|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
161-729 |
3.07e-83 |
|
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: 275.12 E-value: 3.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 161 IYSVVDIQSLICAGLIFTMMFYYPLRMIINPRYAIAFWRRSVKPVFYHKNPLYIFVWLMLLGFILVILCGPFESPVIAGY 240
Cdd:COG2200 4 LLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 241 LMPLIFILFTLAISRLTYALISLLWATSALLLLTYNYNFLNGVESGHSLSFILSVLISFAICLLYMSRIYQRSEWLKRGW 320
Cdd:COG2200 84 ALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 321 QDRALTDPLTGLPNIRALEDYLEIHPDAKVCILRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQKDELLFQLPGSELV 400
Cdd:COG2200 164 LRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 401 LVLLGPEIAERLQHMVDRLNSNKIFWNNTGLDIEFGASWGMVENGEKLHHTLGQLSWLAEQACGEQNVLALtnSLEAASG 480
Cdd:COG2200 244 LLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVV--FFAAAEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 481 QTTERVLMLARIKHALEAGQFHLYAQPIQKADGSG--YYEILTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEKLL 557
Cdd:COG2200 322 RARRRLALESELREALEEGELRLYYQPIVDLRTGRvvGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLERAL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 558 VWLRDNPATHAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAID 637
Cdd:COG2200 402 RQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 638 DFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYL 717
Cdd:COG2200 482 DFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYL 561
|
570
....*....|..
gi 2314424107 718 IGKPKPLEELRA 729
Cdd:COG2200 562 FGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
490-726 |
2.20e-79 |
|
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: 253.62 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 490 ARIKHALEAGQFHLYAQPIQKADGSG--YYEILTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNPAT 566
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRivGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 567 HAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANY 646
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 647 ERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEE 726
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
491-726 |
1.84e-75 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 243.28 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 491 RIKHALEAGQFHLYAQPIQKADGSG--YYEILTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNPATH 567
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRlvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 568 AGA-RFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANY 646
Cdd:smart00052 83 PPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 647 ERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEE 726
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
490-721 |
5.17e-65 |
|
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: 215.26 E-value: 5.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 490 ARIKHALEAGQFHLYAQPIQKADGSG--YYEILTRME-SEGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNpAT 566
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRvvGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 567 HAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANY 646
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314424107 647 ERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKP 721
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
324-727 |
2.32e-35 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 144.43 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 324 ALTDPLTGLPN--------IRALEDYLEIHPDAKVCILRMDNL------------EFLSRHYGIIMRVHckrtiatslqp 383
Cdd:PRK09776 665 ASHDALTHLANrasfekqlRRLLQTVNSTHQRHALVFIDLDRFkavndsaghaagDALLRELASLMLSM----------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 384 lLQKDELLFQLPGSELVLVLL------GPEIAERLQHMVdrlNSNKIFWNNTGLDIefGASWGMVENGEKLHHTlGQLSW 457
Cdd:PRK09776 734 -LRSSDVLARLGGDEFGLLLPdcnvesARFIATRIISAI---NDYHFPWEGRVYRV--GASAGITLIDANNHQA-SEVMS 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 458 LAEQAC------GEQNVLALTNSLEAASGQttERVLMLARIKH-ALEAGQFHLYAQPIQ--KADGSGYYEILTRM-ESEG 527
Cdd:PRK09776 807 QADIACyaaknaGRGRVTVYEPQQAAAHSE--HRALSLAEQWRmIKENQLMMLAHGVASprIPEARNHWLISLRLwDPEG 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 528 EIITPDRFIPLIAQFNLSHRFDMCVMEKLLvwlRDNPATHA--GARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVV 605
Cdd:PRK09776 885 EIIDEGAFRPAAEDPALMHALDRRVIHEFF---RQAAKAVAskGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLH 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 606 IEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAK 685
Cdd:PRK09776 962 LEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQ 1041
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2314424107 686 TKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEEL 727
Cdd:PRK09776 1042 RLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
323-417 |
1.10e-04 |
|
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: 43.48 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 323 RALTDPLTGLPNIRALEDYLEihPDAKVC----------ILRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQKDELLF 392
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLD--SELKRArrfqrsfsvlMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVG 78
|
90 100 110
....*....|....*....|....*....|.
