|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
2-637 |
7.23e-141 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 426.50 E-value: 7.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 2 DARIRVDQLRAALGSAAIALPINLILSGICAAVAWHAGHTLLALIWLAASLAVAAARVSLLRRAREMPSGTPADVERQLR 81
Cdd:COG5001 36 LALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 82 GLWVITLAAGLVWAMLPALCALYTAPQSLFFLAVGCGITAGAVSHGGAYARVPIAFITPPIVSSALALLSVGGFDRNMLA 161
Cdd:COG5001 116 LAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 162 ATMAIYLAALIVTARRAEAAFRGASALGHRLAVVNGSLEAAHACAQASASEMRHRADHDHLTGLLNRAGF---LRAAAVQ 238
Cdd:COG5001 196 LLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFldrLEQALAR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 239 IDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGDEFAVLLAADAALTAPLALADRLI 318
Cdd:COG5001 276 ARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERIL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 319 AAVAAPYPTFGTIARVGLSVGVHLA--HGSAMPEMLCCADLALYAAKSAGRNRCHVFGDDLRTALELRRDIERDLPAALG 396
Cdd:COG5001 356 AALAEPFELDGHELYVSASIGIALYpdDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 397 NGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIVALRARGFDHVTVA 476
Cdd:COG5001 436 RGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVA 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 477 MNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAIDDFGIGYSSLSLLRTLK 555
Cdd:COG5001 516 VNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLeDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLP 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 556 VDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMPMTQCLAFVAD 635
Cdd:COG5001 596 VDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
..
gi 1946821238 636 AH 637
Cdd:COG5001 676 RA 677
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
389-625 |
9.28e-82 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 257.86 E-value: 9.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 389 RDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIVALRAr 468
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 469 GFDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAIDDFGIGYSS 547
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946821238 548 LSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMP 625
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
388-625 |
3.28e-74 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 238.27 E-value: 3.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 388 ERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIVALRA 467
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 468 RGFDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETALDTTSCARKM-AALSHAGIRIAIDDFGIGYS 546
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATlQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946821238 547 SLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMP 625
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
213-628 |
1.73e-59 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 211.08 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 213 MRHRADHDHLTGLLNRAGF--LRAAAVQIDAESAPKcLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLG 290
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIqeLIDHAINAADNNQVG-IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 291 RWGGDEFAVLLAADAALTAPLALaDRLIAAVAAPYptfgtiaRVGL-------SVGVHLA--HGSAMPEMLCCADLALYA 361
Cdd:PRK10060 312 RLGGDEFLVLASHTSQAALEAMA-SRILTRLRLPF-------RIGLievytgcSIGIALApeHGDDSESLIRSADTAMYT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 362 AKSAGRNRCHVFGDDL--RTALELRRDIerDLPAALGNGDVSVWFQPIFgDGGTRILGLEALVRWQHPTLGWITPPDLMA 439
Cdd:PRK10060 384 AKEGGRGQFCVFSPEMnqRVFEYLWLDT--NLRKALENDQLVIHYQPKI-TWRGEVRSLEALVRWQSPERGLIPPLEFIS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 440 TAARAGFARSLMDLILDRVCCMIVALRARGFDhVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETALDT 519
Cdd:PRK10060 461 YAEESGLIVPLGRWVMLDVVRQVAKWRDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIEN 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 520 TSCARK-MAALSHAGIRIAIDDFGIGYSSLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGV 598
Cdd:PRK10060 540 EELALSvIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGV 619
|
410 420 430
....*....|....*....|....*....|
gi 1946821238 599 ESLEDLRMLRTFGCQMMQGYHLARPMPMTQ 628
Cdd:PRK10060 620 ETAKEDAFLTKNGVNERQGFLFAKPMPAVA 649
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
388-623 |
