|
Name |
Accession |
Description |
Interval |
E-value |
| LapD_MoxY_N |
pfam16448 |
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and ... |
23-146 |
3.65e-49 |
|
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and MoxY receptor proteins.
Pssm-ID: 465117 Cd Length: 124 Bit Score: 167.42 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 23 VFFQFTETKSFMKDQMGSDLANVSTSLSLMLKPHLETGDTVMVETLVNVIFEGGFYKRVELTWLADNKKQVWENDVTIEG 102
Cdd:pfam16448 1 FVVSVNNARSYLEQQLQSHAQDTATSLGLSLSPYLENEDPVTAETMINAIFDSGYYRSIRLTDPDGKVLVERQNPVLIEG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 505277618 103 VPQWFINLDLFETQYTETTINSGWLQLATLRIDSNPGIGYQELW 146
Cdd:pfam16448 81 VPQWFIRLVPLEPPPGEAEISSGWLQLGTLEVESHPGYAYQELW 124
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
142-644 |
1.87e-47 |
|
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: 176.13 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 142 YQELWRIMSDTLIVLSILFLISLVVLQIRLKRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLKL 221
Cdd:COG2200 63 ALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 222 VFNALDNEVDTLKKDKLCDPVSQLPNRLYLTGQLNSWLDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQAT 301
Cdd:COG2200 143 LLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 302 LPQLNETVIARISNTEFAFLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLSQADNALQ 381
Cdd:COG2200 223 LARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 382 HAI--NNNKVSHWFHLDMQQDMSREQWRALLTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINN-KIERAGVFMPY 458
Cdd:COG2200 303 AAAagGGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 459 IARLGLGSELDENLLEcIALDKLLMRQKE----PIAINLSRESLVSLEFHQWLKHYLARST-NPGQLHFELPEAGITANI 533
Cdd:COG2200 383 AERSGLIVELDRWVLE-RALRQLARWPERgldlRLSVNLSARSLLDPDFLERLLELLAEYGlPPERLVLEITESALLEDL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 534 SVCRELCDVITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLscydSQEQEHNQQNFELCRALVNIARGLNIKVIL 613
Cdd:COG2200 462 EAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSF----VRDIARDPRDQAIVRAIVALAHRLGLKVVA 537
|
490 500 510
....*....|....*....|....*....|..
gi 505277618 614 TGIENNDHLVAIKSLRADGYQGY-ISSPVDVR 644
Cdd:COG2200 538 EGVETEEQLEALRELGCDYAQGYlFGRPLPLE 569
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
407-636 |
6.51e-44 |
|
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: 157.09 E-value: 6.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 407 RALLTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGLGSELDENLLE--CIALDKLLM 483
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGgLISPARFLPLAEELGLIAELDRWVLEqaLADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 484 RQKEPIAINLSRESLVSLEFHQWLKHYLARS-TNPGQLHFELPEAGITANISVCRELCDVITQGGAQFGIDNCGRQMGSL 562
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAgPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505277618 563 SYLQQLKPYYIKLDLSLscydSQEQEHNQQNFELCRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY 636
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSL----IADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGY 230
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
410-643 |
1.01e-34 |
|
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: 131.90 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 410 LTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGLGSELDENLLE--CIALDKLLMRQK 486
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGgLISPAEFIPLAEETGLIVELGRWVLEeaCRQLARWQAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 487 E-PIAINLSRESLVSLEFHQWLKHYLARST-NPGQLHFELPEAGITANISVCRELCDVITQGGAQFGIDNCGRQMGSLSY 564
Cdd:cd01948 83 DlRLSVNLSARQLRDPDFLDRLLELLAETGlPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 565 LQQLKPYYIKLDLSLscydSQEQEHNQQNFELCRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY-ISSPVDV 643
Cdd:cd01948 163 LKRLPVDYLKIDRSF----VRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYlFSRPLPA 238
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
240-643 |
3.47e-31 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 129.21 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLDTPDF----GGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPQLNETVIARISN 315
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMvgahGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 316 TEFAFLILQ---ADKEQITvylQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLSQADNALQHAI---NNNkv 389
Cdd:PRK11059 311 SDFAVLLPHrslKEADSLA---SQLLKAVDALPPPKMLDRDDFLHIGICAYRSGQSTEQVMEEAEMALRSAQlqgGNG-- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 390 shWFHLD--MQQDMSRE--QWRALLTTAMKDKEFIFQWQPIHhTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGL 464
Cdd:PRK11059 386 --WFVYDkaQLPEKGRGsvRWRTLLEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGeLLSAELFMPMVQQLGL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 465 GSELDENLLECIaLDKLLMRQKEPIAINLSRESLVSLEFHQWLKHYL---ARSTNPgQLHFELPEAGITANISVCRELCD 541
Cdd:PRK11059 463 SEQYDRQVIERV-LPLLRYWPEENLSINLSVDSLLSRAFQRWLRDTLlqcPRSQRK-RLIFELAEADVCQHISRLRPVLR 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 542 VITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLscYDSQEQEHNQQNFelCRALVNIARGLNIKVILTGIENNDH 621
Cdd:PRK11059 541 MLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSL--VRNIHKRTENQLF--VRSLVGACAGTETQVFATGVESREE 616
|
410 420
....*....|....*....|...
