKKIRELEAQIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 569 QLQEELQ------NKSQQLRAWEAEKYNEIRTQ------------------EQNIQHLNHSLSHK----EQLLQEFREll 620
Cdd:pfam01576 275 ELQEDLEseraarNKAEKQRRDLGEELEALKTEledtldttaaqqelrskrEQEVTELKKALEEEtrshEAQLQEMRQ-- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 621 qyrdnsdKTLEANEMLLEKLRQRIHDKAvALERAIDEKFSALEEKEKELRQLRLAVRERDHDLERLRDVLSSNEATMQSM 700
Cdd:pfam01576 353 -------KHTQALEELTEQLEQAKRNKA-NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 701 ESLLRAKGLEVEQLSTTCQNLQWLKEEMETKFSRWQKEQESIIQQLQT-------------SLHDRNKEVEDLSATLLck 767
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDtqellqeetrqklNLSTRLRQLEDERNSLQ-- 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392289 768 lgpGQSEIAEELCQRLQRKERMLQDLLSDRNKQVLEHEMEIQGL----------LQSVSTREQESQAAAEKL 829
Cdd:pfam01576 503 ---EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrlqreLEALTQQLEEKAAAYDKL 571
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
463-625 |
6.26e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 463 LYQVIEGQNDTMAKLREMLhqSQLGQLHSSEGTSPAQQQVALLDLQSALFCSQLEIQKLQRVVRQKERQLADAKQCVQFV 542
Cdd:PRK09039 44 LSREISGKDSALDRLNSQI--AELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 543 EAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAekyneiRTQEQNIQ------HLNHSLSHKEQLLQ-- 614
Cdd:PRK09039 122 AQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEK------RDRESQAKiadlgrRLNVALAQRVQELNry 195
|
170
....*....|....*..
gi 2056392289 615 --EF----RELLQYRDN 625
Cdd:PRK09039 196 rsEFfgrlREILGDREG 212
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
595-1042 |
6.79e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 595 QEQNIQHLNHSLSHKEQLLQEFRELLQYRDNSDKTLEANEML---LEKLRQRIHDKAVALERAIDEKFSALEEKEKELRQ 671
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLhgkAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKH 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 672 LRLAVRERDHDLERLRDVLSSNEATmQSMESLLRAKGLEVEQLSTTCQNLQWLKEEME--TKFSRWQKEQESIIQ--QLQ 747
Cdd:TIGR00618 231 LREALQQTQQSHAYLTQKREAQEEQ-LKKQQLLKQLRARIEELRAQEAVLEETQERINraRKAAPLAAHIKAVTQieQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 748 TSLHDRNKEVEDLSATLLCKLGPGQSEIAEelcqrLQRKERMLQDLLSDRNKQVLEHEmeiqgllQSVSTREQESQAAAE 827
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSS-----IEEQRRLLQTLHSQEIHIRDAHE-------VATSIREISCQQHTL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 828 KlvQALMERNSELQALRQYLGGRDSLMSQapISNQQAEVTPtgrlgkqtdQGSMQIPSRDDSTSLTAKEDVSIPRSTLGD 907
Cdd:TIGR00618 378 T--QHIHTLQQQKTTLTQKLQSLCKELDI--LQREQATIDT---------RTSAFRDLQGQLAHAKKQQELQQRYAELCA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 908 LdTVAGLEKELSNAKEELELMAKKERESQMELSALQSMMAVQEEELQVQAADMESLTRNIQIKEDLIKDLQMQLVD---- 983
Cdd:TIGR00618 445 A-AITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidnp 523
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392289 984 PEDIPAMERLTQEVLLLREKVASVESQGQEISgNRRQQLLLMLEGLVDERSRLNEALQA 1042
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSER-KQRASLKEQMQEIQQSFSILTQCDNR 581
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
535-796 |
6.93e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 535 AKQCVQFVEAAAHESEQQKEASWKHNQELRKALQQLQEELQNKSQQLRAWEAEKYNEI-RTQEQ-------------NIQ 600
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIeELTDEllnlvmdiedpsaALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 601 HLNHSLSHKEQLLQEF-RELLQYRDNSD-----KTLEANEMLLEKLRQRIHDKAVALErAIDEKFSALEEKEKELRQLRL 674
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFqKVIKMYEKGGVcptctQQISEGPDRITKIKDKLKELQHSLE-KLDTAIDELEEIMDEFNEQSK 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 675 AVRErdhdlerLRDVLSSNEATMQSMESllRAKGLEVEqlsttcqnlqwlkeemetkfsrwqkeqesiIQQLQTSLHDRN 754
Cdd:PHA02562 338 KLLE-------LKNKISTNKQSLITLVD--KAKKVKAA------------------------------IEELQAEFVDNA 378
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2056392289 755 KEVEDLSATLLcKLGPGQSEIAEELCQRLqrkerMLQDLLSD 796
Cdd:PHA02562 379 EELAKLQDELD-KIVKTKSELVKEKYHRG-----IVTDLLKD 414
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
408-861 |
8.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 408 QEKIQQTEATNKILQEKLNEmsyELKCAQESSQKQDGTIQNLKETLKSRE--RETEELYQVIEGQN--DTMAKLREMLHQ 483
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKAD---EAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEAKKkaEEAKKADEAKKK 1491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 484 SQLGQLHSSEGTSPAQQQVALLDLQSALfcsqlEIQKLQRVVRQKERQLADAKQCVQFVEAAaheSEQQKEASWKHNQEL 563
Cdd:PTZ00121 1492 AEEAKKKADEAKKAAEAKKKADEAKKAE-----EAKKADEAKKAEEAKKADEAKKAEEKKKA---DELKKAEELKKAEEK 1563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 564 RKALQQLQEELQNKSQQLRAWEAEKYNEIRTQEQNIQHLNHSLSHKEQLLQEfrELLQYRDNSDKTLEANEMLLEKLRQR 643
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 644 IHD---KAVALERAIDE-KFSALEEKEKELRQLRLA--VRERDHDLERLRDVLSSNEATMQSMESLLRAKGLEV------ 711
Cdd:PTZ00121 1642 EAEekkKAEELKKAEEEnKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKkkaeel 1721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 712 ----EQLSTTCQNLQWLKEEMETKFSRWQKEQE--SIIQQLQTSLHDRNKEVEDLSATLLcklgpgQSEIAEELCQRLQR 785
Cdd:PTZ00121 1722 kkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLKKEEEKKAEEIRKEKEAVI------EEELDEEDEKRRME 1795
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392289 786 KERMLQDLLSdrNKQVLEhEMEIQGLLQSVSTREQESQAAAEKLVQALMERNsELQALRQYLGGRDSLMSQAPISN 861
Cdd:PTZ00121 1796 VDKKIKDIFD--NFANII-EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLE-EADAFEKHKFNKNNENGEDGNKE 1867
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
519-666 |
8.95e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392289 519 QKLQRVVRQKERQLADAKQCVQFVEAAAHESEQQKEASWKHNQEL-----RKALQQLQEELQNKSQQLraweAEKYNEIR 593
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQearreREELQREEERLVQKEEQL----DARAEKLD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392289 594 TQEQNIQHLNHSLSHKEQLLQEFRELLQ---YRDNSDKTLEANEMLLEKLRQRIHDKAVALERAIDEKFSALEEKE 666
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDnelYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERK 177
|
|
| |
