|
Name |
Accession |
Description |
Interval |
E-value |
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
34-248 |
2.30e-41 |
|
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 151.32 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 34 QKLKGPVAVVSLFGKALQGKSFIWNQLLSRSIGFEVQTLHRPCNGDIWMWIEPVKRisEDGTEYSLVLLDVELEDAKSI- 112
Cdd:cd01851 1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKD--TDGKKHAVLLLDTEGTDGRERg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 113 ---PTLGLNDIALDLS-RLLEIRKQDHVGEAKDN---------------TFFELGQFSPMFVQLMMDINSETVEGGEDVT 173
Cdd:cd01851 79 efeNDARLFALATLLSsVLIYNMWQTILGDDLDKlmgllktaletlglaGLHNFSKPKPLLLFVVRDFTGPTPLEGLDVT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15219566 174 QNSklkklrplllYGVDALMKFVSERVRPKQ-RGDTIVTGPPLAGFTKAFSENVNNNIVPKISSLWQTVEELEGRR 248
Cdd:cd01851 159 EKS----------ETLIEELNKIWSSIRKPFtPITCFVLPHPGLLHKLLQNDGRLKDLPPEFRKALKALRQRFFSS 224
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
206-441 |
5.82e-11 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 64.62 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 206 GDTIVTGPPLAGFTKAFSENVNNNIVPKISSLWQTVEELEGRRARDTATEVYMSSLER-----SETPDEsmLLEAHNKAV 280
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQkvklpTETLQE--LLDLHRDCE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 281 VEALTAFCESSIGnvEVKQKYKRDLWSFFAKALEDHKRvANVEAYSRCCNAI-----EDMGKKLWALPCSQDANIGDMIK 355
Cdd:pfam02841 79 KEAIAVFMKRSFK--DENQEFQKELVELLEAKKDDFLK-QNEEASSKYCSALlqdlsEPLEEKISQGTFSKPGGYKLFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 356 ALDTAVAEYEASingPMKWQKLSSFLRESVQD-------ILvhrrgnQMDELMSENSK-----------LKLQQQSLEST 417
Cdd:pfam02841 156 ERDKLEAKYNQV---PRKGVKAEEVLQEFLQSkeaveeaIL------QTDQALTAKEKaieaerakaeaAEAEQELLREK 226
|
250 260
....*....|....*....|....
gi 15219566 418 MNLLKKQLEGREKMNKEYQKRYES 441
Cdd:pfam02841 227 QKEEEQMMEAQERSYQEHVKQLIE 250
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
532-922 |
1.30e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 532 EQKAVTEKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRaELKKSA---LKVDECSSEAK 608
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAD-EAKKKAeeaKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 609 DVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKlVDSLKLEAEAAR 688
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-ADEAKKKAEEDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 689 DNENKLQTSLVERcIEIDRAKSRIEELEKVCTLNSGEGEasasKKLVDSMKMEAEASRKNENKLQTLLEDKciEIDRAKS 768
Cdd:PTZ00121 1405 KKADELKKAAAAK-KKADEAKKKAEEKKKADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAK--KADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 769 RIEglerDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMElsetletrAK 848
Cdd:PTZ00121 1478 KAE----EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE--------EK 1545
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15219566 849 QNEEEVTKWQRIINAEKSKNIRENLMEKEDSFMVWDEATPMQRVKRLKVEAAVTCSGSDFAQETEEDSVSQESR 922
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
20-105 |
1.50e-09 |
|
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460516 Cd Length: 260 Bit Score: 59.69 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 20 NGKLKTDPEAIGALQKLKGPVAVVSLFGKALQGKSFIWNQLLSRSIGFEVQ-TLHRPCNGdIWMWIEPVKRisedGTEYS 98
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGgTVESETKG-IWMWCVPHPN----KPKHT 75
|
....*..
gi 15219566 99 LVLLDVE 105
Cdd:pfam02263 76 LVLLDTE 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
565-859 |
1.73e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.00 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 565 LDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDE 644
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 645 LDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEELEKvcTLNSG 724
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER--RIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 725 EGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAKSRIEGLERDCLKLKYAESEA-ATVKEL---VSSMKME 800
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELsEELRELeskRSELRRE 916
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15219566 801 VESARSNEKKLQLSLQEKTIEIDRAKGQIeaLERQKMELsETLETRAKQNEEEVTKWQR 859
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERL--SEEYSLTL-EEAEALENKIEDDEEEARR 972
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
532-869 |
2.77e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 532 EQKAVTEKIAAMEEKLKQASTTEDGLR-AEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDV 610
Cdd:COG1196 207 RQAEKAERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 611 RLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDN 690
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 691 ENKLQTSLVERCIEIDRAKSRIEELEKvctlnsgegeasaskklvdsmkmEAEASRKNENKLQTLLEDKCIEIDRAKSRI 770
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALR-----------------------AAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 771 EGLERDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAKQN 850
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330
....*....|....*....