gi 505277618 622 LVAIKSLRADGYQG-YISSPVDV 643
Cdd:PRK11059 617 WQTLQELGVSGGQGdFFAESQPL 639
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
409-641 |
4.40e-24 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 101.52 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 409 LLTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGLGSELDENLLE--CIALDKLLMRQ 485
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGgIISPDEFIPLAEETGLIVPLGRWVLEqaCQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 486 KEP--IAINLSRESLVSLEFHQWLKHYLAR-STNPGQLHFELPEA----GITANISVCRELCDVitqgGAQFGIDNCGRQ 558
Cdd:smart00052 83 PPPllISINLSARQLISPDLVPRVLELLEEtGLPPQRLELEITESvlldDDESAVATLQRLREL----GVRIALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 559 MGSLSYLQQLKPYYIKLDLSLsCYDSQeqeHNQQNFELCRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY-I 637
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSF-VRDLQ---TDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYlF 234
|
....
gi 505277618 638 SSPV 641
Cdd:smart00052 235 SRPL 238
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
240-383 |
2.88e-11 |
|
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: 62.35 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLD-----TPDFGGLL--LANFEWIEDihnRFGFQVRDETIRLLAKNLQATLPQlnETVIAR 312
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKrarrfQRSFSVLMidIDNFKKIND---TLGHDVGDEVLREVARILQSSVRG--SDVVGR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505277618 313 ISNTEFAFLILQADKEQITVYLQALIRVINQ-EILNAGCEANS-RFSIGVVE-RQDPVNRVEFLSQADNALQHA 383
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSETLTvTVSIGVACyPGHGLTLEELLKRADEALYQA 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LapD_MoxY_N |
pfam16448 |
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and ... |
23-146 |
3.65e-49 |
|
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and MoxY receptor proteins.
Pssm-ID: 465117 Cd Length: 124 Bit Score: 167.42 E-value: 3.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 23 VFFQFTETKSFMKDQMGSDLANVSTSLSLMLKPHLETGDTVMVETLVNVIFEGGFYKRVELTWLADNKKQVWENDVTIEG 102
Cdd:pfam16448 1 FVVSVNNARSYLEQQLQSHAQDTATSLGLSLSPYLENEDPVTAETMINAIFDSGYYRSIRLTDPDGKVLVERQNPVLIEG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 505277618 103 VPQWFINLDLFETQYTETTINSGWLQLATLRIDSNPGIGYQELW 146
Cdd:pfam16448 81 VPQWFIRLVPLEPPPGEAEISSGWLQLGTLEVESHPGYAYQELW 124
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
142-644 |
1.87e-47 |
|
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: 176.13 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 142 YQELWRIMSDTLIVLSILFLISLVVLQIRLKRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLKL 221
Cdd:COG2200 63 ALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 222 VFNALDNEVDTLKKDKLCDPVSQLPNRLYLTGQLNSWLDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQAT 301
Cdd:COG2200 143 LLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 302 LPQLNETVIARISNTEFAFLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLSQADNALQ 381
Cdd:COG2200 223 LARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 382 HAI--NNNKVSHWFHLDMQQDMSREQWRALLTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINN-KIERAGVFMPY 458
Cdd:COG2200 303 AAAagGGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 459 IARLGLGSELDENLLEcIALDKLLMRQKE----PIAINLSRESLVSLEFHQWLKHYLARST-NPGQLHFELPEAGITANI 533
Cdd:COG2200 383 AERSGLIVELDRWVLE-RALRQLARWPERgldlRLSVNLSARSLLDPDFLERLLELLAEYGlPPERLVLEITESALLEDL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 534 SVCRELCDVITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLscydSQEQEHNQQNFELCRALVNIARGLNIKVIL 613
Cdd:COG2200 462 EAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSF----VRDIARDPRDQAIVRAIVALAHRLGLKVVA 537
|
490 500 510
....*....|....*....|....*....|..
