|
Name |
Accession |
Description |
Interval |
E-value |
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
545-726 |
1.77e-77 |
|
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: 251.43 E-value: 1.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 545 SMRGKTIGAIISTLHEKNKREEEHSHRVSRLCQDMGHALGLTESETEELKTIGLLHDIGKIAIEENILNKSEELTEDEWQ 624
Cdd:COG2206 124 ELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 625 EIKRHSEIGYRILNTVNDMLEISEYVLYHHERWDGKGYPKGLKGEEIPLQSRIITIIDAYDAMTSQRSYRSALPEESAIE 704
Cdd:COG2206 204 IIKKHPEYGYEILKKLPGLSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALE 283
|
170 180
....*....|....*....|..
gi 500500343 705 ELKINAGTQFDPDLVRIFIEKV 726
Cdd:COG2206 284 ELRKGAGTQFDPELVEAFIKVL 305
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
379-513 |
3.97e-47 |
|
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: 168.23 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 379 RDIRERKEMENKLEYLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSE 455
Cdd:COG2199 98 EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElarARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVAR 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500500343 456 IIKRGCRYNDIIARLGGDEFVILLPKTDIYET----EQIVKNINALALKETVSAVNISISFG 513
Cdd:COG2199 178 RLRASLRESDLVARLGGDEFAVLLPGTDLEEAealaERLREALEQLPFELEGKELRVTVSIG 239
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
396-513 |
2.08e-39 |
|
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: 142.70 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 396 YHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARLGG 472
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLlarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500500343 473 DEFVILLPKTDIYET----EQIVKNINALALKETVSaVNISISFG 513
Cdd:cd01949 81 DEFAILLPGTDLEEAealaERLREAIEEPFFIDGQE-IRVTASIG 124
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
395-539 |
2.85e-35 |
|
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: 131.22 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 395 SYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARLG 471
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQElqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 472 GDEFVILLPKTDIYETEQIVKNINAL--ALKETVSA----VNISISFGYGTKKKEEEKIEEILKKAEDYMYKKK 539
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLlaKLKIPHTVsglpLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAK 154
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
393-539 |
2.14e-34 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 128.52 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 393 YLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIAR 469
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQElqrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500500343 470 LGGDEFVILLPKTDIYETEQIVKNI-NALALKETV--SAVNISISFGYGTKKKEEEKIEEILKKAEDYMYKKK 539
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERIlQQLREPIIIhgIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAK 153
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
394-540 |
7.89e-31 |
|
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: 118.59 E-value: 7.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 394 LSYHDQLTGLYNRRFFE---NELKRLDVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARL 470
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEemlDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500500343 471 GGDEFVILLPKTDIYET----EQIVKNINALALKETVSA-VNISISFGYGTKKKEEEKIEEILKKAEDYMYKKKL 540
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAlskaERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
131-391 |
2.67e-28 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 114.35 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIInykllDSNASYERLTGLKKEDILGKTLYEIF-PNMEKNLIEK 209
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIIT----DLDGRIL-----YVNPAFERLTGYSAEELLGKTLRDLLpPEDDDEFLEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 210 IQRVAITGQSVHYQRYIKEKD--KYYEAIVYRP------KKLQFAAILTDITERKFAEKALKTSEYNFRNIFESSSDPIL 281
Cdd:COG2202 72 LRAALAGGGVWRGELRNRRKDgsLFWVELSISPvrdedgEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 282 IT-LDNKVIDCNLAMIELLGYDSKSSILHKNPVQFSPEKQPNGESSKEKAIQvykitMKNKKYKFEWWFKRVDGTLLPVE 360
Cdd:COG2202 152 VLdLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLE-----GGRESYELELRLKDGDGRWVWVE 226
|
250 260 270
....*....|....*....|....*....|..
gi 500500343 361 VMMTTILHNGKKV-FHSLCRDIRERKEMENKL 391
Cdd:COG2202 227 ASAVPLRDGGEVIgVLGIVRDITERKRAEEAL 258
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
384-539 |
1.21e-26 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 113.84 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 384 RKEMENKLEyLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRG 460
Cdd:PRK09581 282 RNNLEQSIE-MAVTDGLTGLHNRRYFDMHLKNLierANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNN 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 461 CRYNDIIARLGGDEFVILLPKTDIYETEQIVKNINAL------ALKETVSAVNISISFGYGTKKKEEEKIEEILKKAEDY 534
Cdd:PRK09581 361 IRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKiaeepfIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKA 440
|
....*
gi 500500343 535 MYKKK 539
Cdd:PRK09581 441 LYEAK 445