gi 15219566 851 EEEVTKWQRIINAEKSKNI 869
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
538-891 |
3.35e-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: 61.24 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 538 EKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLL 617
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 618 NEKYESVksaselletetetlKREKDELDKKCH---IHLEELEKLVLRLTnvESEALEAKKLVDSLKLEAEAARDNE--- 691
Cdd:TIGR02169 250 EEELEKL--------------TEEISELEKRLEeieQLLEELNKKIKDLG--EEEQLRVKEKIGELEAEIASLERSIaek 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 692 ----NKLQTSLVERCIEIDRAKSRIEELekvctlnsgEGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAK 767
Cdd:TIGR02169 314 erelEDAEERLAKLEAEIDKLLAEIEEL---------EREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 768 srieglerdclklkyaeSEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRA 847
Cdd:TIGR02169 385 -----------------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15219566 848 KQNEEEVTKWQRIInAEKSKNIRENLMEKEDSFMVWDEATPMQR 891
Cdd:TIGR02169 448 LEIKKQEWKLEQLA-ADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
583-854 |
1.30e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 583 EQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLR 662
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 663 LTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEELEKVctLNSGEGEASASKKLVDSMKMEA 742
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 743 EASRKNENKLQTLLEDKCIEIDRAKSRIEGLERDCLKLkyaESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEI 822
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270
....*....|....*....|....*....|..
gi 15219566 823 DRAKGQIEALeRQKMELSETLETRAKQNEEEV 854
Cdd:TIGR02168 911 SELRRELEEL-REKLAQLELRLEGLEVRIDNL 941
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
395-875 |
1.09e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.80 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 395 NQMDELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYE------SAIDDICKLSDQFKNRINDLESKCKSIH 468
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLklelllSNLKKKIQKNKSLESQISELKKQNNQLK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 469 DEHSNLMEVLGSTRLEASEWKRKYEGTLDENGVSNIRVGVDASITRCSNKLIDWKIKYENTVSEQ-------------KA 535
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnnqkeqdwnKE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 536 VTEKIAAMEEKLKQASTTedglraefsrvLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMS 615
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQ-----------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 616 LLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSL-------KLEAEAAR 688
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLtnqdsvkELIIKNLD 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 689 DNENKLQTSLVERCIEIDRAKSRIEEL-----EKVCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCIEI 763
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKqkelkSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 764 DRAKSRIEGLERDcLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETL 843
Cdd:TIGR04523 541 SDLEDELNKDDFE-LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
490 500 510
....*....|....*....|....*....|..
gi 15219566 844 ETRAKQNEEEVTKwqrIINAEKSKNIRENLME 875
Cdd:TIGR04523 620 EKAKKENEKLSSI---IKNIKSKKNKLKQEVK 648
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
357-954 |
1.66e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.51 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 357 LDTAVAEYEASINGPMKWQKLSSFLRESVQ---DILVHRRGNQmdelmseNSKLKLQQQSLESTMNLLKKQLegrekmnK 433
Cdd:pfam15921 269 IEQLISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQ-------NSMYMRQLSDLESTVSQLRSEL-------R 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 434 EYQKRYESAIDDICKLSDQFKNRINDLESKCKSIHDEHSNLMEVLgsTRLEASEWKRKYEGTLDENgvSNIRV-----GV 508
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL--QKLLADLHKREKELSLEKE--QNKRLwdrdtGN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 509 DASITRCSNKLIDWKIKYENTVSEQKAVT--------EKIAAME---EKLKQASTtedgLRAEFSRVLDEKEKIITEKAA 577
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMKsecqgqmeRQMAAIQgknESLEKVSS----LTAQLESTKEMLRKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 578 KLATLE---QQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSAS---ELLETETETLKREKDELDKKCHI 651
Cdd:pfam15921 487 KKMTLEsseRTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGdhlRNVQTECEALKLQMAEKDKVIEI 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 652 HLEELEKLvLRLTNVESEALEAKkLVDSLKLEAEAardNENKLQtsLVERCIEIDRAKSRIEELE---------KVCTLN 722
Cdd:pfam15921 567 LRQQIENM-TQLVGQHGRTAGAM-QVEKAQLEKEI---NDRRLE--LQEFKILKDKKDAKIRELEarvsdleleKVKLVN 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 723 SGEGEASASKKLV---DSMKMEAEASRkneNKLQTLLEDKCIEIDRAKSRIEGLERDC----LKLKYAESEAATVKELVS 795
Cdd:pfam15921 640 AGSERLRAVKDIKqerDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTnklkMQLKSAQSELEQTRNTLK 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 796 SMkmevESARSNEKKLQLSLQEktiEIDRAKGQIEALERQKMELSETLETRAKQneeevtkwQRIINAEKSKNIRE-NLM 874
Cdd:pfam15921 717 SM----EGSDGHAMKVAMGMQK---QITAKRGQIDALQSKIQFLEEAMTNANKE--------KHFLKEEKNKLSQElSTV 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 875 EKEDSFMVWDEATPMQRVKRLK-----VEAAVTCSGSDFA------QETEEDSV-------------------SQESRKV 924
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQERRLKekvanMEVALDKASLQFAecqdiiQRQEQESVrlklqhtldvkelqgpgytSNSSMKP 861
|
650 660 670
....*....|....*....|....*....|.
