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Conserved domains on  [gi|13472852|ref|NP_104419|]
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adenylate cyclase [Mesorhizobium loti MAFF303099]

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List of domain hits

Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
8-171 1.77e-42

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


:

Pssm-ID: 143636  Cd Length: 177  Bit Score: 150.81  E-value: 1.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   8 AAILAADVVGYSRLASA-DEDRTLARLRALRSdLIDPIIAVHNGRVIKRTGDGALVEF-------RSVVDAVRCAVEVQN 79
Cdd:cd07302   2 VTVLFADIVGFTALSERlGPEELVELLNEYFS-AFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  80 GMVERNAGVPQDRRIEFRIGIHLGDVV------EESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARlDLSVSD 153
Cdd:cd07302  81 ALAELNAEREGGPPLRLRIGIHTGPVVagvvgsERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA-GFEFEE 159
                       170
                ....*....|....*...
gi 13472852 154 LGSTQLKNIAEPIRVYSL 171
Cdd:cd07302 160 LGEVELKGKSGPVRVYRL 177
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
405-487 4.42e-13

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 65.86  E-value: 4.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 405 AQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKT 484
Cdd:cd00189  17 DEALEYYEKALELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNLGLAYYKLGKYEEALEAYEKALE 96

                ...
gi 13472852 485 LNP 487
Cdd:cd00189  97 LDP 99
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
462-557 1.23e-11

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


:

Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 61.63  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 462 LGEALYYSGRPEEALESFARAKTLNPYFPDVLLHfQALAAFQLGRYEEAVDLLLQ--RLARNAVTdvSRALLAACYGHLG 539
Cdd:cd00189   6 LGNLYYKLGDYDEALEYYEKALELDPDNADAYYN-LAAAYYKLGKYEEALEDYEKalELDPDNAK--AYYNLGLAYYKLG 82
                        90
                ....*....|....*...
gi 13472852 540 RFAEARAAWQEVLRLNPD 557
Cdd:cd00189  83 KYEEALEAYEKALELDPN 100
COG5616 COG5616
Predicted integral membrane protein [Function unknown]
180-325 1.40e-73

Predicted integral membrane protein [Function unknown]


:

Pssm-ID: 227903  Cd Length: 152  Bit Score: 234.17  E-value: 1.40e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 180 AAATSETAGRPATAAPPKLSIAVLPFANMSGDAEQDYFADGISEDIITALSKLSQLFVIARNSSFTFKGQNVQVQEVGTK 259
Cdd:COG5616   7 VESTTESLTAPGTSIPAKPSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAVDVREVGEE 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852 260 LGVRHVLEGSVRKSGNRVRITAQLIDAISGGHLWAERFDRELTDIFAVQDDVTQQIVGALALNLTE 325
Cdd:COG5616  87 LGVRYVLEGSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYGI 152
Apc3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
436-514 3.47e-05

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


:

Pssm-ID: 257383 [Multi-domain]  Cd Length: 81  Bit Score: 42.26  E-value: 3.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13472852   436 RRHDGAIDEAERAIVLNPNFAEGHvILGEALYYSGRPEEALEsFARAKTLNPYFPDVLLHFqALAAFQLGRYEEAVDLL 514
Cdd:pfam12895   3 HNYKNAIFLAEKLLALTPSNEDAY-LLAQCYFLQGQYKRAYE-LLRKLKLNNSSLGCRYLL-AQCLLKLKKYDEAIAAL 78
TPR_16 pfam13432
Tetratricopeptide repeat;
497-559 3.41e-04

Tetratricopeptide repeat;


:

Pssm-ID: 257757 [Multi-domain]  Cd Length: 65  Bit Score: 39.21  E-value: 3.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13472852   497 QALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPDYS 559
Cdd:pfam13432   3 LARALLRAGDYDDALAALEAALARAPLAAEALLLLGEALLQQGRLAEAAALLRAALALDPGDP 65
TPR_11 pfam13414
TPR repeat;
379-453 4.37e-04

TPR repeat;


:

Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 38.83  E-value: 4.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852   379 SAHAFLALTYVLDYLNRWsasppesmAQAEEVATRAVALDDSDPWAHWALAIAKLYT-RRHDGAIDEAERAIVLNP 453
Cdd:pfam13414   2 NAEALKNLGNALFKLGDY--------DEAIEAYEKALELDPDNAEAYLNLALAYLKLgKDYEEALEDLEKALELDP 69
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
6-178 3.06e-41

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


:

Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 148.84  E-value: 3.06e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   6 KLAAILAADVVGYSRLASADEDRTLARLRALRSDLIDPIIAVHNGRVIKRTGDGALVEFRSVV---DAVRCAVEVQNGMV 82
Cdd:COG2114  45 RRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSpleDAVACALDLQLALR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  83 ERNAGVPQDrRIEFRIGIHLGDVV--EESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLDlSVSDLGSTQLK 160
Cdd:COG2114 125 NPLARLRRE-SLRVRIGIHTGEVVvgNTGGYTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDLVD-LFSGLGSHRLK 202
                       170
                ....*....|....*...
gi 13472852 161 NIAEPIRVYSLQVGSAGT 178
Cdd:COG2114 203 GLARPVRVYQLCHRSLRR 220
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
8-171 1.77e-42

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636  Cd Length: 177  Bit Score: 150.81  E-value: 1.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   8 AAILAADVVGYSRLASA-DEDRTLARLRALRSdLIDPIIAVHNGRVIKRTGDGALVEF-------RSVVDAVRCAVEVQN 79
Cdd:cd07302   2 VTVLFADIVGFTALSERlGPEELVELLNEYFS-AFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  80 GMVERNAGVPQDRRIEFRIGIHLGDVV------EESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARlDLSVSD 153
Cdd:cd07302  81 ALAELNAEREGGPPLRLRIGIHTGPVVagvvgsERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA-GFEFEE 159
                       170
                ....*....|....*...
gi 13472852 154 LGSTQLKNIAEPIRVYSL 171
Cdd:cd07302 160 LGEVELKGKSGPVRVYRL 177
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
405-487 4.42e-13

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 65.86  E-value: 4.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 405 AQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKT 484
Cdd:cd00189  17 DEALEYYEKALELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNLGLAYYKLGKYEEALEAYEKALE 96

                ...
gi 13472852 485 LNP 487
Cdd:cd00189  97 LDP 99
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
462-557 1.23e-11

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 61.63  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 462 LGEALYYSGRPEEALESFARAKTLNPYFPDVLLHfQALAAFQLGRYEEAVDLLLQ--RLARNAVTdvSRALLAACYGHLG 539
Cdd:cd00189   6 LGNLYYKLGDYDEALEYYEKALELDPDNADAYYN-LAAAYYKLGKYEEALEDYEKalELDPDNAK--AYYNLGLAYYKLG 82
                        90
                ....*....|....*...
gi 13472852 540 RFAEARAAWQEVLRLNPD 557
Cdd:cd00189  83 KYEEALEAYEKALELDPN 100
COG5616 COG5616
Predicted integral membrane protein [Function unknown]
180-325 1.40e-73

Predicted integral membrane protein [Function unknown]


Pssm-ID: 227903  Cd Length: 152  Bit Score: 234.17  E-value: 1.40e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 180 AAATSETAGRPATAAPPKLSIAVLPFANMSGDAEQDYFADGISEDIITALSKLSQLFVIARNSSFTFKGQNVQVQEVGTK 259
Cdd:COG5616   7 VESTTESLTAPGTSIPAKPSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAVDVREVGEE 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852 260 LGVRHVLEGSVRKSGNRVRITAQLIDAISGGHLWAERFDRELTDIFAVQDDVTQQIVGALALNLTE 325
Cdd:COG5616  87 LGVRYVLEGSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYGI 152
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
9-160 1.34e-17

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 80.75  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852     9 AILAADVVGYSRLASA-DEDRTLARLRALRSDlIDPIIAVHNGRVIKRTGDGALVEF---RSVVDAVRCAVEVQNGMVE- 83
Cdd:pfam00211  10 TILFADIVGFTALSSAhSPEEVVRLLNDLYTR-FDELLDEHGVYKVKTIGDAYMAASglpEPSPAHAQTIAEMALDMLEa 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852    84 -RNAGVPQDRRIEFRIGIHLGDVVEESDG------DLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLDLSVSDLGS 156
Cdd:pfam00211  89 iKSVNIPSFEGLRVRVGIHTGPVVAGVIGakrpryDVWGDTVNLASRMESTGVPGKIHVSEETYRLLKTREGFEFTERGE 168

                  ....
gi 13472852   157 TQLK 160
Cdd:pfam00211 169 VEVK 172
TolB_N pfam04052
TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent ...
197-289 1.81e-04

TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent translocation system. This function of this amino terminal domain is uncertain.


