|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
1-635 |
0e+00 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 901.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 1 MKLTRILTKKLTSFWLLSLTTVAFVFLLCAMMSFLQLTYKFQQQKVTELETMLSNQYQPSSNWELESWLPPMLIAYNAAS 80
Cdd:PRK11059 1 MKPTMRLTTKLSAFVTLLVALAMFVTLLGCTLSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLPELLQAANIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 81 FKLWHYDKLLFEYKGN-----IGTENLVRYQS-QLKNNPGIRMELELPQPFSQHRPGWYEVLIILVGVGAVLAFVRFGYL 154
Cdd:PRK11059 81 VDLSQGDKPVYSFQRPasyrpQGSSSLYRELSlPLLKHPGMSLRLKYVDPFGNYFYSLYATASLTLAIGFIVLMLFLGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 155 WYSRQLEGIEELAQRSRLILLGEHEKALAMPGKGKPRLINRALSRLLEELADAQKERARFDKFIRSNTFLDPDTRIGNRL 234
Cdd:PRK11059 161 WLRRQLAGQELLEERARRILNGEREQAVAGSGYEWPRTASRALDHLLSELQDAREERSRFDTFIRSNAFQDAKTGLGNRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 235 FLKNRLDALSNEQGMI-AHGVLYLLELEDLDLLQQQLGDSLTLELLRQNVNGISQILQSQPNSFFARRSHNQFAIVVTQI 313
Cdd:PRK11059 241 FFDNQLATLLEDQEMVgAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALLARYSRSDFAVLLPHR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 314 SLAEADQLAIRLLKVCQSQVLPKLDNADNFYHLGGAYFKVGDGQQQLLEEAEMALRAAQLQGINTWFMYDKgAVDQEFAK 393
Cdd:PRK11059 321 SLKEADSLASQLLKAVDALPPPKMLDRDDFLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDK-AQLPEKGR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 394 GSVRWRSFLEMALVNKRFLAYTQPVMDCDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFeLL 473
Cdd:PRK11059 400 GSVRWRTLLEQTLVRGGPRLYQQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLP-LL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 474 PSEPDKKvcFSINLSLDSLMSRAFIRWLRTTLLEY-RDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQ 552
Cdd:PRK11059 479 RYWPEEN--LSINLSVDSLLSRAFQRWLRDTLLQCpRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGL 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 553 QVISTQYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEP 632
Cdd:PRK11059 557 TVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
...
gi 765523070 633 MPA 635
Cdd:PRK11059 637 QPL 639
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
116-637 |
1.87e-61 |
|
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: 214.65 E-value: 1.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 116 RMELELPQPFSQHRPGWYEVLIILVGVGAVLAFVRFGYLWYSRQLEGIEELAQRSRLILLGEHEKALAMPGKGKPRLINR 195
Cdd:COG2200 49 LAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 196 ALSRLLEELADAQKERARFDKFIRSNTFLDPDTRIGNRLFLKNRLDALSNEQGMIAHGVLYLLELEDLDLLQQQLGDSLT 275
Cdd:COG2200 129 LLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 276 LELLRQNVNGISQILQSQPNSFFARRSHNQFAIVVTQISLAEADQLAIRLLKVCQSQVLPKLDNADNFYHLGGAYFKVGD 355
Cdd:COG2200 209 LLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 356 GQQQLLEEAEMALRAAQLQGINTWFMYDkgAVDQEFAKGSVRWRSFLEMALVNKRFLAYTQPVMDC-DGKLHHREVFTRA 434
Cdd:COG2200 289 ADAALLLAAAAAAAAAAAGGGRGRVVFF--AAAEARARRRLALESELREALEEGELRLYYQPIVDLrTGRVVGYEALLRW 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 435 RDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVL--FELLPsEPDKKVCFSINLSLDSLMSRAFIRWLRTTLLEYRDLT 512
Cdd:COG2200 367 RHPDGGLISPAEFIPAAERSGLIVELDRWVLERALrqLARWP-ERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 513 GRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLI 592
Cdd:COG2200 446 ERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIV 525
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 765523070 593 GGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:COG2200 526 ALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEE 570
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
402-632 |
4.59e-51 |
|
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: 176.35 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 402 LEMALVNKRFLAYTQPVMDC-DGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPSEPDKK 480
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLrTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 481 VCFSINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYI 560
Cdd:pfam00563 84 IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765523070 561 QDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEP 632
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
402-637 |
1.62e-47 |
|
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: 166.95 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 402 LEMALVNKRFLAYTQPVMDC-DGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPS-EPDK 479