gi 15219566 925 RTMTPRRCTSSEAGATSS-STGTGHSKYTMK 954
Cdd:pfam15921 862 RLLQPASFTRTHSNVPSSqSTASFLSHHSRK 892
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
572-854 |
1.76e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 572 ITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHI 651
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 652 HLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEELEKvctlnsgegeasas 731
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE-------------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 732 kklvdsmKMEAEASRKNENKLQTLLEDKciEIDRAKSRIEGLER----------------DCLKLKYAESEAATVKELVS 795
Cdd:TIGR02168 380 -------QLETLRSKVAQLELQIASLNN--EIERLEARLERLEDrrerlqqeieellkklEEAELKELQAELEELEEELE 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15219566 796 SMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALeRQKMELSETLETRAKQNEEEV 854
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGV 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
523-924 |
2.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 523 KIKYENTVSEQKAVTEKIAAMEEKLKQASTTEDGLR--AEFSRVLDEKEKIITEKAAKLATLEQQLASTRA--ELKKSA- 597
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAe 1428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 598 --LKVDECSSEAKDVRlQMSLLNEKYESVKSASELLETETEtlKREKDELDKKChihlEELEKLvlrlTNVESEALEAKK 675
Cdd:PTZ00121 1429 ekKKADEAKKKAEEAK-KADEAKKKAEEAKKAEEAKKKAEE--AKKADEAKKKA----EEAKKA----DEAKKKAEEAKK 1497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 676 LVDSLKLEAEAARDNENKLQTSLVERCIEIDRA--KSRIEELEKVCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQ 753
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 754 TLLEDKCIEIDRAKSRIEGLERDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRA-------- 825
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaee 1657
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 826 --KGQIEALERQKMELSETLETRAKQNEEEVTKWQRIINAEKSKNIRENLMEKE-DSFMVWDEATPMQRVKRLKVEAAvt 902
Cdd:PTZ00121 1658 enKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEaEEKKKAEELKKAEEENKIKAEEA-- 1735
|
410 420
....*....|....*....|..
gi 15219566 903 csgsdfAQETEEDSVSQESRKV 924
Cdd:PTZ00121 1736 ------KKEAEEDKKKAEEAKK 1751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
414-728 |
2.98e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 414 LESTMNLLKKQLEGREKMnKEYQKRYESAIDDICKLS--------DQFKNRINDLESKCKSIHDEHSNLMEVLGSTRLEA 485
Cdd:TIGR02168 198 LERQLKSLERQAEKAERY-KELKAELRELELALLVLRleelreelEELQEELKEAEEELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 486 SEWKRKYEgtldengvsnirvgvdasitrcsnkliDWKIKYENTVSEQKAVTEKIAAMEEKLKQASTTEDGL---RAEFS 562
Cdd:TIGR02168 277 SELEEEIE---------------------------ELQKELYALANEISRLEQQKQILRERLANLERQLEELeaqLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 563 RVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALK--------------VDECSSEAKDVRLQMSLLNEKYESVKSAS 628
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAEleelesrleeleeqLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 629 ELLETETETLKREKDELDKKchIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRA 708
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKK--LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL 487
|
330 340
....*....|....*....|
gi 15219566 709 KSRIEELEKVCTLNSGEGEA 728
Cdd:TIGR02168 488 QARLDSLERLQENLEGFSEG 507
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-839 |
7.28e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 345 SQDANIGDMIKALDTAVAEYEASINgpmkwqKLSSFLRESVQDI-LVHRRGNQMDELMSENSKLKLQQQSLESTMNLLKK 423
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREIN------EISSELPELREELeKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 424 QLEGREKMNKEYQKR----------------YESAIDDICKLSDQFKNRINDLESKCKSIHDEHSNL---MEVLGSTRLE 484
Cdd:PRK03918 260 KIRELEERIEELKKEieeleekvkelkelkeKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeerIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 485 ASEWKRKYEGTLDENGVSNIRV-------GVDASITRCSNKLIDWKI-----KYENTVSEQKAVTEKIAAMEEKLKQAST 552
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHelyeeakAKKEELERLKKRLTGLTPeklekELEELEKAKEEIEEEISKITARIGELKK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 553 TEDGLRAEFS-------------RVLDEKEK--IITEKAAKLATLEQQLASTRA---ELKKSALKVDECSSEAKDVRLQM 614
Cdd:PRK03918 420 EIKELKKAIEelkkakgkcpvcgRELTEEHRkeLLEEYTAELKRIEKELKEIEEkerKLRKELRELEKVLKKESELIKLK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 615 SLLNEKYESVKSASELLETETETLKREKDELdkkchihLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENK- 693
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLEELEKKAEEYEKL-------KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEl 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 694 --LQTSLVERCIE-IDRAKSRIEELEKV----CTLNSGEGEASASKKLVDSMKMEAEASRKNenklqtlLEDKCIEIDRA 766
Cdd:PRK03918 573 aeLLKELEELGFEsVEELEERLKELEPFyneyLELKDAEKELEREEKELKKLEEELDKAFEE-------LAETEKRLEEL 645
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219566 767 KSRIEGLERdclklKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMEL 839
Cdd:PRK03918 646 RKELEELEK-----KYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
395-891 |
1.56e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 395 NQMDELMSENSKLKLQQQSLESTMNL-LKKQLEGREKMNKEYQKRYESAIDDICKL---SDQFKNRINDLESKCKSIHDE 470