Pssm-ID: 252339  Cd Length: 105  Bit Score: 40.34  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   197 KLSIAVLPFANMSGDAEqdyFADGISEdIITALSKLSQLF-VIARNSSFTFKGQNVQVQ-EVGTKLGVRHVLEGSVRKSG 274
Cdd:pfam04052  12 PLPIAVVPFAGEGGAAE---LPRDISE-VIAADLARSGLFrPIDPSAFPSSPTSNSEVDfADWRALGADALVTGSVTSSG 87
                          90
                  ....*....|....*
gi 13472852   275 NRVRITAQLIDAISG 289
Cdd:pfam04052  88 DGLTVEFRLYDVFSG 102
TPR_1 pfam00515
Tetratricopeptide repeat;
531-558 2.07e-03

Tetratricopeptide repeat;


Pssm-ID: 249923  Cd Length: 34  Bit Score: 36.24  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|....*...
gi 13472852   531 LAACYGHLGRFAEARAAWQEVLRLNPDY 558
Cdd:pfam00515   7 LGNAYLKLGKYDEALEYYEKALELNPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
531-558 5.29e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478  Cd Length: 34  Bit Score: 35.11  E-value: 5.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 13472852    531 LAACYGHLGRFAEARAAWQEVLRLNPDY 558
Cdd:smart00028   7 LGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
456-487 7.74e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 254383  Cd Length: 34  Bit Score: 34.80  E-value: 7.74e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 13472852   456 AEGHVILGEALYYSGRPEEALESFARAKTLNP 487
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDP 32
Apc3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
436-514 3.47e-05

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


Pssm-ID: 257383 [Multi-domain]  Cd Length: 81  Bit Score: 42.26  E-value: 3.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13472852   436 RRHDGAIDEAERAIVLNPNFAEGHvILGEALYYSGRPEEALEsFARAKTLNPYFPDVLLHFqALAAFQLGRYEEAVDLL 514
Cdd:pfam12895   3 HNYKNAIFLAEKLLALTPSNEDAY-LLAQCYFLQGQYKRAYE-LLRKLKLNNSSLGCRYLL-AQCLLKLKKYDEAIAAL 78
TPR_16 pfam13432
Tetratricopeptide repeat;
497-559 3.41e-04

Tetratricopeptide repeat;


Pssm-ID: 257757 [Multi-domain]  Cd Length: 65  Bit Score: 39.21  E-value: 3.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13472852   497 QALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPDYS 559
Cdd:pfam13432   3 LARALLRAGDYDDALAALEAALARAPLAAEALLLLGEALLQQGRLAEAAALLRAALALDPGDP 65
TPR_11 pfam13414
TPR repeat;
379-453 4.37e-04

TPR repeat;


Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 38.83  E-value: 4.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852   379 SAHAFLALTYVLDYLNRWsasppesmAQAEEVATRAVALDDSDPWAHWALAIAKLYT-RRHDGAIDEAERAIVLNP 453
Cdd:pfam13414   2 NAEALKNLGNALFKLGDY--------DEAIEAYEKALELDPDNAEAYLNLALAYLKLgKDYEEALEDLEKALELDP 69
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
6-178 3.06e-41

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 148.84  E-value: 3.06e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   6 KLAAILAADVVGYSRLASADEDRTLARLRALRSDLIDPIIAVHNGRVIKRTGDGALVEFRSVV---DAVRCAVEVQNGMV 82
Cdd:COG2114  45 RRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSpleDAVACALDLQLALR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  83 ERNAGVPQDrRIEFRIGIHLGDVV--EESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLDlSVSDLGSTQLK 160
Cdd:COG2114 125 NPLARLRRE-SLRVRIGIHTGEVVvgNTGGYTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDLVD-LFSGLGSHRLK 202
                       170
                ....*....|....*...
gi 13472852 161 NIAEPIRVYSLQVGSAGT 178
Cdd:COG2114 203 GLARPVRVYQLCHRSLRR 220
NrfG COG0457
FOG: TPR repeat [General function prediction only]
318-558 9.12e-16

FOG: TPR repeat [General function prediction only]


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 76.81  E-value: 9.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 318 ALALNLTEGDRQRLAPEHPRNAEAYDCFLRGRELWHRLTKETNVAARDVLQRAIDLDPNFASAHAFLALTYVLDYLNRWS 397
Cdd:COG0457  20 AEALALLEAGLALLELLGELAEALELLEEALELLPNSDLAGLLLLLALALLKLGRLEEALELLEKALELELLPNLAEALL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 398 ASPP-----ESMAQAEEVATRAVALDDSDPWAHWALAIAKLY-TRRHDGAIDEAERAIVLNP---NFAEGHVILGEALYY 468
Cdd:COG0457 100 NLGLllealGKYEEALELLEKALALDPDPDLAEALLALGALYeLGDYEEALELYEKALELDPelnELAEALLALGALLEA 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 469 SGRPEEALESFARAKTLNPYFPDVLLHFQALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAW 548
Cdd:COG0457 180 LGRYEEALELLEKALKLNPDDDAEALLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYNLALLLLELGRYEEALEAL 259
                       250
                ....*....|
gi 13472852 549 QEVLRLNPDY 558
Cdd:COG0457 260 EKALELDPDL 269
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
374-558 6.29e-14

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 73.58  E-value: 6.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   374 DPNFASAHAFLALTYVLDylnrwsasppESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNP 453
Cdd:TIGR02917 121 DEGAAELLALRGLAYLGL----------GQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   454 NFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLhFQALAAFQLGRYEEA---VDLLLQRLARNAVTDVSRAL 530
Cdd:TIGR02917 191 GNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLL-ALATILIEAGEFEEAekhADALLKKAPNSPLAHYLKAL 269
                         170       180
                  ....*....|....*....|....*...
gi 13472852   531 LAAcygHLGRFAEARAAWQEVLRLNPDY 558
Cdd:TIGR02917 270 VDF---QKKNYEDARETLQDALKSAPEY 294
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
8-141 1.17e-13

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 69.21  E-value: 1.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852      8 AAILAADVVGYSRLASAdedRTLARLRALRSDL---IDPIIAVHNGRVIKRTGDGALVEF----RSVVDAVRCAVEVQNG 80
Cdd:smart00044  37 VTILFSDIVGFTSLCST---STPEQVVNLLNDLysrFDQIIDRHGGYKVKTIGDAYMVASglpeEALVDHAELIADEALD 113
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852     81 MVE--RNAGVP-QDRRIEFRIGIHLGDVVEESDG------DLMGDGVNIASRLEGVAAPGAICLSEDAYR 141
Cdd:smart00044 114 MVEelKTVLVQhREEGLRVRIGIHTGPVVAGVVGirmpryCLFGDTVNLASRMESAGDPGQIQVSEETYS 183
PRK10153 PRK10153
DNA-binding transcriptional activator CadC; Provisional
209-487 9.43e-09

