|
Name |
Accession |
Description |
Interval |
E-value |
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
353-451 |
3.66e-32 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 118.93 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 353 EEKKKREG-CVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEIYSSDFYAERAAREKIHE 431
Cdd:pfam16516 1 EELKRKEMeKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80
|
90 100
....*....|....*....|
gi 1207171119 432 EKERLATQLEYVKKQNSQLQ 451
Cdd:pfam16516 81 EKEQLAAQLEYLQRQNQQLK 100
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
365-451 |
2.55e-26 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 102.04 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 365 DDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVK 444
Cdd:cd09803 1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80
|
....*..
gi 1207171119 445 KQNSQLQ 451
Cdd:cd09803 81 RENQELK 87
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
27-92 |
1.53e-18 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 79.83 E-value: 1.53e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171119 27 EETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVE 92
Cdd:pfam11577 2 EETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
496-521 |
4.41e-13 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 62.99 E-value: 4.41e-13
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
90-468 |
1.66e-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: 67.00 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 90 DVENEALKNQVKELEKSGAEcLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIadddlkvtkdls 169
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAE-LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV------------ 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 170 svpeasafsmpkaESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQtslpsaaetNASTEVKN 249
Cdd:TIGR02168 743 -------------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE---------QLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 250 LEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAEndcLKVQMESLQAAIKLEQKKTQD 329
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES---LAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 330 EKNNLNQLKDAYTKLFEDYSELQEEKKKREGCVSK--DDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKD-LETIS 406
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSElrRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAE 957
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207171119 407 VFQAQAEIYSSDFYAE-RAAREKIH----------EEKERLATQLEYVKKQNSQLQEEMESLgRHSMSEMQRR 468
Cdd:TIGR02168 958 ALENKIEDDEEEARRRlKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTEAKETL-EEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-396 |
1.08e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.32 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 1 MASGSSMMNGDISHPRgSGPGNLGSLEETLQQM----NTLIKENRDLKEALKQTNLSMKE---RFEGLSAWKEKQKEERD 73
Cdd:TIGR02169 655 MTGGSRAPRGGILFSR-SEPAELQRLRERLEGLkrelSSLQSELRRIENRLDELSQELSDasrKIGEIEKEIEQLEQEEE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 74 FLEQRLEEARTRLNTMDVENEALKNQVKELEKsgaeclhtELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSN--- 150
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEA--------RIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlee 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 151 --SFIEIRIADDDLKVTKdlssvpeasafSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHAD 228
Cdd:TIGR02169 806 evSRIEARLREIEQKLNR-----------LTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 229 ssaqtslpsAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLgdkqkvqAENDC 308
Cdd:TIGR02169 875 ---------AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-------SEIED 938
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 309 LKVQMESLQAAIKLE---QKKTQDEKNNLNQLKDAYTKLFEDYselqEEKKKRegcvsKDDYDELQTRFATAEKALADKQ 385
Cdd:TIGR02169 939 PKGEDEEIPEEELSLedvQAELQRVEEEIRALEPVNMLAIQEY----EEVLKR-----LDELKEKRAKLEEERKAILERI 1009
|
410
....*....|.
gi 1207171119 386 QKIDEMKMELF 396
Cdd:TIGR02169 1010 EEYEKKKREVF 1020
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
21-457 |
3.01e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.75 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 21 GNLGSLEETLQQmntliKENRDLKE---ALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRL---EEARTRLNTMDVENE 94
Cdd:PRK02224 187 GSLDQLKAQIEE-----KEEKDLHErlnGLESELAELDEEIERYEEQREQARETRDEADEVLeehEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 95 ALKNQVKELEKSGAEcLHTELEALRGQILRIQAEKNDLVAmnselqlKMGQGSPSNSFIEIRIADDDLKVTKDLSSVPEA 174
Cdd:PRK02224 262 DLRETIAETEREREE-LAEEVRDLRERLEELEEERDDLLA-------EAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 175 SAfSMPKAESEEQTVRQLLRSLRAETDEK----ERLQLTLQEARGRIAELESKLEHADSSAQTSlpSAAETNASTEVKNL 250
Cdd:PRK02224 334 RV-AAQAHNEEAESLREDADDLEERAEELreeaAELESELEEAREAVEDRREEIEELEEEIEEL--RERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 251 EDQLLKLCNELKQAQIKLDEAESMKRNLQDR------------CKDLEQDLG------TLKTQLGDKQKVQAENDCLKVQ 312
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTARERveeaealleagkCPECGQPVEgsphveTIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 313 MESLQAAI-KLEQ-KKTQDEKNNLNQLKDAYTKLFEDYSELQEEkkKREGCVSK-DDYDELQTRFATAEKALADKQQKID 389
Cdd:PRK02224 491 VEEVEERLeRAEDlVEAEDRIERLEERREDLEELIAERRETIEE--KRERAEELrERAAELEAEAEEKREAAAEAEEEAE 568
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207171119 390 EMKMELFQKEKDLETIsvfqaQAEIYSSDFYAER-AAREKIHEEKERLATQLEYVKKQNSQLQEEMESL 457
Cdd:PRK02224 569 EAREEVAELNSKLAEL-----KERIESLERIRTLlAAIADAEDEIERLREKREALAELNDERRERLAEK 632
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-330 |
4.89e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 41 RDLKEALKQT-NLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKELEKSGAEcLHTELEALR 119
Cdd:COG1196 216 RELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE-AQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 120 GQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDLKVTKDLSSVPEASAFSMPKAESEEQTVRQLLRSLRAE 199
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 200 TD---EKERLQLTLQEARGRIAELESKLEHADSSAQTSLpsAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKR 276
Cdd:COG1196 375 AEaeeELEELAEELLEALRAAAELAAQLEELEEAEEALL--ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1207171119 277 NLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKTQDE 330
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
193-450 |
7.46e-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: 58.53 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 193 LRSLRAETDEK-ERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEvkNLEDQLLKLCNELKQAQIKLDEA 271
Cdd:TIGR02168 272 LRLEVSELEEEiEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE--ELESKLDELAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 272 ESMKRNLQDRCKDLEQDLGTLKTQLGDKQKvqaendclkvQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSEL 351
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEE----------QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 352 QEEKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEIYSSDFYAERAAREKIHE 431
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
250
....*....|....*....