Cdd:pfam05483 190 NNIEKMILAFEELRVQAENARLEMHFkLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqITEKENKMKDLTFLLEESRDK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 471 HSNLMEvlgSTRLEASEWKRKYEGTldengvsnirvgvdasiTRCSNKLIDWKIKYENTVSEQKA--------------V 536
Cdd:pfam05483 270 ANQLEE---KTKLQDENLKELIEKK-----------------DHLTKELEDIKMSLQRSMSTQKAleedlqiatkticqL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 537 TEKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECS--SEAKDVRLQ- 613
Cdd:pfam05483 330 TEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTkfKNNKEVELEe 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 614 -MSLLNEKyESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEaardNEN 692
Cdd:pfam05483 410 lKKILAED-EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE----KEK 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 693 KLQTSLVERC--IEIDRAKSRIEELEKVCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCIEI----DRA 766
Cdd:pfam05483 485 LKNIELTAHCdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEV 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 767 KSRIEGLERDCLKLKY----AESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSET 842
Cdd:pfam05483 565 KCKLDKSEENARSIEYevlkKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15219566 843 LETRAKQNEEEVTKWQRIInaEKSKNIRENLMEK-EDSFMVWDEATPMQR 891
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEI--EDKKISEEKLLEEvEKAKAIADEAVKLQK 692
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
526-853 |
1.68e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 526 YENTVSEQKAVTEKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLE-QQLASTRAELKKSAL--KVDE 602
Cdd:PRK02224 246 HEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlDDADAEAVEARREELedRDEE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 603 CSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKL 682
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 683 EAEAA-------RDNENKLQTSLVERCIEIDRAKSRIEELEK-------------------VCTLNSGEGE--------- 727
Cdd:PRK02224 406 DLGNAedfleelREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphVETIEEDRERveeleaele 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 728 ------ASASKKL---VDSMKMEAEASRKNENK--LQTLLEDKCIEIDRAKSRIEGLERDCLKLkyaESEAATVKELVSS 796
Cdd:PRK02224 486 dleeevEEVEERLeraEDLVEAEDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAEL---EAEAEEKREAAAE 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219566 797 MKMEVESARSNEKKLQLSLQEKTIEIDRAK------GQIEALERQKMELSETLETRAKQNEEE 853
Cdd:PRK02224 563 AEEEAEEAREEVAELNSKLAELKERIESLErirtllAAIADAEDEIERLREKREALAELNDER 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
654-852 |
2.15e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 654 EELEKLVLRLTNVESEALEAKKlvDSLKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEELEKvcTLNSGEGEASASKK 733
Cdd:TIGR02168 220 AELRELELALLVLRLEELREEL--EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE--EIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 734 LVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAKSRIEGLERDCLKLKYA--------ESEAATVKELVSSMKM------ 799
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKleelkeelESLEAELEELEAELEElesrle 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15219566 800 ----EVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAKQNEE 852
Cdd:TIGR02168 376 eleeQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
398-826 |
4.31e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 398 DELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYESAIDDICKLSDQFKNRINDLESKCKSIHDEHSNL--- 474
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnql 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 475 -MEVLGSTRLEASEWKRKYEGTLD--ENGVSNIRVGVDAS---ITRCSNKLIDWKIKYENTVSEQKAVTEKIAAMEEKLK 548
Cdd:TIGR04523 294 kSEISDLNNQKEQDWNKELKSELKnqEKKLEEIQNQISQNnkiISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 549 QASTTEDGLRAE----------FSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLN 618
Cdd:TIGR04523 374 KLKKENQSYKQEiknlesqindLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 619 EKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSL 698
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 699 VERCIEIDRAKSRIEELEKVCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAKSRIEGLERDCL 778
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 15219566 779 KLKYAESEAATVKELVSSMKMEVESArSNEKKLQLSLQEKTIEIDRAK 826
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSK-KNKLKQEVKQIKETIKEIRNK 660
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
393-715 |
5.56e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 393 RGNQMDELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYESAIDDICKLSDQFK---NRINDLESKCKSIHD 469
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArleAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 470 EHSNLMEVLGSTRLEASEWKRKYEGTLDEngvsniRVGVDASITRCSNKLIDWKIKYENTVSEQKAVTEKIAAMEEKLKQ 549
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAE------IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 550 ASTTedglRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASE 629
Cdd:TIGR02168 829 LERR----IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 630 LLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEakklvdSLKLEAEAARDNENKLQTSLVERCIEIDRAK 709
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....*.