DNA-binding transcriptional activator CadC; Provisional


Pssm-ID: 236658 [Multi-domain]  Cd Length: 517  Bit Score: 56.59  E-value: 9.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  209 SGDAEQDYFADGISEDIITALSKLSQlFVIARNSSFTFKGQNVQVQEVGTKLGVRhvlegsVRKSGNRVRITAQLIDAIS 288
Cdd:PRK10153 214 NNWSSQLSYADGIGQLLMADLNTVST-FVVHDKTNYNINEPSSSGKTLGIAFVNQ------RHYRAQQCFLSVELVDNAD 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  289 GGHLWAERFDRELTDIFAVQDDVTQQIVGALALNLTEGDRQRLAPEHPRNAEAYDCFLRGRELwhrltkeTNVAARDVLQ 368
Cdd:PRK10153 287 GSVMLSKRYFLTNGNQLSVQNDLSNSLSRALNQPWPERMQERLQQGLPHQGAALTLFYQAHHY-------LNSGDAKSLN 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  369 RAIDL-------DPNFASAHAFLALTYVLdyLNRWSASPPESMAQAEEVATRAVALDDSDPWA--HWALAIAKLYtrrhD 439
Cdd:PRK10153 360 KASDLleeilksEPDFTYAQAEKALADIV--RHSQQPLDEKQLAALSTELDNIVALPELNVLPriYEILAVQALV----K 433
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13472852  440 GAIDEAERAI---------VLNpnfaegHVILGEALYYSGRPEEALESFARAKTLNP 487
Cdd:PRK10153 434 GKTDEAYQAInkaidlemsWLN------YVLLGKVYELKGDNRLAADAYSTAFNLRP 484
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
22-148 1.74e-06

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 49.84  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852     22 ASADEDRTLARLRALRSDLIDpiIAV-HNGRVIKRTGDGALVEF-------RSVVDAVRCAVEV--QNGMVERNAGVPQD 91
Cdd:TIGR03903  306 VEEDDEELDLLLRSWLTRCAD--IAVrYGAHVGGVLGDTLLFYFgypsaaeRDARRAARAALEMvrQAGRKGEAAAGEGK 383
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13472852     92 RRIEFRIGIHLGDVVEESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLD 148
Cdd:TIGR03903  384 WRVEIAAGIHTGLVLAQAPHASGGTTPNAAVRMQAQAEPGQILVSEAARKLLRRHAD 440
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
391-570 5.41e-05

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 45.07  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   391 DYLNRWSASPPESMAQaEEVATRAVALddSDP-WAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYS 469
Cdd:PRK11447  240 KYLQVFSDGDSVAAAR-SQLAEQQKQL--ADPaFRARAQGLAAVDSGQGGKAIPELQQAVRANPKDSEALGALGQAYSQQ 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   470 GRPEEALESFARAKTLNPYFPDV-------------LLHFQALAAFQLGRYEEAVDLLLQrlARNAVTDVSRALLAacyg 536
Cdd:PRK11447  317 GDRARAVAQFEKALALDPHSSNRdkwesllkvnrywLLIQQGDAALKANNLAQAERLYQQ--ARQVDNTDSYAVLG---- 390
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 13472852   537 hLGRFAEAR-------AAWQEVLRLNPDYSLEYRRKVLPYK 570
Cdd:PRK11447  391 -LGDVAMARkdyaaaeRYYQQALRMDPGNTNAVRGLANLYR 430
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
424-485 5.59e-03

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 36.51  E-value: 5.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13472852    424 AHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTL 485
Cdd:smart01043  63 ALEALAEALLALGRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLRRL 124
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
190-292 7.62e-03

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear [Transport and binding proteins, Other, Cellular processes, Pathogenesis].


Pssm-ID: 234019 [Multi-domain]  Cd Length: 417  Bit Score: 37.63  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   190 PATAAPPklsIAVLPFANMSGDAEQDYFADGISEdIITALSKLSQLFVIARNSSFTfkGQNVQVQEVG----TKLGVRHV 265
Cdd:TIGR02800  18 GGASALP---IAVAPFSNDGGGSPDANLGEDIAE-VIANDLRRSGLFSPVDKAGLP--SNPISESQVNpaawQALGADAL 91
                          90       100
                  ....*....|....*....|....*...
gi 13472852   266 LEGSVRKSGN-RVRITAQLIDAISGGHL 292
Cdd:TIGR02800  92 VVGSVTPNGNgRYTVRFRLYDVVSGQLQ 119
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
8-171 1.77e-42

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636  Cd Length: 177  Bit Score: 150.81  E-value: 1.77e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   8 AAILAADVVGYSRLASA-DEDRTLARLRALRSdLIDPIIAVHNGRVIKRTGDGALVEF-------RSVVDAVRCAVEVQN 79
Cdd:cd07302   2 VTVLFADIVGFTALSERlGPEELVELLNEYFS-AFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  80 GMVERNAGVPQDRRIEFRIGIHLGDVV------EESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARlDLSVSD 153
Cdd:cd07302  81 ALAELNAEREGGPPLRLRIGIHTGPVVagvvgsERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA-GFEFEE 159
                       170
                ....*....|....*...
gi 13472852 154 LGSTQLKNIAEPIRVYSL 171
Cdd:cd07302 160 LGEVELKGKSGPVRVYRL 177
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
405-487 4.42e-13

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 65.86  E-value: 4.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 405 AQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKT 484
Cdd:cd00189  17 DEALEYYEKALELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNLGLAYYKLGKYEEALEAYEKALE 96

                ...
gi 13472852 485 LNP 487
Cdd:cd00189  97 LDP 99
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
462-557 1.23e-11

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 61.63  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 462 LGEALYYSGRPEEALESFARAKTLNPYFPDVLLHfQALAAFQLGRYEEAVDLLLQ--RLARNAVTdvSRALLAACYGHLG 539
Cdd:cd00189   6 LGNLYYKLGDYDEALEYYEKALELDPDNADAYYN-LAAAYYKLGKYEEALEDYEKalELDPDNAK--AYYNLGLAYYKLG 82
                        90
                ....*....|....*...
gi 13472852 540 RFAEARAAWQEVLRLNPD 557
Cdd:cd00189  83 KYEEALEAYEKALELDPN 100
COG5616 COG5616
Predicted integral membrane protein [Function unknown]
180-325 1.40e-73

Predicted integral membrane protein [Function unknown]


Pssm-ID: 227903  Cd Length: 152  Bit Score: 234.17  E-value: 1.40e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 180 AAATSETAGRPATAAPPKLSIAVLPFANMSGDAEQDYFADGISEDIITALSKLSQLFVIARNSSFTFKGQNVQVQEVGTK 259
Cdd:COG5616   7 VESTTESLTAPGTSIPAKPSIAVLPFVNLSGDPEQEYFADGLTEDIITDLSRFRELFVIARNSSFTYKGKAVDVREVGEE 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852 260 LGVRHVLEGSVRKSGNRVRITAQLIDAISGGHLWAERFDRELTDIFAVQDDVTQQIVGALALNLTE 325
Cdd:COG5616  87 LGVRYVLEGSVRRAGGRVRVTAQLVDASSGGHLWAERYDRDLDDIFALQDEVTERIVSAIAGPYGI 152
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
9-160 1.34e-17

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 249682  Cd Length: 184  Bit Score: 80.75  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852     9 AILAADVVGYSRLASA-DEDRTLARLRALRSDlIDPIIAVHNGRVIKRTGDGALVEF---RSVVDAVRCAVEVQNGMVE- 83
Cdd:pfam00211  10 TILFADIVGFTALSSAhSPEEVVRLLNDLYTR-FDELLDEHGVYKVKTIGDAYMAASglpEPSPAHAQTIAEMALDMLEa 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852    84 -RNAGVPQDRRIEFRIGIHLGDVVEESDG------DLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLDLSVSDLGS 156
Cdd:pfam00211  89 iKSVNIPSFEGLRVRVGIHTGPVVAGVIGakrpryDVWGDTVNLASRMESTGVPGKIHVSEETYRLLKTREGFEFTERGE 168

                  ....
gi 13472852   157 TQLK 160
Cdd:pfam00211 169 VEVK 172
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
7-133 4.57e-13

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  Cd Length: 133  Bit Score: 66.61  E-value: 4.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   7 LAAILAADVVGYSRLASADEDRTLARLRALRSDLIDPIIAVHNGRVIKRTGDGALVEFRsvVDAVRCAVEVQNGMVERNA 86
Cdd:cd07556   1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG--LDHPAAAVAFAEDMREAVS 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 13472852  87 GVPQDRR--IEFRIGIHLGDVV-----EESDGDLMGDGVNIASRLEGVAAPGAI 133
Cdd:cd07556  79 ALNQSEGnpVRVRIGIHTGPVVvgvigSRPQYDVWGALVNLASRMESQAKAGQV 132
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
436-516 2.89e-10

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 57.78  E-value: 2.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 436 RRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHFqALAAFQLGRYEEAVDLLL 515
Cdd:cd00189  14 GDYDEALEYYEKALELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNL-GLAYYKLGKYEEALEAYE 92