gi 505277618 614 TGIENNDHLVAIKSLRADGYQGY-ISSPVDVR 644
Cdd:COG2200 538 EGVETEEQLEALRELGCDYAQGYlFGRPLPLE 569
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
407-636 |
6.51e-44 |
|
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: 157.09 E-value: 6.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 407 RALLTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGLGSELDENLLE--CIALDKLLM 483
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGgLISPARFLPLAEELGLIAELDRWVLEqaLADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 484 RQKEPIAINLSRESLVSLEFHQWLKHYLARS-TNPGQLHFELPEAGITANISVCRELCDVITQGGAQFGIDNCGRQMGSL 562
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAgPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505277618 563 SYLQQLKPYYIKLDLSLscydSQEQEHNQQNFELCRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY 636
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSL----IADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGY 230
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
410-643 |
1.01e-34 |
|
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: 131.90 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 410 LTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGLGSELDENLLE--CIALDKLLMRQK 486
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGgLISPAEFIPLAEETGLIVELGRWVLEeaCRQLARWQAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 487 E-PIAINLSRESLVSLEFHQWLKHYLARST-NPGQLHFELPEAGITANISVCRELCDVITQGGAQFGIDNCGRQMGSLSY 564
Cdd:cd01948 83 DlRLSVNLSARQLRDPDFLDRLLELLAETGlPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 565 LQQLKPYYIKLDLSLscydSQEQEHNQQNFELCRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY-ISSPVDV 643
Cdd:cd01948 163 LKRLPVDYLKIDRSF----VRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYlFSRPLPA 238
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
240-643 |
3.00e-33 |
|
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: 135.67 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLDTPDFGGLLLA-------NFEWIEDihnRFGFQVRDETIRLLAKNLQATLPQlnETVIAR 312
Cdd:COG5001 254 DPLTGLPNRRLFLDRLEQALARARRSGRRLAllfidldRFKEIND---TLGHAAGDELLREVARRLRACLRE--GDTVAR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 313 ISNTEFAFLILQ-ADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVER-QDPVNRVEFLSQADNALQHAINN--NK 388
Cdd:COG5001 329 LGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYpDDGADAEELLRNADLAMYRAKAAgrNR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 389 VsHWFHLDMQQDM-SREQWRALLTTAMKDKEFIFQWQPIHHTLTGGVMHREiyCRLKINNKiER----AGVFMPYIARLG 463
Cdd:COG5001 409 Y-RFFDPEMDERArERLELEADLRRALERGELELHYQPQVDLATGRIVGAE--ALLRWQHP-ERglvsPAEFIPLAEETG 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 464 LGSELDENLLE--CIALDKLLMRQKEP--IAINLSRESLVSLEFHQWLKHYLARS-TNPGQLHFELPEAGITANISVCRE 538
Cdd:COG5001 485 LIVPLGEWVLReaCRQLAAWQDAGLPDlrVAVNLSARQLRDPDLVDRVRRALAETgLPPSRLELEITESALLEDPEEALE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 539 LCDVITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLScydsQEQEHNQQNFELCRALVNIARGLNIKVILTGIEN 618
Cdd:COG5001 565 TLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFV----RDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVET 640
|
410 420
....*....|....*....|....*.