gi 1207171119 432 EKERLATQLEYVKKQNSQL 450
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGL 518
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
37-457 |
1.41e-08 |
|
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: 57.54 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 37 IKENRDLKEALKQTNLSMKERF--EGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQV----------KELE 104
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESElrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLEnfderierarEEQE 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 105 KSGA--ECLHTELEALRG----QILRIQAEKNDLVAMNSELQLKMGQGSP-SNSFIEI-------------RIADDDLKV 164
Cdd:pfam12128 482 AANAevERLQSELRQARKrrdqASEALRQASRRLEERQSALDELELQLFPqAGTLLHFlrkeapdweqsigKVISPELLH 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 165 TKDLssVPEASAFSmPKAESEEQTVR------------QLLRSLRAETDEKERlqlTLQEARGRIAELESKLEHAdsSAQ 232
Cdd:pfam12128 562 RTDL--DPEVWDGS-VGGELNLYGVKldlkridvpewaASEEELRERLDKAEE---ALQSAREKQAAAEEQLVQA--NGE 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 233 TSLPSAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEA-ESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAEnDCLKV 311
Cdd:pfam12128 634 LEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE-QKREA 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 312 QMESLQAAIKLEqkktQDEKNNLNQLKDAYTKLfedyselqEEKKKREgcvskddYDELQTRFATAEKALADKQQKIDEM 391
Cdd:pfam12128 713 RTEKQAYWQVVE----GALDAQLALLKAAIAAR--------RSGAKAE-------LKALETWYKRDLASLGVDPDVIAKL 773
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171119 392 KMELFQKEKDLETISVFQAQAEIYsSDFYaeraaREKIHEEKERLATQLEYVKKQNSQLQEEMESL 457
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVLRY-FDWY-----QETWLQRRPRLATQLSNIERAISELQQQLARL 833
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
76-392 |
2.39e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 76 EQRLEEARTRLNT-MDVENEaLKNQVKELEK------------------------SGAECLHTELEALRGQILRIQAEKN 130
Cdd:COG1196 178 ERKLEATEENLERlEDILGE-LERQLEPLERqaekaeryrelkeelkeleaelllLKLRELEAELEELEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 131 DLVAMNSELQLKMGQgspsnsfIEIRIADDDLKVTKDLSSVPEASAfsmpKAESEEQTVRQLLRSLRAETDEKERLQLTL 210
Cdd:COG1196 257 ELEAELAELEAELEE-------LRLELEELELELEEAQAEEYELLA----ELARLEQDIARLEERRRELEERLEELEEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 211 QEARGRIAELESKLEHADSSAQTSLPSAAETNAstEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLG 290
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEA--ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 291 TLKTQLGDKQKVQAEndcLKVQMESLQAAIKLEQKKTQDEKnnlNQLKDAYTKLFEDYSELQEEKKKREgcvskddydEL 370
Cdd:COG1196 404 ELEEAEEALLERLER---LEEELEELEEALAELEEEEEEEE---EALEEAAEEEAELEEEEEALLELLA---------EL 468
|
330 340
....*....|....*....|..
gi 1207171119 371 QTRFATAEKALADKQQKIDEMK 392
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-359 |
2.59e-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: 57.00 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 65 KEKQKEERDFLEQRLE-------EARTRLNTMDVE-NEALKNQVKELEKSGAE---------CLHTELEALRGQILRIQA 127
Cdd:TIGR02169 172 KEKALEELEEVEENIErldliidEKRQQLERLRRErEKAERYQALLKEKREYEgyellkekeALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 128 EKNDLVAMNSELQLKMGQgspsnsfIEIRIADDDLKVtKDLSSvpEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQ 207
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEE-------IEQLLEELNKKI-KDLGE--EEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 208 LTLQEARGRIAELESKLEHADSSAQTSlpSAAETNASTEVKNLEDQLLKLCN--------------ELKQAQIKLD---- 269
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEE--RKRRDKLTEEYAELKEELEDLRAeleevdkefaetrdELKDYREKLEklkr 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 270 EAESMKRN---LQDRCKDLEQDLGTLKTQLGDKQKVQAEndcLKVQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFE 346
Cdd:TIGR02169 400 EINELKREldrLQEELQRLSEELADLNAAIAGIEAKINE---LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
330
....*....|...
gi 1207171119 347 DYSELQEEKKKRE 359
Cdd:TIGR02169 477 EYDRVEKELSKLQ 489
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-410 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 22 NLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVK 101
Cdd:TIGR02168 713 ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 102 ELEKsgaeclhtELEALRGQILRIQAEKNDLVAMNSELQLKMGQgspsnsfieiriadddlkvtkdlssvpeasafSMPK 181
Cdd:TIGR02168 793 QLKE--------ELKALREALDELRAELTLLNEEAANLRERLES--------------------------------LERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 182 AESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHAdsSAQTSLPSAAETNASTEVKNLEDQLLKLCNEL 261
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL--LNERASLEEALALLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 262 KQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENdclkvqMESLQAAIKLEQKKTQDEKNNLNQLKDAY 341
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE------AEALENKIEDDEEEARRRLKRLENKIKEL 984
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207171119 342 TKLFEDYSELQEEKKKRegcvskddYDELQTRFATAEKALADKQQKIDEMkmelfqkekDLETISVFQA 410
Cdd:TIGR02168 985 GPVNLAAIEEYEELKER--------YDFLTAQKEDLTEAKETLEEAIEEI---------DREARERFKD 1036
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
23-467 |
2.32e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 23 LGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQK--EERDFLEQRLEEARTRLNtmDVENEALKNQV 100
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRLT--GLTPEKLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 101 KELEKSGAEcLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDL-KVTKDLSSVPEasafSM 179
Cdd:PRK03918 394 EELEKAKEE-IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLeEYTAELKRIEK----EL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 180 PKAESEEQTVRQLLRSLRAETDEKERLqLTLQEARGRIAELESKLEHADSSAQTSlpsaaetnASTEVKNLEDQLLKLCN 259
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNLEELEK--------KAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 260 E---LKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQ-----------MESLQAAIKLEQK 325
Cdd:PRK03918 540 EiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKelepfyneyleLKDAEKELEREEK 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 326 KTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLEti 405
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE-- 697
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207171119 406 svfqaqaeiyssDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHSMSEMQR 467
Cdd:PRK03918 698 ------------KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGE 747
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
192-403 |
1.16e-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: 50.92 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 192 LLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLpsaaetnasTEVKNLEDQLLKLCNELKQAQIKLDEA 271
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALL---------KQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 272 ESMKRNLQDRCKDLEQDLGTLKTQLGD-----------------------------KQKVQAENDCLKVQMESLQAAIKL 322
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 323 EQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKREGCVSKddydeLQTRFATAEKALADKQQKIDEMKMELFQKEKDL 402
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR-----LEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
.
gi 1207171119 403 E 403
Cdd:COG4942 237 A 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
170-458 |
1.99e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 170 SVPEASAFSMPKAESEEqtVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEhaDSSAQTSLPSAAETNASTEVKN 249
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAE--LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS--DASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 250 LEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDK---------QKVQAENDCLKVQMESLQAAI 320
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlshsriPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 321 KLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKREGCVSKDDYD---------ELQTRFATAEKALADKQQKIDEM 391
Cdd:TIGR02169 815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeleELEAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207171119 392 KMELFQKEKDLETISVFQAQAEIYSSDFYAERAAREKIHEEKERLATQLEY----------VKKQNSQLQEEMESLG 458
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsledVQAELQRVEEEIRALE 971
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-280 |
3.39e-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: 50.06 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 24 GSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKEL 103
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 104 EKSGAEcLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGSpsnsfIEIRIADDDLkvtkdlssvpeasafsmpkaE 183
Cdd:TIGR02168 357 EAELEE-LEAELEELESRLEELEEQLETLRSKVAQLELQIASLN-----NEIERLEARL--------------------E 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 184 SEEQTVRQLLRSLRAETDEKERLQL-TLQEARGRIAELESKLEHADSSAQTSLPSAAEtnastEVKNLEDQLLKLCNELK 262
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELkELQAELEELEEELEELQEELERLEEALEELRE-----ELEEAEQALDAAERELA 485
|
250
....*....|....*...