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
567-706 |
4.66e-22 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 92.79 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLTESETEELKTIGLLHDIGKIAIEENIlnkseelTEDEWQEIKRHSEIGYRILNTVNDMLEI 646
Cdd:cd00077 5 EHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAI-------TEEESELEKDHAIVGAEILRELLLEEVI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500500343 647 SEY-------VLYHHERWDGKGYPKGLKGEEIPLQSRIITIIDAYDAMTS-QRSYRSALPEESAIEEL 706
Cdd:cd00077 78 KLIdelilavDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRdSREKRRRIAEEDLEELL 145
|
|
| HD_5 |
pfam13487 |
HD domain; HD domains are metal dependent phosphohydrolases. |
616-678 |
4.39e-20 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 433249 [Multi-domain] Cd Length: 64 Bit Score: 84.19 E-value: 4.39e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 616 EELTEDEWQEIKRHSEIGYRILNTVNDML-EISEYVLYHHERWDGKGYPKGLKGEEIPLQSRII 678
Cdd:pfam13487 1 GTLTPEEREIINRHPEHTARLLSTLPRLPkEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
567-694 |
4.56e-16 |
|
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: 75.03 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLTESEteELKTIGLLHDIGKIAIEENILNKSEELtedewqeiKRHSEIGYRIL--NTVNDML 644
Cdd:smart00471 7 EHSLRVAQLAAALAEELGLLDIE--LLLLAALLHDIGKPGTPDSFLVKTSVL--------EDHHFIGAEILleEEEPRIL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 500500343 645 E--ISEYVLYHHERWDgkgypkGLKGEEIPLQSRIITIIDAYDAMTSQRSYR 694
Cdd:smart00471 77 EeiLRTAILSHHERPD------GLRGEPITLEARIVKVADRLDALRADRRYR 122
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
265-391 |
2.03e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 56.15 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 265 SEYNFRNIFESSSDPI-LITLDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEkqPNGESSKEKAIQVykITMKNKKY 343
Cdd:TIGR00229 1 SEERYRAIFESSPDAIiVIDLEGNILYVNPAFEEIFGY-SAEELIGRNVLELIPE--EDREEVRERIERR--LEGEPEPV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 500500343 344 KFEWWFKRVDGTLLPVEVMMTTILHNG-KKVFHSLCRDIRERKEMENKL 391
Cdd:TIGR00229 76 SEERRVRRKDGSEIWVEVSVSPIRTNGgELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
269-381 |
1.31e-08 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 53.19 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 269 FRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEKQPngesSKEKAIQVYKITMKNKKYKFEW 347
Cdd:pfam00989 3 LRAILESLPDGIFVVdEDGRILYVNAAAEELLGL-SREEVIGKSLLDLIPEEDD----AEVAELLRQALLQGEESRGFEV 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 500500343 348 WFKRVDGTLLPVEVMMTTILHNGKKVFHSLC--RDI 381
Cdd:pfam00989 78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGvlRDI 113
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
141-213 |
2.56e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 39.69 E-value: 2.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 141 ERYKALVSEMQQGLVLFqgsdNEEGKIinyklLDSNASYERLTGLKKEDILGKTLYEIF-PNMEKNLIEKIQRV 213
Cdd:smart00091 1 ERLRAILESLPDGIFVL----DLDGRI-----LYANPAAEELLGYSPEELIGKSLLELIhPEDRERVQEALQRL 65
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
123-391 |
1.28e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 42.35 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 123 KIQYDQTIESEKKLSKSEERYKALVSEMQQglVLFQGSDNEEGKIINYKLLDSNASYERLTGLKKEDILGKTLYEIFPNM 202
Cdd:PRK13560 179 DDQVDGFAEDITERKRAEERIDEALHFLQQ--LLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 203 EKNLIEKIQRVAITGQSVH-YQRYIKEKDKYYEAIVYRPKKLQF----------AAILTDITERKFAEKALKTSEYNFRN 271
Cdd:PRK13560 257 PADDYQEADAAKFDADGSQiIEAEFQNKDGRTRPVDVIFNHAEFddkenhcaglVGAITDISGRRAAERELLEKEDMLRA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 272 IFESSSDPILIT-LDNKVIDCNLAMIELLGYDSKSSILHKNPVQFSPEKQ------------PNGESSKEKAIQVYKITM 338
Cdd:PRK13560 337 IIEAAPIAAIGLdADGNICFVNNNAAERMLGWSAAEVMGKPLPGMDPELNeefwcgdfqewyPDGRPMAFDACPMAKTIK 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 500500343 339 KNKKYK-FEWWFKRVDGTLLPVEVMMTTILHNGKKVFHSLCR--DIRERKEMENKL 391
Cdd:PRK13560 417 GGKIFDgQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALlvDITERKQVEEQL 472
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
57-157 |
2.23e-03 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 40.70 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 57 LIIISTYKGW---LYVIITAPILYLIIRSILKKVYLAEKKLNKSYEELLAV-NEKLESY--VKRLTNSKEELKiQYDQTI 130
Cdd:pfam00664 132 GIIVMFYYGWkltLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVaEESLSGIrtVKAFGREEYELE-KYDKAL 210
|
90 100
....*....|....*....|....*..
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLF 157
Cdd:pfam00664 211 EEALKAGIKKAVANGLSFGITQFIGYL 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
80-152 |
4.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500500343 80 IRSILKKVYLAEKKLNKSYEELLAVNEKLESYVKRLTNSKEELKIQYDQTIESEKKLSKSEERYKALVSEMQQ 152
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
276-381 |
6.69e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 36.84 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 276 SSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEkqpngESSKEKAIQVYKITMKNKKYKFEWWFKRVDG 354
Cdd:cd00130 1 LPDGVIVLdLDGRILYANPAAEQLLGY-SPEELIGKSLLDLIHP-----EDREELRERLENLLSGGEPVTLEVRLRRKDG 74
|
90 100
....*....|....*....|....*....