gi 505277618 619 NDHLVAIKSLRADGYQGY-ISSPVDV 643
Cdd:COG5001 641 EEQLEFLRELGCDYAQGYlFSRPLPA 666
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
240-643 |
3.47e-31 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 129.21 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLDTPDF----GGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPQLNETVIARISN 315
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMvgahGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 316 TEFAFLILQ---ADKEQITvylQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLSQADNALQHAI---NNNkv 389
Cdd:PRK11059 311 SDFAVLLPHrslKEADSLA---SQLLKAVDALPPPKMLDRDDFLHIGICAYRSGQSTEQVMEEAEMALRSAQlqgGNG-- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 390 shWFHLD--MQQDMSRE--QWRALLTTAMKDKEFIFQWQPIHhTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGL 464
Cdd:PRK11059 386 --WFVYDkaQLPEKGRGsvRWRTLLEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGeLLSAELFMPMVQQLGL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 465 GSELDENLLECIaLDKLLMRQKEPIAINLSRESLVSLEFHQWLKHYL---ARSTNPgQLHFELPEAGITANISVCRELCD 541
Cdd:PRK11059 463 SEQYDRQVIERV-LPLLRYWPEENLSINLSVDSLLSRAFQRWLRDTLlqcPRSQRK-RLIFELAEADVCQHISRLRPVLR 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 542 VITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLscYDSQEQEHNQQNFelCRALVNIARGLNIKVILTGIENNDH 621
Cdd:PRK11059 541 MLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSL--VRNIHKRTENQLF--VRSLVGACAGTETQVFATGVESREE 616
|
410 420
....*....|....*....|...
gi 505277618 622 LVAIKSLRADGYQG-YISSPVDV 643
Cdd:PRK11059 617 WQTLQELGVSGGQGdFFAESQPL 639
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
409-641 |
4.40e-24 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 101.52 E-value: 4.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 409 LLTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINNK-IERAGVFMPYIARLGLGSELDENLLE--CIALDKLLMRQ 485
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGgIISPDEFIPLAEETGLIVPLGRWVLEqaCQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 486 KEP--IAINLSRESLVSLEFHQWLKHYLAR-STNPGQLHFELPEA----GITANISVCRELCDVitqgGAQFGIDNCGRQ 558
Cdd:smart00052 83 PPPllISINLSARQLISPDLVPRVLELLEEtGLPPQRLELEITESvlldDDESAVATLQRLREL----GVRIALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 559 MGSLSYLQQLKPYYIKLDLSLsCYDSQeqeHNQQNFELCRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY-I 637
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSF-VRDLQ---TDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYlF 234
|
....
gi 505277618 638 SSPV 641
Cdd:smart00052 235 SRPL 238
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
240-383 |
2.87e-17 |
|
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: 79.14 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLDTPDFGGLLLA-------NFEWIEDihnRFGFQVRDETIRLLAKNLQATLPQlnETVIAR 312
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARRSGRPLAlllididHFKQIND---TYGHAAGDEVLKEVAERLRSSLRE--SDLVAR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505277618 313 ISNTEFAFLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVE-RQDPVNRVEFLSQADNALQHA 383
Cdd:cd01949 78 LGGDEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATyPEDGEDAEELLRRADEALYRA 149
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
122-383 |
5.19e-17 |
|
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: 81.56 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 122 INSGWLQLATLRIDSNPGIGYQELWRIMSDTLIVLSILFLISLVVLQIRLKRILKPLHEVAVHAkDIAERKFHPDMALPS 201
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLL-LALGLLLLALLLLSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 202 TTELSEVVGAINSMSSQLKLVfNALDNEVDTLKKDKLCDPVSQLPNRLYLTGQLNSWLD----TPDFGGLLLANFEWIED 277
Cdd:COG2199 80 VLELLLLLLALLLLLLALEDI-TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArarrEGRPLALLLIDLDHFKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 278 IHNRFGFQVRDETIRLLAKNLQATLPQlnETVIARISNTEFAFLILQADKEQITVYLQALIRVINQEILNA-GCEANSRF 356
Cdd:COG2199 159 INDTYGHAAGDEVLKEVARRLRASLRE--SDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELeGKELRVTV 236
|
250 260
....*....|....*....|....*...