gi 2314424107 393 QLPGSELVLVLLGP------EIAERLQHMVD 417
Cdd:TIGR00254 79 RYGGEEFVVILPGTpledalSKAERLRDAIN 109
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
161-729 |
3.07e-83 |
|
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: 275.12 E-value: 3.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 161 IYSVVDIQSLICAGLIFTMMFYYPLRMIINPRYAIAFWRRSVKPVFYHKNPLYIFVWLMLLGFILVILCGPFESPVIAGY 240
Cdd:COG2200 4 LLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 241 LMPLIFILFTLAISRLTYALISLLWATSALLLLTYNYNFLNGVESGHSLSFILSVLISFAICLLYMSRIYQRSEWLKRGW 320
Cdd:COG2200 84 ALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 321 QDRALTDPLTGLPNIRALEDYLEIHPDAKVCILRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQKDELLFQLPGSELV 400
Cdd:COG2200 164 LRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 401 LVLLGPEIAERLQHMVDRLNSNKIFWNNTGLDIEFGASWGMVENGEKLHHTLGQLSWLAEQACGEQNVLALtnSLEAASG 480
Cdd:COG2200 244 LLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVV--FFAAAEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 481 QTTERVLMLARIKHALEAGQFHLYAQPIQKADGSG--YYEILTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEKLL 557
Cdd:COG2200 322 RARRRLALESELREALEEGELRLYYQPIVDLRTGRvvGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLERAL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 558 VWLRDNPATHAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAID 637
Cdd:COG2200 402 RQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 638 DFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYL 717
Cdd:COG2200 482 DFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYL 561
|
570
....*....|..
gi 2314424107 718 IGKPKPLEELRA 729
Cdd:COG2200 562 FGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
490-726 |
2.20e-79 |
|
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: 253.62 E-value: 2.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 490 ARIKHALEAGQFHLYAQPIQKADGSG--YYEILTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNPAT 566
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRivGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 567 HAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANY 646
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 647 ERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEE 726
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
491-726 |
1.84e-75 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 243.28 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 491 RIKHALEAGQFHLYAQPIQKADGSG--YYEILTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNPATH 567
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRlvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 568 AGA-RFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANY 646
Cdd:smart00052 83 PPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 647 ERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEE 726
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
74-729 |
1.24e-65 |
|
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: 230.05 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 74 LFYVDLAPLQYSVLLFCQTFALFAACGLLRLMLGKRWRHSIPNKHIGLRIFWLGFMVPLGIKLSMYMAGYLFDFPVTIST 153
Cdd:COG5001 10 LLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 154 YFGEGTVIYSVVDIQSLICAGLIFTMMFYYPLRMIINPRYAIAFWRRSVKPVFYHKNPLYIFVWLMLLGFILVILCGPFE 233
Cdd:COG5001 90 LLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 234 SPviAGYLMPLIFILFTLAISRLTYALISLLWATSALLLLTYNYNFLNGVESGHSLSFILSVLISFAICLLYMSRIYQRS 313
Cdd:COG5001 170 LA--LLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 314 EWLkrgwqdrALTDPLTGLPNIRALEDYLE------IHPDAKVCILRMDnlefLSR------HYGiimrvHCK-----RT 376
Cdd:COG5001 248 RHL-------AYHDPLTGLPNRRLFLDRLEqalaraRRSGRRLALLFID----LDRfkeindTLG-----HAAgdellRE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 377 IATSLQPLLQKDELLFQLPGSELVLVLLGPEIAERLQHMVDRLN---SNKIFWNNTGLDIefGASWGMV---ENGeklhH 450
Cdd:COG5001 312 VARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILaalAEPFELDGHELYV--SASIGIAlypDDG----A 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 451 TLGQLSWLAEQAC------GEQNVLALTNSLEAasgQTTERVLMLARIKHALEAGQFHLYAQPI-----QKADGsgyYEI 519
Cdd:COG5001 386 DAEELLRNADLAMyrakaaGRNRYRFFDPEMDE---RARERLELEADLRRALERGELELHYQPQvdlatGRIVG---AEA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 520 LTRMES-EGEIITPDRFIPLIAQFNLSHRFDMCVMEK----LLVWLRdnpATHAGARFSVNLMPLTLMQKEVATEICALF 594
