|
Name |
Accession |
Description |
Interval |
E-value |
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
538-776 |
1.67e-75 |
|
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];
Pssm-ID: 441808 [Multi-domain] Cd Length: 316 Bit Score: 247.58 E-value: 1.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 538 IEEYNKGALYHLSIAVGESRLRSDSGIRKSISDWKMEADLNMYRdkVRYHKPVENNENQNLKDLISCLITVEEAKDSYTA 617
Cdd:COG2206 68 LLLLLLLLLSLLLAVALLLAELLLLLAALESLLAELFEELRLGL--LEELKKLVEELDELLPDALLALLAALDAKDPYTY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 618 HHSDRVKAFSEQIARLLGLSEGSVSLITHAAHLHDIGKMGISDNVLGKPGKLTDDEFSIIKQHPVIGAKILMQSNYTHEL 697
Cdd:COG2206 146 GHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPGLSEV 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509286273 698 VQIVLHHHERYDGRGYPEGLKGEDIPIGARIIAIADSVDAMTSKRVYRDALSLDYCRQEIEKNLGVMYDPAIGKVVLDH 776
Cdd:COG2206 226 AEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKV 304
|
|
| FIST |
COG3287 |
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms] ... |
54-376 |
3.87e-64 |
|
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms];
Pssm-ID: 442517 [Multi-domain] Cd Length: 382 Bit Score: 219.44 E-value: 3.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 54 IERVFPDVPWFGNSTSGNIVDCEQTVDiSVSAIIFEKPASKFRVFQYDFSKESVGGIANEIVKEADRN----PWVKAVEI 129
Cdd:COG3287 54 LRAAFPGAPIIGCSTAGEISPGGVLEG-SVVLLAFSFDKFRVGVAVGDGLSDDSREAGRELARRLLAAlgpdPDLRFALL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 130 YHCISPFSTTALCEGL-DALAPDIQVFGGIvCSPDITSPNSCVFSSvGGFSKSGLLVVFYGGaDLHVDSRKISGWKPIGR 208
Cdd:COG3287 133 LSDGLSGNEEELLEGLySALGPDVPIFGGS-AGDDLRFEKTYVFHN-GEVLSDAAVVALLGT-SLPVGVGSSHGWKPTGP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 209 NFHVTRSEGNILYELGGVPAYEVYNKYLNIKnDKNFFYNALEFP-MLYEHNGVSIVRAAGASNPDGSLTMSSDIDEGSIV 287
Cdd:COG3287 210 EMVVTKAEGRVVYEIDGEPAAEVYARYLGDD-AEELPASFLLFPlGVRIGGGEYLVRSPLAVEEDGSLTFAGDIPEGSVL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 288 RLSYGEPQLIVQRIKEESEKCVKF---APEVQHIFSCAARKAFWSQRePTYEISPFKGL--ASSTGFFSHGEFLREKGHL 362
Cdd:COG3287 289 RLMEGNPDDLIEAAERAAEAALARlggKPEAALLFDCVGRRLVLGQR-VEEELEAVSELlgAPVAGFYTYGEIGPFGGGG 367
|
330
....*....|....*
gi 2509286273 363 NQ-HNITLVFASMRE 376
Cdd:COG3287 368 NQhHNQTLTGVAFGE 382
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
387-583 |
3.59e-31 |
|
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: 123.55 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 387 VEDIQEGMSTRLPLAARMATFIRETSFELEQInSKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKISQEDADASGTWT 466
Cdd:COG2199 69 LLLLALLLLSLVLELLLLLLALLLLLLALEDI-TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 467 MVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIGGDEFAVV-THAPLDSLFVLYSNLKKCIEEYN--- 542
Cdd:COG2199 148 LLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLlPGTDLEEAEALAERLREALEQLPfel 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2509286273 543 KGALYHLSIAVGESRLRSDSgirKSISDWKMEADLNMYRDK 583
Cdd:COG2199 228 EGKELRVTVSIGVALYPEDG---DSAEELLRRADLALYRAK 265
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
434-583 |
4.12e-26 |
|
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: 104.95 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 434 TTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIGG 513
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509286273 514 DEFAVV-THAPLDSLFVLYSNLKKCIEEYN--KGALYHLSIAVGESRLRSDSgirKSISDWKMEADLNMYRDK 583
Cdd:cd01949 81 DEFAILlPGTDLEEAEALAERLREAIEEPFfiDGQEIRVTASIGIATYPEDG---EDAEELLRRADEALYRAK 150
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
433-585 |
6.46e-24 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 98.86 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 433 ATTDSLTGLENRLAFDEILrKISQEDADASGTWTMVLM-DVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRI 511
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEEL-EQELQRAQRQGSPFALLLiDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509286273 512 GGDEFAVV-THAPLDSLFVLYSNLKKCIEEY--NKGALYHLSIAVGESRLRSDsgiRKSISDWKMEADLNMYRDKVR 585