4.47e-59 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 198.31 E-value: 4.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 388 ERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIvaLRA 467
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADL--AQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 468 RGFDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAIDDFGIGYS 546
Cdd:pfam00563 79 QLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLaRLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946821238 547 SLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARP 623
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
216-373 |
2.20e-28 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 111.27 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 216 RADHDHLTGLLNRAGFLRAAAVQID---AESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRW 292
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKrarRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 293 GGDEFAVLLAADAALTAPLALADR--LIAAVAAPYPTFGTIaRVGLSVGVHLA--HGSAMPEMLCCADLALYAAKSAGRN 368
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLrdAINSKPIEVAGSETL-TVTVSIGVACYpgHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 1946821238 369 RCHVF 373
Cdd:TIGR00254 160 RVVVA 164
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
2-637 |
7.23e-141 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 426.50 E-value: 7.23e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 2 DARIRVDQLRAALGSAAIALPINLILSGICAAVAWHAGHTLLALIWLAASLAVAAARVSLLRRAREMPSGTPADVERQLR 81
Cdd:COG5001 36 LALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 82 GLWVITLAAGLVWAMLPALCALYTAPQSLFFLAVGCGITAGAVSHGGAYARVPIAFITPPIVSSALALLSVGGFDRNMLA 161
Cdd:COG5001 116 LAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 162 ATMAIYLAALIVTARRAEAAFRGASALGHRLAVVNGSLEAAHACAQASASEMRHRADHDHLTGLLNRAGF---LRAAAVQ 238
Cdd:COG5001 196 LLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFldrLEQALAR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 239 IDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGDEFAVLLAADAALTAPLALADRLI 318
Cdd:COG5001 276 ARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERIL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 319 AAVAAPYPTFGTIARVGLSVGVHLA--HGSAMPEMLCCADLALYAAKSAGRNRCHVFGDDLRTALELRRDIERDLPAALG 396
Cdd:COG5001 356 AALAEPFELDGHELYVSASIGIALYpdDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 397 NGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIVALRARGFDHVTVA 476
Cdd:COG5001 436 RGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVA 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 477 MNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAIDDFGIGYSSLSLLRTLK 555
Cdd:COG5001 516 VNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLeDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLP 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 556 VDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMPMTQCLAFVAD 635
Cdd:COG5001 596 VDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
..
gi 1946821238 636 AH 637
Cdd:COG5001 676 RA 677
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
61-634 |
7.44e-84 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 274.74 E-value: 7.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 61 LLRRAREMPSGTPADVERQLRGLWVITLAAGLVWAMLPALCALYTAPQSLFFLAVGCGITAGAVSHGGAYARVPIAFITP 140
Cdd:COG2200 2 LLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 141 PIVSSALALLSVGGFDRNMLAATMAIYLAALIVTARRAEAAFRGASALGHRLAVVNGSLEAAHACAQASASEMRHRADHD 220
Cdd:COG2200 82 LLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 221 HLTGLLNRAGFLRAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGDEFAVL 300
Cdd:COG2200 162 LLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 301 LAADAALTAPLALADRLIAAVAAPYPTFGTIARVGLSVGVHLAH-GSAMPEMLCCADLALYAAKSAGRNRCHVFGDDLRT 379
Cdd:COG2200 242 LLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPdDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 380 ALELRRDIERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVC 459
Cdd:COG2200 322 RARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERAL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 460 CMIVALRARGFDhVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAI 538
Cdd:COG2200 402 RQLARWPERGLD-LRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLeDLEAAIELLARLRALGVRIAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 539 DDFGIGYSSLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGY 618
Cdd:COG2200 481 DDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
|
570
....*....|....*.
