|
Name |
Accession |
Description |
Interval |
E-value |
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
44-456 |
1.65e-84 |
|
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: 264.70 E-value: 1.65e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 44 LSPDELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLS 123
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 124 VREDGVKASLRERRGVLAEVLAALQRMGRNPPPALLVSPEDALASVRSAILLGAVVPGIRGETDKLVAALKELTDLRQAI 203
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 204 AREKDDLTGMMTASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAmekarae 283
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 284 eqrlarlseaerekqraaaeagmpdknriAPAYPFASLKGKLEFPVAGEVLRRFGDADGTGHFSKGVVVASGPEAIVTAP 363
Cdd:COG4942 243 -----------------------------TPAAGFAALKGKLPWPVSGRVVRRFGERDGGGGRNKGIDIAAPPGAPVRAV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 364 ADGFVVFAGDFRSYGRMVILNTGDGYHVVMTGMDNVRTRQGMFVFSGEPIASMGAKRvasaaalalETDRPTLYIEFRKD 443
Cdd:COG4942 294 ADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSG---------GQGGPTLYFELRKN 364
|
410
....*....|...
gi 739226812 444 GVPVDSQPWWTAK 456
Cdd:COG4942 365 GKPVDPLPWLAKR 377
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
345-448 |
3.05e-23 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 93.38 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 345 HFSKGVVVASGPEAIVTAPADGFVVFAGDFRSYGRMVILNTGDGYHVVMTGMDNVRTRQGMFVFSGEPIASMGAkrvasa 424
Cdd:pfam01551 1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGS------ 74
|
90 100
....*....|....*....|....*..
gi 739226812 425 aalaleTDR---PTLYIEFRKDGVPVD 448
Cdd:pfam01551 75 ------TGRstgPHLHFEIRKNGKPVD 95
|
|
| NlpD |
COG0739 |
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ... |
264-455 |
1.55e-20 |
|
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440502 [Multi-domain] Cd Length: 196 Bit Score: 89.26 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 264 SSLEGEITSVREAMEKARAEEQRLARLSEAEREKQRAAAEAGMPDKNRIAPAYPFASLKGKLEFPVAGEVLRRFGD---- 339
Cdd:COG0739 10 ALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYrrhp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 340 ADGTGHFSKGVVVASGPEAIVTAPADGFVVFAGDFRSYGRMVILNTGDGYHVVMTGMDNVRTRQGMFVFSGEPIASMGAk 419
Cdd:COG0739 90 VTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGN- 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 739226812 420 rvasaaalaleTDRPT---LYIEFRKDGVPVDSQPWWTA 455
Cdd:COG0739 169 -----------TGRSTgphLHFEVRVNGKPVDPLPFLPA 196
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
59-452 |
8.87e-17 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 82.05 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 59 NRQDLEELVDSIGLSEDKTRKLEESIASLdQDSARIREELIASAARrkaletKISDGEDRLAKLSVREDGVKASLR---- 134
Cdd:PRK11637 45 NRDQLKSIQQDIAAKEKSVRQQQQQRASL-LAQLKKQEEAISQASR------KLRETQNTLNQLNKQIDELNASIAkleq 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 135 ---ERRGVLAEVLAALQRMGRNPPPALLVSPEDalaSVRSAILLgAVVPGIRGETDKLVAALKELtdlRQAIAREKDDLT 211
Cdd:PRK11637 118 qqaAQERLLAAQLDAAFRQGEHTGLQLILSGEE---SQRGERIL-AYFGYLNQARQETIAELKQT---REELAAQKAELE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 212 GMMTA-----SLEEEKRLDLLIAENDRKNSQTAAE--LEAERKRSEELASKATSLEGLVSSLEgeitsvREAmeKARAEe 284
Cdd:PRK11637 191 EKQSQqktllYEQQAQQQKLEQARNERKKTLTGLEssLQKDQQQLSELRANESRLRDSIARAE------REA--KARAE- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 285 qRLARLSEAEREKQRAAAEAGMP------DKNRIAPAYPFASLKGKLEFPVAGEVLRRFGDA-DGTGHFsKGVVVASGPE 357
Cdd:PRK11637 262 -REAREAARVRDKQKQAKRKGSTykptesERSLMSRTGGLGRPRGQAFWPVRGPTLHRFGEQlQGELRW-KGMVIGASEG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 358 AIVTAPADGFVVFAGDFRSYGRMVILNTGDG----YHVVMTGMDNVrtrqGMFVFSGEPIASMGAkrvaSAAalaleTDR 433
Cdd:PRK11637 340 TEVKAIADGRVLLADWLQGYGLVVVVEHGKGdmslYGYNQSALVSV----GAQVRAGQPIALVGS----SGG-----QGR 406
|
410
....*....|....*....