Cdd:smart00267 82 GGDEFALLlPETSLEEAIALAERILQQLREPiiIHGIPLYLTISIGVAAYPNP---GEDAEDLLKRADTALYQAKKA 155
|
|
| FIST_C |
pfam10442 |
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal ... |
228-357 |
1.04e-23 |
|
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 463094 Cd Length: 135 Bit Score: 97.38 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 228 AYEVYNKYLNIKNDKNFFYNALEFPM-LYEHNGVSIVRAAGASNP-DGSLTMSSDIDEGSIVRLSYGEPQLIVQRIKEES 305
Cdd:pfam10442 1 ALEVYKEYLGGEEDEELPASALEFPLgVVVGGGDYLVRSPLGVDPeDGSLAFAGDVPEGSVVQLMLRDADDLIEAAERAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2509286273 306 EKCVKFAPEVQHIFSCAARKAFWSQREpTYEISPFK----GLASSTGFFSHGEFLR 357
Cdd:pfam10442 81 EAALANPPEGALLFSCAGRGLGLGERF-DEELEAIRealgDGVPLAGFYTYGEIGP 135
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
615-751 |
2.20e-22 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 93.94 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 615 YTAHHSDRVKAFSEQIARLLGLSEGSVSLITHAAHLHDIGKMGISDnvlgkpgKLTDDEFSIIKQHPVIGAKILMQS--- 691
Cdd:cd00077 2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPD-------AITEEESELEKDHAIVGAEILRELlle 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509286273 692 ---NYTHELVQIVL-HHHERYDGRGYPEGLKGEDIPIGARIIAIADSVDAMTS----KRVYRDALSLD 751
Cdd:cd00077 75 eviKLIDELILAVDaSHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRdsreKRRRIAEEDLE 142
|
|
| HD_5 |
pfam13487 |
HD domain; HD domains are metal dependent phosphohydrolases. |
667-729 |
3.99e-20 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 433249 [Multi-domain] Cd Length: 64 Bit Score: 84.57 E-value: 3.99e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509286273 667 GKLTDDEFSIIKQHPVIGAKILMQSNYT-HELVQIVLHHHERYDGRGYPEGLKGEDIPIGARII 729
Cdd:pfam13487 1 GTLTPEEREIINRHPEHTARLLSTLPRLpKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
|
|
| FIST |
smart00897 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
30-225 |
5.13e-20 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 214894 Cd Length: 196 Bit Score: 88.91 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 30 NPLMCFQIHTAILDPEKLKliwDVIERVFPD-VPWFGNSTSGNIvdCEQTV-----DISVSAIIFEKPASKFRVFQYDFS 103
Cdd:smart00897 1 KPLLVLFFSSPAYDAEALL---AALRERFPGaTPIVGCSTAGEI--TTGVVqefedEPALSVMLFELPLVSFDVFSLVDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 104 KES-VGGIANEIVKEADRNPWVKAVEIYHCISPFSTTALCEGLDALAPDIQVFGGIVCSPDITSPNSCVFSSvGGFSKSG 182
Cdd:smart00897 76 LPDlVAGLLLAALLAAIDPRNTFALLLLDDLSSSNEEELLEGLDEALPEGIPIGGGSAGDNLRFQETYVFTN-GRVHSGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2509286273 183 LLVVFYGgaDLHVDSRKISGWKPIGRNFHVTRSEGNILYELGG 225
Cdd:smart00897 155 VVVAFGG--GLRFGTGVTQGWRPIGPPFVVTKAEGNVVYELDG 195
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
433-583 |
5.58e-20 |
|
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: 87.31 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 433 ATTDSLTGLENRLAFDEILrKISQEDADASGTWTMVLM-DVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRI 511
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQL-EQELQRALREGSPVAVLLiDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509286273 512 GGDEFAVV-THAPLDSLFVLYSNLKKCIEE-----YNKGALYHLSIAVGESRLRSDsgiRKSISDWKMEADLNMYRDK 583
Cdd:pfam00990 80 GGDEFAILlPETSLEGAQELAERIRRLLAKlkiphTVSGLPLYVTISIGIAAYPND---GEDPEDLLKRADTALYQAK 154
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
433-583 |
4.50e-19 |
|
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: 85.08 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 433 ATTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIG 512
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2509286273 513 GDEFAVVT-HAPLDSLFVLYSNLKKCIE----EYNKGALYHLSIAVGESRLRSDSgirKSISDWKMEADLNMYRDK 583
Cdd:TIGR00254 82 GEEFVVILpGTPLEDALSKAERLRDAINskpiEVAGSETLTVTVSIGVACYPGHG---LTLEELLKRADEALYQAK 154
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
613-745 |
1.43e-17 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).