gi 500500343 355 TLLPVEVMMTTILHNGKKV--FHSLCRDI 381
Cdd:cd00130 75 SVIWVLVSLTPIRDEGGEVigLLGVVRDI 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HDGYP |
COG2206 |
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ... |
545-726 |
1.77e-77 |
|
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: 251.43 E-value: 1.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 545 SMRGKTIGAIISTLHEKNKREEEHSHRVSRLCQDMGHALGLTESETEELKTIGLLHDIGKIAIEENILNKSEELTEDEWQ 624
Cdd:COG2206 124 ELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARELGLSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 625 EIKRHSEIGYRILNTVNDMLEISEYVLYHHERWDGKGYPKGLKGEEIPLQSRIITIIDAYDAMTSQRSYRSALPEESAIE 704
Cdd:COG2206 204 IIKKHPEYGYEILKKLPGLSEVAEIVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALE 283
|
170 180
....*....|....*....|..
gi 500500343 705 ELKINAGTQFDPDLVRIFIEKV 726
Cdd:COG2206 284 ELRKGAGTQFDPELVEAFIKVL 305
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
379-513 |
3.97e-47 |
|
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: 168.23 E-value: 3.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 379 RDIRERKEMENKLEYLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSE 455
Cdd:COG2199 98 EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERElarARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVAR 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500500343 456 IIKRGCRYNDIIARLGGDEFVILLPKTDIYET----EQIVKNINALALKETVSAVNISISFG 513
Cdd:COG2199 178 RLRASLRESDLVARLGGDEFAVLLPGTDLEEAealaERLREALEQLPFELEGKELRVTVSIG 239
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
396-513 |
2.08e-39 |
|
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: 142.70 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 396 YHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARLGG 472
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLlarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 500500343 473 DEFVILLPKTDIYET----EQIVKNINALALKETVSaVNISISFG 513
Cdd:cd01949 81 DEFAILLPGTDLEEAealaERLREAIEEPFFIDGQE-IRVTASIG 124
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
379-513 |
2.54e-36 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 145.69 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 379 RDIRERKEMENKLEYLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSE 455
Cdd:COG5001 235 RLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQAlarARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVAR 314
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500500343 456 IIKRGCRYNDIIARLGGDEFVILLP-KTDIYETEQIVKNINAlALKETVS----AVNISISFG 513
Cdd:COG5001 315 RLRACLREGDTVARLGGDEFAVLLPdLDDPEDAEAVAERILA-ALAEPFEldghELYVSASIG 376
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
395-539 |
2.85e-35 |
|
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: 131.22 E-value: 2.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 395 SYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARLG 471
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQElqrALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 472 GDEFVILLPKTDIYETEQIVKNINAL--ALKETVSA----VNISISFGYGTKKKEEEKIEEILKKAEDYMYKKK 539
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLlaKLKIPHTVsglpLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAK 154
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
393-539 |
2.14e-34 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 128.52 E-value: 2.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 393 YLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIAR 469
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQElqrAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500500343 470 LGGDEFVILLPKTDIYETEQIVKNI-NALALKETV--SAVNISISFGYGTKKKEEEKIEEILKKAEDYMYKKK 539
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERIlQQLREPIIIhgIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAK 153
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
394-540 |
7.89e-31 |
|
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: 118.59 E-value: 7.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 394 LSYHDQLTGLYNRRFFE---NELKRLDVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARL 470
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEemlDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500500343 471 GGDEFVILLPKTDIYET----EQIVKNINALALKETVSA-VNISISFGYGTKKKEEEKIEEILKKAEDYMYKKKL 540
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAlskaERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
131-391 |
2.67e-28 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 114.35 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIInykllDSNASYERLTGLKKEDILGKTLYEIF-PNMEKNLIEK 209
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIIT----DLDGRIL-----YVNPAFERLTGYSAEELLGKTLRDLLpPEDDDEFLEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 210 IQRVAITGQSVHYQRYIKEKD--KYYEAIVYRP------KKLQFAAILTDITERKFAEKALKTSEYNFRNIFESSSDPIL 281
Cdd:COG2202 72 LRAALAGGGVWRGELRNRRKDgsLFWVELSISPvrdedgEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 282 IT-LDNKVIDCNLAMIELLGYDSKSSILHKNPVQFSPEKQPNGESSKEKAIQvykitMKNKKYKFEWWFKRVDGTLLPVE 360
Cdd:COG2202 152 VLdLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLE-----GGRESYELELRLKDGDGRWVWVE 226
|
250 260 270
....*....|....*....|....*....|..
gi 500500343 361 VMMTTILHNGKKV-FHSLCRDIRERKEMENKL 391
Cdd:COG2202 227 ASAVPLRDGGEVIgVLGIVRDITERKRAEEAL 258
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
384-539 |
1.21e-26 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 113.84 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 384 RKEMENKLEyLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRG 460
Cdd:PRK09581 282 RNNLEQSIE-MAVTDGLTGLHNRRYFDMHLKNLierANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNN 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 461 CRYNDIIARLGGDEFVILLPKTDIYETEQIVKNINAL------ALKETVSAVNISISFGYGTKKKEEEKIEEILKKAEDY 534
Cdd:PRK09581 361 IRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKiaeepfIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKA 440
|
....*
gi 500500343 535 MYKKK 539
Cdd:PRK09581 441 LYEAK 445
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
349-513 |
2.88e-25 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 110.87 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 349 FKRVDGTLLPVEVMMTTILHNGKKVFHSLcrdIRERKEMENKLEYLSYHDQLTGLYNRR-FFEN---ELKRLDvEENLPL 424
Cdd:PRK15426 355 FGSISIALTLLWALFTAMLLISWYVIRRM---VSNMFVLQSSLQWQAWHDPLTRLYNRGaLFEKaraLAKRCQ-RDQQPF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 425 TIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARLGGDEFVILLPKTDIYETEQIVKNIN-ALALKETV 503
Cdd:PRK15426 431 SVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRlRINEKEIL 510
|
170
....*....|....