                .
gi 13472852 516 Q 516
Cdd:cd00189  93 K 93
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
493-585 9.30e-09

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 53.15  E-value: 9.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 493 LLHFQALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPDYSLEYRRKVLPYKNP 572
Cdd:cd00189   2 ALLNLGNLYYKLGDYDEALEYYEKALELDPDNADAYYNLAAAYYKLGKYEEALEDYEKALELDPDNAKAYYNLGLAYYKL 81
                        90
                ....*....|...
gi 13472852 573 ADFELVVDGLRKA 585
Cdd:cd00189  82 GKYEEALEAYEKA 94
TPR cd00189
Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2) ...
363-454 2.08e-08

Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here


Pssm-ID: 238112 [Multi-domain]  Cd Length: 100  Bit Score: 52.00  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 363 ARDVLQRAIDLDPNFASAHAFLALTYVldYLNRWsasppesmAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAI 442
Cdd:cd00189  19 ALEYYEKALELDPDNADAYYNLAAAYY--KLGKY--------EEALEDYEKALELDPDNAKAYYNLGLAYYKLGKYEEAL 88
                        90
                ....*....|..
gi 13472852 443 DEAERAIVLNPN 454
Cdd:cd00189  89 EAYEKALELDPN 100
TolB_N pfam04052
TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent ...
197-289 1.81e-04

TolB amino-terminal domain; TolB is an essential periplasmic component of the tol-dependent translocation system. This function of this amino terminal domain is uncertain.


Pssm-ID: 252339  Cd Length: 105  Bit Score: 40.34  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   197 KLSIAVLPFANMSGDAEqdyFADGISEdIITALSKLSQLF-VIARNSSFTFKGQNVQVQ-EVGTKLGVRHVLEGSVRKSG 274
Cdd:pfam04052  12 PLPIAVVPFAGEGGAAE---LPRDISE-VIAADLARSGLFrPIDPSAFPSSPTSNSEVDfADWRALGADALVTGSVTSSG 87
                          90
                  ....*....|....*
gi 13472852   275 NRVRITAQLIDAISG 289
Cdd:pfam04052  88 DGLTVEFRLYDVFSG 102
StaR_like cd05804
StaR_like; a well-conserved protein found in bacteria, plants, and animals. A family member ...
330-568 2.51e-04

StaR_like; a well-conserved protein found in bacteria, plants, and animals. A family member from Streptomyces toyocaensis, StaR is part of a gene cluster involved in the biosynthesis of glycopeptide antibiotics (GPAs), specifically A47934. It has been speculated that StaR could be a flavoprotein hydroxylating a tyrosine sidechain. Some family members have been annotated as proteins containing tetratricopeptide (TPR) repeats, which may at least indicate mostly alpha-helical secondary structure.


Pssm-ID: 100115 [Multi-domain]  Cd Length: 355  Bit Score: 42.27  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 330 RLAPEHPRNAEAYDCFLrGRELWHRLTKETNVAAR--DVLQRAIDLDPNFASAHAFlALTYVLDYlnrwsasppesmAQA 407
Cdd:cd05804  68 QLLDDYPRDLLALKLHL-GAFGLGDFSGMRDHVARvlPLWAPENPDYWYLLGMLAF-GLEEAGQY------------DRA 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 408 EEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAI---DEAERAIVLNPNFAeGHVILGEALYY--SGRPEEALESFA-- 480
Cdd:cd05804 134 EEAARRALELNPDDAWAVHAVAHVLEMQGRFKEGIafmESWRDTWDCSSMLR-GHNWWHLALFYleRGDYEAALAIYDth 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 481 RAKTLNPYFPDVL---------LHFQALAAFQlGRYEEAVDLLLQR--LARNAVTDVSRALLAACYGHLGRFAEARAAWQ 549
Cdd:cd05804 213 IAPSAESDPALDLldaasllwrLELAGHVDVG-DRWEDLADYAAWHfpDHGLAFNDLHAALALAGAGDKDALDKLLAALK 291
                       250
                ....*....|....*....
gi 13472852 550 EVLRLNPDYSLEYRRKVLP 568
Cdd:cd05804 292 GRASSADDNKQPARDVGLP 310
TPR_1 pfam00515
Tetratricopeptide repeat;
531-558 2.07e-03

Tetratricopeptide repeat;


Pssm-ID: 249923  Cd Length: 34  Bit Score: 36.24  E-value: 2.07e-03
                          10        20
                  ....*....|....*....|....*...
gi 13472852   531 LAACYGHLGRFAEARAAWQEVLRLNPDY 558
Cdd:pfam00515   7 LGNAYLKLGKYDEALEYYEKALELNPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
531-558 5.29e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478  Cd Length: 34  Bit Score: 35.11  E-value: 5.29e-03
                           10        20
                   ....*....|....*....|....*...
gi 13472852    531 LAACYGHLGRFAEARAAWQEVLRLNPDY 558
Cdd:smart00028   7 LGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
530-558 6.86e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 254383  Cd Length: 34  Bit Score: 34.80  E-value: 6.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 13472852   530 LLAACYGHLGRFAEARAAWQEVLRLNPDY 558
Cdd:pfam07719   6 NLGLAYYKLGDYEEALEAYEKALELDPNN 34
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
456-487 7.74e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 254383  Cd Length: 34  Bit Score: 34.80  E-value: 7.74e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 13472852   456 AEGHVILGEALYYSGRPEEALESFARAKTLNP 487
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDP 32
TPR_1 pfam00515
Tetratricopeptide repeat;
456-489 9.72e-03

Tetratricopeptide repeat;


Pssm-ID: 249923  Cd Length: 34  Bit Score: 34.32  E-value: 9.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 13472852   456 AEGHVILGEALYYSGRPEEALESFARAKTLNPYF 489
Cdd:pfam00515   1 AKALYNLGNAYLKLGKYDEALEYYEKALELNPNN 34
Apc3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
436-514 3.47e-05

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


Pssm-ID: 257383 [Multi-domain]  Cd Length: 81  Bit Score: 42.26  E-value: 3.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13472852   436 RRHDGAIDEAERAIVLNPNFAEGHvILGEALYYSGRPEEALEsFARAKTLNPYFPDVLLHFqALAAFQLGRYEEAVDLL 514
Cdd:pfam12895   3 HNYKNAIFLAEKLLALTPSNEDAY-LLAQCYFLQGQYKRAYE-LLRKLKLNNSSLGCRYLL-AQCLLKLKKYDEAIAAL 78
TPR_16 pfam13432
Tetratricopeptide repeat;
497-559 3.41e-04

Tetratricopeptide repeat;


Pssm-ID: 257757 [Multi-domain]  Cd Length: 65  Bit Score: 39.21  E-value: 3.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13472852   497 QALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPDYS 559
Cdd:pfam13432   3 LARALLRAGDYDDALAALEAALARAPLAAEALLLLGEALLQQGRLAEAAALLRAALALDPGDP 65
TPR_11 pfam13414
TPR repeat;
379-453 4.37e-04

TPR repeat;


Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 38.83  E-value: 4.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852   379 SAHAFLALTYVLDYLNRWsasppesmAQAEEVATRAVALDDSDPWAHWALAIAKLYT-RRHDGAIDEAERAIVLNP 453
Cdd:pfam13414   2 NAEALKNLGNALFKLGDY--------DEAIEAYEKALELDPDNAEAYLNLALAYLKLgKDYEEALEDLEKALELDP 69
CyaA COG2114
Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction ...
6-178 3.06e-41

Adenylate cyclase, family 3 (some proteins contain HAMP domain) [Signal transduction mechanisms]


Pssm-ID: 225025 [Multi-domain]  Cd Length: 227  Bit Score: 148.84  E-value: 3.06e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   6 KLAAILAADVVGYSRLASADEDRTLARLRALRSDLIDPIIAVHNGRVIKRTGDGALVEFRSVV---DAVRCAVEVQNGMV 82
Cdd:COG2114  45 RRVTLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSpleDAVACALDLQLALR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  83 ERNAGVPQDrRIEFRIGIHLGDVV--EESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLDlSVSDLGSTQLK 160
Cdd:COG2114 125 NPLARLRRE-SLRVRIGIHTGEVVvgNTGGYTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDLVD-LFSGLGSHRLK 202
                       170
                ....*....|....*...
gi 13472852 161 NIAEPIRVYSLQVGSAGT 178
Cdd:COG2114 203 GLARPVRVYQLCHRSLRR 220
NrfG COG0457
FOG: TPR repeat [General function prediction only]
318-558 9.12e-16