gi 1207171119 263 QAQIKLDEAESMKRNLQD 280
Cdd:TIGR02168 486 QLQARLDSLERLQENLEG 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-307 |
3.73e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 26 LEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKELEK 105
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 106 SGAEcLHTELEALRGQILRIQAEKNDLVAMNSELQLkmgqgspsnsfieiriadddlkvtkdlssvpeasafsmpKAESE 185
Cdd:COG1196 345 ELEE-AEEELEEAEAELAEAEEALLEAEAELAEAEE---------------------------------------ELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 186 EQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLpsAAETNASTEVKNLEDQLLKLCNELKQAQ 265
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1207171119 266 IKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAEND 307
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-264 |
3.81e-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: 48.99 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 37 IKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKELEKsgaeclhtELE 116
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK--------EIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 117 ALRGQilrIQAEKNDLVAMNSELQlKMGQGSPSNSFIEIRIADDDLKVTKDLSSVPEASAFSMPKAESEEQTVRQLLRSL 196
Cdd:COG4942 94 ELRAE---LEAQKEELAELLRALY-RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 197 RAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNAS--TEVKNLEDQLLKLCNELKQA 264
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqQEAEELEALIARLEAEAAAA 239
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-460 |
1.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 25 SLEETLQQMNTLIKENRDLKEAL------KQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKN 98
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELeklekeVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 99 QVKELEK-SGAECLHTELEALRGQIL----RIQAEKNDLVAMNSELQLKMGQGSPSNSFIEiRIADDDLKVTKDLSSV-P 172
Cdd:PRK03918 281 KVKELKElKEKAEEYIKLSEFYEEYLdelrEIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELeE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 173 EASAFSMPKAESEE----------QTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADS------SAQTSLP 236
Cdd:PRK03918 360 RHELYEEAKAKKEElerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaieelkKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 237 ------------------SAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQ--DRCKDLEQDLGTLktql 296
Cdd:PRK03918 440 vcgrelteehrkelleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKY---- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 297 gDKQKVQAENDCLKvQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKREGCVSK---DDYDELQTR 373
Cdd:PRK03918 516 -NLEELEKKAEEYE-KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 374 -------------FATAEKALADKQQKIDEMKMELFQKEKDLEtiSVFQAQAEIYSSDFYAERAAREKIHEEKERLATQL 440
Cdd:PRK03918 594 lkelepfyneyleLKDAEKELEREEKELKKLEEELDKAFEELA--ETEKRLEELRKELEELEKKYSEEEYEELREEYLEL 671
|
490 500
....*....|....*....|
gi 1207171119 441 EyvkKQNSQLQEEMESLGRH 460
Cdd:PRK03918 672 S---RELAGLRAELEELEKR 688
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
20-393 |
1.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 20 PGNLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQ----KEERDFLEQRLEEARTRLNTMDVENEA 95
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 96 LKNQVKELEKsgaeclhtelEALRGQILRIQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIAdddlkVTKDLSSVPEAS 175
Cdd:COG4717 225 LEEELEQLEN----------ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG-----VLFLVLGLLALL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 176 AFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELE----SKLEHADSSAQTSLPSAAETNASTEVKNLE 251
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeelLELLDRIEELQELLREAEELEEELQLEELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 252 DQLLKLcneLKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKvQAENDCLKVQMESLQAAIkleqkktQDEK 331
Cdd:COG4717 370 QEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG-ELEELLEALDEEELEEEL-------EELE 438
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207171119 332 NNLNQLKDAYTKLFEDYSELQEEKKKREgcvSKDDYDELQTRFATAEKALADKQQKIDEMKM 393
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLE---EDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
187-398 |
1.94e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 187 QTVRQLLRSLRAETDEKER---LQLTLQEARGRIAELESKLEHADSSAQtslPSAAETNASTEVKNLEDQLLKLCNELKQ 263
Cdd:PRK11281 63 QDLEQTLALLDKIDRQKEEteqLKQQLAQAPAKLRQAQAELEALKDDND---EETRETLSTLSLRQLESRLAQTLDQLQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 264 AQIKLDEAESMKRNLQDRckdLEQDLGTLKTQLgdkQKVQAENDCLKVQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTK 343
Cdd:PRK11281 140 AQNDLAEYNSQLVSLQTQ---PERAQAALYANS---QRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRK 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207171119 344 LFEDYSELQEEKKKRegcvskddYDELQTRFATAEKALADKQQKIDEMKMELFQK 398
Cdd:PRK11281 214 SLEGNTQLQDLLQKQ--------RDYLTARIQRLEHQLQLLQEAINSKRLTLSEK 260
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-461 |
6.65e-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: 45.82 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 346 EDYSELQEEKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLET----ISVFQAQAEIYSSDFYA 421
Cdd:TIGR02168 213 ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEElrleVSELEEEIEELQKELYA 292
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207171119 422 ERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHS 461
Cdd:TIGR02168 293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-406 |
8.42e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 189 VRQLLRSLRAETDE-KERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKNLEDQLLklcnelkQAQIK 267
Cdd:COG3206 162 LEQNLELRREEARKaLEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLA-------EARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 268 LDEAESMKRNLQDRCK-----------------------DLEQDLGTLKTQLGD--------KQKVQAENDCLKVQMESL 316
Cdd:COG3206 235 LAEAEARLAALRAQLGsgpdalpellqspviqqlraqlaELEAELAELSARYTPnhpdvialRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 317 QAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEkkkregcvskddYDELQTRFATAEKALADKQQKIDEMKMELF 396
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAE------------LRRLEREVEVARELYESLLQRLEEARLAEA 382
|
250
....*....|
gi 1207171119 397 QKEKDLETIS 406
Cdd:COG3206 383 LTVGNVRVID 392
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
47-339 |
1.19e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 47 LKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLntmdvenealknQVKELEKSGAECLHTELEALRGQIL-RI 125
Cdd:PLN02939 147 LNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARI------------KLAAQEKIHVEILEEQLEKLRNELLiRG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 126 QAEKNDLVAMNSELQLKMGQgspsnsfiEIRIADDDLKVTKDLSSVpeasafsmpkAESEEQTVrqllrslraeTDEKER 205
Cdd:PLN02939 215 ATEGLCVHSLSKELDVLKEE--------NMLLKDDIQFLKAELIEV----------AETEERVF----------KLEKER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 206 lqlTLQEARGRiaELESKLEHADSSAQTSLPSAAETnASTEVKNLEDQLLKLCNELKQAQIKLDEaesmKRNLQDRCKDL 285
Cdd:PLN02939 267 ---SLLDASLR--ELESKFIVAQEDVSKLSPLQYDC-WWEKVENLQDLLDRATNQVEKAALVLDQ----NQDLRDKVDKL 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207171119 286 EQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAA-------IKLEQKKTQDEKNNLNQLKD 339
Cdd:PLN02939 337 EASLKEANVSKFSSYKVELLQQKLKLLEERLQASdheihsyIQLYQESIKEFQDTLSKLKE 397
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
227-455 |
2.52e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 227 ADSSAQTSLPSAAEtnasteVKNledQLLKLcnelkqAQIKLDEAEsmKRNLQdrcKDLEQDLgtlkTQLGDKQKVQAEN 306
Cdd:PRK11281 27 ARAASNGDLPTEAD------VQA---QLDAL------NKQKLLEAE--DKLVQ---QDLEQTL----ALLDKIDRQKEET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 307 DCLKVQMEslQAaikleQKKTQDEKNNLNQLKDAYTK-LFEDYSELqeekkkregcvskdDYDELQTRFATAEKALADKQ 385
Cdd:PRK11281 83 EQLKQQLA--QA-----PAKLRQAQAELEALKDDNDEeTRETLSTL--------------SLRQLESRLAQTLDQLQNAQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 386 QKIDEMKMELFQKEKDLEtisvfQAQAEIYSSdfyAER-------------AAREKIHEEKERLATQLEYVKKQNSQLQE 452
Cdd:PRK11281 142 NDLAEYNSQLVSLQTQPE-----RAQAALYAN---SQRlqqirnllkggkvGGKALRPSQRVLLQAEQALLNAQNDLQRK 213
|
...