gi 500500343 504 SAVN----ISISFG 513
Cdd:PRK15426 511 VAKSttirISASLG 524
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
373-507 |
5.12e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 108.22 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 373 VFHslcrDIRERKEMENKLEYLSYHDQLTGLYNRRFFENELKRL---DVEENLPLTIVMADVNGLKLVNDSFGHAAGDEL 449
Cdd:PRK09776 647 VIQ----DVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLlqtVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDAL 722
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 500500343 450 LKKVSEIIKRGCRYNDIIARLGGDEFVILLPKTDIYETEQIVKNInalalketVSAVN 507
Cdd:PRK09776 723 LRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI--------ISAIN 772
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
567-706 |
4.66e-22 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 92.79 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLTESETEELKTIGLLHDIGKIAIEENIlnkseelTEDEWQEIKRHSEIGYRILNTVNDMLEI 646
Cdd:cd00077 5 EHSLRVAQLARRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAI-------TEEESELEKDHAIVGAEILRELLLEEVI 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500500343 647 SEY-------VLYHHERWDGKGYPKGLKGEEIPLQSRIITIIDAYDAMTS-QRSYRSALPEESAIEEL 706
Cdd:cd00077 78 KLIdelilavDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRdSREKRRRIAEEDLEELL 145
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
131-393 |
6.38e-21 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 96.58 E-value: 6.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIINYklldsNASYERLTGLKKEDILGKTLYEIFPNM-EKNLIEK 209
Cdd:COG5809 5 KMELQLRKSEQRFRSLFENAPDAILIL----DLEGKILKV-----NPAAERIFGYTEDELLGTNILDFLHPDdEKELREI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 210 IQRVAITGQSVHY--QRYIKEKDKYYEAIVYRPKKLQ------FAAILTDITERKFAEKALKTSEYNFRNIFESSSDPIL 281
Cdd:COG5809 76 LKLLKEGESRDELefELRHKNGKRLEFSSKLSPIFDQngdiegMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 282 IT-LDNKVIDCNLAMIELLGYdSKSSILHKnpvQFSPEKQPNGESSKEKAIQvyKITMKNKKYKFEWWFKRVDGTLLPVE 360
Cdd:COG5809 156 VTdLDGRIIYANPAACKLLGI-SIEELIGK---SILELIHSDDQENVAAFIS--QLLKDGGIAQGEVRFWTKDGRWRLLE 229
|
250 260 270
....*....|....*....|....*....|....
gi 500500343 361 VMMTTILHNGK-KVFHSLCRDIRERKEMENKLEY 393
Cdd:COG5809 230 ASGAPIKKNGEvDGIVIIFRDITERKKLEELLRK 263
|
|
| HD_5 |
pfam13487 |
HD domain; HD domains are metal dependent phosphohydrolases. |
616-678 |
4.39e-20 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 433249 [Multi-domain] Cd Length: 64 Bit Score: 84.19 E-value: 4.39e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 616 EELTEDEWQEIKRHSEIGYRILNTVNDML-EISEYVLYHHERWDGKGYPKGLKGEEIPLQSRII 678
Cdd:pfam13487 1 GTLTPEEREIINRHPEHTARLLSTLPRLPkEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
391-513 |
1.15e-19 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 90.13 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 391 LEYLSYHDQLTGLYNRRF----FENELKRLdveENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDI 466
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVldesFDHQLRNR---EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYET 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 500500343 467 IARLGGDEFVILLPKTDIYETEQIVKNI-NALALKETVSA---VNISISFG 513
Cdd:PRK09894 202 VYRYGGEEFIICLKAATDEEACRAGERIrQLIANHAITHSdgrINITATFG 252
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
567-694 |
4.56e-16 |
|
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: 75.03 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLTESEteELKTIGLLHDIGKIAIEENILNKSEELtedewqeiKRHSEIGYRIL--NTVNDML 644
Cdd:smart00471 7 EHSLRVAQLAAALAEELGLLDIE--LLLLAALLHDIGKPGTPDSFLVKTSVL--------EDHHFIGAEILleEEEPRIL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 500500343 645 E--ISEYVLYHHERWDgkgypkGLKGEEIPLQSRIITIIDAYDAMTSQRSYR 694
Cdd:smart00471 77 EeiLRTAILSHHERPD------GLRGEPITLEARIVKVADRLDALRADRRYR 122
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
567-687 |
5.09e-16 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 74.58 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLTESETeeLKTIGLLHDIGKIAIEENIlnkseelteDEWQEIKRHSEIGYRIL---NTVNDM 643
Cdd:pfam01966 3 EHSLRVALLARELAEELGELDREL--LLLAALLHDIGKGPFGDEK---------PEFEIFLGHAVVGAEILrelEKRLGL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 500500343 644 LEISEYVLYHHERWDGKGYPkglkgEEIPLQSRIITIIDAYDAM 687
Cdd:pfam01966 72 EDVLKLILEHHESWEGAGYP-----EEISLEARIVKLADRLDAL 110
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
258-457 |
2.14e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 73.91 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 258 AEKALKTSEYNFRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPekqpnGESSKEKAIQVYKI 336
Cdd:COG2202 2 AEEALEESERRLRALVESSPDAIIITdLDGRILYVNPAFERLTGY-SAEELLGKTLRDLLP-----PEDDDEFLELLRAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 337 TMKNKKYKFEWWFKRVDGTLLPVEVMMTTIL-HNGKKV-FHSLCRDIRERKEMENKLEylsyhdqltglynrrffENELK 414
Cdd:COG2202 76 LAGGGVWRGELRNRRKDGSLFWVELSISPVRdEDGEITgFVGIARDITERKRAEEALR-----------------ESEER 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500500343 415 RLDVEENLPLTIVMADVNGLKL-VNDS----FGHAAGDELLKKVSEII 457
Cdd:COG2202 139 LRLLVENAPDGIFVLDLDGRILyVNPAaeelLGYSPEELLGKSLLDLL 186
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
380-494 |
1.93e-13 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 73.95 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 380 DIRERKEMENKLEYLSYHDQLTGLYNRRFFeNELKR--LDVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEII 457
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAI-QELIDhaINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
|
90 100 110
....*....|....*....|....*....|....*...