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLrTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWqAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 480 KVCFSINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQY 559
Cdd:cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523070 560 IQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
401-635 |
1.09e-45 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 162.00 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 401 FLEMALVNKRFLAYTQPVMD-CDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPSEPDK 479
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSlRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 480 KVCF--SINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVIST 557
Cdd:smart00052 83 PPPLliSINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523070 558 QYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPA 635
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
1-635 |
0e+00 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 901.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 1 MKLTRILTKKLTSFWLLSLTTVAFVFLLCAMMSFLQLTYKFQQQKVTELETMLSNQYQPSSNWELESWLPPMLIAYNAAS 80
Cdd:PRK11059 1 MKPTMRLTTKLSAFVTLLVALAMFVTLLGCTLSFYQLTQEKQQHRVQALATAIDQHLLTQDAASLQRWLPELLQAANIVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 81 FKLWHYDKLLFEYKGN-----IGTENLVRYQS-QLKNNPGIRMELELPQPFSQHRPGWYEVLIILVGVGAVLAFVRFGYL 154
Cdd:PRK11059 81 VDLSQGDKPVYSFQRPasyrpQGSSSLYRELSlPLLKHPGMSLRLKYVDPFGNYFYSLYATASLTLAIGFIVLMLFLGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 155 WYSRQLEGIEELAQRSRLILLGEHEKALAMPGKGKPRLINRALSRLLEELADAQKERARFDKFIRSNTFLDPDTRIGNRL 234
Cdd:PRK11059 161 WLRRQLAGQELLEERARRILNGEREQAVAGSGYEWPRTASRALDHLLSELQDAREERSRFDTFIRSNAFQDAKTGLGNRL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 235 FLKNRLDALSNEQGMI-AHGVLYLLELEDLDLLQQQLGDSLTLELLRQNVNGISQILQSQPNSFFARRSHNQFAIVVTQI 313
Cdd:PRK11059 241 FFDNQLATLLEDQEMVgAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALLARYSRSDFAVLLPHR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 314 SLAEADQLAIRLLKVCQSQVLPKLDNADNFYHLGGAYFKVGDGQQQLLEEAEMALRAAQLQGINTWFMYDKgAVDQEFAK 393
Cdd:PRK11059 321 SLKEADSLASQLLKAVDALPPPKMLDRDDFLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDK-AQLPEKGR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 394 GSVRWRSFLEMALVNKRFLAYTQPVMDCDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFeLL 473
Cdd:PRK11059 400 GSVRWRTLLEQTLVRGGPRLYQQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLP-LL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 474 PSEPDKKvcFSINLSLDSLMSRAFIRWLRTTLLEY-RDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQ 552
Cdd:PRK11059 479 RYWPEEN--LSINLSVDSLLSRAFQRWLRDTLLQCpRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGL 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 553 QVISTQYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEP 632
Cdd:PRK11059 557 TVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
...
gi 765523070 633 MPA 635
Cdd:PRK11059 637 QPL 639
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
116-637 |
1.87e-61 |
|
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: 214.65 E-value: 1.87e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 116 RMELELPQPFSQHRPGWYEVLIILVGVGAVLAFVRFGYLWYSRQLEGIEELAQRSRLILLGEHEKALAMPGKGKPRLINR 195
Cdd:COG2200 49 LAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 196 ALSRLLEELADAQKERARFDKFIRSNTFLDPDTRIGNRLFLKNRLDALSNEQGMIAHGVLYLLELEDLDLLQQQLGDSLT 275
Cdd:COG2200 129 LLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 276 LELLRQNVNGISQILQSQPNSFFARRSHNQFAIVVTQISLAEADQLAIRLLKVCQSQVLPKLDNADNFYHLGGAYFKVGD 355
Cdd:COG2200 209 LLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 356 GQQQLLEEAEMALRAAQLQGINTWFMYDkgAVDQEFAKGSVRWRSFLEMALVNKRFLAYTQPVMDC-DGKLHHREVFTRA 434
Cdd:COG2200 289 ADAALLLAAAAAAAAAAAGGGRGRVVFF--AAAEARARRRLALESELREALEEGELRLYYQPIVDLrTGRVVGYEALLRW 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 435 RDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVL--FELLPsEPDKKVCFSINLSLDSLMSRAFIRWLRTTLLEYRDLT 512
Cdd:COG2200 367 RHPDGGLISPAEFIPAAERSGLIVELDRWVLERALrqLARWP-ERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 513 GRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLI 592
Cdd:COG2200 446 ERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIV 525
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 765523070 593 GGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:COG2200 526 ALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEE 570