gi 1207171119 453 EME 455
Cdd:PRK11281 214 SLE 216
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
183-459 |
2.95e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 183 ESEEQTVRQLLRSLRAETDEKeRLQLTLQEARGRIAELESKLehadssaqtslpsAAETNASTEVKNLEDQLLKLCNELK 262
Cdd:PRK03918 145 ESREKVVRQILGLDDYENAYK-NLGEVIKEIKRRIERLEKFI-------------KRTENIEELIKEKEKELEEVLREIN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 263 QAQIKLDEAESMKRNLQDRCKDLEQ---DLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKTQDEKNNLNQLK- 338
Cdd:PRK03918 211 EISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKe 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 339 --DAYTKLFEDYSELqeEKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVF-QAQAEIY 415
Cdd:PRK03918 291 kaEEYIKLSEFYEEY--LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhELYEEAK 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1207171119 416 SSDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESLGR 459
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
187-363 |
3.50e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 187 QTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKNLEDQLLKLCNELKQAQI 266
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 267 KLD---EAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENdcLKVQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTK 343
Cdd:COG4717 154 RLEelrELEEELEELEAELAELQEELEELLEQLSLATEEELQD--LAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180
....*....|....*....|
gi 1207171119 344 LFEDYSELQEEKKKREGCVS 363
Cdd:COG4717 232 LENELEAAALEERLKEARLL 251
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
32-460 |
3.71e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 32 QMNTLIKENRDLKEALKQTNlsmKERFEGLSAWKEKqkeERDFLEQRLEEARTRLNTMDVENEALKNQVK---------- 101
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQH---QDRIEQLISEHEV---EITGLTEKASSARSQANSIQSQLEIIQEQARnqnsmymrql 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 102 -ELEKSGAEcLHTEL-EALRGQILRIQAEKNDLVAMNSEL--------QLKMGQGSPSNSFIeiRIADDDLKVTKDLSSV 171
Cdd:pfam15921 320 sDLESTVSQ-LRSELrEAKRMYEDKIEELEKQLVLANSELtearterdQFSQESGNLDDQLQ--KLLADLHKREKELSLE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 172 PEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARgriAELESKLEHADSSAQTSLPSAAETNAST-EVKNL 250
Cdd:pfam15921 397 KEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK---SECQGQMERQMAAIQGKNESLEKVSSLTaQLEST 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 251 EDQLLKLCNELKQAQIKLDEAE----SMKRNLQDRCKDLE-----------------QDLGTLKTQLGDKQKVQAENDCL 309
Cdd:pfam15921 474 KEMLRKVVEELTAKKMTLESSErtvsDLTASLQEKERAIEatnaeitklrsrvdlklQELQHLKNEGDHLRNVQTECEAL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 310 KVQMESLQAAIKLEQKKTQdeknNLNQLKDAYTKlfeDYSELQEEKKKREGCVSkDDYDELQTRfataeKALADKQQ-KI 388
Cdd:pfam15921 554 KLQMAEKDKVIEILRQQIE----NMTQLVGQHGR---TAGAMQVEKAQLEKEIN-DRRLELQEF-----KILKDKKDaKI 620
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207171119 389 DEMKMELfqKEKDLETISVFQAQAEIYssdfyaeRAAREkIHEEKERLATQLEYVKKQNSQLQEEMESLGRH 460
Cdd:pfam15921 621 RELEARV--SDLELEKVKLVNAGSERL-------RAVKD-IKQERDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-392 |
3.85e-04 |
|
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: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 185 EEQTVRQLLRSLRAETDEKERLQLTLQEAR------GRIAELESKLEHADSSAQT--SLPSAAET-NASTEVKNLEDQLL 255
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAReqiellEPIRELAERYAAARERLAEleYLRAALRLwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 256 KLCNELKQAQIKLDEAESMKRNLQDRCKDLE--------QDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKT 327
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207171119 328 QDEknnLNQLKDAYTKLFEDYSELQEEkkkregcvSKDDYDELQTRFATAEKALADKQQKIDEMK 392
Cdd:COG4913 379 AEE---FAALRAEAAALLEALEEELEA--------LEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
23-474 |
4.26e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 23 LGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQ-KEERDFLEQRLEEARTRLNTMDVENEALKNQVK 101
Cdd:pfam12128 253 LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQwKEKRDELNGELSAADAAVAKDRSELEALEDQHG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 102 ELEKSGAECLHTELE-----------------ALRGQILRIQAEKNDLVAMNSElqlkmgqgspsnsfieiRIADDDLKV 164
Cdd:pfam12128 333 AFLDADIETAAADQEqlpswqselenleerlkALTGKHQDVTAKYNRRRSKIKE-----------------QNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 165 TKDLSSVPEASAFSMPKAESEEQTVRQLLRS-----LRAETDEKERLQLTLQEARGRI----AELESKLEHADSSAQTSL 235
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREqleagKLEFNEEEYRLKSRLGELKLRLnqatATPELLLQLENFDERIER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 236 PSAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDL----GTLKTQLgDKQKVQAENDCLKV 311
Cdd:pfam12128 476 AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqaGTLLHFL-RKEAPDWEQSIGKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 312 QMESLQAAIKLEQKKTQDE---KNNLNQLKDAYTKLFEDYSELQEEKKKREGCVSKDDYDELQTRFATAEKALADKQQKI 388
Cdd:pfam12128 555 ISPELLHRTDLDPEVWDGSvggELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 389 DEMKMELFQ-----KEKDLETISVFQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVKKQNSQ-LQEEMESLGRHSM 462
Cdd:pfam12128 635 EKASREETFartalKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAwLEEQKEQKREART 714
|
490
....*....|..