Pssm-ID: 214679 [Multi-domain] Cd Length: 124 Bit Score: 79.65 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 613 DSYTAHHSDRVKAFSEQIARLLGLSEGSVSLIthAAHLHDIGKMGISDNVLGKpgkltddeFSIIKQHPVIGAKILMQSN 692
Cdd:smart00471 2 DYHVFEHSLRVAQLAAALAEELGLLDIELLLL--AALLHDIGKPGTPDSFLVK--------TSVLEDHHFIGAEILLEEE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2509286273 693 YTHELV----QIVLHHHERYDGrgypegLKGEDIPIGARIIAIADSVDAMTSKRVYR 745
Cdd:smart00471 72 EPRILEeilrTAILSHHERPDG------LRGEPITLEARIVKVADRLDALRADRRYR 122
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
414-519 |
3.70e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 75.43 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 414 ELEQINSKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKIsQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVA 493
Cdd:PRK09966 229 EMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTL-MNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIE 307
|
90 100
....*....|....*....|....*.
gi 2509286273 494 AGEAIKNAYGAAGNCFRIGGDEFAVV 519
Cdd:PRK09966 308 IAKRLAEFGGLRHKAYRLGGDEFAMV 333
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
435-519 |
4.09e-11 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 66.14 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 435 TDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNA-----YGaagncF 509
Cdd:NF040885 343 SDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASirksdYG-----I 417
|
90
....*....|
gi 2509286273 510 RIGGDEFAVV 519
Cdd:NF040885 418 RLGGDEFCII 427
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
618-706 |
4.81e-07 |
|
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.
Pssm-ID: 272994 [Multi-domain] Cd Length: 80 Bit Score: 48.10 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 618 HHSDRVKAFSEQIARLLGLSegsVSLITHAAHLHDIGKMgisdnvlgkpgklTDDEFSIIKQHPVIGAKILMQSNYTHEL 697
Cdd:TIGR00277 7 QHSLEVAKLAEALARELGLD---VELARRGALLHDIGKP-------------ITREGVIFESHVVVGAEIARKYGEPLEV 70
|
....*....
gi 2509286273 698 VQIVLHHHE 706
Cdd:TIGR00277 71 IDIIAEHHG 79
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
619-737 |
1.62e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 619 HSDRVKAFSEQIARLLGLSegsVSLITHAAHLHDIGKmgisdnvlgkpgkltDDEFSIIKQHPVIGAKILMQSNYTHELV 698
Cdd:PRK12705 327 HSLEVAHLAGIIAAEIGLD---PALAKRAGLLHDIGK---------------SIDRESDGNHVEIGAELARKFNEPDEVI 388
|
90 100 110
....*....|....*....|....*....|....*....