gi 500500343 458 kRGC-RYNDIIARLGGDEFVILLPKTDIYETEQIVKNI 494
Cdd:PRK10060 301 -LSClEEDQTLARLGGDEFLVLASHTSQAALEAMASRI 337
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
346-482 |
2.89e-13 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 71.78 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 346 EWWFKrvdgtlLPVEVMMTTILhngKKVFHSLCRDIRERKEmenKLEYLSYHDQLTGLYNRRFFEnELKRLDVE----EN 421
Cdd:PRK10245 168 EWWLS------LPVIVIYPLLF---AWVSYQTATKLAEHKR---RLQVMSTRDGMTGVYNRRHWE-TLLRNEFDncrrHH 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500500343 422 LPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGCRYNDIIARLGGDEFVILLPKT 482
Cdd:PRK10245 235 RDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGT 295
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
591-707 |
3.80e-13 |
|
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: 69.42 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 591 EELKTIGLLHDIGKIAIEENILNKSEELTEDEWQEIKRHSEIGYRILNtvndMLEISEYVLYHHERWDGKGypkglkgee 670
Cdd:COG3437 138 LYLKLAAPLHDIGKIGIPDAILLKPGKLTPEEWEITHAHIGAEILSGS----LLPLLQLAAEIHERWDGSG--------- 204
|
90 100 110
....*....|....*....|....*....|....*..
gi 500500343 671 iplqsriitiIDAYDAMTSQrsyrsalPEESAIEELK 707
Cdd:COG3437 205 ----------LSARDALTSK-------KLEEALEEIR 224
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
377-505 |
2.04e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 70.57 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 377 LCRDIRERKEMENKLEYLSYHDQLTGLYNRRFFENELKRLdVEENLPLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEI 456
Cdd:PRK11359 358 LAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDL-VDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNR 436
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 500500343 457 IKRGCRYNDIIARLGGDEFVILLPKTDIYETEQIvkninALALKETVSA 505
Cdd:PRK11359 437 FREKLKPDQYLCRIEGTQFVLVSLENDVSNITQI-----ADELRNVVSK 480
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
423-509 |
5.04e-10 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 58.14 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 423 PLTIVMADVNGLKLVNDSFGHAAGDELLKKVSEIIKRGC-RYNDIIARLGGDEFVILLPKTDIYETEQIvkninALALKE 501
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAF-----AEDMRE 75
|
....*...
gi 500500343 502 TVSAVNIS 509
Cdd:cd07556 76 AVSALNQS 83
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
374-490 |
7.74e-10 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 61.56 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 374 FHSLCRDIRE---RKEMEN-KLEYLSYHDQLTGLYNRRFFENELKRL--DVEENLPLTIVMADVNGLKLVNDSFGHAAGD 447
Cdd:PRK09966 223 FNSLLDEMEEwqlRLQAKNaQLLRTALHDPLTGLANRAAFRSGINTLmnNSDARKTSALLFLDGDNFKYINDTWGHATGD 302
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 500500343 448 ELLKKVSEIIKR--GCRYNDIiaRLGGDEFVILLPKTDI-YETEQI 490
Cdd:PRK09966 303 RVLIEIAKRLAEfgGLRHKAY--RLGGDEFAMVLYDVQSeSEVQQI 346
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
135-266 |
1.98e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 59.86 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 135 KLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIInykllDSNASYERLTGLKKEDILGKTLYEIFPNMEKnLIEKIQRVA 214
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVL----DADGRIT-----YVNPAAERLLGLSAEELLGRPLAELFPEDSP-LRELLERAL 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 215 ITGQSVHYQRYIKE----KDKYYEAIVY----RPKKLQFAAILTDITERKFAEKALKTSE 266
Cdd:COG3852 71 AEGQPVTEREVTLRrkdgEERPVDVSVSplrdAEGEGGVLLVLRDITERKRLERELRRAE 130
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
265-391 |
2.03e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 56.15 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 265 SEYNFRNIFESSSDPI-LITLDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEkqPNGESSKEKAIQVykITMKNKKY 343
Cdd:TIGR00229 1 SEERYRAIFESSPDAIiVIDLEGNILYVNPAFEEIFGY-SAEELIGRNVLELIPE--EDREEVRERIERR--LEGEPEPV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 500500343 344 KFEWWFKRVDGTLLPVEVMMTTILHNG-KKVFHSLCRDIRERKEMENKL 391
Cdd:TIGR00229 76 SEERRVRRKDGSEIWVEVSVSPIRTNGgELGVVGIVRDITERKEAEEAL 124
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
140-401 |
2.42e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 60.52 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 140 EERYKALVsemqQGLVLFQGSDNEEGKIINYklldsNASYERLTGLKKEDILGKTLYE-IFPNMEKNLIEKIQRVAITGQ 218
Cdd:COG5805 33 TEELETIL----ENLPDAIIAVNREGKVIYI-----NPAMEKLLGYTSEEIIGKTIFDfLEKEYHYRVKTRIERLQKGYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 219 SVHY-QRYIKEKDKYYEAIVYRP--KKLQFAAILT--DITERKFAEKALKTSEYNFRNIFESSSDPI-LITLDNKVIDCN 292
Cdd:COG5805 104 VVMIeQIYCKDGELIYVEVKLFPiyNQNGQAAILAlrDITKKKKIEEILQEQEERLQTLIENSPDLIcVIDTDGRILFIN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 293 LAMIELLGYdSKSSILHKNPVQFSPEKQPngESSKEkAIQVYKITMKNKKYKFEWWFKrvDGTLLPVEVMMTTILH--NG 370
Cdd:COG5805 184 ESIERLFGA-PREELIGKNLLELLHPCDK--EEFKE-RIESITEVWQEFIIEREIITK--DGRIRYFEAVIVPLIDtdGS 257
|
250 260 270
....*....|....*....|....*....|....