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
402-632 |
4.59e-51 |
|
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: 176.35 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 402 LEMALVNKRFLAYTQPVMDC-DGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPSEPDKK 480
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLrTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 481 VCFSINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYI 560
Cdd:pfam00563 84 IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765523070 561 QDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEP 632
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
402-637 |
1.62e-47 |
|
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: 166.95 E-value: 1.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 402 LEMALVNKRFLAYTQPVMDC-DGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPS-EPDK 479
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLrTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWqAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 480 KVCFSINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQY 559
Cdd:cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523070 560 IQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
401-635 |
1.09e-45 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 162.00 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 401 FLEMALVNKRFLAYTQPVMD-CDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPSEPDK 479
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSlRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 480 KVCF--SINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVIST 557
Cdd:smart00052 83 PPPLliSINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523070 558 QYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPA 635
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
132-637 |
1.68e-36 |
|
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: 145.30 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 132 WYEVLIILVGVGAVLAFVRFGYLWYSRQLEGIEELAQRSRLILLGEHEKALAMPGKGKPRLINRALSRLLEELADAQKER 211
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 212 ARFDKFIRSNTFLDPDTRIGNRLFLKNRLD-ALSN---EQGMIA-----------------HGVlylleledldllqqql 270
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEqALARarrSGRRLAllfidldrfkeindtlgHAA---------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 271 GDsltlELLRQnvngISQILQSQ--PNSFFARRSHNQFAIVVTQI-SLAEADQLAIRLLKVCQSqvlPkldnadnfYHLG 347
Cdd:COG5001 305 GD----ELLRE----VARRLRAClrEGDTVARLGGDEFAVLLPDLdDPEDAEAVAERILAALAE---P--------FELD 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 348 GAYFKVG----------DGQ--QQLLEEAEMALRAAQLQGINTWFMYDKGAvdQEFAKGSVRWRSFLEMALVNKRFLAYT 415
Cdd:COG5001 366 GHELYVSasigialypdDGAdaEELLRNADLAMYRAKAAGRNRYRFFDPEM--DERARERLELEADLRRALERGELELHY 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 416 QPVMD-CDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFEL--LPSEPDKKVCFSINLSLDSL 492
Cdd:COG5001 444 QPQVDlATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLaaWQDAGLPDLRVAVNLSARQL 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 493 MSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGqqvisT-----QYIQDTGFEL 567
Cdd:COG5001 524 RDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFG-----TgysslSYLKRLPVDT 598
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 765523070 568 IKLHRSIVRQIHLRPENQLFVRSLIG-----GLyrtevQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:COG5001 599 LKIDRSFVRDLAEDPDDAAIVRAIIAlahslGL-----EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEE 668
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
395-637 |
1.27e-25 |
|
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: 111.16 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 395 SVRWRsfLEMALVNKRFLAYTQPVMD-CDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFEL- 472
Cdd:COG4943 271 SPRRR--LRRAIKRREFYVHYQPIVDlKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLg 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 473 --LPSEPDKKVcfSINLSLDSLMSRAFIRWLRTTLLEYRDLTGRLIFEVSEDIAApNQEKIASRLQMIRKMGARLCVDHV 550
Cdd:COG4943 349 dlLAADPDFHI--SINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDF 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 551 GQQVISTQYIQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFS 630
Cdd:COG4943 426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
|
....*..