gi 739226812 434 PTLYIEFRKDGVPVDSQPW 452
Cdd:PRK11637 407 PSLYFEIRRQGQAVNPQPW 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-339 |
3.69e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRED 127
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 128 GVKASLRERRGVLAEVLAALQRMgrnpppallvspEDALASVRSAILlgavvpgirGETDKLVAALKELTDLRQAIAREK 207
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEA------------EEALLEAEAELA---------EAEEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 208 DDLTGMMTASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEK-ARAEEQR 286
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEaALLEAAL 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 739226812 287 LARLSEAEREKQRAAAEAGMPDKNRIAPAYPFASLKGKLEFPVAGEVLRRFGD 339
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
348-417 |
2.03e-12 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 62.61 E-value: 2.03e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 348 KGVVVASGPEAIVTAPADGFVVFAGDFRSYGRMVILNTGDGYHVVMTGMDNVRTRQGMFVFSGEPIASMG 417
Cdd:cd12797 2 NGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVG 71
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
62-410 |
3.24e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.85 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 62 DLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLsvredgvKASLRERRGVLA 141
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-------EAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 142 EVLAALQRMGRNPPPALLV----SPEDALASVRsaiLLGAVVPGIRGETDKLVAALKELTDLRQAIAREKDDLTGMMTAS 217
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLlgseSFSDFLDRLS---ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 218 LEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAEEQRLARLSEAEREK 297
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 298 QRAAAEAGMPDKNRIAPAYPFASLKGKLEFPVAGEVLRRFGDADGTGHFSKGVVVASGPEAIVTAPADGFVVFAGDFRSY 377
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGA 326
|
330 340 350
....*....|....*....|....*....|...
gi 739226812 378 GRMVILNTGDGYHVVMTGMDNVRTRQGMFVFSG 410
Cdd:COG3883 327 SAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSS 359
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-303 |
2.46e-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: 59.69 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRe 126
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE- 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 dgvKASLRERRGVLAEVLAALQRMgrnpppalLVSPEDALASVRsaILLGAVVPGIRGETDKLVAALKELTDLRQAIARE 206
Cdd:TIGR02168 784 ---IEELEAQIEQLKEELKALREA--------LDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 207 KDDLTGMmtasleeekrldlliaendrknsqtAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAEEQR 286
Cdd:TIGR02168 851 SEDIESL-------------------------AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
250
....*....|....*...
gi 739226812 287 L-ARLSEAEREKQRAAAE 303
Cdd:TIGR02168 906 LeSKRSELRRELEELREK 923
|
|
| SpoIVFA |
COG5833 |
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ... |
327-448 |
3.42e-09 |
|
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444535 [Multi-domain] Cd Length: 219 Bit Score: 56.92 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 327 FPVAGEVLRRFGDaDGtghfsKGVVVASGPEAIVTAPADGFVVFAGDFRSYGRMVILNTGDGYHVVMTGMDNVRTRQGMF 406
Cdd:COG5833 106 LPVSGKVVESFQE-NG-----KGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDF 179
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 739226812 407 VFSGEPIASMGakrvasaaalALETDRPTLYIEFRKDGVPVD 448
Cdd:COG5833 180 VEAGQKIGTVP----------ATEGEEGTFYFAIKKGGKFID 211
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
47-304 |
4.26e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRE 126
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLRERRGVLAEVLAALQRMgrnpppallvspEDALASVRSAILlgavvpgirgetdKLVAALKELTDLRQAIARE 206
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEAL------------LERLERLEEELE-------------ELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 207 KDDLTGMMTASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAE--E 284
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglA 523
|
250 260
....*....|....*....|
gi 739226812 285 QRLARLSEAEREKQRAAAEA 304
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAA 543
|
|
| SpoIIQ2 |
COG5821 |