gi 1207171119 463 SEMQRRHVPRGA 474
Cdd:pfam12128 715 EKQAYWQVVEGA 726
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
24-470 |
4.46e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 24 GSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKEL 103
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 104 EKSGAE--CLHTELEALRGQILRIQAEKNDLVAmnsELQLKMGQgspsnsfIEIRIADDDLKVTKDLSSVPEASAFSmpK 181
Cdd:PRK02224 446 EALLEAgkCPECGQPVEGSPHVETIEEDRERVE---ELEAELED-------LEEEVEEVEERLERAEDLVEAEDRIE--R 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 182 AESEEQTVRQLLRSLRAETDEKErlqLTLQEARGRIAELESKLEHADSSAQTSLPSAAEtnASTEVKNLEDQLlklcNEL 261
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKR---ERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKL----AEL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 262 KQAQIKLDEAESmkrnLQDRCKDLEQDLGTLKtqlgdkqkvqaendclkvqmeslqaaiklEQKKTQDEKNNLNQlkday 341
Cdd:PRK02224 585 KERIESLERIRT----LLAAIADAEDEIERLR-----------------------------EKREALAELNDERR----- 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 342 tklfEDYSELQEEKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDemkmELFQKEKDLetisvfqaQAEIYSSDfyA 421
Cdd:PRK02224 627 ----ERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLD----ELREERDDL--------QAEIGAVE--N 688
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1207171119 422 ERAAREKIHEEKERLATQLEYVKKQNSQLqEEMESLGRHSMSEMQRRHV 470
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYDEA-EELESMYGDLRAELRQRNV 736
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
26-249 |
4.81e-04 |
|
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: 43.13 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 26 LEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEartrlntMDVENEALKNQVKELEK 105
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-------VDKEFAETRDELKDYRE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 106 sgaeclhtELEALrgqilriQAEKNDLVAMNSELQLKMGQGSPSNSFIEIRIADDDLKVTKdLSSVPEASAFSMPKAESE 185
Cdd:TIGR02169 393 --------KLEKL-------KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE-LEEEKEDKALEIKKQEWK 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207171119 186 EQTVRQLLRSLRaetDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKN 249
Cdd:TIGR02169 457 LEQLAADLSKYE---QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
145-276 |
4.99e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 145 QGSPSNSFIEIRIADDDlkvTKDLSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKL 224
Cdd:COG2433 374 RGLSIEEALEELIEKEL---PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLEREL 450
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1207171119 225 EHADSSAQTSLPSAAETNA-STEVKNLEDQLLKLCNELKQAQIKLDEAESMKR 276
Cdd:COG2433 451 SEARSEERREIRKDREISRlDREIERLERELEEERERIEELKRKLERLKELWK 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
226-456 |
5.79e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 226 HADSSAQTSLPSAAET-----NASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQ 300
Cdd:COG3883 13 FADPQIQAKQKELSELqaeleAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 301 KVQAENDCLKVQMESLqaaikLEQKKTQD---EKNNLNQLKDAYTKLFEDYSELQEEKKKREgcvskddyDELQTRFATA 377
Cdd:COG3883 93 RALYRSGGSVSYLDVL-----LGSESFSDfldRLSALSKIADADADLLEELKADKAELEAKK--------AELEAKLAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207171119 378 EKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEiyssdfyAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMES 456
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAE-------AQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-297 |
6.48e-04 |
|
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: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 23 LGSLEETLQQMNTLIKENRDLKEALKQT---------------NLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLN 87
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLleelnkkikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 88 TMDVENEALKNQVKELEKSGAEcLHTELEALRGQILRIQAEKNDLVAmnselqlkmgqgspsnsfieiriadddlkvtkD 167
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEE-ERKRRDKLTEEYAELKEELEDLRA--------------------------------E 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 168 LSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSsAQTSLPSAAETnASTEV 247
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA-KINELEEEKED-KALEI 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1207171119 248 KNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLG 297
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-296 |
7.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 26 LEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLE-----QRLEEARTRLNTMDVENEALKNQV 100
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 101 KELEKSGAEcLHTELEALRGQILRIQAEKNDLVAmnselqlkmgqgspsnsfiEIRIADDDLKVTKDLSSVPEASAF-SM 179
Cdd:COG4913 695 EELEAELEE-LEEELDELKGEIGRLEKELEQAEE-------------------ELDELQDRLEAAEDLARLELRALLeER 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 180 PKAESEEQTVRQLLRSLRAETDekerlqltlqEARGRIAELESKLEHADSSAQTSLPSAAeTNASTEVKNLEDqLLKLCN 259
Cdd:COG4913 755 FAAALGDAVERELRENLEERID----------ALRARLNRAEEELERAMRAFNREWPAET-ADLDADLESLPE-YLALLD 822
|
250 260 270
....*....|....*....|....*....|....*..
gi 1207171119 260 ELKqaQIKLDEAESMKRNLQDRCKdlEQDLGTLKTQL 296
Cdd:COG4913 823 RLE--EDGLPEYEERFKELLNENS--IEFVADLLSKL 855
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-455 |
7.86e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 45 EALKQTNLSMKERFEGLSAWKEKQKEE-RDFLEQRLEEARTRLNTMDVENEALKNQVKELE-KSGAECLHTELEALRGQI 122
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 123 LRIQAE---KNDLVAMNSELQLKMGQGSPSNSFIEIR---IADDDLKVTKDLSSVPEASAFSMPKAESEEQTVRQLLRSL 196
Cdd:PTZ00121 1307 AKKKAEeakKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 197 RAETDEKERLQLTLQEARGRIAELESKlEHADSSAQTSLPSAAETNASTEVKNLEDQLLKlCNELKQAQIKLDEAESMKR 276
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKAEEAKK 1464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 277 NLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQ--MESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEE 354
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 355 KKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETISVFQAQAEiySSDFYAERAAREKIHEEKE 434
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKA 1622
|
410 420
....*....|....*....|.
gi 1207171119 435 RLATQLEYVKKQNSQLQEEME 455
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEA 1643
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
181-377 |
8.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 181 KAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKNLED---QLLKL 257
Cdd:COG3883 45 ELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDfldRLSAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 258 CNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKTQDEKNNLNQL 337
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1207171119 338 KDAYTKLFEDYSELQEEKKKREGCVSKDDYDELQTRFATA 377
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
246-409 |
1.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 246 EVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGtLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQK 325
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 326 KTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKREGcVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETI 405
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
....