FOG: TPR repeat [General function prediction only]


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 76.81  E-value: 9.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 318 ALALNLTEGDRQRLAPEHPRNAEAYDCFLRGRELWHRLTKETNVAARDVLQRAIDLDPNFASAHAFLALTYVLDYLNRWS 397
Cdd:COG0457  20 AEALALLEAGLALLELLGELAEALELLEEALELLPNSDLAGLLLLLALALLKLGRLEEALELLEKALELELLPNLAEALL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 398 ASPP-----ESMAQAEEVATRAVALDDSDPWAHWALAIAKLY-TRRHDGAIDEAERAIVLNP---NFAEGHVILGEALYY 468
Cdd:COG0457 100 NLGLllealGKYEEALELLEKALALDPDPDLAEALLALGALYeLGDYEEALELYEKALELDPelnELAEALLALGALLEA 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 469 SGRPEEALESFARAKTLNPYFPDVLLHFQALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAW 548
Cdd:COG0457 180 LGRYEEALELLEKALKLNPDDDAEALLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYNLALLLLELGRYEEALEAL 259
                       250
                ....*....|
gi 13472852 549 QEVLRLNPDY 558
Cdd:COG0457 260 EKALELDPDL 269
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
374-558 6.29e-14

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 73.58  E-value: 6.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   374 DPNFASAHAFLALTYVLDylnrwsasppESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNP 453
Cdd:TIGR02917 121 DEGAAELLALRGLAYLGL----------GQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   454 NFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLhFQALAAFQLGRYEEA---VDLLLQRLARNAVTDVSRAL 530
Cdd:TIGR02917 191 GNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLL-ALATILIEAGEFEEAekhADALLKKAPNSPLAHYLKAL 269
                         170       180
                  ....*....|....*....|....*...
gi 13472852   531 LAAcygHLGRFAEARAAWQEVLRLNPDY 558
Cdd:TIGR02917 270 VDF---QKKNYEDARETLQDALKSAPEY 294
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
8-141 1.17e-13

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485 [Multi-domain]  Cd Length: 194  Bit Score: 69.21  E-value: 1.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852      8 AAILAADVVGYSRLASAdedRTLARLRALRSDL---IDPIIAVHNGRVIKRTGDGALVEF----RSVVDAVRCAVEVQNG 80
Cdd:smart00044  37 VTILFSDIVGFTSLCST---STPEQVVNLLNDLysrFDQIIDRHGGYKVKTIGDAYMVASglpeEALVDHAELIADEALD 113
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852     81 MVE--RNAGVP-QDRRIEFRIGIHLGDVVEESDG------DLMGDGVNIASRLEGVAAPGAICLSEDAYR 141
Cdd:smart00044 114 MVEelKTVLVQhREEGLRVRIGIHTGPVVAGVVGirmpryCLFGDTVNLASRMESAGDPGQIQVSEETYS 183
type_IV_pilW TIGR02521
type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF in ...
434-560 4.24e-13

type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF in ref (PMID:8973346) and PilW in ref (PMID:15612916). This outer membrane protein is required both for pilus stability and for pilus function such as adherence to human cells. Members of this family contain copies of the TPR (tetratricopeptide repeat) domain.


Pssm-ID: 131573 [Multi-domain]  Cd Length: 234  Bit Score: 68.13  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   434 YTRRHD--GAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHFQALAaFQLGRYEEAV 511
Cdd:TIGR02521  41 YLEQGDleVAKENLDKALEHDPDDYLAYLALALYYQQLGELEKAEDSFRRALTLNPNNGDVLNNYGTFL-CQQGKYEQAM 119
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13472852   512 DLLLQRLARNAVTDVSRALLAA--CYGHLGRFAEARAAWQEVLRLNPDYSL 560
Cdd:TIGR02521 120 QQFEQAIEDPLYPQPARSLENAglCALKAGDFDKAEKYLTRALQIDPQRPE 170
NrfG COG0457
FOG: TPR repeat [General function prediction only]
337-585 1.97e-12

FOG: TPR repeat [General function prediction only]


Pssm-ID: 223533 [Multi-domain]  Cd Length: 291  Bit Score: 66.79  E-value: 1.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 337 RNAEAYDCFLRGRELWHRLTKetNVAARDVLQRAIDLDPNFASAHAFLALTYVLDYLNRWsaspPESMAQAEEVATRAVA 416
Cdd:COG0457  18 LLAEALALLEAGLALLELLGE--LAEALELLEEALELLPNSDLAGLLLLLALALLKLGRL----EEALELLEKALELELL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 417 LDDSDPWAHWALAIAKLytRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYS-GRPEEALESFARAKTLNPYFPDVLLH 495
Cdd:COG0457  92 PNLAEALLNLGLLLEAL--GKYEEALELLEKALALDPDPDLAEALLALGALYElGDYEEALELYEKALELDPELNELAEA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 496 FQALAA--FQLGRYEEAVDLLLQRLARNAVTDVS-RALLAACYGHLGRFAEARAAWQEVLRLNPDYSLEYRRKVLPYKNP 572
Cdd:COG0457 170 LLALGAllEALGRYEEALELLEKALKLNPDDDAEaLLNLGLLYLKLGKYEEALEYYEKALELDPDNAEALYNLALLLLEL 249
                       250
                ....*....|...
gi 13472852 573 ADFELVVDGLRKA 585
Cdd:COG0457 250 GRYEEALEALEKA 262
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
363-557 1.42e-11

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 66.26  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   363 ARDVLQRAIDLDPNFASAHAFLA-LTYVLdylnrwsasppESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGA 441
Cdd:TIGR02917 178 ARALIDEVLTADPGNVDALLLKGdLLLSL-----------GNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEA 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   442 IDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNP-YFPDVLLhfQALAAFQLGRYEEAVDLLLQRLAR 520
Cdd:TIGR02917 247 EKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDALKSAPeYLPALLL--AGASEYQLGNLEQAYQYLNQILKY 324
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 13472852   521 NAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR02917 325 APNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPD 361
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
355-557 3.34e-10

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 61.64  E-value: 3.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   355 LTKETNVAARDVLQRAIDLDPNFASAHAFLALtyVLDYLNRwsasppesMAQAEEVATRAVALDDSDPWAHWALAIAKLY 434
Cdd:TIGR02917 204 LSLGNIELALAAYRKAIALRPNNIAVLLALAT--ILIEAGE--------FEEAEKHADALLKKAPNSPLAHYLKALVDFQ 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   435 TRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTlnpYFPDVLLHFQALAAFQL--GRYEEAVD 512
Cdd:TIGR02917 274 KKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLNQILK---YAPNSHQARRLLASIQLrlGRVDEAIA 350
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 13472852   513 LLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR02917 351 TLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPE 395
PRK10153 PRK10153
DNA-binding transcriptional activator CadC; Provisional
209-487 9.43e-09