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ... |
319-451 |
7.00e-09 |
|
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444523 [Multi-domain] Cd Length: 200 Bit Score: 55.42 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 319 ASLKGKLEFPVAGEVLRRFGDaDGTGH-------FSKGVVVASGPEAIVTAPADGFVVFAGDFRSYGRMVILNTGDGYHV 391
Cdd:COG5821 63 ASTSNKFLKPVSGKITREFGE-DLVYSktlnewrTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKT 141
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739226812 392 VMTGMD-NVRTRQGMFVFSGEPIASMGakrvaSAAALALETDrPTLYIEFRKDGVPVDSQP 451
Cdd:COG5821 142 VYANLDsKIKVKVGQKVKKGQVIGKVG-----STALFESSEG-PHLHFEVLKNGKPVDPMK 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-300 |
3.01e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.22 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 43 DLSPDELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKL 122
Cdd:TIGR02168 228 ALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 123 SVREDGVKASLRERRGVLAEVLAALQRMGrnpppALLVSPEDALASVRsaillgAVVPGIRGETDKLVAALKELTDLRQA 202
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELA-----EELAELEEKLEELK------EELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 203 IAREKDDLTGMMTASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEglVSSLEGEITSVREAMEKARA 282
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQE 454
|
250 260
....*....|....*....|..
gi 739226812 283 E----EQRLARLSEAEREKQRA 300
Cdd:TIGR02168 455 ElerlEEALEELREELEEAEQA 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-305 |
4.67e-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: 55.84 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSI-GLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRE 126
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLRERRGVLAEVLAALQrmgrnpppallvSPEDALASVRSAIllgavvpgirGETDKLVAALKELTDLRQaiaRE 206
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYA------------ELKEELEDLRAEL----------EEVDKEFAETRDELKDYR---EK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 207 KDDLTGMMTASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAEEQR 286
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260
....*....|....*....|....*..
gi 739226812 287 LA--------RLSEAEREKQRAAAEAG 305
Cdd:TIGR02169 474 LKeeydrvekELSKLQRELAEAEAQAR 500
|
|
| nlpD |
PRK10871 |
murein hydrolase activator NlpD; |
327-423 |
4.01e-07 |
|
murein hydrolase activator NlpD;
Pssm-ID: 236782 [Multi-domain] Cd Length: 319 Bit Score: 51.76 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 327 FPVAGEVLRRFGDADGTghfSKGVVVASGPEAIVTAPADGFVVFAGD-FRSYGRMVILNTGDGYHVVMTGMDNVRTRQGM 405
Cdd:PRK10871 202 WPTDGKVIENFSASEGG---NKGIDIAGSKGQAIIATADGRVVYAGNaLRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQ 278
|
90
....*....|....*...
gi 739226812 406 FVFSGEPIASMGAKRVAS 423
Cdd:PRK10871 279 EVKAGQKIATMGSTGTSS 296
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
48-255 |
1.97e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSIglsedktRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRED 127
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAEL-------AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 128 GVKaSLRERRGVLAEvLAALQRMgrnpppallvspedalasvrsaillgavvpgIRGETDKLVAALKELTDLRQAIAREK 207
Cdd:COG1579 84 NVR-NNKEYEALQKE-IESLKRR-------------------------------ISDLEDEILELMERIEELEEELAELE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 739226812 208 DDLTgmmtaslEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASK 255
Cdd:COG1579 131 AELA-------ELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-299 |
2.15e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSIglsEDKTRKLEESIASLDQDSARI--REELIAsaarrkALETKISDGEDRLAKLSVR 125
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDL---SSLEQEIENVKSELKELEARIeeLEEDLH------KLEEALNDLEARLSHSRIP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 126 E-----DGVKASLRERRGVLAEVLAALQRmgRNPPPALLVSP-----------EDALASVRSAI-LLGAVVPGIRGETDK 188
Cdd:TIGR02169 795 EiqaelSKLEEEVSRIEARLREIEQKLNR--LTLEKEYLEKEiqelqeqridlKEQIKSIEKEIeNLNGKKEELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 189 LVAALKELTDLRQAIAREKDDltgmmtasLEEEKRldlliaENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEG 268
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDE--------LEAQLR------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED 938
|
250 260 270
....*....|....*....|....*....|.