gi 2509286273 699 QIVLHHHErydgrgypeglKGEDIPIGARIIAIADSVDA 737
Cdd:PRK12705 389 NAIASHHN-----------KVNPETVYSVLVQIADALSA 416
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
538-776 |
1.67e-75 |
|
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];
Pssm-ID: 441808 [Multi-domain] Cd Length: 316 Bit Score: 247.58 E-value: 1.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 538 IEEYNKGALYHLSIAVGESRLRSDSGIRKSISDWKMEADLNMYRdkVRYHKPVENNENQNLKDLISCLITVEEAKDSYTA 617
Cdd:COG2206 68 LLLLLLLLLSLLLAVALLLAELLLLLAALESLLAELFEELRLGL--LEELKKLVEELDELLPDALLALLAALDAKDPYTY 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 618 HHSDRVKAFSEQIARLLGLSEGSVSLITHAAHLHDIGKMGISDNVLGKPGKLTDDEFSIIKQHPVIGAKILMQSNYTHEL 697
Cdd:COG2206 146 GHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILKKLPGLSEV 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2509286273 698 VQIVLHHHERYDGRGYPEGLKGEDIPIGARIIAIADSVDAMTSKRVYRDALSLDYCRQEIEKNLGVMYDPAIGKVVLDH 776
Cdd:COG2206 226 AEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKV 304
|
|
| FIST |
COG3287 |
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms] ... |
54-376 |
3.87e-64 |
|
FIST domain protein MJ1623, contains FIST_N and FIST_C domains [Signal transduction mechanisms];
Pssm-ID: 442517 [Multi-domain] Cd Length: 382 Bit Score: 219.44 E-value: 3.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 54 IERVFPDVPWFGNSTSGNIVDCEQTVDiSVSAIIFEKPASKFRVFQYDFSKESVGGIANEIVKEADRN----PWVKAVEI 129
Cdd:COG3287 54 LRAAFPGAPIIGCSTAGEISPGGVLEG-SVVLLAFSFDKFRVGVAVGDGLSDDSREAGRELARRLLAAlgpdPDLRFALL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 130 YHCISPFSTTALCEGL-DALAPDIQVFGGIvCSPDITSPNSCVFSSvGGFSKSGLLVVFYGGaDLHVDSRKISGWKPIGR 208
Cdd:COG3287 133 LSDGLSGNEEELLEGLySALGPDVPIFGGS-AGDDLRFEKTYVFHN-GEVLSDAAVVALLGT-SLPVGVGSSHGWKPTGP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 209 NFHVTRSEGNILYELGGVPAYEVYNKYLNIKnDKNFFYNALEFP-MLYEHNGVSIVRAAGASNPDGSLTMSSDIDEGSIV 287
Cdd:COG3287 210 EMVVTKAEGRVVYEIDGEPAAEVYARYLGDD-AEELPASFLLFPlGVRIGGGEYLVRSPLAVEEDGSLTFAGDIPEGSVL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 288 RLSYGEPQLIVQRIKEESEKCVKF---APEVQHIFSCAARKAFWSQRePTYEISPFKGL--ASSTGFFSHGEFLREKGHL 362
Cdd:COG3287 289 RLMEGNPDDLIEAAERAAEAALARlggKPEAALLFDCVGRRLVLGQR-VEEELEAVSELlgAPVAGFYTYGEIGPFGGGG 367
|
330
....*....|....*
gi 2509286273 363 NQ-HNITLVFASMRE 376
Cdd:COG3287 368 NQhHNQTLTGVAFGE 382
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
387-583 |
3.59e-31 |
|
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: 123.55 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 387 VEDIQEGMSTRLPLAARMATFIRETSFELEQInSKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKISQEDADASGTWT 466
Cdd:COG2199 69 LLLLALLLLSLVLELLLLLLALLLLLLALEDI-TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 467 MVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIGGDEFAVV-THAPLDSLFVLYSNLKKCIEEYN--- 542
Cdd:COG2199 148 LLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLlPGTDLEEAEALAERLREALEQLPfel 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2509286273 543 KGALYHLSIAVGESRLRSDSgirKSISDWKMEADLNMYRDK 583
Cdd:COG2199 228 EGKELRVTVSIGVALYPEDG---DSAEELLRRADLALYRAK 265
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
434-583 |
4.12e-26 |
|
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: 104.95 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 434 TTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIGG 513
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509286273 514 DEFAVV-THAPLDSLFVLYSNLKKCIEEYN--KGALYHLSIAVGESRLRSDSgirKSISDWKMEADLNMYRDK 583
Cdd:cd01949 81 DEFAILlPGTDLEEAEALAERLREAIEEPFfiDGQEIRVTASIGIATYPEDG---EDAEELLRRADEALYRAK 150
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
433-585 |
6.46e-24 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 98.86 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 433 ATTDSLTGLENRLAFDEILrKISQEDADASGTWTMVLM-DVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRI 511
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEEL-EQELQRAQRQGSPFALLLiDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509286273 512 GGDEFAVV-THAPLDSLFVLYSNLKKCIEEY--NKGALYHLSIAVGESRLRSDsgiRKSISDWKMEADLNMYRDKVR 585
Cdd:smart00267 82 GGDEFALLlPETSLEEAIALAERILQQLREPiiIHGIPLYLTISIGVAAYPNP---GEDAEDLLKRADTALYQAKKA 155
|
|
| FIST_C |
pfam10442 |
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal ... |
228-357 |
1.04e-23 |
|
FIST C domain; The FIST C domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 463094 Cd Length: 135 Bit Score: 97.38 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 228 AYEVYNKYLNIKNDKNFFYNALEFPM-LYEHNGVSIVRAAGASNP-DGSLTMSSDIDEGSIVRLSYGEPQLIVQRIKEES 305