DNA-binding transcriptional activator CadC; Provisional


Pssm-ID: 236658 [Multi-domain]  Cd Length: 517  Bit Score: 56.59  E-value: 9.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  209 SGDAEQDYFADGISEDIITALSKLSQlFVIARNSSFTFKGQNVQVQEVGTKLGVRhvlegsVRKSGNRVRITAQLIDAIS 288
Cdd:PRK10153 214 NNWSSQLSYADGIGQLLMADLNTVST-FVVHDKTNYNINEPSSSGKTLGIAFVNQ------RHYRAQQCFLSVELVDNAD 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  289 GGHLWAERFDRELTDIFAVQDDVTQQIVGALALNLTEGDRQRLAPEHPRNAEAYDCFLRGRELwhrltkeTNVAARDVLQ 368
Cdd:PRK10153 287 GSVMLSKRYFLTNGNQLSVQNDLSNSLSRALNQPWPERMQERLQQGLPHQGAALTLFYQAHHY-------LNSGDAKSLN 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  369 RAIDL-------DPNFASAHAFLALTYVLdyLNRWSASPPESMAQAEEVATRAVALDDSDPWA--HWALAIAKLYtrrhD 439
Cdd:PRK10153 360 KASDLleeilksEPDFTYAQAEKALADIV--RHSQQPLDEKQLAALSTELDNIVALPELNVLPriYEILAVQALV----K 433
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13472852  440 GAIDEAERAI---------VLNpnfaegHVILGEALYYSGRPEEALESFARAKTLNP 487
Cdd:PRK10153 434 GKTDEAYQAInkaidlemsWLN------YVLLGKVYELKGDNRLAADAYSTAFNLRP 484
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
335-557 3.90e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 55.09  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   335 HPRNAEAYDCFLRGRELWHRLTKetnvaARDVLQRAIDLDPNFASAHAFLALTYvldylnrWSASppeSMAQAEEVATRA 414
Cdd:TIGR02917 597 APDSPEAWLMLGRAQLAAGDLNK-----AVSSFKKLLALQPDSALALLLLADAY-------AVMK---NYAKAITSLKRA 661
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   415 VALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPyfPDVLL 494
Cdd:TIGR02917 662 LELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAP--SSQNA 739
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13472852   495 HFQALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR02917 740 IKLHRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKAPD 802
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
367-557 5.79e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 54.32  E-value: 5.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   367 LQRAIDLDPNFASAHAFLALTYVLdyLNRWSasppesmaQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAE 446
Cdd:TIGR02917 386 LAKATELDPENAAARTQLGISKLS--QGDPS--------EAIADLETAAQLDPELGRADLLLILSYLRSGQFDKALAAAK 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   447 RAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVlLHFQALAAFQLGRYEEAVDLLLQRLARNAVTDV 526
Cdd:TIGR02917 456 KLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPA-AANLARIDIQEGNPDDAIQRFEKVLTIDPKNLR 534
                         170       180       190
                  ....*....|....*....|....*....|.
gi 13472852   527 SRALLAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR02917 535 AILALAGLYLRTGNEEEAVAWLEKAAELNPQ 565
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
363-557 6.48e-08

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 54.32  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   363 ARDVLQRAIDLDPNFASAHAFLALTYVldYLNRWSasppesmaQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAI 442
Cdd:TIGR02917 280 ARETLQDALKSAPEYLPALLLAGASEY--QLGNLE--------QAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAI 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   443 DEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHfQALAAFQLGRYEEAVDLLLQRLARNA 522
Cdd:TIGR02917 350 ATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQ-LGISKLSQGDPSEAIADLETAAQLDP 428
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 13472852   523 VTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR02917 429 ELGRADLLLILSYLRSGQFDKALAAAKKLEKKQPD 463
COG4235 COG4235
Cytochrome c biogenesis factor [Posttranslational modification, protein turnover, chaperones]
438-556 1.33e-07

Cytochrome c biogenesis factor [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 226687 [Multi-domain]  Cd Length: 287  Bit Score: 51.99  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 438 HDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHF-QALAAFQLGRYEEAVDLLLQ 516
Cdd:COG4235 138 MEALIARLETHLQQNPGDAEGWDLLGRAYMALGRASDALLAYRNALRLAGDNPEILLGLaEALYYQAGQQMTAKARALLR 217
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13472852 517 RLARNAVTDV-SRALLAACYGHLGRFAEARAAWQEVLRLNP 556
Cdd:COG4235 218 QALALDPANIrALSLLAFAAFEQGDYAEAAAAWQMLLDLLP 258
PilF COG3063
Tfp pilus assembly protein PilF [Cell motility and secretion / Intracellular trafficking and ...
390-546 4.33e-07

Tfp pilus assembly protein PilF [Cell motility and secretion / Intracellular trafficking and secretion]


Pssm-ID: 225605 [Multi-domain]  Cd Length: 250  Bit Score: 50.12  E-value: 4.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 390 LDYLNRwsasppESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYS 469
Cdd:COG3063  43 LGYLQQ------GDYAQAKKNLEKALEHDPSYYLAHLVRAHYYQKLGENDLADESYRKALSLAPNNGDVLNNYGAFLCAQ 116
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13472852 470 GRPEEALESFARAkTLNPYFPDVLLHFQ--ALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARA 546
Cdd:COG3063 117 GRPEEAMQQFERA-LADPAYGEPSDTLEnlGLCALKAGQFDQAEEYLKRALELDPQFPPALLELARLHYKAGDYAPARL 194
Apc3 pfam12895
Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of ...
473-547 1.44e-06

Anaphase-promoting complex, cyclosome, subunit 3; Apc3, otherwise known as Cdc27, is one of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. The protein members of this family contain TPR repeats just as those of Apc7 do, and it appears that these TPR units bind the C-termini of the APC co-activators CDH1 and CDC20.


Pssm-ID: 257383 [Multi-domain]  Cd Length: 81  Bit Score: 46.50  E-value: 1.44e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13472852   473 EEALESFARAKTLNPYFPDVLLHfqALAAFQLGRYEEAVDLLlQRLARNAVTDVSRALLAACYGHLGRFAEARAA 547
Cdd:pfam12895   6 KNAIFLAEKLLALTPSNEDAYLL--AQCYFLQGQYKRAYELL-RKLKLNNSSLGCRYLLAQCLLKLKKYDEAIAA 77
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
22-148 1.74e-06

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein [Cellular processes, Toxin production and resistance].


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 49.84  E-value: 1.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852     22 ASADEDRTLARLRALRSDLIDpiIAV-HNGRVIKRTGDGALVEF-------RSVVDAVRCAVEV--QNGMVERNAGVPQD 91
Cdd:TIGR03903  306 VEEDDEELDLLLRSWLTRCAD--IAVrYGAHVGGVLGDTLLFYFgypsaaeRDARRAARAALEMvrQAGRKGEAAAGEGK 383
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 13472852     92 RRIEFRIGIHLGDVVEESDGDLMGDGVNIASRLEGVAAPGAICLSEDAYRQVKARLD 148
Cdd:TIGR03903  384 WRVEIAAGIHTGLVLAQAPHASGGTTPNAAVRMQAQAEPGQILVSEAARKLLRRHAD 440
TPR_11 pfam13414
TPR repeat;
427-487 2.85e-06

TPR repeat;


Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 45.38  E-value: 2.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13472852   427 ALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSG-RPEEALESFARAKTLNP 487
Cdd:pfam13414   8 NLGNALFKLGDYDEAIEAYEKALELDPDNAEAYLNLALAYLKLGkDYEEALEDLEKALELDP 69
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
366-557 2.87e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 48.93  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   366 VLQRAIDLDPNFASAHAFLALTYVLDylnrwsasppESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEA 445
Cdd:TIGR02917 589 ILNEAADAAPDSPEAWLMLGRAQLAA----------GDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSL 658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   446 ERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPdVLLHFQALAAFQLGRYEEAVDLLLQRLARnAVTD 525
Cdd:TIGR02917 659 KRALELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAA-LGFELEGDLYLRQKDYPAAIQAYRKALKR-APSS 736
                         170       180       190
                  ....*....|....*....|....*....|..
gi 13472852   526 VSRALLAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR02917 737 QNAIKLHRALLASGNTAEAVKTLEAWLKTHPN 768
PilF COG3063
Tfp pilus assembly protein PilF [Cell motility and secretion / Intracellular trafficking and ...
428-557 4.68e-06

Tfp pilus assembly protein PilF [Cell motility and secretion / Intracellular trafficking and secretion]


Pssm-ID: 225605 [Multi-domain]  Cd Length: 250  Bit Score: 47.03  E-value: 4.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 428 LAIAKLYTRRHD--GAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHFqalAAF--Q 503
Cdd:COG3063  39 LQLALGYLQQGDyaQAKKNLEKALEHDPSYYLAHLVRAHYYQKLGENDLADESYRKALSLAPNNGDVLNNY---GAFlcA 115
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852 504 LGRYEEAVDLLLQRLARNAVTDVSRALLAA--CYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:COG3063 116 QGRPEEAMQQFERALADPAYGEPSDTLENLglCALKAGQFDQAEEYLKRALELDPQ 171
COG4783 COG4783
Putative Zn-dependent protease, contains TPR repeats [General function prediction only]
424-558 1.03e-05

Putative Zn-dependent protease, contains TPR repeats [General function prediction only]


Pssm-ID: 227122 [Multi-domain]  Cd Length: 484  Bit Score: 47.01  E-value: 1.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 424 AHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPdVLLHFQALAAFQ 503
Cdd:COG4783 308 AQYGRALQTYLAGQYDEALKLLQPLIAAQPDNPYYLELAGDILLEANKAKEAIERLKKALALDPNSP-LLQLNLAQALLK 386
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13472852 504 LGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPDY 558
Cdd:COG4783 387 GGKPQEAIRILNRYLFNDPEDPNGWDLLAQAYAELGNRAEALLARAEGYALAGRL 441
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
340-557 1.36e-05

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines].