gi 739226812 269 EITSVREAMEKARAEEQRLARLSEAEREKQR 299
Cdd:TIGR02169 939 PKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
47-282 |
2.48e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIglsEDKTRKLEEsIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRE 126
Cdd:PRK02224 220 EEIERYEEQREQARETRDEADEVL---EEHEERREE-LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEER 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLrERRGVLAEVLAALqrmgRNPPPALLVSPEDALASVRSAIllGAVVPGIRGETDKLVAALKELTDLRQAIARE 206
Cdd:PRK02224 296 DDLLAEA-GLDDADAEAVEAR----REELEDRDEELRDRLEECRVAA--QAHNEEAESLREDADDLEERAEELREEAAEL 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739226812 207 KDDLTGMMTASLEEEKRLDLL---IAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARA 282
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELeeeIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-303 |
4.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIGLSEDKT-RKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVR 125
Cdd:COG4717 163 EELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 126 EdgvkaSLRERRGVLAEVLAALQRMGRNPPPALLVSPEDALASVRSAILLGAVVPGIRGETD--------KLVAALKELT 197
Cdd:COG4717 243 E-----RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASlgkeaeelQALPALEELE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 198 DLRQAIAREKDDLTGMMTAS---------------------LEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKA 256
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEellelldrieelqellreaeeLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 739226812 257 TSLEGLVSSLEGEITSVREAMEKARA---EEQRLARLSEAEREKQRAAAE 303
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEaldEEELEEELEELEEELEELEEE 447
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
48-298 |
4.74e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSIGLSEDktrKLEESIASLDQDS--ARIREELIASAARRKALETKISDGEDRLAKLSVR 125
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYED---KLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDE 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 126 EDG---VKASLRERRGVLAEVLAALQRMGRNPPPAlLVSPEDALASV--RSAILLGaVVPGIRGETDKLVAALKELTD-- 198
Cdd:TIGR00606 676 NQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDK-LKSTESELKKKekRRDEMLG-LAPGRQSIIDLKEKEIPELRNkl 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 199 --LRQAIAREKDDLTgmmtaslEEEKRLDLLIAENDRKN---------SQTAAELEAERKRSEELASKATSLEGL--VSS 265
Cdd:TIGR00606 754 qkVNRDIQRLKNDIE-------EQETLLGTIMPEEESAKvcltdvtimERFQMELKDVERKIAQQAAKLQGSDLDrtVQQ 826
|
250 260 270
....*....|....*....|....*....|...
gi 739226812 266 LEGEITSVREAMEKARAEEQRLARLSEaEREKQ 298
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNRKLIQ-DQQEQ 858
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
47-280 |
6.31e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQ-----DLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKI-SDGEDRLA 120
Cdd:COG4913 262 ERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 121 KLSVREDGVKASLRERRGVLAEVLAALQRMGrnpppalLVSPEDAlasvrsaillgavvpgirgetdklvaalKELTDLR 200
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALG-------LPLPASA----------------------------EEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 201 QAIAREKDDLTgmmtaslEEEKRLDLLIAEndrknsqTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKA 280
Cdd:COG4913 387 AEAAALLEALE-------EELEALEEALAE-------AEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
46-148 |
6.59e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 46 PDELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREEL---------------IASAARRKA-LE 109
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnnkeyealqkeIESLKRRISdLE 109
|
90 100 110
....*....|....*....|....*....|....*....