gi 500500343 371 KKVFHSLCRDIRERKEME---NKLEYLSYHDQLT 401
Cdd:COG5805 258 VKGILVILRDITEKKEAEelmARSEKLSIAGQLA 291
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
139-262 |
4.80e-09 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 54.99 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 139 SEERYKALVSEMQQGLVLFqgsdNEEGKIinyklLDSNASYERLTGLKKEDILGKTLYEIFPNMEKNLIEKIQRVAITGQ 218
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVI----DLEGNI-----LYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 500500343 219 S--VHYQRYIKEKD--KYYEAIVYRP-----KKLQFAAILTDITERKFAEKAL 262
Cdd:TIGR00229 72 PepVSEERRVRRKDgsEIWVEVSVSPirtngGELGVVGIVRDITERKEAEEAL 124
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
261-391 |
6.24e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 58.32 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 261 ALKTSEYNFRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEKQPngesskekAIQVYKITMK 339
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLdADGRITYVNPAAERLLGL-SAEELLGRPLAELFPEDSP--------LRELLERALA 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 500500343 340 NKK--YKFEWWFKRVDGTLLPVEVMMTTIL-HNGKKVFHSLCRDIRERKEMENKL 391
Cdd:COG3852 72 EGQpvTEREVTLRRKDGEERPVDVSVSPLRdAEGEGGVLLVLRDITERKRLEREL 126
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
131-266 |
8.16e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 58.59 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIINYklldsNASYERLTGLKKEDILGKTLYEIFPNMEKNLI-EK 209
Cdd:COG5805 147 KIEEILQEQEERLQTLIENSPDLICVI----DTDGRILFI-----NESIERLFGAPREELIGKNLLELLHPCDKEEFkER 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500500343 210 IQRVAITGQSVHYQRYI---KEKDKYYEAIV-------YRPKKLQFaaILTDITERKFAEKALKTSE 266
Cdd:COG5805 218 IESITEVWQEFIIEREIitkDGRIRYFEAVIvplidtdGSVKGILV--ILRDITEKKEAEELMARSE 282
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
269-381 |
1.31e-08 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 53.19 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 269 FRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEKQPngesSKEKAIQVYKITMKNKKYKFEW 347
Cdd:pfam00989 3 LRAILESLPDGIFVVdEDGRILYVNAAAEELLGL-SREEVIGKSLLDLIPEEDD----AEVAELLRQALLQGEESRGFEV 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 500500343 348 WFKRVDGTLLPVEVMMTTILHNGKKVFHSLC--RDI 381
Cdd:pfam00989 78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGvlRDI 113
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
131-272 |
6.38e-08 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 55.55 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIINYklldsNASYERLTGLKKEDILGKTLYEIFPNmeknliEKI 210
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVV----DADGRITYV-----NRAAERILGLPREEVIGKNVTELIPN------SPL 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500500343 211 QRVAITGQSVhYQRYIKEKDKYYEAIV-----YRPKKLQFA-AILTDITERKFAEKALKTSE--------YNFRNI 272
Cdd:COG3829 66 LEVLKTGKPV-TGVIQKTGGKGKTVIVtaipiFEDGEVIGAvETFRDITELKRLERKLREEElerglsakYTFDDI 140
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
131-266 |
8.26e-08 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 55.37 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLFqgsdNEEGKIInykllDSNASYERLTGLKKEDILGKTLYEIFPNMEK-NLIEK 209
Cdd:COG5809 131 RMEEALRESEEKFRLIFNHSPDGIIVT----DLDGRII-----YANPAACKLLGISIEELIGKSILELIHSDDQeNVAAF 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 210 IQRVAITGQSVHYQRYIKEKD---KYYEA----IVYRPKKLQFAAILTDITERKFAEKALKTSE 266
Cdd:COG5809 202 ISQLLKDGGIAQGEVRFWTKDgrwRLLEAsgapIKKNGEVDGIVIIFRDITERKKLEELLRKSE 265
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
285-383 |
1.06e-06 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 47.46 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 285 DNKVIDCNLAMIELLGYDSKSsILHKNPVQFSPEkqPNGESSKEKAIQvykitMKNKKYKFEWWFKRVDGTLLPVEVMMT 364
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREE-LLGKSITDLFAE--PEDSERLREALR-----EGKAVREFEVVLYRKDGEPFPVLVSLA 72
|
90 100
....*....|....*....|.