Cdd:pfam10442 1 ALEVYKEYLGGEEDEELPASALEFPLgVVVGGGDYLVRSPLGVDPeDGSLAFAGDVPEGSVVQLMLRDADDLIEAAERAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2509286273 306 EKCVKFAPEVQHIFSCAARKAFWSQREpTYEISPFK----GLASSTGFFSHGEFLR 357
Cdd:pfam10442 81 EAALANPPEGALLFSCAGRGLGLGERF-DEELEAIRealgDGVPLAGFYTYGEIGP 135
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
615-751 |
2.20e-22 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 93.94 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 615 YTAHHSDRVKAFSEQIARLLGLSEGSVSLITHAAHLHDIGKMGISDnvlgkpgKLTDDEFSIIKQHPVIGAKILMQS--- 691
Cdd:cd00077 2 HRFEHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPD-------AITEEESELEKDHAIVGAEILRELlle 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509286273 692 ---NYTHELVQIVL-HHHERYDGRGYPEGLKGEDIPIGARIIAIADSVDAMTS----KRVYRDALSLD 751
Cdd:cd00077 75 eviKLIDELILAVDaSHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRdsreKRRRIAEEDLE 142
|
|
| HD_5 |
pfam13487 |
HD domain; HD domains are metal dependent phosphohydrolases. |
667-729 |
3.99e-20 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 433249 [Multi-domain] Cd Length: 64 Bit Score: 84.57 E-value: 3.99e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2509286273 667 GKLTDDEFSIIKQHPVIGAKILMQSNYT-HELVQIVLHHHERYDGRGYPEGLKGEDIPIGARII 729
Cdd:pfam13487 1 GTLTPEEREIINRHPEHTARLLSTLPRLpKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
|
|
| FIST |
smart00897 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
30-225 |
5.13e-20 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 214894 Cd Length: 196 Bit Score: 88.91 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 30 NPLMCFQIHTAILDPEKLKliwDVIERVFPD-VPWFGNSTSGNIvdCEQTV-----DISVSAIIFEKPASKFRVFQYDFS 103
Cdd:smart00897 1 KPLLVLFFSSPAYDAEALL---AALRERFPGaTPIVGCSTAGEI--TTGVVqefedEPALSVMLFELPLVSFDVFSLVDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 104 KES-VGGIANEIVKEADRNPWVKAVEIYHCISPFSTTALCEGLDALAPDIQVFGGIVCSPDITSPNSCVFSSvGGFSKSG 182
Cdd:smart00897 76 LPDlVAGLLLAALLAAIDPRNTFALLLLDDLSSSNEEELLEGLDEALPEGIPIGGGSAGDNLRFQETYVFTN-GRVHSGA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2509286273 183 LLVVFYGgaDLHVDSRKISGWKPIGRNFHVTRSEGNILYELGG 225
Cdd:smart00897 155 VVVAFGG--GLRFGTGVTQGWRPIGPPFVVTKAEGNVVYELDG 195
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
433-583 |
5.58e-20 |
|
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: 87.31 E-value: 5.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 433 ATTDSLTGLENRLAFDEILrKISQEDADASGTWTMVLM-DVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRI 511
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQL-EQELQRALREGSPVAVLLiDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2509286273 512 GGDEFAVV-THAPLDSLFVLYSNLKKCIEE-----YNKGALYHLSIAVGESRLRSDsgiRKSISDWKMEADLNMYRDK 583
Cdd:pfam00990 80 GGDEFAILlPETSLEGAQELAERIRRLLAKlkiphTVSGLPLYVTISIGIAAYPND---GEDPEDLLKRADTALYQAK 154
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
392-519 |
7.33e-20 |
|
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: 94.46 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 392 EGMSTRLPLAARMATFIRETSFELEQINSKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMD 471
Cdd:COG5001 210 LRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFID 289
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2509286273 472 VNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIGGDEFAVV 519
Cdd:COG5001 290 LDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVL 337
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
433-583 |
4.50e-19 |
|
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: 85.08 E-value: 4.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 433 ATTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIG 512
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2509286273 513 GDEFAVVT-HAPLDSLFVLYSNLKKCIE----EYNKGALYHLSIAVGESRLRSDSgirKSISDWKMEADLNMYRDK 583
Cdd:TIGR00254 82 GEEFVVILpGTPLEDALSKAERLRDAINskpiEVAGSETLTVTVSIGVACYPGHG---LTLEELLKRADEALYQAK 154
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
621-743 |
5.19e-19 |
|
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];
Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 86.76 E-value: 5.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 621 DRVKAFSEQiARLLGLSEGSVSLITHAAHLHDIGKMGISDNVLGKPGKLTDDEFSIIKQHPVIGAKILMQSNYTHELVQI 700
Cdd:COG3437 118 ARVRNALEL-RRLQRELDDLVLYLKLAAPLHDIGKIGIPDAILLKPGKLTPEEWEITHAHIGAEILSGSLLPLLQLAAEI 196
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2509286273 701 vlhhHERYDGRGypeglkgedipIGARiiaiadsvDAMTSKRV 743
Cdd:COG3437 197 ----HERWDGSG-----------LSAR--------DALTSKKL 216
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
613-745 |
1.43e-17 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).