Cdd:COG5001 460 LLRWQHpERGLVSPAEFIPLAEETGLIVPLGEWVLREacrqLAAWQD---AGLPDLRVAVNLSARQLRDPDLVDRVRRAL 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 595 ERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDA 674
Cdd:COG5001 537 AETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDA 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 2314424107 675 MIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEELRA 729
Cdd:COG5001 617 AIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
490-721 |
5.17e-65 |
|
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: 215.26 E-value: 5.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 490 ARIKHALEAGQFHLYAQPIQKADGSG--YYEILTRME-SEGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNpAT 566
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRvvGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL-QL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 567 HAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANY 646
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2314424107 647 ERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKP 721
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
484-729 |
2.80e-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: 181.27 E-value: 2.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 484 ERVLMLARIKHALEAGQFHLYAQPI-QKADGS--GYyEILTRME-SEGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVW 559
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIvDLKTGRcvGA-EALVRWRdPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 560 LRDNPATHAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQaFSNSGSSINNIQQLRDYGFRIAIDDF 639
Cdd:COG4943 347 LGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERG-FIDPAKARAVIAALREAGHRIAIDDF 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 640 GTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIG 719
Cdd:COG4943 426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
|
250
....*....|
gi 2314424107 720 KPKPLEELRA 729
Cdd:COG4943 506 KPLPAEEFIA 515
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
324-727 |
2.32e-35 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 144.43 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 324 ALTDPLTGLPN--------IRALEDYLEIHPDAKVCILRMDNL------------EFLSRHYGIIMRVHckrtiatslqp 383
Cdd:PRK09776 665 ASHDALTHLANrasfekqlRRLLQTVNSTHQRHALVFIDLDRFkavndsaghaagDALLRELASLMLSM----------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 384 lLQKDELLFQLPGSELVLVLL------GPEIAERLQHMVdrlNSNKIFWNNTGLDIefGASWGMVENGEKLHHTlGQLSW 457
Cdd:PRK09776 734 -LRSSDVLARLGGDEFGLLLPdcnvesARFIATRIISAI---NDYHFPWEGRVYRV--GASAGITLIDANNHQA-SEVMS 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 458 LAEQAC------GEQNVLALTNSLEAASGQttERVLMLARIKH-ALEAGQFHLYAQPIQ--KADGSGYYEILTRM-ESEG 527
Cdd:PRK09776 807 QADIACyaaknaGRGRVTVYEPQQAAAHSE--HRALSLAEQWRmIKENQLMMLAHGVASprIPEARNHWLISLRLwDPEG 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 528 EIITPDRFIPLIAQFNLSHRFDMCVMEKLLvwlRDNPATHA--GARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVV 605
Cdd:PRK09776 885 EIIDEGAFRPAAEDPALMHALDRRVIHEFF---RQAAKAVAskGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLH 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 606 IEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAK 685
Cdd:PRK09776 962 LEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQ 1041
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2314424107 686 TKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEEL 727
Cdd:PRK09776 1042 RLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
475-729 |
1.80e-33 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 136.77 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 475 LEAASGQTTERVLMLarikHALEAGQFHLYAQPiQKADGSGYY---EILTRM-ESEGEIITPDRFIPLIAQFNLSHRFDM 550
Cdd:PRK13561 392 MEAAQKRLTEESDIL----NALENHQFAIWLQP-QVEMRSGKLvsaEALLRMqQPDGSWDLPEGLIDRIESCGLMVTVGH 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 551 CVMEKLLVWLRDNPATHAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDY 630
Cdd:PRK13561 467 WVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNA 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 631 GFRIAIDDFGTGYANYERLRRLQA---DIIKIDGCFVKDICTDdmDAMiVQSMCNLAKTKSLCVVAEYVETPAQREMLLR 707
Cdd:PRK13561 547 GVRVALDDFGMGYAGLRQLQHMKSlpiDVLKIDKMFVDGLPED--DSM-VAAIIMLAQSLNLQVIAEGVETEAQRDWLLK 623
|
250 260
....*....|....*....|..