gi 505277618 357 SIGVVE-RQDPVNRVEFLSQADNALQHA 383
Cdd:COG2199 237 SIGVALyPEDGDSAEELLRRADLALYRA 264
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
240-394 |
8.64e-17 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 78.06 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLN-SW---LDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPQlnETVIARISN 315
Cdd:smart00267 6 DPLTGLPNRRYFEEELEqELqraQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRP--GDLLARLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 316 TEFAFLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVE-FLSQADNALQHAINNNKVSHWFH 394
Cdd:smart00267 84 DEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEdLLKRADTALYQAKKAGRNQVAVY 163
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
146-618 |
1.10e-11 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 67.82 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 146 WR----IMSdTLIVLSILFLISLVVLQIRL-----KRILKPLHEVAVHAKDI-AERKFHPDMALPSTTELSEVVGAINSM 215
Cdd:PRK13561 135 FRmykfVMS-ALSTLVTIYLLLSLILTVAIswcinRLIVHPLRNIARELNDIpPQELVGHQLALPRLHQDDEIGMLVRSY 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 216 SSQLKlvfnALDNEVDTLKKDKLCDPVSQLPNRLYLTGQLNSWLDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLA 295
Cdd:PRK13561 214 NLNQQ----LLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 296 KNLQATLPQlnETVIARISNTEFAFLILQADKEQITVYL-QALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLS 374
Cdd:PRK13561 290 EKLKSVLSP--RMVLAQISGYDFAIIANGVKEPWHAITLgQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 375 QADNALQHAINNNKVSHWFHLDMQqdMSREQWRalLT------TAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLKINN- 447
Cdd:PRK13561 368 RAISAAFTARRKGKNQIQFFDPQQ--MEAAQKR--LTeesdilNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDg 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 448 KIERAGVFMPYIARLGLGSELDENLLE--CialdKLLMRQKE-----PIAINLSRESLVSLEFHQWLKHYLAR-STNPGQ 519
Cdd:PRK13561 444 SWDLPEGLIDRIESCGLMVTVGHWVLEesC----RLLAAWQErgimlPLSVNLSALQLMHPNMVADMLELLTRyRIQPGT 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 520 LHFELPEAG----ITANISVCRELCDVitqgGAQFGIDNCGRQMGSLSYLQQLKPYYI---KLDLSLSC---YDSQeqeh 589
Cdd:PRK13561 520 LILEVTESRriddPHAAVAILRPLRNA----GVRVALDDFGMGYAGLRQLQHMKSLPIdvlKIDKMFVDglpEDDS---- 591
|
490 500
....*....|....*....|....*....
gi 505277618 590 nqqnfeLCRALVNIARGLNIKVILTGIEN 618
Cdd:PRK13561 592 ------MVAAIIMLAQSLNLQVIAEGVET 614
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
240-383 |
2.88e-11 |
|
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: 62.35 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLD-----TPDFGGLL--LANFEWIEDihnRFGFQVRDETIRLLAKNLQATLPQlnETVIAR 312
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKrarrfQRSFSVLMidIDNFKKIND---TLGHDVGDEVLREVARILQSSVRG--SDVVGR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505277618 313 ISNTEFAFLILQADKEQITVYLQALIRVINQ-EILNAGCEANS-RFSIGVVE-RQDPVNRVEFLSQADNALQHA 383
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDALSKAERLRDAINSkPIEVAGSETLTvTVSIGVACyPGHGLTLEELLKRADEALYQA 153
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
240-637 |
1.04e-10 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 64.70 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLDTPDFG--GLL---LANFEWIEDihnRFGFQVRDetiRLLAKNLQATLPQLNE-TVIARI 313
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNqvGIVyldLDNFKKVND---AYGHMFGD---QLLQDVSLAILSCLEEdQTLARL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 314 SNTEFAFLILQADkeqitvylQALIRVINQEILNagcEANSRFSIGVVE------------RQDPVNRVEFLSQADNALQ 381
Cdd:PRK10060 314 GGDEFLVLASHTS--------QAALEAMASRILT---RLRLPFRIGLIEvytgcsigialaPEHGDDSESLIRSADTAMY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 382 HAINNNKVSHW-FHLDMQQDMSREQWralLTT----AMKDKEFIFQWQPIHhTLTGGVMHREIYCRLkinNKIERAGV-- 454
Cdd:PRK10060 383 TAKEGGRGQFCvFSPEMNQRVFEYLW---LDTnlrkALENDQLVIHYQPKI-TWRGEVRSLEALVRW---QSPERGLIpp 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 455 --FMPYIARLGLGSELDENLLECIALDKLLMRQKE---PIAINLSRESLVSLEFHQWLKHYLAR-STNPGQLHFELPEAG 528
Cdd:PRK10060 456 leFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGinlRVAVNVSARQLADQTIFTALKQALQElNFEYCPIDVELTESC 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 529 ITANISVCRELCDVITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLsCYDSQEQEHNQQnfeLCRALVNIARGLN 608
Cdd:PRK10060 536 LIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSF-VRDIHKQPVSQS---LVRAIVAVAQALN 611
|
410 420
....*....|....*....|....*....