gi 500500343 365 TILHNGKKVFH--SLCRDIRE 383
Cdd:pfam13426 73 PIRDDGGELVGiiAILRDITE 93
|
|
| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
566-723 |
1.49e-06 |
|
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: 49.58 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 566 EEHSHRV----SRLCQDMGHALGLTESETEE-LKTIGLLHDIGKIAIE--ENILNKSEELTEDEWQEIkRHSEIGYRILN 638
Cdd:cd09641 10 LEHLLDVaawdAELAEEFARKLGLELGLSRElLALAGLLHDLGKATPAfqKYLRGGKEALREGKRKEV-RHSLLGALLLY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 639 TVNDMLEISEY--------VLYHHERWDGKGYPKGLKGEEIpLQSRIITIIDAYDAMTSQRSYRSALPEESAIEELKINA 710
Cdd:cd09641 89 ELLKELGLDEElalllayaIAGHHGGLPDVLLLLDEDDESA-LKERLEELDEEKLLLELWEEELEELLDELLKELLLLLL 167
|
170
....*....|...
gi 500500343 711 GTQFDPDLVRIFI 723
Cdd:cd09641 168 PELLSFELYLLLR 180
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
269-328 |
1.54e-06 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 46.00 E-value: 1.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500500343 269 FRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYDSKSSILHKNPVQFSPEKQPNGESSKE 328
Cdd:pfam13188 3 LRALFESSPDGILVLdEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELLRE 63
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
398-508 |
2.17e-06 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 51.02 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 398 DQLTGLYNRRFFENELKRLdVEENLPLT----IVMADVNGLKLVNDSFGHAAGDELL----KKVSEIIKrgcRYND-IIA 468
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATL-LEDQEMVGahgvVMLIRLPDFDLLQEEWGESQVEELLfeliNLLSTFVM---RYPGaLLA 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 500500343 469 RLGGDEFVILLPKTDIYETEQI----VKNINALALKETVSAVNI 508
Cdd:PRK11059 307 RYSRSDFAVLLPHRSLKEADSLasqlLKAVDALPPPKMLDRDDF 350
|
|
| HDOD |
COG1639 |
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms]; |
567-663 |
3.43e-06 |
|
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
Pssm-ID: 441246 [Multi-domain] Cd Length: 244 Bit Score: 48.81 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLteSETEELKTIGLLHDIGKIA-----------IEENILNKSEELTEDEWQEIKR-HSEIGY 634
Cdd:COG1639 107 RHSLAVAAAARALARRLGL--LDPEEAFLAGLLHDIGKLVllslfpeeyaeLLALAEADGLSLAEAEREVLGTdHAELGA 184
|
90 100 110
....*....|....*....|....*....|.
gi 500500343 635 RILNT--VNDmlEISEYVLYHHERWDGKGYP 663
Cdd:COG1639 185 ALARKwgLPE--ELVEAIRYHHDPEAAGEHR 213
|
|
| HDOD |
pfam08668 |
HDOD domain; |
567-655 |
4.30e-06 |
|
HDOD domain;
Pssm-ID: 430141 [Multi-domain] Cd Length: 196 Bit Score: 47.99 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLteSETEELKTIGLLHDIGKIAIE-------ENILNKSEE----LTEDEwQEI--KRHSEIG 633
Cdd:pfam08668 97 EHSLACALAARLLARRLGL--DDPEEAFLAGLLHDIGKLILLsllpdkyEELLEKAAEegisLLEAE-RELlgTDHAEVG 173
|
90 100
....*....|....*....|..
gi 500500343 634 YRILNTVNDMLEISEYVLYHHE 655
Cdd:pfam08668 174 AALLERWNLPEELVEAIAYHHN 195
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
465-513 |
5.78e-06 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 47.21 E-value: 5.78e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500500343 465 DIIARLGGDEFVILLPKTDIYETEQIVKNINAlALKETVSaVNISISFG 513
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIRE-AVAELPS-LRVTVSIG 162
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
567-687 |
3.42e-05 |
|
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: 45.27 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 567 EHSHRVSRLCQDMGHALGLtesETEELKTIGLLHDIGKIaieenilnkseelteDEWQEIKRHSEIGYRI----LNTVND 642
Cdd:COG1418 21 QHSLRVAKLAGLIAAEEGA---DVEVAKRAALLHDIGKA---------------KDHEVEGSHAEIGAELarkyLESLGF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 500500343 643 MLEISEYVLY----HHerWDGKGYPKglkgeeiPLQSRIITIIDAYDAM 687
Cdd:COG1418 83 PEEEIEAVVHaieaHS--FSGGIEPE-------SLEAKIVQDADRLDAL 122
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
259-392 |
1.87e-04 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 44.76 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 259 EKALKTSEYNFRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEKqpngesskekaiqVYKIT 337
Cdd:COG3829 3 ELELKELEEELEAILDSLDDGIIVVdADGRITYVNRAAERILGL-PREEVIGKNVTELIPNS-------------PLLEV 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 500500343 338 MKNKKYKFEwWFKRVDGTLLPVEVMMTTILHNGKKVFH-SLCRDIRERKEMENKLE 392
Cdd:COG3829 69 LKTGKPVTG-VIQKTGGKGKTVIVTAIPIFEDGEVIGAvETFRDITELKRLERKLR 123
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
141-213 |