gi 2314424107 708 FGVDYLQGYLIGKPKPLEELRA 729
Cdd:PRK13561 624 AGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
318-727 |
2.62e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 130.19 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 318 RGWQDR----ALTDPLTGLPNIRALEDY----LEIHPDAKVCI--LRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQK 387
Cdd:PRK10060 227 RRAQERlrilANTDSITGLPNRNAIQELidhaINAADNNQVGIvyLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 388 DELLFQLPGSELvLVLLGPEIAERLQHMVDRLNSNKIFWNNTGLdIEF--GASWGMV---ENGEKLHhtlgqlswlaeqa 462
Cdd:PRK10060 307 DQTLARLGGDEF-LVLASHTSQAALEAMASRILTRLRLPFRIGL-IEVytGCSIGIAlapEHGDDSE------------- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 463 cgeqnvlALTNSLEAA------SGQTTERVL---MLARI----------KHALEAGQFHLYAQPiqKADGSGYY---EIL 520
Cdd:PRK10060 372 -------SLIRSADTAmytakeGGRGQFCVFspeMNQRVfeylwldtnlRKALENDQLVIHYQP--KITWRGEVrslEAL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 521 TRMES-EGEIITPDRFIP------LIAQFNlshRFDM-CVMEKLLVWLRDNpathAGARFSVNLMPLTLMQKEVATEICA 592
Cdd:PRK10060 443 VRWQSpERGLIPPLEFISyaeesgLIVPLG---RWVMlDVVRQVAKWRDKG----INLRVAVNVSARQLADQTIFTALKQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 593 LFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAIDDFGTGYANYERLRRLQADIIKIDGCFVKDICTDDM 672
Cdd:PRK10060 516 ALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPV 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2314424107 673 DAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEEL 727
Cdd:PRK10060 596 SQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
327-727 |
4.11e-31 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 130.27 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 327 DPLTGLPNIRALEDYLE--IHPDAKVCI--LRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQKDELLFQLPGSELVLV 402
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDdlVDKAVSPVVylIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 403 LLGPE------IAERLQHMVDR--LNSNKIFwnntGLDIEFGASWGMVENGEKL----HHTLGQLSwlAEQACGEQNVLA 470
Cdd:PRK11359 459 SLENDvsnitqIADELRNVVSKpiMIDDKPF----PLTLSIGISYDVGKNRDYLlstaHNAMDYIR--KNGGNGWQFFSP 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 471 LTNslEAASgqttERVLMLARIKHALEAGQFHLYAQP-IQKADGSGY-YEILTRM-ESEGEIITPDRFIPL---IAQFNL 544
Cdd:PRK11359 533 AMN--EMVK----ERLVLGAALKEAISNNQLKLVYQPqIFAETGELYgIEALARWhDPLHGHVPPSRFIPLaeeIGEIEN 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 545 SHRFDMC-VMEKLLVWlrDNPATHAGArFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINN 623
Cdd:PRK11359 607 IGRWVIAeACRQLAEW--RSQNIHIPA-LSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKR 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 624 IQQLRDYGFRIAIDDFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQRE 703
Cdd:PRK11359 684 IQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFE 763
|
410 420
....*....|....*....|....
gi 2314424107 704 MLLRFGVDYLQGYLIGKPKPLEEL 727
Cdd:PRK11359 764 MLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
481-729 |
5.43e-28 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 120.05 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 481 QTTERVLMLARIKHALEAGQFHLYAQP---IQKADGSGYYEILTRMESEGEIITPDRFIPLIAQFNLSHRFDMCVMEKLL 557
Cdd:PRK11829 399 KTHKRLTQENDLLQAIENHDFTLFLQPqwdMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEAC 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 558 VWLRDNPATHAGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSGSSINNIQQLRDYGFRIAID 637
Cdd:PRK11829 479 RILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALD 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 638 DFGTGYA--NYER-LRRLQADIIKIDGCFVKDICTDDMDAMIVQSmcnLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQ 714
Cdd:PRK11829 559 DFGIGYSslRYLNhLKSLPIHMIKLDKSFVKNLPEDDAIARIISC---VSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQ 635
|
250
....*....|....*
gi 2314424107 715 GYLIGKPKPLEELRA 729
Cdd:PRK11829 636 GFLFSPPLPRAEFEA 650
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
13-314 |
1.22e-26 |
|
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins. This entry also includes members of the 8 transmembrane UhpB type (8TMR-UT) domain family.