gi 505277618 609 IKVILTGIENNDHLVAIKSLRADGYQGYI 637
Cdd:PRK10060 612 LQVIAEGVETAKEDAFLTKNGVNERQGFL 640
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
240-639 |
1.56e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 64.41 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPQlnETVIARISNTEFA 319
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKP--DQYLCRIEGTQFV 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 320 FLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGvVERQDPVNRVEFLSQADNALQHaINNNKVSHW--FHLDM 397
Cdd:PRK11359 457 LVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIG-ISYDVGKNRDYLLSTAHNAMDY-IRKNGGNGWqfFSPAM 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 398 QQdMSREqwRALLTTAMK----DKEFIFQWQPIHHTLTGGVMHREIYCRLkinnKIERAGVFMP--YIArlgLGSELDEn 471
Cdd:PRK11359 535 NE-MVKE--RLVLGAALKeaisNNQLKLVYQPQIFAETGELYGIEALARW----HDPLHGHVPPsrFIP---LAEEIGE- 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 472 lLECI-------ALDKLLMRQKEPIAINLSRESLVSLEFHQ-WLKHYLARSTN----PG-QLHFELPEAGITANISVCRE 538
Cdd:PRK11359 604 -IENIgrwviaeACRQLAEWRSQNIHIPALSVNLSALHFRSnQLPNQVSDAMQawgiDGhQLTVEITESMMMEHDTEIFK 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 539 LCDVITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLscYDSQEQEHNQQNfeLCRALVNIARGLNIKVILTGIEN 618
Cdd:PRK11359 683 RIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSF--VDRCLTEKRILA--LLEAITSIGQSLNLTVVAEGVET 758
|
410 420
....*....|....*....|.
gi 505277618 619 NDHLVAIKSLRADGYQGYISS 639
Cdd:PRK11359 759 KEQFEMLRKIHCRVIQGYFFS 779
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
240-383 |
1.91e-09 |
|
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: 56.88 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 240 DPVSQLPNRLYLTGQLNSWLD----TPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPqlNETVIARISN 315
Cdd:pfam00990 4 DPLTGLPNRRYFEEQLEQELQralrEGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLR--RSDLVARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505277618 316 TEFAFLILQADKE---QITVYLQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFL-SQADNALQHA 383
Cdd:pfam00990 82 DEFAILLPETSLEgaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLlKRADTALYQA 153
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
309-636 |
5.13e-09 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 59.69 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 309 VIARISNTEFAFLILQADKEQItvylqaliRVINQEILNAGCEAnsRF-----------SIGVVERQDPVNRV-EFLSQA 376
Cdd:PRK09776 739 VLARLGGDEFGLLLPDCNVESA--------RFIATRIISAINDY--HFpwegrvyrvgaSAGITLIDANNHQAsEVMSQA 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 377 DNALQHAINN--NKVS---------HWFHLDMQQDmsrEQWRALLttamKDKEFIFQWQPIHHTLTGGVMHREIYCRL-K 444
Cdd:PRK09776 809 DIACYAAKNAgrGRVTvyepqqaaaHSEHRALSLA---EQWRMIK----ENQLMMLAHGVASPRIPEARNHWLISLRLwD 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 445 INNKIERAGVFMPYIARLGLGSELDENLLEcialdKLLMRQKEPIA-------INLSRESLVSLEFHQWLKHYLARSTNP 517
Cdd:PRK09776 882 PEGEIIDEGAFRPAAEDPALMHALDRRVIH-----EFFRQAAKAVAskglsiaLPLSVAGLSSPTLLPFLLEQLENSPLP 956
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 518 GQ-LHFELPEAGITANISVCRELCDVITQGGAQFGIDNCGRQMGSLSYLQQLKPYYIKLDLSLsCYDSQEqehNQQNFEL 596
Cdd:PRK09776 957 PRlLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGEL-VANLHG---NLMDEML 1032
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 505277618 597 CRALVNIARGLNIKVILTGIENNDHLVAIKSLRADGYQGY 636
Cdd:PRK09776 1033 ISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGY 1072
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
152-420 |
1.72e-05 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 47.57 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 152 TLIVLSILFLISLVVLQIRLKRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLKLVFNALDNEVD 231
Cdd:COG3850 120 ALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 232 TLKKDKLCDPVSQLPNRLYLTGQLN----SWLDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPQLNE 307
Cdd:COG3850 200 LEAELELLALLDELLLLAALLLLLAlllaLLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 308 TVIARISNTEFAFLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLSQADNALQHAINNN 387
Cdd:COG3850 280 LLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAG 359
|
250 260 270
....*....|....*....|....*....|...