Pssm-ID: 233223 [Multi-domain]  Cd Length: 615  Bit Score: 46.52  E-value: 1.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   340 EAYDCFLRGreLWHRLTKETNVAARDvLQRAIDLDPNFASAHAFLALtyvldyLNRWSASPPEsmaqAEEVATRAVALDD 419
Cdd:TIGR00990 330 EAIALNLRG--TFKCLKGKHLEALAD-LSKSIELDPRVTQSYIKRAS------MNLELGDPDK----AEEDFDKALKLNS 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   420 SDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHFQAL 499
Cdd:TIGR00990 397 EDPDIYYHRAQLHFIKGEFAQAGKDYQKSIDLDPDFIFSHIQLGVTQYKEGSIASSMATFRRCKKNFPEAPDVYNYYGEL 476
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852   500 AAFQ------LGRYEEAVDL--LLQRLARNAVTDVSRALlaACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:TIGR00990 477 LLDQnkfdeaIEKFDTAIELekETKPMYMNVLPLINKAL--ALFQWKQDFIEAENLCEKALIIDPE 540
BTAD pfam03704
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
393-485 2.03e-05

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 202730 [Multi-domain]  Cd Length: 146  Bit Score: 43.41  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   393 LNRWSASPPESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRP 472
Cdd:pfam03704  33 LALWRGPALADVPAGPWLEAERARLEELRLRALEARIEADLRLGRHREALAELRALVALHPLRERLHRQLMRALYRSGRQ 112
                          90
                  ....*....|...
gi 13472852   473 EEALESFARAKTL 485
Cdd:pfam03704 113 AEALRVYRRLRRR 125
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
391-570 5.41e-05

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 45.07  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   391 DYLNRWSASPPESMAQaEEVATRAVALddSDP-WAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYS 469
Cdd:PRK11447  240 KYLQVFSDGDSVAAAR-SQLAEQQKQL--ADPaFRARAQGLAAVDSGQGGKAIPELQQAVRANPKDSEALGALGQAYSQQ 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   470 GRPEEALESFARAKTLNPYFPDV-------------LLHFQALAAFQLGRYEEAVDLLLQrlARNAVTDVSRALLAacyg 536
Cdd:PRK11447  317 GDRARAVAQFEKALALDPHSSNRdkwesllkvnrywLLIQQGDAALKANNLAQAERLYQQ--ARQVDNTDSYAVLG---- 390
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 13472852   537 hLGRFAEAR-------AAWQEVLRLNPDYSLEYRRKVLPYK 570
Cdd:PRK11447  391 -LGDVAMARkdyaaaeRYYQQALRMDPGNTNAVRGLANLYR 430
COG4235 COG4235
Cytochrome c biogenesis factor [Posttranslational modification, protein turnover, chaperones]
401-531 5.65e-05

Cytochrome c biogenesis factor [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 226687 [Multi-domain]  Cd Length: 287  Bit Score: 43.90  E-value: 5.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 401 PESMAQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPE---EALE 477
Cdd:COG4235 135 EQEMEALIARLETHLQQNPGDAEGWDLLGRAYMALGRASDALLAYRNALRLAGDNPEILLGLAEALYYQAGQQmtaKARA 214
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 13472852 478 SFARAKTLNPYFPDVLlHFQALAAFQLGRYEEAVDlLLQRLARNAVTDVSRALL 531
Cdd:COG4235 215 LLRQALALDPANIRAL-SLLAFAAFEQGDYAEAAA-AWQMLLDLLPADDPRRSL 266
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
441-514 6.38e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 44.69  E-value: 6.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13472852   441 AIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHFqALAAFQLGRYEEAVDLL 514
Cdd:TIGR02917 822 ALEYAERALKLAPNIPAILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAIRYHL-ALALLATGRKAEARKEL 894
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
393-510 1.33e-04

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines].


Pssm-ID: 233223 [Multi-domain]  Cd Length: 615  Bit Score: 43.44  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   393 LNRWSASPPESMAQAEEVATRAV--ALDDSDPWAHWALA-----IAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEA 465
Cdd:TIGR00990 295 LQLGLKSPESKADESYEEAARAFekALDLGKLGEKEAIAlnlrgTFKCLKGKHLEALADLSKSIELDPRVTQSYIKRASM 374
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 13472852   466 LYYSGRPEEALESFARAKTLNPYFPDVLLHfQALAAFQLGRYEEA 510
Cdd:TIGR00990 375 NLELGDPDKAEEDFDKALKLNSEDPDIYYH-RAQLHFIKGEFAQA 418
PRK12370 PRK12370
invasion protein regulator; Provisional
190-487 3.34e-04

invasion protein regulator; Provisional


Pssm-ID: 237080 [Multi-domain]  Cd Length: 553  Bit Score: 42.15  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  190 PATAAPPKLSIAVLPFaNMSG--DAEQDYFAdgisedIITALSKLSQLFVIARNSSFTFKGQNVQ-VQEVGTKLGVRHVL 266
Cdd:PRK12370 114 PPAPQPTTHTLAILPF-QMQDqvQSESLHYS------IVKGLSQYAPFGLSVLPVTITKNCRSVKdILELMDQLRPDYYI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  267 EGSVRKSGNRVRITAQLIDAiSGGHLwaerFDRELTDIFAVQD-DVTQQIVGALALNLTEGDRQrlapeHPRNAEAYDC- 344
Cdd:PRK12370 187 SGQMIPDGNDNIVQIEIVRV-KGYHL----LHQESIKLIEHQPaSLLQNKIANLLLRCIPGLRW-----DTKQISELNSi 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  345 -----FLRGRELWHRLTKETNVAARDVLQRAIDLDPN-------FASAHAFLALTYVLDYLNrwsasppeSMAQAEEVAT 412
Cdd:PRK12370 257 dstmvYLRGKHELNQYTPYSLQQALKLLTQCVNMSPNsiapycaLAECYLSMAQMGIFDKQN--------AMIKAKEHAI 328
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13472852  413 RAVALDDSDPWAHWALAIakLYTRRHDGAIDEA--ERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNP 487
Cdd:PRK12370 329 KATELDHNNPQALGLLGL--INTIHSEYIVGSLlfKQANLLSPISADIKYYYGWNLFMAGQLEEALQTINECLKLDP 403
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking and secretion]
410-571 4.37e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking and secretion]


Pssm-ID: 227343 [Multi-domain]  Cd Length: 257  Bit Score: 40.88  E-value: 4.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 410 VATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYF 489
Cdd:COG5010  88 VLQKSAIAYPKDRELLAAQGKNQIRNGNFGEAVSVLRKAARLAPTDWEAWNLLGAALDQLGRFDEARRAYRQALELAPNE 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 490 PDVLLHFQALAAFQlGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLGRFAEARA-AWQEVLRLNPDYSLEYRRKVLP 568
Cdd:COG5010 168 PSIANNLGMSLLLR-GDLEDAETLLLPAYLSPAADSRVRQNLALVVGLQGDFREAEDiAVQELLSEQAANNVAALRAAAS 246

                ...
gi 13472852 569 YKN 571
Cdd:COG5010 247 QSG 249
TPR_11 pfam13414
TPR repeat;
492-556 4.49e-04

TPR repeat;


Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 38.83  E-value: 4.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852   492 VLLHFQALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAACYGHLG-RFAEARAAWQEVLRLNP 556
Cdd:pfam13414   4 EALKNLGNALFKLGDYDEAIEAYEKALELDPDNAEAYLNLALAYLKLGkDYEEALEDLEKALELDP 69
TPR_16 pfam13432
Tetratricopeptide repeat;
427-490 4.83e-04