gi 15219566 710 SRIEEL 715
Cdd:TIGR02168 979 NKIKEL 984
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
524-855 |
6.27e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 524 IKYENTVSEQKAvTEKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATL--EQQLASTRAELKKSALKVD 601
Cdd:pfam17380 278 VQHQKAVSERQQ-QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIyaEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 602 ECSSEAKDVRLQMslLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKlvlrltnvESEALEAKKLVDSLK 681
Cdd:pfam17380 357 ERKRELERIRQEE--IAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEER--------QRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 682 LEAEAARDNEnkLQTSLVERCIEIDRAksRIEELEKVCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLLEDKCI 761
Cdd:pfam17380 427 AEQEEARQRE--VRRLEEERAREMERV--RLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 762 EidRAKSRIEGLERDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSE 841
Cdd:pfam17380 503 E--RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
330
....*....|....
gi 15219566 842 TLETRAKQNEEEVT 855
Cdd:pfam17380 581 IVESEKARAEYEAT 594
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
538-928 |
9.25e-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: 49.97 E-value: 9.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 538 EKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKdvrlQMSLL 617
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE----RIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 618 NEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTS 697
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 698 LVERCIEIDRAKSRIEELEKVctlnsgEGEASASKKLVDSMKMEAEA-SRKNENKLQTLLEDKCIEIDRAKSRIEGLERD 776
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKE------LKELEIKREAEEEEEEELEKlQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 777 CLKLKYAESEAATVKELvSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAKQNEEEVTK 856
Cdd:pfam02463 397 LELKSEEEKEAQLLLEL-ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219566 857 WQRIINAEKSKNIRENLMEKEDSFMVWDEATPMQRVKRLKVEAAVTCSGSDFAQETEEDSVSQESRKVRTMT 928
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
643-895 |
1.19e-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: 49.30 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 643 DELDKKCHIHLEELEKLVLRLTNVESEALEAKKLVDSLKLEAEAArdnenklqtslvERCIEIDRAKSRIEELEKVCTLN 722
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKA------------ERYQALLKEKREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 723 SGEGEASASKKLVDSMKMEAEasrknenKLQTLLEDKCIEIDRAKSRIEGLERDCLKLkyAESEAATVKELVSSMKMEVE 802
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 803 SARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAKqneeEVTKWQ-RIINAEKSKN-IRENLMEKEDSF 880
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK----RRDKLTeEYAELKEELEdLRAELEEVDKEF 380
|
250
....*....|....*
gi 15219566 881 MVWDEATpMQRVKRL 895
Cdd:TIGR02169 381 AETRDEL-KDYREKL 394
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
533-875 |
1.66e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 533 QKAVTEKIAAMEEKLKQASTtedgLRAEFSRVLDEKEK---IITEKAAKLATLEQQLASTRAELKKSALKVDEcsSEAKD 609
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGE----IEKEIEQLEQEEEKlkeRLEELEEDLSSLEQEIENVKSELKELEARIEE--LEEDL 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 610 VRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKChIHLE-ELEKLVLRLTNVESEALEAKKLVDSLKLEAEAAR 688
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARL-REIEqKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 689 DNENKLQTSLVERCIEIDRAKSRIEELEKvctlnsgegEASASKKLVDSMKMEAEASRKNENKLQTlledkciEIDRAKS 768
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLES---------RLGDLKKERDELEAQLRELERKIEELEA-------QIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 769 RIEGLErdcLKLKYAESEAATVKELVSSMKMEVESARSNEkKLQLSLQEKTIEIDRAK----GQIEALERQKMELSETLE 844
Cdd:TIGR02169 918 RLSELK---AKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKE 993
|
330 340 350
....*....|....*....|....*....|.