gi 505277618 388 KVSHWFHLDMQQDMSREQWRALLTTAMKDKEFI 420
Cdd:COG3850 360 AALAAAAAAAGLARALAQAGADAAEALGLLAEA 392
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
152-227 |
3.56e-05 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 46.49 E-value: 3.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505277618 152 TLIVLSILFLISLVVLQIRL-KRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLKLVFNALD 227
Cdd:COG5000 10 LLLLIALLLLLLALWLALLLaRRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQREELE 86
|
|
| HAMP |
pfam00672 |
HAMP domain; |
172-220 |
5.88e-05 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 41.07 E-value: 5.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505277618 172 KRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLK 220
Cdd:pfam00672 4 RRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLR 52
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
172-220 |
1.79e-04 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 39.54 E-value: 1.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505277618 172 KRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLK 220
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
410-643 |
2.88e-04 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 43.83 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 410 LTTAMKDKEFIFQWQPIHHTLTGGVMHREIYCRLK--INNKIErAGVFMPYIARLGLGSELDENLLECIALDKLLMRQKE 487
Cdd:PRK10551 268 ILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRhpTAGEIP-PDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 488 P----IAINLSRESLVSLEFHQWLKHYLAR-STNPGQLHFELPEAGITANiSVCRELCDVITQGGAQFGIDNCGRQMGSL 562
Cdd:PRK10551 347 PvgakLGINISPAHLHSDSFKADVQRLLASlPADHFQIVLEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFGTGHSAL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 563 SYLQQLKPYYIKLDlslscydsqeqehnqqnfelcRALVN-----------------IARGLNIKVILTGIENNDHLvai 625
Cdd:PRK10551 426 IYLERFTLDYLKID---------------------RGFIQaigtetvtspvldavltLAKRLNMLTVAEGVETPEQA--- 481
|
250 260
....*....|....*....|..
gi 505277618 626 KSLRADG---YQGY-ISSPVDV 643
Cdd:PRK10551 482 RWLRERGvnfLQGYwISRPLPL 503
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
152-389 |
1.20e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 42.02 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 152 TLIVLSILFLISLVVLQIRL-KRILKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQLKLVFNALDNEV 230
Cdd:COG2770 213 LLLLLALLALLLALLLALLLaRRITRPLRRLAEAARRIAAGDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505277618 231 DTLKKDKLCDPVSQLPNRLYLTGQLNSWLDTPDFGGLLLANFEWIEDIHNRFGFQVRDETIRLLAKNLQATLPQLNETVI 310
Cdd:COG2770 293 ELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAE 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505277618 311 ARISNTEFAFLILQADKEQITVYLQALIRVINQEILNAGCEANSRFSIGVVERQDPVNRVEFLSQADNALQHAINNNKV 389
Cdd:COG2770 373 LLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAA 451
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
175-219 |
4.26e-03 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 35.50 E-value: 4.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 505277618 175 LKPLHEVAVHAKDIAERKFHPDMALPSTTELSEVVGAINSMSSQL 219
Cdd:cd06225 1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
|
|
| |