gi 739226812 110 TKISDGEDRLAKLSVREDGVKASLRERRGVLAEVLAALQ 148
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
47-299 |
8.30e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREE--------------LIASAARRKALETKI 112
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEaaeleseleeareaVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 113 SDGEDRLAKLSVREDGV---KASLRER----RGVLAEVLAALQ--RMGRNPPPALLVS---PE-----------DALASV 169
Cdd:PRK02224 394 EELRERFGDAPVDLGNAedfLEELREErdelREREAELEATLRtaRERVEEAEALLEAgkcPEcgqpvegsphvETIEED 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 170 RSAIL-LGAVVPGIRGETDKLVAALKELTDLRQAIAR-----EKDDLTGMMTASLEEEKRLDLLIAENDRKNsqtAAELE 243
Cdd:PRK02224 474 RERVEeLEAELEDLEEEVEEVEERLERAEDLVEAEDRierleERREDLEELIAERRETIEEKRERAEELRER---AAELE 550
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 244 AE----RKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAEEQRLARLSEAEREKQR 299
Cdd:PRK02224 551 AEaeekREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIER 610
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
30-305 |
2.48e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 30 SRDDAGAVPTENGDLSpDELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALE 109
Cdd:PRK02224 263 LRETIAETEREREELA-EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 110 TKISDGEDRLAKLSVREDGvkasLRERRGVLAEVLAAlqrmgrnpppallvsPEDALASVRSAI-LLGAVVPGIRGETDK 188
Cdd:PRK02224 342 EEAESLREDADDLEERAEE----LREEAAELESELEE---------------AREAVEDRREEIeELEEEIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 189 LVAALKELTDLRQAIAREKDDLTGMMT---ASLEE-----EKRLDLLIA------ENDRKNSQTAAELEAERKRSEELAS 254
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAeleATLRTarervEEAEALLEAgkcpecGQPVEGSPHVETIEEDRERVEELEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 255 KATSLEGLVSSLEGEITSVREAME----------------------KARAEEQRLARLS------------EAEREKQRA 300
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLVEaedrierleerredleeliaerRETIEEKRERAEElreraaeleaeaEEKREAAAE 562
|
....*
gi 739226812 301 AAEAG 305
Cdd:PRK02224 563 AEEEA 567
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-302 |
3.15e-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: 43.52 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELvdsiglsedktrklEESIASLDQDSARIREELIASAARRKALETKISD-GEDRLAKLSVRE 126
Cdd:TIGR02169 231 EKEALERQKEAIERQLASL--------------EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLRERRGVLAEvlaALQRMgrnpppallvspEDALASVRSAILlgavvpgirgETDKLvaaLKELTDLRQAIARE 206
Cdd:TIGR02169 297 GELEAEIASLERSIAE---KEREL------------EDAEERLAKLEA----------EIDKL---LAEIEELEREIEEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 207 KDDLTGMMTASLEEEKRLDLL---IAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSL-------EGEITSVREA 276
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLraeLEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeelqrlSEELADLNAA 428
|
250 260 270
....*....|....*....|....*....|....
gi 739226812 277 MEKARAE--------EQRLARLSEAEREKQRAAA 302
Cdd:TIGR02169 429 IAGIEAKineleeekEDKALEIKKQEWKLEQLAA 462
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
43-149 |
4.04e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 43 DLSPDELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELiaSAARRKALETKISDGEDRLAKL 122
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAA 758
|
90 100
....*....|....*....|....*....
gi 739226812 123 SV--REDGVKASLRERRGVLAEVLAALQR 149
Cdd:COG4913 759 LGdaVERELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-278 |
1.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSiglsEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVR-E 126
Cdd:COG4913 662 DVASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRlE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLRERRGVLAEVLAALQRmgrnpppallvspEDALASVRSAIllgavVPGIRGETDKLVAALKELTDLRQAIARE 206
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALG-------------DAVERELRENL-----EERIDALRARLNRAEEELERAMRAFNRE 799
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739226812 207 KDDLTGMMTASLEE----EKRLDLLIAENdrknsqtaaeLEAERKRSEELASKAT--SLEGLVSSLEGEITSVREAME 278
Cdd:COG4913 800 WPAETADLDADLESlpeyLALLDRLEEDG----------LPEYEERFKELLNENSieFVADLLSKLRRAIREIKERID 867
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
30-184 |
2.16e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 30 SRDDAGAVPTENGDLSpDELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALE 109