Pssm-ID: 214679 [Multi-domain] Cd Length: 124 Bit Score: 79.65 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 613 DSYTAHHSDRVKAFSEQIARLLGLSEGSVSLIthAAHLHDIGKMGISDNVLGKpgkltddeFSIIKQHPVIGAKILMQSN 692
Cdd:smart00471 2 DYHVFEHSLRVAQLAAALAEELGLLDIELLLL--AALLHDIGKPGTPDSFLVK--------TSVLEDHHFIGAEILLEEE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2509286273 693 YTHELV----QIVLHHHERYDGrgypegLKGEDIPIGARIIAIADSVDAMTSKRVYR 745
Cdd:smart00471 72 EPRILEeilrTAILSHHERPDG------LRGEPITLEARIVKVADRLDALRADRRYR 122
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
616-738 |
8.82e-17 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 76.89 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 616 TAHHSDRVKAFSEQIARLLGLSEGSVSLIthAAHLHDIGKMGISDNvlgkpgkltDDEFSIIKQHPVIGAKILMQSNY-- 693
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGELDRELLLL--AALLHDIGKGPFGDE---------KPEFEIFLGHAVVGAEILRELEKrl 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2509286273 694 -THELVQIVLHHHERYDGRGYPEglkgeDIPIGARIIAIADSVDAM 738
Cdd:pfam01966 70 gLEDVLKLILEHHESWEGAGYPE-----EISLEARIVKLADRLDAL 110
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
414-519 |
3.70e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 75.43 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 414 ELEQINSKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKIsQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVA 493
Cdd:PRK09966 229 EMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFRSGINTL-MNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIE 307
|
90 100
....*....|....*....|....*.
gi 2509286273 494 AGEAIKNAYGAAGNCFRIGGDEFAVV 519
Cdd:PRK09966 308 IAKRLAEFGGLRHKAYRLGGDEFAMV 333
|
|
| FIST |
pfam08495 |
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal ... |
140-225 |
3.73e-13 |
|
FIST N domain; The FIST N domain is a novel sensory domain, which is present in signal transduction proteins from Bacteria, Archaea and Eukarya. Chromosomal proximity of FIST-encoding genes to those coding for proteins involved in amino acid metabolism and transport suggest that FIST domains bind small ligands, such as amino acids.
Pssm-ID: 462495 Cd Length: 126 Bit Score: 66.84 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 140 ALCEGLDALA--PDIQVFGGiVCSPDITSPNSCVFSSvGGFSKSGLLVVFYGGADLHVDSRKISGWKPIGRNFHVTRSEG 217
Cdd:pfam08495 40 ELLEGLDSALgyPGVPVVGG-LAGDGLRFERTWVLFN-GEVYSDGAVAVALYGDALKVGVGVSQGWRPIGPPFVVTKADG 117
|
....*...
gi 2509286273 218 NILYELGG 225
Cdd:pfam08495 118 NRVYELDG 125
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
424-519 |
5.13e-12 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 69.27 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 424 VMNEHLQDVATTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNAYG 503
Cdd:PRK15426 389 VLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLR 468
|
90
....*....|....*.
gi 2509286273 504 AAGNCFRIGGDEFAVV 519
Cdd:PRK15426 469 AQDVAGRVGGEEFCVV 484
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
423-527 |
2.21e-11 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 67.40 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 423 RVMNEHLQDVATTDSLTGLENRLAFDEILRK-ISQEDADASGtwtMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNA 501
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIQELIDHaINAADNNQVG---IVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSC 303
|
90 100
....*....|....*....|....*..
gi 2509286273 502 YGAAGNCFRIGGDEFAV-VTHAPLDSL 527
Cdd:PRK10060 304 LEEDQTLARLGGDEFLVlASHTSQAAL 330
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
435-519 |
4.09e-11 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 66.14 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 435 TDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIKNA-----YGaagncF 509
Cdd:NF040885 343 SDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASirksdYG-----I 417
|
90
....*....|
gi 2509286273 510 RIGGDEFAVV 519
Cdd:NF040885 418 RLGGDEFCII 427
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
420-518 |
5.25e-10 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 63.15 E-value: 5.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 420 SKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKISQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVAAGEAIK 499
Cdd:PRK09776 652 TESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLML 731
|
90
....*....|....*....