gi 1207171119 406 SVFQ 409
Cdd:COG4717 240 ALEE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-387 |
1.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 181 KAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHadSSAQTSLPSAAEtnastEVKNLEDQLLKL--- 257
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEY--SWDEIDVASAER-----EIAELEAELERLdas 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 258 CNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAEndcLKVQMESLQAAIKLEQKKTQDEKNNLNQL 337
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDE---LQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207171119 338 KDAYTKLFEDYSElqeekkkregcvskdDYDELQTRFATAEKALADKQQK 387
Cdd:COG4913 761 DAVERELRENLEE---------------RIDALRARLNRAEEELERAMRA 795
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
26-455 |
1.19e-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: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 26 LEETLQQMNTLIKEN---RDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKE 102
Cdd:pfam05483 136 LEEEIQENKDLIKENnatRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHF 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 103 LEKSGAECLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQGS--------PSNSFIE-IRIADDDLK--------VT 165
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTflleesrdKANQLEEkTKLQDENLKeliekkdhLT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 166 KDLSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTSLPSAAEtnast 245
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQ----- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 246 EVKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQK 325
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 326 KTQDEKNNLNQLKDA---YTKLFEDY-SELQEEKKKREGCVSKDDYDELQTRFATaekaladkqQKIDEMKMELFQKEKD 401
Cdd:pfam05483 451 EIHDLEIQLTAIKTSeehYLKEVEDLkTELEKEKLKNIELTAHCDKLLLENKELT---------QEASDMTLELKKHQED 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171119 402 letisvfqaqaeIYSSDFYAERAAR--EKIHEEKERLATQLEYVKKQNSQLQEEME 455
Cdd:pfam05483 522 ------------IINCKKQEERMLKqiENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
210-457 |
1.37e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 210 LQEARGRIAELESKLEHADSSAQTSLPS-----AAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMkrnLQDRCKD 284
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQILEEldellESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDE---LEKQLAE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 285 LEQDLGTLKTQLGDKQKVQAEN--DCLKVQMESLQAAI----KLEQKKTQDEKNNLNQLKDAYTKLFE-----DYSELQE 353
Cdd:pfam06160 158 IEEEFSQFEELTESGDYLEAREvlEKLEEETDALEELMedipPLYEELKTELPDQLEELKEGYREMEEegyalEHLNVDK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 354 EKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMkMELFQKEKDletisvfqaqaeiyssdfyaeraAREKIHEEK 433
Cdd:pfam06160 238 EIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQL-YDLLEKEVD-----------------------AKKYVEKNL 293
|
250 260
....*....|....*....|....
gi 1207171119 434 ERLATQLEYVKKQNSQLQEEMESL 457
Cdd:pfam06160 294 PEIEDYLEHAEEQNKELKEELERV 317
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-225 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 26 LEETLQQMNTL--IKENRDLKEALKQTNLSMKERFEGLSAWKEKQKeeRDFLEQRLEEARTRLNTMDVENEALKNQVKEL 103
Cdd:COG4913 244 LEDAREQIELLepIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 104 EksgaeclhTELEALRGQIL-----RIQAEKNDLVAMNSELQLKMGqgspsnsfiEIRIADDDLKVTkDLSSVPEASAFs 178
Cdd:COG4913 322 R--------EELDELEAQIRgnggdRLEQLEREIERLERELEERER---------RRARLEALLAAL-GLPLPASAEEF- 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207171119 179 mpkaeseEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLE 225
Cdd:COG4913 383 -------AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-457 |
1.66e-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: 41.20 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 22 NLGSLEETLQQMNTLIKENRDLKEALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLntmdvenEALKNQVK 101
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-------ETLRSKVA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 102 ELEKsgaeclhtELEALRGQILRIQAEKNDLVAMNSELQlkmgqgspsnSFIEIRIADDDLKVTKDLSSVPEASAFSMPK 181
Cdd:TIGR02168 390 QLEL--------QIASLNNEIERLEARLERLEDRRERLQ----------QEIEELLKKLEEAELKELQAELEELEEELEE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 182 AESEEQTVRQLLRSLRAETDEKERLQLT----LQEARGRIAELESKLEHADSSAQTSLPSAAETNASTEVKNLEDQLLKL 257
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAaereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 258 CNELKQAqIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKKTQDEKNNLNQL 337
Cdd:TIGR02168 532 DEGYEAA-IEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKF 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 338 KDAYTKLFEDYS-------------ELQEEKKKREGCVSKDDY--------------------------DELQTRFATAE 378
Cdd:TIGR02168 611 DPKLRKALSYLLggvlvvddldnalELAKKLRPGYRIVTLDGDlvrpggvitggsaktnssilerrreiEELEEKIEELE 690
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207171119 379 KALADKQQKIDEMKMELFQKEKDLETIsvfQAQAEIYSSDFYAERAAREKIHEEKERLATQLEYVKKQNSQLQEEMESL 457
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQL---RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
70-225 |
1.82e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 70 EERDFLEQRLEEARTRLNTMDVENEALKNQVKELEKSGAECLHTELEALRGQIlrIQAEKNDLVAMNSELQLKMGQGSPS 149
Cdd:COG3206 212 EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPV--IQQLRAQLAELEAELAELSARYTPN 289
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207171119 150 NSfiEIRIADDDLKVTKDLssVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLE 225
Cdd:COG3206 290 HP--DVIALRAQIAALRAQ--LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE 361
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
245-447 |
1.95e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 40.98 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 245 TEVKNLEDQLLKLCNELKQAQIKLDEAesmkrNLQDRCKDLEQDLGTLKTQL--GDKQKVQAENDCLKVQMESLQAAIKL 322
Cdd:COG4477 225 TELPDQLEELKSGYREMKEQGYVLEHL-----NIEKEIEQLEEQLKEALELLeeLDLDEAEEELEEIEEEIDELYDLLEK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 323 E-------QKKTQDEKNNLNQLKDAYTKLFEDYSELQ-------EEKKKREGCvsKDDYDELQTRFATAEKALADKQQKI 388
Cdd:COG4477 300 EveakkyvDKNQEELEEYLEHLKEQNRELKEEIDRVQqsyrlneNELEKVRNL--EKQIEELEKRYDEIDERIEEEKVAY 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 389 DEMKMELFQKEKDLETISVFQAQAEIYSSDFYA-ERAAREKIHEEKERLATQLEYVKKQN 447
Cdd:COG4477 378 SELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKdELEAREKLDELKKKLREIKRRLEKSN 437
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
298-437 |
2.15e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.42 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 298 DKQKVQAENDCLKVQMESLQAAIKLEQKKTQDEkNNLNQLKDAYTKLFEDYSELQEEKKKreGCVSKDDYDELQTRFATA 377
Cdd:COG1566 84 ALAQAEAQLAAAEAQLARLEAELGAEAEIAAAE-AQLAAAQAQLDLAQRELERYQALYKK--GAVSQQELDEARAALDAA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 378 EKALADKQQKIDEMKMELFQKEKdletisVFQAQAEIyssdfyaeRAAREKIHEEKERLA 437
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEEE------LAAAQAQV--------AQAEAALAQAELNLA 206
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
247-357 |
2.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 247 VKNLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLgdKQKVQAENDCLKVQMESLQAAIKLEQKK 326
Cdd:PRK00409 522 IASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA--EKEAQQAIKEAKKEADEIIKELRQLQKG 599
|
90 100 110
....*....|....*....|....*....|.