Cdd:TIGR02169 369 LRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739226812 110 TKISDGEDRLAKLSVREDGVKASLRERRGVLAEV---LAALQRMGRNPPPALLVSPEDALASVRSAILLGAVVPGIRG 184
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVekeLSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
48-294 |
2.58e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEE--------------LVDSIGLSEDKTRKLEESIASLDQDSARIR------EELIASAARRKA 107
Cdd:PRK02224 434 TLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEerleraEDLVEAEDRIER 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 108 LETKISDGEDRLA--KLSVREDGVKA-SLRERrgvlAEVLAALQRMGRNPPPALLVSPEDALASVRSAILLGAVVPGIRG 184
Cdd:PRK02224 514 LEERREDLEELIAerRETIEEKRERAeELRER----AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 185 ETDKLVAALKELTDLRQAIAREKDDLTGMmtASLEEEKRlDLLIAENDRKnSQTAAELEAER--------KRSE------ 250
Cdd:PRK02224 590 SLERIRTLLAAIADAEDEIERLREKREAL--AELNDERR-ERLAEKRERK-RELEAEFDEARieearedkERAEeyleqv 665
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 739226812 251 -----ELASKATSLEGLVSSLEGEITSVREAMEKARAEEQRLARL----SEAE 294
Cdd:PRK02224 666 eekldELREERDDLQAEIGAVENELEELEELRERREALENRVEALealyDEAE 718
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-299 |
2.90e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 55 RRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVREDgvkaSLR 134
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD----TLL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 135 ERRGVLAEVLAALQRMGRNPPPALLVSPEDALASVRSAILLGAVvpgiRGETDKLVAALKELTDLRQAIAREKDDLTGMM 214
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR----RELLAALLEAEAELEELAERLAEEELELEEAL 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 215 TASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAE----EQRLARL 290
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERElerlEREIEAL 779
|
250
....*....|....*..
gi 739226812 291 --------SEAEREKQR 299
Cdd:COG1196 780 gpvnllaiEEYEELEER 796
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
47-353 |
3.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRE 126
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLRERRGVLAEVLAALQRMGRNPPPALLVSPEDALASVRSAILLGAVVpgirGETDKLVAALKELTDLRQAIARE 206
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK----EEELAEAEKLIESLPRELAEELL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 207 KDDLTGMMTASLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAEEQR 286
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALL 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739226812 287 LARLSEAEREKQRAAAEAGMPDKNRIAPAYPFASLKGKLEFPVAGEVLRRFGDADGTGHFSKGVVVA 353
Cdd:COG4372 302 LNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
47-300 |
3.83e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREELIASAARRKALETKISDGEDRLAKLSVRE 126
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 DGVKASLRERRGVLAEVlAALQRMGRNPPPALLV--SPE-DALASVRSAIL-LGAVVPGIRGETDKLVAALKELTDLRQA 202
Cdd:PRK02224 429 AELEATLRTARERVEEA-EALLEAGKCPECGQPVegSPHvETIEEDRERVEeLEAELEDLEEEVEEVEERLERAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 203 IAR------EKDDLTGMMT---ASLEEE--------KRLDLLIAENDRKNSQ-TAAELEAERKRSE---------ELASK 255
Cdd:PRK02224 508 EDRierleeRREDLEELIAerrETIEEKreraeelrERAAELEAEAEEKREAaAEAEEEAEEAREEvaelnsklaELKER 587
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739226812 256 ATSLEGLVSSL------EGEITSVREAME-KARAEEQRL-------------------ARLSEAEREKQRA 300
Cdd:PRK02224 588 IESLERIRTLLaaiadaEDEIERLREKREaLAELNDERRerlaekrerkreleaefdeARIEEAREDKERA 658
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-301 |
5.49e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 54 KRRDQNRQDLEELVDSIGLSEDKTRKLEESIASLDQ---DSARIREELIASAARRKALETKISDgEDRLAKLSVREDGVK 130
Cdd:PTZ00121 1140 RKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAkkaEAARKAEEVRKAEELRKAEDARKAE-AARKAEEERKAEEAR 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 131 ASLRERRgvlAEVLAALQRMGRNPPPALLVSPEDALASVRsaillgavvpgiRGETDKLVAALKELTDLRQAIAREKDDL 210
Cdd:PTZ00121 1219 KAEDAKK---AEAVKKAEEAKKDAEEAKKAEEERNNEEIR------------KFEEARMAHFARRQAAIKAEEARKADEL 1283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 211 TgmmtaSLEEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKARAEEQRLARL 290
Cdd:PTZ00121 1284 K-----KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
250
....*....|.