Pssm-ID: 428383 [Multi-domain] Cd Length: 299 Bit Score: 110.58 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 13 MIALALCLIAVPVsRYLSPRAIVNGHDVYLAWLPLSVMLAVILIFGRRAILPIVLGFTVTNLF---YVDLAPLQYSVLLF 89
Cdd:pfam05231 2 LLLLLLLYALLAA-VSLSLALALVSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLMaglLSGLNLLLALAIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 90 CQTFALFAACGLLRLMLGKRWRHSIPnkhiglrIFWLGFMVPLGIKLSMYMAGYLFDFPVTISTYFGEGTVIYSVVDIQS 169
Cdd:pfam05231 81 VNALEALLGAALLRRLLPGRNRLQRL-------RFWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWWLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 170 LICAGLIFTMMFYYPLRMIINPRYAIAFWRRSVKPVFYHKNPLYIFVWLMLLGFILVILCGPFESPvIAGYLM--PLIFI 247
Cdd:pfam05231 154 SATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMPEINY-PLGYLLlpPLLWA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2314424107 248 LFTLAISRLTYALIsLLWATSALLLLTYNYNFLNGVESGHSLSFILSVLISFAICLLY-MSRIYQRSE 314
Cdd:pfam05231 233 AFRFGVRGGSLAAL-LLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALlVSAAISEQR 299
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
484-729 |
2.04e-26 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 113.93 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 484 ERVLMLArIKHaleaGQFHLYAQPI---QKADGSGYyEILTRME--SEGEIiTPDRFIPLIAQFNL-----SHRF----- 548
Cdd:PRK10551 265 GKEILTG-IKR----GQFYVEYQPVvdtQTLRVTGL-EALLRWRhpTAGEI-PPDAFINYAEAQKLivpltQHLFeliar 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 549 DMCVMEKLLvwlrdnPAthaGARFSVNLMPLTLMQKEVATEICALFERYGVAPQAVVIEITEEQAFSNSgSSINNIQQLR 628
Cdd:PRK10551 338 DAAELQKVL------PV---GAKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEE-EATKLFAWLH 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 629 DYGFRIAIDDFGTGYANYERLRRLQADIIKIDGCFVKDICTDDMDAMIVQSMCNLAKTKSLCVVAEYVETPAQREMLLRF 708
Cdd:PRK10551 408 SQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRER 487
|
250 260
....*....|....*....|.
gi 2314424107 709 GVDYLQGYLIGKPKPLEELRA 729
Cdd:PRK10551 488 GVNFLQGYWISRPLPLEDFVR 508
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
323-462 |
2.10e-19 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 85.76 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 323 RALTDPLTGLPNIRALEDYLE----IHPDAK----VCILRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQKDELLFQL 394
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEqelqRAQRQGspfaLLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2314424107 395 PGSELVLVLLGPE------IAERLQHMVDRLnsnkifWNNTGLDIEFGASWGMVEnGEKLHHTLGQLSWLAEQA 462
Cdd:smart00267 82 GGDEFALLLPETSleeaiaLAERILQQLREP------IIIHGIPLYLTISIGVAA-YPNPGEDAEDLLKRADTA 148
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
601-725 |
1.01e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 76.76 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 601 PQAVVIEITEEQAFSNSGssINNIQQLRDYGFRIAIDDFgTGYANYERLRRLqADIIKIDgcfVKDICTDDMDAMIvqsm 680
Cdd:COG3434 83 PERVVLEILEDVEPDEEL--LEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID---VLALDLEELAELV---- 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2314424107 681 cNLAKTKSLCVVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLE 725
Cdd:COG3434 152 -ARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
324-463 |
1.43e-11 |
|
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: 63.04 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 324 ALTDPLTGLPNIRALEDYLEI--------HPDAKVCILRMDNLEFLSRHYGiimrvH-----CKRTIATSLQPLLQKDEL 390
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQelqralreGSPVAVLLIDLDNFKRINDTYG-----HsvgdeVLQEVAQRLSSSLRRSDL 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2314424107 391 LFQLPGSELVLVLLGP------EIAERLQHMVDRLnsnKIFWNNTGLDIEFGASWGMVEnGEKLHHTLGQLSWLAEQAC 463
Cdd:pfam00990 76 VARLGGDEFAILLPETslegaqELAERIRRLLAKL---KIPHTVSGLPLYVTISIGIAA-YPNDGEDPEDLLKRADTAL 150
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