gi 1207171119 327 tQDEKNNLNQLKDAYTKLFEDYSELQEEKKK 357
Cdd:PRK00409 600 -GYASVKAHELIEARKRLNKANEKKEKKKKK 629
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
27-468 |
2.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 27 EETLQQMNTLIKENRDLKEALkqtnLSMKERFEGLSAWKEKQKEErdfLEQRLEEARTRLNTMDVENEALKNQVKELE-- 104
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKF----IKRTENIEELIKEKEKELEE---VLREINEISSELPELREELEKLEKEVKELEel 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 105 KSGAECLHTELEALRGQILRIQAEKNDLVAMNSELQLKMGQ-GSPSNSFIEIR-IADDDLKVTKDLSSVPEASAfsmpKA 182
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEElEEKVKELKELKeKAEEYIKLSEFYEEYLDELR----EI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 183 ESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQtslpsaaetnASTEVKNLEDQLLKL----- 257
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHE----------LYEEAKAKKEELERLkkrlt 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 258 CNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQKK------TQDEK 331
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelleeyTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 332 NNLNQLKDAYTKLfedySELQEEKKKREGCVSKDdyDELQTRFATAE--KALADKQQKIDEMKMElfQKEKDLETIS--V 407
Cdd:PRK03918 463 RIEKELKEIEEKE----RKLRKELRELEKVLKKE--SELIKLKELAEqlKELEEKLKKYNLEELE--KKAEEYEKLKekL 534
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207171119 408 FQAQAEIYSSDFYAERAarEKIHEEKERLATQLEYVKKQNSQLQEEMESLGRHSMSEMQRR 468
Cdd:PRK03918 535 IKLKGEIKSLKKELEKL--EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEER 593
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
25-450 |
2.54e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 25 SLEETLQQMNTLIKENRDLKeALKQTNLSMKERFEGLSAWKEKQKEERDFLEQRLEEARTRLNTMDvenEALKNQVKELE 104
Cdd:TIGR01612 905 SIEEEYQNINTLKKVDEYIK-ICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFD---NTLIDKINELD 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 105 KSGAECLHTELEALRGQILRIQAEKNDLVAMNSE--LQLKMGQGSPSNSFIEIRIADddlkVTKDLSSVPEASAFSMPKA 182
Cdd:TIGR01612 981 KAFKDASLNDYEAKNNELIKYFNDLKANLGKNKEnmLYHQFDEKEKATNDIEQKIED----ANKNIPNIEIAIHTSIYNI 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 183 ESE-EQTVRQLLRSLRAETDEKERLQLTlqeargRIAELESKLEH---ADSSAQTSLPSAAETNA-STEVKNLEDQLLKL 257
Cdd:TIGR01612 1057 IDEiEKEIGKNIELLNKEILEEAEINIT------NFNEIKEKLKHynfDDFGKEENIKYADEINKiKDDIKNLDQKIDHH 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 258 CNELKQAQIK----LDEAESMKRNLQ---------DRCKDLEQDLGTLKTQLgDKQKVQAENdclkvqMESLQAAI-KLE 323
Cdd:TIGR01612 1131 IKALEEIKKKsenyIDEIKAQINDLEdvadkaisnDDPEEIEKKIENIVTKI-DKKKNIYDE------IKKLLNEIaEIE 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 324 QKKTQDEK-NNLN-QLKDAYTKLFedYSELQEEKKKREGCVSK-----DDYDELQTRFATAEKALADKQQKIDEMKMELF 396
Cdd:TIGR01612 1204 KDKTSLEEvKGINlSYGKNLGKLF--LEKIDEEKKKSEHMIKAmeayiEDLDEIKEKSPEIENEMGIEMDIKAEMETFNI 1281
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207171119 397 QKEKDL----------ETISVFQAQAEIYSSDFYAEraarEKIHEEKERLATQLEYVKKQNSQL 450
Cdd:TIGR01612 1282 SHDDDKdhhiiskkhdENISDIREKSLKIIEDFSEE----SDINDIKKELQKNLLDAQKHNSDI 1341
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
168-425 |
2.63e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 168 LSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEhadssaqtslpsaaetNASTEV 247
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----------------ALQAEI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 248 KNLEDQLLKLCNELKQAQIKLDE-AESMKRNLQDRcKDLE-----QDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIK 321
Cdd:COG3883 68 DKLQAEIAEAEAEIEERREELGErARALYRSGGSV-SYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 322 LEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEKKKRegcvskddYDELQTRFATAEKALADKQQKIDEMKMELFQKEKD 401
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL--------LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
250 260
....*....|....*....|....
gi 1207171119 402 LETISVFQAQAEIYSSDFYAERAA 425
Cdd:COG3883 219 AAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-457 |
2.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 346 EDYSELQEEKKKREGCVSKDDYDELQTRFATAEKALADKQQKIDEMKMELFQKEKDLETI---------SVFQAQAEIYS 416
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELrleleelelELEEAQAEEYE 292
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1207171119 417 SDFYAERAAREKIH--EEKERLATQLEYVKKQNSQLQEEMESL 457
Cdd:COG1196 293 LLAELARLEQDIARleERRRELEERLEELEEELAELEEELEEL 335
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
210-458 |
3.16e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 210 LQEARGRIAELESKLEHADSSAQ------TSLPSAAETNaSTEVKNLEDQLLKLCNELKQAQIKLDEAESmkrNLQDRCK 283
Cdd:PRK04778 100 FRKAKHEINEIESLLDLIEEDIEqileelQELLESEEKN-REEVEQLKDLYRELRKSLLANRFSFGPALD---ELEKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 284 DLEQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIKLEQ-----KKTQDE-KNNLNQLKDAYTKLFED-Y-------- 348
Cdd:PRK04778 176 NLEEEFSQFVELTESGDYVEAREILDQLEEELAALEQIMEEipellKELQTElPDQLQELKAGYRELVEEgYhldhldie 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 349 SELQEEKKKREGCvsKDDYDELqtRFATAEKALADKQQKIDEMkMELFQKEKDletisvfqaqaeiyssdfyaeraAREK 428
Cdd:PRK04778 256 KEIQDLKEQIDEN--LALLEEL--DLDEAEEKNEEIQERIDQL-YDILEREVK-----------------------ARKY 307
|
250 260 270
....*....|....*....|....*....|
gi 1207171119 429 IHEEKERLATQLEYVKKQNSQLQEEMESLG 458
Cdd:PRK04778 308 VEKNSDTLPDFLEHAKEQNKELKEEIDRVK 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
276-459 |
3.92e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 276 RNLQDRCKDLEQDLGTLKtQLGDKQKVQAEndclKVQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSELQEEK 355
Cdd:COG4913 258 RELAERYAAARERLAELE-YLRAALRLWFA----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 356 KKREGcvskDDYDELQTRFATAEKALADKQQKIDEMKmELFQ--KEKDLETISVFQAQAEIYSSDFYAERAAREKIHEEK 433
Cdd:COG4913 333 RGNGG----DRLEQLEREIERLERELEERERRRARLE-ALLAalGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL 407
|
170 180
....*....|....*....|....*.