gi 1946821238 619 HLARPMPMTQCLAFVA 634
Cdd:COG2200 561 LFGRPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
389-625 |
9.28e-82 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 257.86 E-value: 9.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 389 RDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIVALRAr 468
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 469 GFDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAIDDFGIGYSS 547
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIdDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946821238 548 LSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMP 625
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
388-625 |
3.28e-74 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 238.27 E-value: 3.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 388 ERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIVALRA 467
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 468 RGFDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETALDTTSCARKM-AALSHAGIRIAIDDFGIGYS 546
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATlQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1946821238 547 SLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMP 625
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
213-628 |
1.73e-59 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 211.08 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 213 MRHRADHDHLTGLLNRAGF--LRAAAVQIDAESAPKcLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLG 290
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIqeLIDHAINAADNNQVG-IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 291 RWGGDEFAVLLAADAALTAPLALaDRLIAAVAAPYptfgtiaRVGL-------SVGVHLA--HGSAMPEMLCCADLALYA 361
Cdd:PRK10060 312 RLGGDEFLVLASHTSQAALEAMA-SRILTRLRLPF-------RIGLievytgcSIGIALApeHGDDSESLIRSADTAMYT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 362 AKSAGRNRCHVFGDDL--RTALELRRDIerDLPAALGNGDVSVWFQPIFgDGGTRILGLEALVRWQHPTLGWITPPDLMA 439
Cdd:PRK10060 384 AKEGGRGQFCVFSPEMnqRVFEYLWLDT--NLRKALENDQLVIHYQPKI-TWRGEVRSLEALVRWQSPERGLIPPLEFIS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 440 TAARAGFARSLMDLILDRVCCMIVALRARGFDhVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETALDT 519
Cdd:PRK10060 461 YAEESGLIVPLGRWVMLDVVRQVAKWRDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIEN 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 520 TSCARK-MAALSHAGIRIAIDDFGIGYSSLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGV 598
Cdd:PRK10060 540 EELALSvIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGV 619
|
410 420 430
....*....|....*....|....*....|
gi 1946821238 599 ESLEDLRMLRTFGCQMMQGYHLARPMPMTQ 628
Cdd:PRK10060 620 ETAKEDAFLTKNGVNERQGFLFAKPMPAVA 649
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
388-623 |
4.47e-59 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 198.31 E-value: 4.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 388 ERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDRVCCMIvaLRA 467
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADL--AQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 468 RGFDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRIAIDDFGIGYS 546
Cdd:pfam00563 79 QLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLaRLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946821238 547 SLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARP 623
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
212-625 |
5.98e-54 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 197.68 E-value: 5.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 212 EMRHRADH----DHLTGLLNRaGFLRAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAV 287
Cdd:PRK11359 367 KSRQHIEQliqfDPLTGLPNR-NNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 288 LLGRWGGDEFAVLLAADAALTAPLALaDRLIAAVAAPYPTFGTIARVGLSVGVHLAHGSAMPEMLCCADLALYAAKSAGR 367
Cdd:PRK11359 446 YLCRIEGTQFVLVSLENDVSNITQIA-DELRNVVSKPIMIDDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDYIRKNGG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 368 NRCHVFGDDLRTALELRRDIERDLPAALGNGDVSVWFQP-IFGDGGtRILGLEALVRWQHPTLGWITPPDLMATAARAGF 446
Cdd:PRK11359 525 NGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPqIFAETG-ELYGIEALARWHDPLHGHVPPSRFIPLAEEIGE 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 447 ARSLMDLILDRVCCMIVALRARGFDHVTVAMNVSPREM--SQLPvdRMILSALAERQLPPAALEIEITEETALD-TTSCA 523
Cdd:PRK11359 604 IENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFrsNQLP--NQVSDAMQAWGIDGHQLTVEITESMMMEhDTEIF 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 524 RKMAALSHAGIRIAIDDFGIGYSSLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLED 603
Cdd:PRK11359 682 KRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQ 761
|
410 420
....*....|....*....|..
gi 1946821238 604 LRMLRTFGCQMMQGYHLARPMP 625
Cdd:PRK11359 762 FEMLRKIHCRVIQGYFFSRPLP 783
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
384-644 |
1.46e-49 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 180.88 E-value: 1.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 384 RRDIERDLPAALGNGDVSVWFQPIF--GDGgtRILGLEALVRWQHPTLGWItPPDLMATAA-RAGFARSLMDLILDRVCC 460
Cdd:COG4943 269 RLSPRRRLRRAIKRREFYVHYQPIVdlKTG--RCVGAEALVRWRDPDGSVI-SPDIFIPLAeQSGLISPLTRQVIEQVFR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 461 -MIVALRARgfDHVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETALDTTSCARKMAALSHAGIRIAID 539
Cdd:COG4943 346 dLGDLLAAD--PDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 540 DFGIGYSSLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYH 619
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250 260
....*....|....*....|....*
gi 1946821238 620 LARPMPMTQCLAFVADAHTQAVPPN 644
Cdd:COG4943 504 FAKPLPAEEFIAWLAAQRAPASAPA 528
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
212-628 |
4.69e-44 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 167.58 E-value: 4.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 212 EMRHRADHDHLTGLLNRAgFLRAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGR 291
Cdd:PRK13561 226 EQSRNATRFPVSDLPNKA-LLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 292 WGGDEFAVLLAADAALTAPLALADRLIAAVAAPYPTFGTIARVGLSVGVHLAHGS-AMPEMLCCADLALYAAKSAGRNRC 370
Cdd:PRK13561 305 ISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDlTAEQLYSRAISAAFTARRKGKNQI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 371 HVFGDDLRTALELRRDIERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSL 450
Cdd:PRK13561 385 QFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTV 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 451 MDLILDRVCCMIVALRARGFDhVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETALDTTSCA-RKMAAL 529
Cdd:PRK13561 465 GHWVLEESCRLLAAWQERGIM-LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAvAILRPL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 530 SHAGIRIAIDDFGIGYSSLSLL---RTLKVDAIKIDRCFVSGLSgsnGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRM 606
Cdd:PRK13561 544 RNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLP---EDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDW 620
|
410 420
....*....|....*....|..