gi 739226812 291 SEAEREKQRAA 301
Cdd:PTZ00121 1359 AEAAEEKAEAA 1369
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
54-304 |
5.88e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 54 KRRDQNRQDLEEL--VDSIGLSEDKTRKLEESIASLDQDSARIR-EELIASAARRKALETKISDgEDRLAKLSVREDGVK 130
Cdd:PTZ00121 1230 KKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 131 ASLRERRGvlAEVLAALQRMGRNPPPALLVSPEDALASVRSAillgavVPGIRGETDKLVAALK--ELTDLRQAIAREKD 208
Cdd:PTZ00121 1309 KKAEEAKK--ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA------KAEAEAAADEAEAAEEkaEAAEKKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 209 DltgMMTASLEEEKRLDLLI--AENDRKNSQTAAELEAERKRSEELASKATSLEGlVSSLEGEITSVREAME-KARAEEQ 285
Cdd:PTZ00121 1381 D---AAKKKAEEKKKADEAKkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-ADEAKKKAEEAKKADEaKKKAEEA 1456
|
250
....*....|....*....
gi 739226812 286 RLARLSEAEREKQRAAAEA 304
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEA 1475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-279 |
6.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRdqnrQDLEELVDSIGLSEDKTRKLEESIASLDQDSARIREeliasaaRRKALETKISDGEDRLAKLSVREd 127
Cdd:PRK03918 222 ELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-------RIEELKKEIEELEEKVKELKELK- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 128 GVKASLRERRGVLAEVLAALQRMgrnpppallvspEDALASVRSAIllgAVVPGIRGETDKLVAALKELTDLRQAIAREK 207
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREI------------EKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739226812 208 DDLTG------MMTASLEEEKRLDLLIAENDRKnsQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEK 279
Cdd:PRK03918 355 EELEErhelyeEAKAKKEELERLKKRLTGLTPE--KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
47-313 |
8.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 47 DEL-QSLEKRRDQNRQDLEELVDSiglseDKTRKLEESIASldqDSARIREELIASAARRKALETKISDgEDRLAKLSVR 125
Cdd:PTZ00121 1513 DEAkKAEEAKKADEAKKAEEAKKA-----DEAKKAEEKKKA---DELKKAEELKKAEEKKKAEEAKKAE-EDKNMALRKA 1583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 126 EDGVKAslRERRgvLAEVLAALQRMGRNPPPALLVSPEDALAS--VRSAillgavvpgirGETDKLVAALK--ELTDLRQ 201
Cdd:PTZ00121 1584 EEAKKA--EEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKA-----------EEEKKKVEQLKkkEAEEKKK 1648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 202 AIAREKDDLTGMMTAslEEEKRLDlliAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEITSVREAMEKAR 281
Cdd:PTZ00121 1649 AEELKKAEEENKIKA--AEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
250 260 270
....*....|....*....|....*....|....*..
gi 739226812 282 AEEQRLARLSEAER---EKQRAAAEAGMP--DKNRIA 313
Cdd:PTZ00121 1724 AEEENKIKAEEAKKeaeEDKKKAEEAKKDeeEKKKIA 1760
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
48-303 |
8.84e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 48 ELQSLEKRRDQNRQDLEELVDSIGLSEDKTRKLEEsiasLDQDSARIREELIASAARR-KALETKISDGEDRLAKLSVRe 126
Cdd:PRK03918 339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEE----LERLKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITAR- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 127 dgvKASLRERRGVLAEVLAALQRM-GRNPPPALLVSPEDALASVRSAIL-LGAVVPGIRGETDKLVAALKELTDLRQAIA 204
Cdd:PRK03918 414 ---IGELKKEIKELKKAIEELKKAkGKCPVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739226812 205 REKDDLTgmmtasleEEKRLDLLIAENDRKNSQTAAELEAERKRSEELASKATSLEGLVSSLEGEItsvreamEKARAEE 284
Cdd:PRK03918 491 KESELIK--------LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKEL-------EKLEELK 555
|
250
....*....|....*....
gi 739226812 285 QRLARLSEAEREKQRAAAE 303
Cdd:PRK03918 556 KKLAELEKKLDELEEELAE 574
|
|
| |