gi 1207171119 434 ERLATQLEYVKKQNSQLQEEMESLGR 459
Cdd:COG4913 408 AEAEAALRDLRRELRELEAEIASLER 433
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
241-358 |
3.96e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 241 TNASTEVKNLEDQLlklcNELKQAQIKLDEAESMKRNLQDRCKDLEQDLGTLKTQLgdkQKVQAENDCLKVQMESLQAAI 320
Cdd:PHA02562 302 TKIKDKLKELQHSL----EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL---ITLVDKAKKVKAAIEELQAEF 374
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207171119 321 KleqkktqDEKNNLNQLKDAYTKLFEDYSELQEEKKKR 358
Cdd:PHA02562 375 V-------DNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
61-460 |
4.89e-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: 39.77 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 61 LSAWKEKQKEERDFLEQRLEEARTRLNTMDVENEALKNQVKELEKSGAE------CLHTELEALRGQILRIQAEKNDLVA 134
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqKLQLEKVTTEAKIKKLEEDILLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 135 MNSELQLKMGQGSPSNSFIEIRIADDDLKVtKDLSSVPEASAFSMPKAE----SEEQTVRQLLRSLRAETDEKERLQLTL 210
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEerlkKEEKGRQELEKAKRKLEGESTDLQEQI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 211 QEARGRIAELESKLEHADSSAQTSL-----PSAAETNASTEVKNLEDQLLKLCNELKQAQIKLDEAESMKRnlqdrckDL 285
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALarleeETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRR-------DL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 286 EQDLGTLKTQLGDKQKVQAENDCLKVQMESLQAAIK--LEQKKTQDEKnNLNQLKDAYTKLFEDYSELQEEKKKREGCVS 363
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaLEEETRSHEA-QLQEMRQKHTQALEELTEQLEQAKRNKANLE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 364 K------DDYDELQTRFATAEKALADKQQKIDEMkmelfqkEKDLETISVFQAQAEIYSSDFyAERAAreKIHEEKERLA 437
Cdd:pfam01576 377 KakqaleSENAELQAELRTLQQAKQDSEHKRKKL-------EGQLQELQARLSESERQRAEL-AEKLS--KLQSELESVS 446
|
410 420
....*....|....*....|...
gi 1207171119 438 TQLEYVKKQNSQLQEEMESLGRH 460
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
72-281 |
5.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 72 RDFLEQRLEEARTRLNTMDVENEALKNQVKELEKSGAEC---------------LHTELEALRGQILRIQAEKNDLVAMN 136
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 137 SELQlkmgqgspsnsfieiriadddlkvtkdlssvpeasafsmpKAESEEQTVRQLLRSLRaetDEKERLQLTLQEARGR 216
Cdd:COG4913 692 EQLE----------------------------------------ELEAELEELEEELDELK---GEIGRLEKELEQAEEE 728
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207171119 217 IAELESKLEHADSSAQTSL-PSAAETNASTEVKNLEDQLLK-LCNELKQAQIKLDEAESMKRNLQDR 281
Cdd:COG4913 729 LDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
299-453 |
7.83e-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: 39.28 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 299 KQKVQAENDCLKVQMESLQAAIKleqkktqDEKNNLNQLKDAYTKLfEDYSELQEEKKKREGCVSKDDYDELQTRFATAE 378
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIID-------EKRQQLERLRREREKA-ERYQALLKEKREYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 379 KALADKQQKIDEMKMELFQKEKDLETISVFQAQAEIYSSDFYAERAAR-----EKIHEEKERLATQLEYVKKQNSQLQEE 453
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekiGELEAEIASLERSIAEKERELEDAEER 323
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
174-307 |
8.64e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 38.41 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 174 ASAFSMPKAESE--EQTVRQLLRSLRAETDEKERLQLTLQE-------ARGRIAELESKLehaDSSAQTSlpsaAETNAS 244
Cdd:PRK09039 66 ADLLSLERQGNQdlQDSVANLRASLSAAEAERSRLQALLAElagagaaAEGRAGELAQEL---DSEKQVS----ARALAQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 245 TEVknLEDQLLKLCNELKQAQIKLDEAESMKRNLQDRCKDLEQDL-------------------GTLKTQLGDKQKVQAE 305
Cdd:PRK09039 139 VEL--LNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLnvalaqrvqelnryrseffGRLREILGDREGIRIV 216
|
..
gi 1207171119 306 ND 307
Cdd:PRK09039 217 GD 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
115-431 |
9.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 115 LEALRGQILRIQAEKNDLVAMNSELQLKMgqgspsnsfieiriadDDLKVTKDLSSVPEASAFS---MPKAESEEQTVRQ 191
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAEL----------------DALQERREALQRLAEYSWDeidVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 192 LLRSLRAETDEKERLQLTLQEARGRIAELESKLEHADSSAQTslpsaaetnASTEVKNLEDqllklcnELKQAQIKLDEA 271
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGR---------LEKELEQAEE-------ELDELQDRLEAA 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 272 ESMKRnlqdrcKDLEQDLGTLKTQLGDKQKVQAendclkvQMESLQAAIKLEQKKTQDEKNNLNQLKDAYTKLFEDYSel 351
Cdd:COG4913 740 EDLAR------LELRALLEERFAAALGDAVERE-------LRENLEERIDALRARLNRAEEELERAMRAFNREWPAET-- 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 352 qeekkkREGCVSKDDYDELQTRFAT-AEKALADKQQKIDEMKMElfQKEKDLETIsvfqaQAEIYSsdfyAERAAREKIH 430
Cdd:COG4913 805 ------ADLDADLESLPEYLALLDRlEEDGLPEYEERFKELLNE--NSIEFVADL-----LSKLRR----AIREIKERID 867
|
.
gi 1207171119 431 E 431
Cdd:COG4913 868 P 868
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
149-289 |
9.94e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 38.89 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207171119 149 SNSFIEIRIADDDLKVTKDLSSVPEASAFSMPKAESEEQTVRQLLRSLRAETDEKERLQLTLQEARGRIAELESKLEHAD 228
Cdd:pfam05911 657 DNLSSDPEIPSDGPLVSGSNDLKTEENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLK 736
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207171119 229 SS---AQTSLPSAAETNastevKNLEDQLLKLCNELKQAQIKLD----EAESMKRNLQD---RCKDLEQDL 289
Cdd:pfam05911 737 ESnslAETQLKCMAESY-----EDLETRLTELEAELNELRQKFEalevELEEEKNCHEEleaKCLELQEQL 802
|
|
| |