gi 1946821238 607 LRTFGCQMMQGYHLARPMPMTQ 628
Cdd:PRK13561 621 LLKAGVGIAQGFLFARALPIEI 642
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
212-631 |
2.03e-42 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 165.23 E-value: 2.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 212 EMRHRADHDHLTGLLNRAGF---LRAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVL 288
Cdd:PRK09776 660 QLSYSASHDALTHLANRASFekqLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 289 LGRWGGDEFAVLLAADAALTAPLALAdRLIAAVAA-PYPTFGTIARVGLSVGVHLAHGSAMP--EMLCCADLALYAAKSA 365
Cdd:PRK09776 740 LARLGGDEFGLLLPDCNVESARFIAT-RIISAINDyHFPWEGRVYRVGASAGITLIDANNHQasEVMSQADIACYAAKNA 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 366 GRNRCHVFGDDLRTALELRRDIERD--LPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTlGWITPPdlmaTAAR 443
Cdd:PRK09776 819 GRGRVTVYEPQQAAAHSEHRALSLAeqWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPE-GEIIDE----GAFR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 444 AGFAR-SLMDLILDRVC-----CMIVALRARGfdhVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL 517
Cdd:PRK09776 894 PAAEDpALMHALDRRVIheffrQAAKAVASKG---LSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALL 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 518 DTTSCA-RKMAALSHAGIRIAIDDFGIGYSSLSLLRTLKVDAIKIDRCFVSGLSGSNGDQVLVKALLNLGQSLRIDVTAE 596
Cdd:PRK09776 971 NHAESAsRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAG 1050
|
410 420 430
....*....|....*....|....*....|....*
gi 1946821238 597 GVESLEDLRMLRTFGCQMMQGYHLARPMPMTQCLA 631
Cdd:PRK09776 1051 PVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLN 1085
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
223-637 |
2.06e-41 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 160.11 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 223 TGLLNRAGFLRAAAVQID--AESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGDEFAVL 300
Cdd:PRK11829 238 TELPNRSLFISLLEKEIAssTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 301 LAADAALTAPLALADRLIAAVAAPYpTFGTIA-RVGLSVGVHLAHGS--AMPEMLCCADLALYAAKSAGRNRCHVFGDDL 377
Cdd:PRK11829 318 ARGTRRSFPAMQLARRIMSQVTQPL-FFDEITlRPSASIGITRYQAQqdTAESMMRNASTAMMAAHHEGRNQIMVFEPHL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 378 RTALELRRDIERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWITPPDLMATAARAGFARSLMDLILDR 457
Cdd:PRK11829 397 IEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 458 VCCMIVALRARGFDhVTVAMNVSPREMSQLPVDRMILSALAERQLPPAALEIEITEETAL-DTTSCARKMAALSHAGIRI 536
Cdd:PRK11829 477 ACRILADWKARGVS-LPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIqDLDEALRLLRELQGLGLLI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 537 AIDDFGIGYSSLSLLRTLK---VDAIKIDRCFVSGLSgsnGDQVLVKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQ 613
Cdd:PRK11829 556 ALDDFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQ 632
|
410 420
....*....|....*....|....*.