gi 2509286273 500 NAYGAAGNCFRIGGDEFAV 518
Cdd:PRK09776 732 SMLRSSDVLARLGGDEFGL 750
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
400-583 |
9.76e-10 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 61.46 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 400 LAARMATFIREtsfelEQINSKLRVMNEHLQDVATTDSLTGLENRLAFDEILRKISqEDADASGTWTMVLM-DVNGLKYA 478
Cdd:PRK09581 264 LLARVRTQIRR-----KRYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLI-ERANERGKPLSLMMiDIDHFKKV 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 479 NDTFGHQAGDALIVAAGEAIKNAYGAAGNCFRIGGDEFAVV-THAPLDSLFVLYSNLKKCIEEYN----KGALYH---LS 550
Cdd:PRK09581 338 NDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVmPDTDIEDAIAVAERIRRKIAEEPfiisDGKERLnvtVS 417
|
170 180 190
....*....|....*....|....*....|...
gi 2509286273 551 IAVGESRLRSDsgirkSISDWKMEADLNMYRDK 583
Cdd:PRK09581 418 IGVAELRPSGD-----TIEALIKRADKALYEAK 445
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
417-583 |
2.42e-09 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 59.84 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 417 QINSKLRVMNEHLQDVATTDSLTGLENRLAFDEILR----KISQEDADAsgtwTMVLMDVNGLKYANDTFGHQAGDALIV 492
Cdd:PRK10245 189 QTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRnefdNCRRHHRDA----TLLIIDIDHFKSINDTWGHDVGDEAIV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 493 AAGEAIKNAYGAAGNCFRIGGDEFAVV-THAPLDSLFVLYSNLKkciEEYNKGAL-----YHLSIAVGESRLRSDSGIRK 566
Cdd:PRK10245 265 ALTRQLQITLRGSDVIGRFGGDEFAVImSGTPAESAITAMSRVH---EGLNTLRLpnapqVTLRISVGVAPLNPQMSHYR 341
|
170
....*....|....*..
gi 2509286273 567 sisDWKMEADLNMYRDK 583
Cdd:PRK10245 342 ---EWLKSADLALYKAK 355
|
|
| FIST |
COG4398 |
Small ligand-binding sensory domain FIST [Signal transduction mechanisms]; |
135-231 |
8.21e-09 |
|
Small ligand-binding sensory domain FIST [Signal transduction mechanisms];
Pssm-ID: 443524 [Multi-domain] Cd Length: 386 Bit Score: 58.30 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 135 PFS--TTALCEGLDALAPDIQVFGGIVCSPdiTSPNSCVFSSVGGFSkSGLL-VVFygGADLHVDSRKISGWKPIGRNFH 211
Cdd:COG4398 129 PFSpdLPDLLEGLAEAYPGGPLVGGLASGR--GAPGQNLFAAGEVYE-GGLVgVAF--SGNVTLETRVSQGCRPIGPPHQ 203
|
90 100
....*....|....*....|
gi 2509286273 212 VTRSEGNILYELGGVPAYEV 231
Cdd:COG4398 204 VTEAERNVILELDGRPALDV 223
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
608-738 |
3.83e-08 |
|
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];
Pssm-ID: 441028 [Multi-domain] Cd Length: 191 Bit Score: 54.13 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 608 VEEAKDSYTAH---HSDRVKAFSEQIARLLGLSEGSVSLithAAHLHDIGKMgisdnvlgkpgkltdDEFSIIKQHPVIG 684
Cdd:COG1418 8 VKYLRTSYGQHdlqHSLRVAKLAGLIAAEEGADVEVAKR---AALLHDIGKA---------------KDHEVEGSHAEIG 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2509286273 685 A----KILMQSNYTHELVQIVLH----HHerYDGRGYPEGLkgEdipigARIIAIADSVDAM 738
Cdd:COG1418 70 AelarKYLESLGFPEEEIEAVVHaieaHS--FSGGIEPESL--E-----AKIVQDADRLDAL 122
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
415-516 |
3.04e-07 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 52.76 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 415 LEQINSKLRVMNEHLQDVATT-DSLTGLENRLAFDEILRkiSQEDADASGTWTMVLMDVNGLKYANDTFGHQAGDALIVA 493
Cdd:PRK09894 110 LLSFTAALTDYKIYLLTIRSNmDVLTGLPGRRVLDESFD--HQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRT 187
|
90 100
....*....|....*....|...
gi 2509286273 494 AGEAIKNAYGAAGNCFRIGGDEF 516
Cdd:PRK09894 188 LATYLASWTRDYETVYRYGGEEF 210
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
618-706 |
4.81e-07 |
|
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.