gi 765523070 631 EPMPASA 637
Cdd:COG4943 506 KPLPAEE 512
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
198-636 |
2.95e-21 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 98.69 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 198 SRLLEELADAQKE-RARFDKFIRsntfLDPDTRIGNRLFLKNRLDALSNEQGMIahgVLYLLELEDLDLLQQQLGDSLTL 276
Cdd:PRK11359 355 SQHLAALALEQEKsRQHIEQLIQ----FDPLTGLPNRNNLHNYLDDLVDKAVSP---VVYLIGVDHFQDVIDSLGYAWAD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 277 ELLRQNVNGISQILQsqPNSFFARRSHNQFAIVVTQISLAEADQLAIRLlkvcQSQVLPKLDNADNFYHLG---GAYFKV 353
Cdd:PRK11359 428 QALLEVVNRFREKLK--PDQYLCRIEGTQFVLVSLENDVSNITQIADEL----RNVVSKPIMIDDKPFPLTlsiGISYDV 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 354 GDGQQQLLEEAEMALRAAQLQGINTWFMYDKG---AVDQEFAKGSVrwrsfLEMALVNKRFLAYTQP-VMDCDGKLHHRE 429
Cdd:PRK11359 502 GKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAmneMVKERLVLGAA-----LKEAISNNQLKLVYQPqIFAETGELYGIE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 430 VFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELlpSEPDKK----VCFSINLSLDSLMSRAFIRWLRTTL 505
Cdd:PRK11359 577 ALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQL--AEWRSQnihiPALSVNLSALHFRSNQLPNQVSDAM 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 506 LEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYIQDTGFELIKLHRSIVRQIHLRPENQ 585
Cdd:PRK11359 655 QAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRIL 734
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 765523070 586 LFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPAS 636
Cdd:PRK11359 735 ALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
271-637 |
9.84e-20 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 93.97 E-value: 9.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 271 GDSLTLELlrqnvngiSQILQS--QPNSFFARRSHNQFAIVVTQISLAEADQLAIRLLkvcqSQVlpkldNADNFYHLGG 348
Cdd:PRK09776 719 GDALLREL--------ASLMLSmlRSSDVLARLGGDEFGLLLPDCNVESARFIATRII----SAI-----NDYHFPWEGR 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 349 AYfKVG--------DGQ----QQLLEEAEMALRAAQLQGINTWFMYDKGAVDQEFAKGSVRWRSFLEMALVNKRFLAYTQ 416
Cdd:PRK09776 782 VY-RVGasagitliDANnhqaSEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHG 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 417 ------PVMDCdgklhHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLPSEPDKKVCFSINLSLD 490
Cdd:PRK09776 861 vaspriPEARN-----HWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVASKGLSIALPLSVA 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 491 SLMSRAFIRWLrTTLLEYRDLTGRLI-FEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYIQDTGFELIK 569
Cdd:PRK09776 936 GLSSPTLLPFL-LEQLENSPLPPRLLhLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLK 1014
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523070 570 LHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:PRK09776 1015 LDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDL 1082
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
402-637 |
2.64e-17 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 85.89 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 402 LEMALVNKRFLAYTQPVMDCDGKLHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLERVLFELLP-SEPDKK 480
Cdd:PRK10060 413 LRKALENDQLVIHYQPKITWRGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKwRDKGIN 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 481 VCFSINLSLDSLMSRAFIRWLrTTLLEYRDLTGRLI-FEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQY 559
Cdd:PRK10060 493 LRVAVNVSARQLADQTIFTAL-KQALQELNFEYCPIdVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQ 571
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523070 560 IQDTGFELIKLHRSIVRQIHLRPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVA 649
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
346-637 |
4.01e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 85.15 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 346 LGGAYFKVGDGQQQLLEEAEMALRAAQLQGINTWFMYDKGAVdqEFAKGSVRWRSFLEMALVNKRFLAYTQPVMDC-DGK 424
Cdd:PRK13561 351 IGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQM--EAAQKRLTEESDILNALENHQFAIWLQPQVEMrSGK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 425 LHHREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLE---RVLFE------LLPsepdkkvcFSINLSLDSLMSR 495
Cdd:PRK13561 429 LVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEescRLLAAwqergiMLP--------LSVNLSALQLMHP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 496 AFIRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYIQDTG---FELIKLHR 572
Cdd:PRK13561 501 NMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDK 580
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 765523070 573 SIVRQIhlrPENQLFVRSLIGGLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMPASA 637
Cdd:PRK13561 581 MFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
272-634 |