492-724 |
5.42e-11 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 66.04 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 492 IKHALEAGQFHLYAQPIQKADGSG-YYEILTRM-ESEGEIITPDRFIPLIAQFNLSHRFDMCVMEKLLVWLRDNPathaG 569
Cdd:PRK11059 408 LEQTLVRGGPRLYQQPAVTRDGKVhHRELFCRIrDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWP----E 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 570 ARFSVNLMPLTLMQKEvateicalFERY----------GVAPQaVVIEITEEQAfsnsgssINNIQQLRD-------YGF 632
Cdd:PRK11059 484 ENLSINLSVDSLLSRA--------FQRWlrdtllqcprSQRKR-LIFELAEADV-------CQHISRLRPvlrmlrgLGC 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 633 RIAIDDFG-----TGYanyerLRRLQADIIKIDGCFVKDICTDDMDAMIVQSM---CNLAKTKslcVVAEYVETPAQREM 704
Cdd:PRK11059 548 RLAVDQAGltvvsTSY-----IKELNVELIKLHPSLVRNIHKRTENQLFVRSLvgaCAGTETQ---VFATGVESREEWQT 619
|
250 260
....*....|....*....|
gi 2314424107 705 LLRFGVDYLQGYLIGKPKPL 724
Cdd:PRK11059 620 LQELGVSGGQGDFFAESQPL 639
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
212-463 |
1.01e-10 |
|
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: 63.07 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 212 LYIFVWLMLLGFILVILCGPFESPVIAGYLMPLIFILFTLAISRLTYALISLLWATSALLLLTYNYNFLNGVESGHSLSF 291
Cdd:COG2199 3 LLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 292 ILSVLISFAICLLYMSRIYQRSEWLKRgWQDRALTDPLTGLPNIRALEDYLE-IHPDAK-------VCILRMDNLEFLSR 363
Cdd:COG2199 83 LLLLLLALLLLLLALEDITELRRLEER-LRRLATHDPLTGLPNRRAFEERLErELARARregrplaLLLIDLDHFKRIND 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 364 HYGIIMRVHCKRTIATSLQPLLQKDELLFQLPGSELVLVLLGP------EIAERLQHMVDRLNsnkifWNNTGLDIEFGA 437
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTdleeaeALAERLREALEQLP-----FELEGKELRVTV 236
|
250 260
....*....|....*....|....*....
gi 2314424107 438 SWGMV---ENGEKLHHTLGQlswlAEQAC 463
Cdd:COG2199 237 SIGVAlypEDGDSAEELLRR----ADLAL 261
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
506-727 |
6.91e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 48.07 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 506 QPIQKADGSGY-YEILTRM---ESEGEIITPDRFIpliAQFNLSHRFDMcVMEKL-LVWLRDNPATHAGARFSVNLMPLT 580
Cdd:PRK11596 35 QPIYRTSGRLMaIELLTAVthpSNPSQRLSPERYF---AEITVSHRLDV-VKEQLdLLAQWADFFVRHGLLASVNIDGPT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 581 LMQKEVATEICALFERYgvaPQaVVIEITEEQAFSNSGSsinnIQQLRDYGfRIAIDDFGTGYANYERLRRLQADIIKID 660
Cdd:PRK11596 111 LIALRQQPAILRLIERL---PW-LRFELVEHIRLPKDSP----FASMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2314424107 661 gcfvkdictDDMDAMIVQS-------MCNLAKTKSLC--VVAEYVETPAQREMLLRFGVDYLQGYLIGKPKPLEEL 727
Cdd:PRK11596 182 ---------RELFIMLRQSeegrnlfSQLLHLMNRYCrgVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETL 248
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
323-417 |
1.10e-04 |
|
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: 43.48 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 323 RALTDPLTGLPNIRALEDYLEihPDAKVC----------ILRMDNLEFLSRHYGIIMRVHCKRTIATSLQPLLQKDELLF 392
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLD--SELKRArrfqrsfsvlMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVG 78
|
90 100 110
....*....|....*....|....*....|.
gi 2314424107 393 QLPGSELVLVLLGP------EIAERLQHMVD 417
Cdd:TIGR00254 79 RYGGEEFVVILPGTpledalSKAERLRDAIN 109
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
325-420 |
1.46e-03 |
|
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: 39.85 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2314424107 325 LTDPLTGLPNIRALEDYLE-IHPDAK-------VCILRMDNLEFLSRHYGiimrvHCK-----RTIATSLQPLLQKDELL 391
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLErLLARARrsgrplaLLLIDIDHFKQINDTYG-----HAAgdevlKEVAERLRSSLRESDLV 75
|
90 100 110
....*....|....*....|....*....|....*
gi 2314424107 392 FQLPGSELVLVLLGP------EIAERLQHMVDRLN 420
Cdd:cd01949 76 ARLGGDEFAILLPGTdleeaeALAERLREAIEEPF 110
|
|
| |