gi 1946821238 614 MMQGYHLARPMPMTQCLA--FVADAH 637
Cdd:PRK11829 633 CGQGFLFSPPLPRAEFEAqyFSSAHH 658
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
219-371 |
2.54e-41 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 147.32 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 219 HDHLTGLLNRAGF---LRAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGD 295
Cdd:cd01949 2 TDPLTGLPNRRAFeerLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946821238 296 EFaVLLAADAALTAPLALADRLIAAVAAPYPTFGTIARVGLSVGV--HLAHGSAMPEMLCCADLALYAAKSAGRNRCH 371
Cdd:cd01949 82 EF-AILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIatYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
212-373 |
6.74e-40 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 147.43 E-value: 6.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 212 EMRHRADHDHLTGLLNRAGFLRAAAVQIDA---ESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVL 288
Cdd:COG2199 109 RLRRLATHDPLTGLPNRRAFEERLERELARarrEGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 289 LGRWGGDEFaVLLAADAALTAPLALADRLIAAVAA-PYPTFGTIARVGLSVGVHL--AHGSAMPEMLCCADLALYAAKSA 365
Cdd:COG2199 189 VARLGGDEF-AVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALypEDGDSAEELLRRADLALYRAKRA 267
|
....*...
gi 1946821238 366 GRNRCHVF 373
Cdd:COG2199 268 GRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
215-373 |
1.70e-35 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 131.60 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 215 HRADHDHLTGLLNRAGFLRAAAVQIDAESAPK---CLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGR 291
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 292 WGGDEFaVLLAADAALTAPLALADRLIAAVAAPYPTFGTIARVGLSVGVHLA--HGSAMPEMLCCADLALYAAKSAGRNR 369
Cdd:smart00267 81 LGGDEF-ALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpnPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1946821238 370 CHVF 373
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
217-369 |
7.87e-34 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 126.60 E-value: 7.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 217 ADHDHLTGLLNRAGFLRAAAVQI-DAESAPKC--LMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWG 293
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELqRALREGSPvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 294 GDEFA--VLLAADAALTAPLALADRLIAAVAAPYPTFGTIARVGLSVGVHLA--HGSAMPEMLCCADLALYAAKSAGRNR 369
Cdd:pfam00990 81 GDEFAilLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYpnDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
381-632 |
8.08e-32 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 129.73 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 381 LELRRDIERDLPAALGNGDVSVWFQPIFGDGGTRILGLEALVRWQHPTLGWItPPDLMATAARAG-----FARSLMDLIL 455
Cdd:PRK10551 258 LSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEI-PPDAFINYAEAQklivpLTQHLFELIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 456 DRVCCMIVALRArgfdHVTVAMNVSPREMSQlPVDRMILSALAErQLPPAALEI--EITEETALDTTSCARKMAALSHAG 533
Cdd:PRK10551 337 RDAAELQKVLPV----GAKLGINISPAHLHS-DSFKADVQRLLA-SLPADHFQIvlEITERDMVQEEEATKLFAWLHSQG 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 534 IRIAIDDFGIGYSSLSLLRTLKVDAIKIDRCFVSGLsGSNG--DQVLvKALLNLGQSLRIDVTAEGVESLEDLRMLRTFG 611
Cdd:PRK10551 411 IEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAI-GTETvtSPVL-DAVLTLAKRLNMLTVAEGVETPEQARWLRERG 488
|
250 260
....*....|....*....|.
gi 1946821238 612 CQMMQGYHLARPMPMTQCLAF 632
Cdd:PRK10551 489 VNFLQGYWISRPLPLEDFVRW 509
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
216-373 |
2.20e-28 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 111.27 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 216 RADHDHLTGLLNRAGFLRAAAVQID---AESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRW 292
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKrarRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 293 GGDEFAVLLAADAALTAPLALADR--LIAAVAAPYPTFGTIaRVGLSVGVHLA--HGSAMPEMLCCADLALYAAKSAGRN 368
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLrdAINSKPIEVAGSETL-TVTVSIGVACYpgHGLTLEELLKRADEALYQAKKAGRN 159
|
....*
gi 1946821238 369 RCHVF 373
Cdd:TIGR00254 160 RVVVA 164
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
216-376 |
1.31e-22 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 98.60 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 216 RADHDHLTGLLNRAGFLRAAAVQ-IDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGG 294
Cdd:PRK09894 128 RSNMDVLTGLPGRRVLDESFDHQlRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 295 DEFaVLLAADAALTAPLALADRLIAAVAAPYPTFGTIA-RVGLSVGVHLAH-GSAMPEMLCCADLALYAAKSAGRNRChV 372
Cdd:PRK09894 208 EEF-IICLKAATDEEACRAGERIRQLIANHAITHSDGRiNITATFGVSRAFpEETLDVVIGRADRAMYEGKQTGRNRV-M 285
|
....