gi 15219566 845 TRAKQNEEEVTKWQRIINAEKSKniRENLME 875
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKK--REVFME 1022
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
378-880 |
1.88e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 378 SSFLRESVQDILVHRRGNQMDELMSEnsklKLQQQSLESTMNLLKKQLegrekmnkeyqKRYESAIDDICKLSDQFKNRI 457
Cdd:PRK01156 132 SIFVGQGEMDSLISGDPAQRKKILDE----ILEINSLERNYDKLKDVI-----------DMLRAEISNIDYLEEKLKSSN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 458 NDLESKCKSIHDEHSNLMEVLgstrleasewKRKYEGTLDENGVSNIRVGVDASITRCsNKLIDWKIKYENTVseQKAVT 537
Cdd:PRK01156 197 LELENIKKQIADDEKSHSITL----------KEIERLSIEYNNAMDDYNNLKSALNEL-SSLEDMKNRYESEI--KTAES 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 538 EKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKI---------ITEKAAKLATLEQQLASTRAELKKSAL---------- 598
Cdd:PRK01156 264 DLSMELEKNNYYKELEERHMKIINDPVYKNRNYIndyfkykndIENKKQILSNIDAEINKYHAIIKKLSVlqkdyndyik 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 599 ---KVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKK 675
Cdd:PRK01156 344 kksRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 676 LVDSLKLEAEAARDNENKLQ----------------TSLVERCIE-----IDRAKSRIEElekvcTLNSGEGEASA-SKK 733
Cdd:PRK01156 424 KVSSLNQRIRALRENLDELSrnmemlngqsvcpvcgTTLGEEKSNhiinhYNEKKSRLEE-----KIREIEIEVKDiDEK 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 734 LVDSMKMEAEASRKNENKLQTllEDKCIEIDRAKsrIEGLERDCLKLKYAESEAATVKELVSSMKMEVESARsNEKKLQL 813
Cdd:PRK01156 499 IVDLKKRKEYLESEEINKSIN--EYNKIESARAD--LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK-RTSWLNA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 814 SLQEKTIEIDRAKGQIEALERQKMELSETL--------------ETRAKQNEEEVTKWQRIIN-AEKSKNIRENLMEKED 878
Cdd:PRK01156 574 LAVISLIDIETNRSRSNEIKKQLNDLESRLqeieigfpddksyiDKSIREIENEANNLNNKYNeIQENKILIEKLRGKID 653
|
..
gi 15219566 879 SF 880
Cdd:PRK01156 654 NY 655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
395-672 |
2.14e-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: 48.51 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 395 NQMDELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYESAIDDICKLSDQ---FKNRINDLESKCKSIHDEH 471
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEieeLEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 472 SNLMEVLGSTRLEASEWKRKYEGTLDENGVSNIRVGVDAS-ITRCSNKLIDWKIKYENTVSEQKAVTEKIAAMEEKLKQA 550
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRErLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 551 STTEDGLRAEFSRVLDEKEKIITEKAA---KLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMS----LLNEKYES 623
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEglevRIDNLQER 944
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15219566 624 VKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALE 672
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIE 993
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
527-747 |
2.31e-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: 47.84 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 527 ENTVSEQKAVTEKIAAMEEKLKQASTTEDGLRAEfsrvLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSE 606
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 607 AKDVRLQMS-LLNEKYES---------VKSASELLETETETLKREKDELDKKchiHLEELEKLVLRLTNVESEALEAKKL 676
Cdd:COG4942 99 LEAQKEELAeLLRALYRLgrqpplallLSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15219566 677 VDSLKLEAEAARdneNKLQTSLVERCIEIDRAKSRIEELEKvcTLNSGEGEASASKKLVDSMKMEAEASRK 747
Cdd:COG4942 176 LEALLAELEEER---AALEALKAERQKLLARLEKELAELAA--ELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
404-806 |
2.76e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 404 NSKLKL-QQQSLESTMNLLKKQLEGR----EKMNKEYQKrYESAI---------DDICKLSDQFKNRINDLESKCKSIHD 469
Cdd:TIGR01612 1305 EKSLKIiEDFSEESDINDIKKELQKNlldaQKHNSDINL-YLNEIaniynilklNKIKKIIDEVKEYTKEIEENNKNIKD 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 470 EHSNLMEVLGSTRLEAS--EWKRKYEGTLDengvsnirvgvDASITRCSNKLidwkikyenTVSEQKAVTEKiAAMEEKL 547
Cdd:TIGR01612 1384 ELDKSEKLIKKIKDDINleECKSKIESTLD-----------DKDIDECIKKI---------KELKNHILSEE-SNIDTYF 1442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 548 KQASTTEDGLRAEFSRV--LDEKEKIITEKAAKLATLEQQLASTraELKKSALKVDECSSEAKDVRLQMSLLNEKYESVK 625
Cdd:TIGR01612 1443 KNADENNENVLLLFKNIemADNKSQHILKIKKDNATNDHDFNIN--ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYK 1520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 626 SASEL--LETETETLKREKDELDKKCHIHLEELE----KLVLRLTNVESEALEAKKlvDSLKLEAEAARDNE-NK----L 694
Cdd:TIGR01612 1521 KDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKdahkKFILEAEKSEQKIKEIKK--EKFRIEDDAAKNDKsNKaaidI 1598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 695 QTSL---VERCIEIDRAKSRIEElekvCTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLL----------EDKCI 761
Cdd:TIGR01612 1599 QLSLenfENKFLKISDIKKKIND----CLKETESIEKKISSFSIDSQDTELKENGDNLNSLQEFLeslkdqkkniEDKKK 1674
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15219566 762 EIDRAKSRIEGLERDCLKLK--YAESEAATVKELVSSMKMEVESARS 806
Cdd:TIGR01612 1675 ELDELDSEIEKIEIDVDQHKknYEIGIIEKIKEIAIANKEEIESIKE 1721
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
382-646 |
5.00e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 382 RESVQDILVHRRGNQMD--------ELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYESAIDDICKLSDQF 453
Cdd:PHA02562 153 RKLVEDLLDISVLSEMDklnkdkirELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 454 KNRINDLESKCKSIHDEHSNLMEVLGSTRLEASEWKRKYEG------TLDENGVSnirvgvdasiTRCSNKLIDwkikYE 527
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqkvikMYEKGGVC----------PTCTQQISE----GP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 528 NTVSEqkaVTEKIAAMEEKLKQASTTEDGLRAEFSRvLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEA 607
Cdd:PHA02562 299 DRITK---IKDKLKELQHSLEKLDTAIDELEEIMDE-FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
250 260 270
....*....|....*....|....*....|....*....