Pssm-ID: 272994 [Multi-domain] Cd Length: 80 Bit Score: 48.10 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 618 HHSDRVKAFSEQIARLLGLSegsVSLITHAAHLHDIGKMgisdnvlgkpgklTDDEFSIIKQHPVIGAKILMQSNYTHEL 697
Cdd:TIGR00277 7 QHSLEVAKLAEALARELGLD---VELARRGALLHDIGKP-------------ITREGVIFESHVVVGAEIARKYGEPLEV 70
|
....*....
gi 2509286273 698 VQIVLHHHE 706
Cdd:TIGR00277 71 IDIIAEHHG 79
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
412-522 |
2.04e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 51.31 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 412 SFELEQINSKLRVmnEHLqdvATTDSLTGLENRLAFDEILRKISQEDADAsgtwTMVLMDVNGLKYANDTFGHQAGDALI 491
Cdd:PRK11359 360 ALALEQEKSRQHI--EQL---IQFDPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQAL 430
|
90 100 110
....*....|....*....|....*....|.
gi 2509286273 492 VAAGEAIKNAYGAAGNCFRIGGDEFAVVTHA 522
Cdd:PRK11359 431 LEVVNRFREKLKPDQYLCRIEGTQFVLVSLE 461
|
|
| HDOD |
pfam08668 |
HDOD domain; |
619-706 |
2.21e-04 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 42.98 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 619 HSDRVKAFSEQIARLLGLSEGSVSLIthAAHLHDIGKM-----------GISDNVLGKPGKLTDDEFSIIKQ-HPVIGAK 686
Cdd:pfam08668 98 HSLACALAARLLARRLGLDDPEEAFL--AGLLHDIGKLillsllpdkyeELLEKAAEEGISLLEAERELLGTdHAEVGAA 175
|
90 100
....*....|....*....|
gi 2509286273 687 ILMQSNYTHELVQIVLHHHE 706
Cdd:pfam08668 176 LLERWNLPEELVEAIAYHHN 195
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
402-500 |
3.16e-04 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 44.08 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 402 ARMATFIRetSFeleqinsklrvmnehlqdvATTDSLTGLENRLAFDEILRKISqEDADASGTWTMVLM-DVNGLKYAND 480
Cdd:PRK11059 218 SRFDTFIR--SN-------------------AFQDAKTGLGNRLFFDNQLATLL-EDQEMVGAHGVVMLiRLPDFDLLQE 275
|
90 100
....*....|....*....|
gi 2509286273 481 TFGHQAGDALIVAAGEAIKN 500
Cdd:PRK11059 276 EWGESQVEELLFELINLLST 295
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
619-737 |
1.62e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 619 HSDRVKAFSEQIARLLGLSegsVSLITHAAHLHDIGKmgisdnvlgkpgkltDDEFSIIKQHPVIGAKILMQSNYTHELV 698
Cdd:PRK12705 327 HSLEVAHLAGIIAAEIGLD---PALAKRAGLLHDIGK---------------SIDRESDGNHVEIGAELARKFNEPDEVI 388
|
90 100 110
....*....|....*....|....*....|....*....
gi 2509286273 699 QIVLHHHErydgrgypeglKGEDIPIGARIIAIADSVDA 737
Cdd:PRK12705 389 NAIASHHN-----------KVNPETVYSVLVQIADALSA 416
|
|
| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
619-707 |
8.91e-03 |
|
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I
Pssm-ID: 193608 [Multi-domain] Cd Length: 200 Bit Score: 38.41 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509286273 619 HSDRVKAF----SEQIARLLGLSEG-SVSLITHAAHLHDIGKmgISD---NVLGKPGKLTDDEFSIIKQHPVIGAKILMQ 690
Cdd:cd09641 12 HLLDVAAWdaelAEEFARKLGLELGlSRELLALAGLLHDLGK--ATPafqKYLRGGKEALREGKRKEVRHSLLGALLLYE 89
|
90 100
....*....|....*....|....*
gi 2509286273 691 SNYTHE--------LVQIVLHHHER 707
Cdd:cd09641 90 LLKELGldeelallLAYAIAGHHGG 114
|
|
| |