gi 1946821238 373 FGDD 376
Cdd:PRK09894 286 FIDE 289
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
211-376 |
3.94e-20 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 94.31 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 211 SEMRHRADHDHLTGLLNRAGFL---RAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAV 287
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFekaRALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 288 LLGRWGGDEFaVLLAADAALTAPLALADRLIAAVAAP--YPTFGTIARVGLSVGVHLAHGSA---MPEMLCCADLALYAA 362
Cdd:PRK15426 472 VAGRVGGEEF-CVVLPGASLAEAAQVAERIRLRINEKeiLVAKSTTIRISASLGVSSAEEDGdydFEQLQSLADRRLYLA 550
|
170
....*....|....
gi 1946821238 363 KSAGRNRchVFGDD 376
Cdd:PRK15426 551 KQAGRNR--VCASD 562
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
220-369 |
1.13e-17 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 86.11 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 220 DHLTGLLNR---AGFLRAAAVQIDAESAPKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGDE 296
Cdd:PRK09581 295 DGLTGLHNRryfDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1946821238 297 FaVLLAADAALTAPLALADRLIAAVA-APYPTFGTIAR--VGLSVGV--HLAHGSAMPEMLCCADLALYAAKSAGRNR 369
Cdd:PRK09581 375 F-VVVMPDTDIEDAIAVAERIRRKIAeEPFIISDGKERlnVTVSIGVaeLRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
211-363 |
1.10e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 76.58 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 211 SEMRHRADHDHLTGLLNRAGFLRAAAVQIDAESAPKC--LMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVL 288
Cdd:PRK09966 242 AQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTsaLLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1946821238 289 LGRWGGDEFAVLLAADAALTAPLALADRLIAAVAAPYPTF-GTIARVGLSVGVHLAHGSAMPEMLC-CADLALYAAK 363
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMTIEHASAEKLQeLADHNMYQAK 398
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
492-628 |
2.13e-12 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 69.45 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 492 MILSALAErQLPPAALEIEITEETALDTTSCARkMAALSHAGIRIAIDDFGIGYSSLSLLRtlKVDAIKIDrcfvsgLSG 571
Cdd:COG3434 72 LLLSDLPE-LLPPERVVLEILEDVEPDEELLEA-LKELKEKGYRIALDDFVLDPEWDPLLP--LADIIKID------VLA 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946821238 572 SNGDQVlvKALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMPMTQ 628
Cdd:COG3434 142 LDLEEL--AELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
248-372 |
3.31e-12 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 68.32 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 248 LMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRRELPDAVLLGRWGGDEFavllaadaALTAPLALADRLIAAVAAPYPT 327
Cdd:PRK10245 239 LLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEF--------AVIMSGTPAESAITAMSRVHEG 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1946821238 328 FGTI-------ARVGLSVGV-----HLAHgsaMPEMLCCADLALYAAKSAGRNRCHV 372
Cdd:PRK10245 311 LNTLrlpnapqVTLRISVGVaplnpQMSH---YREWLKSADLALYKAKNAGRNRTEV 364
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
404-626 |
4.99e-09 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 57.70 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 404 FQPIFGDGGtRILGLEALVRWQHPTL--GWITPPDLMATAAragfARSLMDLILDRVccMIVALRARGF--DHVTVAMNV 479
Cdd:PRK11596 34 FQPIYRTSG-RLMAIELLTAVTHPSNpsQRLSPERYFAEIT----VSHRLDVVKEQL--DLLAQWADFFvrHGLLASVNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1946821238 480 spremsqlpvDRMILSALaeRQLPPAA--------LEIEITEETALDTTScarKMAALSHAGiRIAIDDFGIGYSSLSLL 551
Cdd:PRK11596 107 ----------DGPTLIAL--RQQPAILrlierlpwLRFELVEHIRLPKDS---PFASMCEFG-PLWLDDFGTGMANFSAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1946821238 552 RTLKVDAIKIDR-CFVSGLSGSNGDQVLVkALLNLGQSLRIDVTAEGVESLEDLRMLRTFGCQMMQGYHLARPMPM 626
Cdd:PRK11596 171 SEVRYDYIKVAReLFIMLRQSEEGRNLFS-QLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPF 245
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
245-297 |
1.25e-05 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 45.04 E-value: 1.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1946821238 245 PKCLMLLDLDGFKAINDVFGHAAGDAVLVEVAQRLRREL-PDAVLLGRWGGDEF 297
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEF 54
|
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| |