gi 15219566 608 KDVRLQMSLLNEKYESVKSAselleteTETLKREKDELD 646
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKT-------KSELVKEKYHRG 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
576-776 |
8.29e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 576 AAKLATLEQQLASTRAELkksalkvDECSSEAKDVRLQMSLLNEKYESVKSASELLETET--ETLKREKDELDKKchihL 653
Cdd:COG4913 609 RAKLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAE----L 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 654 EELEKLVLRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEELEKVCTLnsgEGEASASKK 733
Cdd:COG4913 678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL---ELRALLEER 754
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15219566 734 LvdsmkmEAEASRKNENKLQTLLEDkciEIDRAKSRIEGLERD 776
Cdd:COG4913 755 F------AAALGDAVERELRENLEE---RIDALRARLNRAEEE 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
607-845 |
4.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 607 AKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKL---VDSLKLE 683
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 684 AEAARDNENKLQTSLVERCIEIDRAKSRIEELE-KVCTLNSGEGEASASKKLVDSMKMEAEASRKNEnKLQTLLEDKCIE 762
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEeKVKELKELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 763 IDRAKSRIEGLERDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQ-LSLQEKTIEIDRAKGQIEALERQKMELSE 841
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELErLKKRLTGLTPEKLEKELEELEKAKEEIEE 405
|
....
gi 15219566 842 TLET 845
Cdd:PRK03918 406 EISK 409
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
707-873 |
7.58e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 707 RAKSRIEELEKvcTLNSGEGEASASKKLVDSMKMEAEASRKNENKLQTLLE---------DKCIEIDRAKSRIEGLERDC 777
Cdd:COG4913 607 DNRAKLAALEA--ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 778 LKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALE-RQKMELSETLETRakqneeevtk 856
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEER---------- 754
|
170
....*....|....*..
gi 15219566 857 WQRIINAEKSKNIRENL 873
Cdd:COG4913 755 FAAALGDAVERELRENL 771
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
516-923 |
9.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 516 SNKLIDWKIKYENTVSEQKAVTEKIAAMEE--------KLKQASTTEDGLRAEFSRVLDEKEKIitEKAAKLATLEQQLA 587
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEarkaedarKAEEARKAEDAKRVEIARKAEDARKA--EEARKAEDAKKAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 588 STRAELKKSALKVdecsSEAKDVR-LQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNV 666
Cdd:PTZ00121 1181 ARKAEEVRKAEEL----RKAEDARkAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRK 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 667 ESEALEAKKLVDSLKLEAEAARDNENKLQTSLVERCIEIDRA--KSRIEELEKvctlnsgegeASASKKLVDSMKMEAEA 744
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAeeKKKADEAKK----------KAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 745 SRKNENKLQTLLEDKcIEIDRAKSRIEGLERDCLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDR 824
Cdd:PTZ00121 1327 AKKKADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 825 AKGQIEALERQKMELSEtletrAKQNEEEVTKwqriinAEKSKNIREnlmEKEDSFMVWDEATPMQRVKRLKVEAAVTCS 904
Cdd:PTZ00121 1406 KADELKKAAAAKKKADE-----AKKKAEEKKK------ADEAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410
....*....|....*....
gi 15219566 905 GSDFAQETEEDSVSQESRK 923
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKK 1490
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
528-613 |
1.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 528 NTVSEQKAVTEKIAAMEEKLKQASTTEDGLRAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELK--KSALKVDECSS 605
Cdd:PRK09039 88 ASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAalEAALDASEKRD 167
|
....*...
gi 15219566 606 EAKDVRLQ 613
Cdd:PRK09039 168 RESQAKIA 175
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
762-856 |
1.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 762 EIDRAKSRIEGLERDCLKLK-----YAESEAATVKELVSSMKMEVESARS---NEKKLQLSLQEKTIEIDRAKGQIEALE 833
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKkeqdeASFERLAELRDELAELEEELEALKArweAEKELIEEIQELKEELEQRYGKIPELE 491
|
90 100
....*....|....*....|...