4.32e-15 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 78.83 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 272 DSLTLELLRQNVNGISqilqsqPNSFFARRSHNQFAIVVTQISL-AEADQLAIRLLKVCQSQVLpkLDNAD--NFYHLGG 348
Cdd:PRK11829 286 QQLLLTIVQRIEQCID------DSDLLAQLSKTEFAVLARGTRRsFPAMQLARRIMSQVTQPLF--FDEITlrPSASIGI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 349 AYFKVG-DGQQQLLEEAEMALRAAQLQGINTWFMYDKGAVdqEFAKGSVRWRSFLEMALVNKRFLAYTQPVMDCDG-KLH 426
Cdd:PRK11829 358 TRYQAQqDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLI--EKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRqQVI 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 427 HREVFTRARDPEGNLVRATLFLPMAVKCGLMPQIERQTLE---RVLFE------LLPsepdkkvcFSINLSLDSLMSRAF 497
Cdd:PRK11829 436 GAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEeacRILADwkargvSLP--------LSVNISGLQVQNKQF 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 498 IRWLRTTLLEYRDLTGRLIFEVSEDIAAPNQEKIASRLQMIRKMGARLCVDHVGQQVISTQYIQDTG---FELIKLHRSI 574
Cdd:PRK11829 508 LPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKslpIHMIKLDKSF 587
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 765523070 575 VRQIhlrPENQLFVRsLIGGLYRT-EVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMP 634
Cdd:PRK11829 588 VKNL---PEDDAIAR-IISCVSDVlKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
223-382 |
1.81e-08 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 54.18 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 223 FLDPDTRIGNRLFLKNRLD-ALSNEQGMIAHGVLYLLELEDLDLLQQQLGDSLTLELLRQnvngISQILQS--QPNSFFA 299
Cdd:smart00267 4 FRDPLTGLPNRRYFEEELEqELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQE----VAQRLSSclRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 300 RRSHNQFAIVVTQISLAEADQLAIRLLKVCQSQVLPKLDNADNFYHLGGAYFKVGDGQ-QQLLEEAEMALRAAQLQGINT 378
Cdd:smart00267 80 RLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDaEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 765523070 379 WFMY 382
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
222-377 |
1.09e-06 |
|
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: 48.79 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 222 TFLDPDTRIGNRLFLKNRLD-ALSN---EQGMIA-----------------HGVlylleledldllqqqlGDsltlELLR 280
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEqELQRalrEGSPVAvllidldnfkrindtygHSV----------------GD----EVLQ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 281 QnvngISQILQS--QPNSFFARRSHNQFAIVVTQISLAEADQLAIRLLKVCQSQVLPKLDNADNFY---HLG-GAYFKVG 354
Cdd:pfam00990 61 E----VAQRLSSslRRSDLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPLYvtiSIGiAAYPNDG 136
|
170 180
....*....|....*....|...
gi 765523070 355 DGQQQLLEEAEMALRAAQLQGIN 377
Cdd:pfam00990 137 EDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
114-382 |
2.06e-06 |
|
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: 49.98 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 114 GIRMELELPQPFSQHRPGWYEVLIILVGVGAVLAFVRFGYLWYSRQLEGIEELAQRSRLILLGEHEKALAMPGKGKPRLI 193
Cdd:COG2199 7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 194 NRALSRLLEELADAQKERARFDKfIRSNTFLDPDTRIGNRLFLKNRLDAL---SNEQG------MI----------AHGV 254
Cdd:COG2199 87 LLALLLLLLALEDITELRRLEER-LRRLATHDPLTGLPNRRAFEERLERElarARREGrplallLIdldhfkrindTYGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 255 LYlleledldllqqqlGDsltlELLRQnvngISQILQSQ--PNSFFARRSHNQFAIVVTQISLAEADQLAIRLLKVCQSQ 332
Cdd:COG2199 166 AA--------------GD----EVLKE----VARRLRASlrESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQL 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 765523070 333 VLPKLDNADNF-YHLGGAYF-KVGDGQQQLLEEAEMALRAAQLQGINTWFMY 382
Cdd:COG2199 224 PFELEGKELRVtVSIGVALYpEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
271-379 |
6.11e-04 |
|
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: 40.62 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 271 GDsltlELLRQnvngISQILQSQ--PNSFFARRSHNQFAIVVTQISLAEADQLAIRLLKVCQSQVLPkldnADNFYHLG- 347
Cdd:cd01949 54 GD----EVLKE----VAERLRSSlrESDLVARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFFI----DGQEIRVTa 121
|
90 100 110
....*....|....*....|....*....|....*.
gi 765523070 348 --GAYFKVGDGQ--QQLLEEAEMALRAAQLQGINTW 379
Cdd:cd01949 122 siGIATYPEDGEdaEELLRRADEALYRAKRSGRNRV 157
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
517-634 |
4.90e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 39.21 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523070 517 FEVSEDIAAPNQEKIASrlqmIRKMGaRLCVDHVGQQVISTQYIQDTGFELIKLHRSIVrqIHLR--PE-NQLFVrSLIG 593
Cdd:PRK11596 132 FELVEHIRLPKDSPFAS----MCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVARELF--IMLRqsEEgRNLFS-QLLH 203
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 765523070 594 GLYRTEVQVCAEGVELFEEWQTLRILGVSAAQGSWFSEPMP 634
Cdd:PRK11596 204 LMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAP 244
|
|
| |