2.56e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 39.69 E-value: 2.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500500343 141 ERYKALVSEMQQGLVLFqgsdNEEGKIinyklLDSNASYERLTGLKKEDILGKTLYEIF-PNMEKNLIEKIQRV 213
Cdd:smart00091 1 ERLRAILESLPDGIFVL----DLDGRI-----LYANPAAEELLGYSPEELIGKSLLELIhPEDRERVQEALQRL 65
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
268-332 |
4.86e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 38.92 E-value: 4.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500500343 268 NFRNIFESSSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQF-SPEKQPNGESSKEKAIQ 332
Cdd:smart00091 2 RLRAILESLPDGIFVLdLDGRILYANPAAEELLGY-SPEELIGKSLLELiHPEDRERVQEALQRLLS 67
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
123-391 |
1.28e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 42.35 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 123 KIQYDQTIESEKKLSKSEERYKALVSEMQQglVLFQGSDNEEGKIINYKLLDSNASYERLTGLKKEDILGKTLYEIFPNM 202
Cdd:PRK13560 179 DDQVDGFAEDITERKRAEERIDEALHFLQQ--LLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 203 EKNLIEKIQRVAITGQSVH-YQRYIKEKDKYYEAIVYRPKKLQF----------AAILTDITERKFAEKALKTSEYNFRN 271
Cdd:PRK13560 257 PADDYQEADAAKFDADGSQiIEAEFQNKDGRTRPVDVIFNHAEFddkenhcaglVGAITDISGRRAAERELLEKEDMLRA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 272 IFESSSDPILIT-LDNKVIDCNLAMIELLGYDSKSSILHKNPVQFSPEKQ------------PNGESSKEKAIQVYKITM 338
Cdd:PRK13560 337 IIEAAPIAAIGLdADGNICFVNNNAAERMLGWSAAEVMGKPLPGMDPELNeefwcgdfqewyPDGRPMAFDACPMAKTIK 416
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 500500343 339 KNKKYK-FEWWFKRVDGTLLPVEVMMTTILHNGKKVFHSLCR--DIRERKEMENKL 391
Cdd:PRK13560 417 GGKIFDgQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALlvDITERKQVEEQL 472
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
169-256 |
2.20e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 38.16 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 169 NYKLLDSNASYERLTGLKKEDILGKTLYEIFPNMEK-NLIEKIQRVAITGQSVHYQRYIKE--KDKYYEaIVYRP----- 240
Cdd:pfam08448 14 DGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAaRLERALRRALEGEEPIDFLEELLLngEERHYE-LRLTPlrdpd 92
|
90
....*....|....*..
gi 500500343 241 -KKLQFAAILTDITERK 256
Cdd:pfam08448 93 gEVIGVLVISRDITERR 109
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
57-157 |
2.23e-03 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 40.70 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 57 LIIISTYKGW---LYVIITAPILYLIIRSILKKVYLAEKKLNKSYEELLAV-NEKLESY--VKRLTNSKEELKiQYDQTI 130
Cdd:pfam00664 132 GIIVMFYYGWkltLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVaEESLSGIrtVKAFGREEYELE-KYDKAL 210
|
90 100
....*....|....*....|....*..
gi 500500343 131 ESEKKLSKSEERYKALVSEMQQGLVLF 157
Cdd:pfam00664 211 EEALKAGIKKAVANGLSFGITQFIGYL 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
80-152 |
4.35e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 4.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500500343 80 IRSILKKVYLAEKKLNKSYEELLAVNEKLESYVKRLTNSKEELKIQYDQTIESEKKLSKSEERYKALVSEMQQ 152
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
169-254 |
6.02e-03 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 36.67 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 169 NYKLLDSNASYERLTGLKKEDILGKTLYEIFPN-----MEKNLIEKIQRVaitgQSVHYQRYIKEKDKYYEAIVYRPKKL 243
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEpedseRLREALREGKAV----REFEVVLYRKDGEPFPVLVSLAPIRD 76
|
90
....*....|....*..
gi 500500343 244 Q------FAAILTDITE 254
Cdd:pfam13426 77 DggelvgIIAILRDITE 93
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
276-381 |
6.69e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 36.84 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500500343 276 SSDPILIT-LDNKVIDCNLAMIELLGYdSKSSILHKNPVQFSPEkqpngESSKEKAIQVYKITMKNKKYKFEWWFKRVDG 354
Cdd:cd00130 1 LPDGVIVLdLDGRILYANPAAEQLLGY-SPEELIGKSLLDLIHP-----EDREELRERLENLLSGGEPVTLEVRLRRKDG 74
|
90 100
....*....|....*....|....*....
gi 500500343 355 TLLPVEVMMTTILHNGKKV--FHSLCRDI 381
Cdd:cd00130 75 SVIWVLVSLTPIRDEGGEVigLLGVVRDI 103
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
162-233 |
8.28e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 36.46 E-value: 8.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500500343 162 NEEGKIINYklldsNASYERLTGLKKEDILGKTLYEIF-PNMEKNLIEKIQRVAITGQSVHYQRYIKEKDKYY 233
Cdd:cd00130 9 DLDGRILYA-----NPAAEQLLGYSPEELIGKSLLDLIhPEDREELRERLENLLSGGEPVTLEVRLRRKDGSV 76
|
|
| |