gi 15219566 834 RQKMELSETLETRAKQNEEEVTK 856
Cdd:COG0542 492 KELAELEEELAELAPLLREEVTE 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
398-719 |
1.54e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 398 DELMSENSKLKLQQQSLESTMNLLKKQLEGREKMNKEYQKRYESAIDDIcklsDQFKNRINDLESKCKSIHDEHSNLMEV 477
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE----EKLKERLEELEEDLSSLEQEIENVKSE 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 478 LGSTRLEASEWKRKYEGTLDEngVSNIRVGVDASITRCSNKLIDwkiKYENTVSEQKAVTEKIAAMEEKLKQASTTEDGL 557
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEA--LNDLEARLSHSRIPEIQAELS---KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 558 RAEFSRVLDEKEKIITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVrlqmsllnekyesvksaselletetet 637
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL--------------------------- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 638 lKREKDELDKkchiHLEELEKlvlRLTNVESEALEAKKLVDSLKLEAEAARDNENKLQtSLVERCIEIDRAKSRIEELEK 717
Cdd:TIGR02169 888 -KKERDELEA----QLRELER---KIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQA 958
|
..
gi 15219566 718 VC 719
Cdd:TIGR02169 959 EL 960
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
523-871 |
2.99e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 523 KIKYENTvsEQKAVTEKIAAMEEKLKQASTTEDGLRAEFSRVLDEkekiITEKAAKLATLEQQLASTRAELKKSALKVDE 602
Cdd:TIGR04523 69 KINNSNN--KIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE----IKNDKEQKNKLEVELNKLEKQKKENKKNIDK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 603 CSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLTNVESEALEAKKL---VDS 679
Cdd:TIGR04523 143 FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLesqISE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 680 LKLEAEAARDNENKLQTSLVERCIEIDRAKSRIEEL-----EKVCTLNSGEGEASASKKLVDSM-----KMEAEASRKNE 749
Cdd:TIGR04523 223 LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkdeqnKIKKQLSEKQKELEQNNKKIKELekqlnQLKSEISDLNN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 750 NKLQTLLEDKCIEIDRAKSRIEGLErdcLKLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEI------- 822
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEIQ---NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIeklkken 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15219566 823 DRAKGQIEALERQKMELSETLETRAKQNEEevtKWQRIINAEKSKNIRE 871
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQ---KDEQIKKLQQEKELLE 425
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
525-867 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 525 KYENTVSEQKAVTEKIAAMEEKLKQASTTEDGLRAEFSR----------------VLDEKEKIITEKAAKL----ATLEQ 584
Cdd:TIGR00618 335 KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhtltqhihtlqqqktTLTQKLQSLCKELDILqreqATIDT 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 585 QLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHIHLEELEKLVLRLT 664
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 665 NVESEALE-----------AKKLVDSLKLEAEAAR-----DNENKLQTSLVERCIEIDRAKSRIEELEKVCTLNSGEGEA 728
Cdd:TIGR00618 495 RLLELQEEpcplcgscihpNPARQDIDNPGPLTRRmqrgeQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 729 SASK----------------KLVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAKSRIEG---LERDCLKLKYAESEAAT 789
Cdd:TIGR00618 575 LTQCdnrskedipnlqnitvRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLqqcSQELALKLTALHALQLT 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 790 V---KELVSSMKMEVESARSNEKKlQLSLQEKTIEIDRAKGQIEALErQKMELSETLETRAKQNEEEVTKWQRIINAEKS 866
Cdd:TIGR00618 655 LtqeRVREHALSIRVLPKELLASR-QLALQKMQSEKEQLTYWKEMLA-QCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
.
gi 15219566 867 K 867
Cdd:TIGR00618 733 D 733
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
704-856 |
4.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 704 EIDRAKSRIEELEKVctlnsgegeasaskklVDSMKMEAEASRKNENKLQTLLEDKCIEIDRAKSRIEGLERDCLKLKYA 783
Cdd:COG1579 18 ELDRLEHRLKELPAE----------------LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15219566 784 ESEAATVKELvSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAKQNEEEVTK 856
Cdd:COG1579 82 LGNVRNNKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
779-864 |
7.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 779 KLKYAESEAATVKELVSSMKMEVESARSNEKKLQLSLQEKTIEIDRAKGQIEALERQKMELSETLETRAK---QNEEEVT 855
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyRSGGSVS 103
|
....*....
gi 15219566 856 KWQRIINAE 864
Cdd:COG3883 104 YLDVLLGSE 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
572-806 |
7.79e-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: 39.75 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 572 ITEKAAKLATLEQQLASTRAELKKSALKVDECSSEAKDVRLQMSLLNEKYESVKSASELLETETETLKREKDELDKKCHI 651
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219566 652 HLEELEKLVLRLtnVESEALEAKKLVDSLKLEAEAARDNENkLQTSLVERCIEIDRAKSRIEELEKVctlnsgEGEASAS 731
Cdd:COG4942 102 QKEELAELLRAL--YRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAAL------RAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15219566 732 KKLVDSMKMEAEASRKnenKLQTLLEDKCIEIDRAKSRIEGLERdclKLKYAESEAATVKELVSSMKMEVESARS 806
Cdd:COG4942 173 RAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAA---ELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| |