Tetratricopeptide repeat;


Pssm-ID: 257757 [Multi-domain]  Cd Length: 65  Bit Score: 38.44  E-value: 4.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13472852   427 ALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTLNPYFP 490
Cdd:pfam13432   2 ALARALLRAGDYDDALAALEAALARAPLAAEALLLLGEALLQQGRLAEAAALLRAALALDPGDP 65
TPR_11 pfam13414
TPR repeat;
456-516 4.88e-04

TPR repeat;


Pssm-ID: 257739 [Multi-domain]  Cd Length: 69  Bit Score: 38.45  E-value: 4.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13472852   456 AEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHFqALAAFQLG-RYEEAVDLLLQ 516
Cdd:pfam13414   3 AEALKNLGNALFKLGDYDEAIEAYEKALELDPDNAEAYLNL-ALAYLKLGkDYEEALEDLEK 63
TPR_12 pfam13424
Tetratricopeptide repeat;
493-557 5.03e-04

Tetratricopeptide repeat;


Pssm-ID: 257749 [Multi-domain]  Cd Length: 78  Bit Score: 38.51  E-value: 5.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13472852   493 LLHFQALAAFQLGRYEEAVDLLLQRLARNAVT-----DVSRAL--LAACYGHLGRFAEARAAWQEVLRLNPD 557
Cdd:pfam13424   7 ALNNLALVLRRLGDYDEALELLEKALEIARELgedhpETATALnnLARLYLALGDYDEALELLEKALEIRRA 78
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
363-576 5.42e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 234059 [Multi-domain]  Cd Length: 899  Bit Score: 41.61  E-value: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   363 ARDVLQRAIDLDPNFASAHAFLALtyvldyLNRWSASPPESMAQAEEVatraVALDDSDPWAHWALAIAKLYTRRHDGAI 442
Cdd:TIGR02917 484 AREAFEKALSIEPDFFPAAANLAR------IDIQEGNPDDAIQRFEKV----LTIDPKNLRAILALAGLYLRTGNEEEAV 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   443 DEAERAIVLNPNFAEGHVILGEALYYSGRPEEALesfARAKTLNPYFPDVLLHFQALAAFQL--GRYEEAVDLLLQRLAR 520
Cdd:TIGR02917 554 AWLEKAAELNPQEIEPALALAQYYLGKGQLKKAL---AILNEAADAAPDSPEAWLMLGRAQLaaGDLNKAVSSFKKLLAL 630
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 13472852   521 NAVTDVSRALLAACYGHLGRFAEARAAWQEVLRLNPDYSLEYRRKVLPYKNPADFE 576
Cdd:TIGR02917 631 QPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTE 686
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
406-563 6.19e-04

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 40.95  E-value: 6.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  406 QAEEVATRAVALDDsDPW----AHWA--LAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESF 479
Cdd:PRK11788 159 KAIDVAERLEKLGG-DSLrveiAHFYceLAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEAL 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852  480 ARAKTLNP-YFPDVLLHFQALAAfQLGRYEEAVDLLLQRLARNAVTDVSRAL---LAACYGHlgrfAEARAAWQEVLRLN 555
Cdd:PRK11788 238 ERVEEQDPeYLSEVLPKLMECYQ-ALGDEAEGLEFLRRALEEYPGADLLLALaqlLEEQEGP----EAAQALLREQLRRH 312

                 ....*...
gi 13472852  556 PDYSLEYR 563
Cdd:PRK11788 313 PSLRGFHR 320
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
360-557 6.38e-04

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 41.61  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   360 NVAARDVLQRAIDLDPNFASAHAFLALTY-------VLDYLNRWSASPPESM-------------------------AQA 407
Cdd:PRK11447  401 YAAAERYYQQALRMDPGNTNAVRGLANLYrqqspekALAFIASLSASQRRSIddierslqndrlaqqaealenqgkwAQA 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   408 EEVATRAVALDDSDPWAHWALAiaklYTRRHDGAIDEAE----RAIVLNPNFAEghVILGEALYYSG--RPEEALESFAR 481
Cdd:PRK11447  481 AELQRQRLALDPGSVWLTYRLA----QDLRQAGQRSQADalmrRLAQQKPNDPE--QVYAYGLYLSGsdRDRAALAHLNT 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   482 --AKTLNPYFPD---------VLLHFQALAAfqLGRYEEAVDLLLQrlaRNAVTDVSrALLAACYGHLGRFAEARAAWQE 550
Cdd:PRK11447  555 lpRAQWNSNIQElaqrlqsdqVLETANRLRD--SGKEAEAEALLRQ---QPPSTRID-LTLADWAQQRGDYAAARAAYQR 628

                  ....*..
gi 13472852   551 VLRLNPD 557
Cdd:PRK11447  629 VLTREPG 635
COG2956 COG2956
Predicted N-acetylglucosaminyl transferase [Carbohydrate transport and metabolism]
406-563 9.22e-04

Predicted N-acetylglucosaminyl transferase [Carbohydrate transport and metabolism]


Pssm-ID: 225504 [Multi-domain]  Cd Length: 389  Bit Score: 40.46  E-value: 9.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 406 QAEEVATRAVALDDSD---PWAHW--ALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFA 480
Cdd:COG2956 159 KAIDVAERLVKLGGQTyrvEIAQFycELAQQALASSDVDRARELLKKALQADKKCVRASIILGRVELAKGDYQKAVEALE 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 481 RAKTLNP-YFPDVLLHFQALAAfQLGRYEEAVDLLLQRLARN---AVTDVSRALLAACYGHlgrfAEARAAWQEVLRLNP 556
Cdd:COG2956 239 RVLEQNPeYLSEVLEMLYECYA-QLGKPAEGLNFLRRAMETNtgaDAELMLADLIELQEGI----DAAQAYLTRQLRRKP 313

                ....*..
gi 13472852 557 DYSLEYR 563
Cdd:COG2956 314 TMRGFHR 320
TPR_16 pfam13432
Tetratricopeptide repeat;
462-514 1.52e-03

Tetratricopeptide repeat;


Pssm-ID: 257757 [Multi-domain]  Cd Length: 65  Bit Score: 37.28  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13472852   462 LGEALYYSGRPEEALESFARAKTLNPYFPDVLLhFQALAAFQLGRYEEAVDLL 514
Cdd:pfam13432   3 LARALLRAGDYDDALAALEAALARAPLAAEALL-LLGEALLQQGRLAEAAALL 54
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
415-562 1.78e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 226428 [Multi-domain]  Cd Length: 620  Bit Score: 39.76  E-value: 1.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 415 VALDDSDPWAHWALAIAKLYTRRHD--GAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFAR-AKTLNPYFPD 491
Cdd:COG3914  58 IAINDVNPELLLAAFLSILLAPLADstLAFLAKRIPLSVNPENCPAVQNLAAALELDGLQFLALADISEiAEWLSPDNAE 137
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13472852 492 VLLHfqALAAFQLGRYEEavdlLLQRLARNAvTDVSRA--LLAACYGHLGRFAearAAWQEVLRLNPDYSLEY 562
Cdd:COG3914 138 FLGH--LIRFYQLGRYLK----LLGRTAEAE-LALERAvdLLPKYPRVLGALM---TARQEQCSWPEEAPTNL 200
COG4783 COG4783
Putative Zn-dependent protease, contains TPR repeats [General function prediction only]
405-486 2.30e-03

Putative Zn-dependent protease, contains TPR repeats [General function prediction only]


Pssm-ID: 227122 [Multi-domain]  Cd Length: 484  Bit Score: 39.31  E-value: 2.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 405 AQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEG-----------------HVILGEALY 467
Cdd:COG4783 357 KEAIERLKKALALDPNSPLLQLNLAQALLKGGKPQEAIRILNRYLFNDPEDPNGwdllaqayaelgnraeaLLARAEGYA 436
                        90
                ....*....|....*....
gi 13472852 468 YSGRPEEALESFARAKTLN 486
Cdd:COG4783 437 LAGRLEQAIIFLMRASQQV 455
PGA_TPR_OMP TIGR03939
poly-beta-1,6 N-acetyl-D-glucosamine export porin PgaA; Members of this protein family are the ...
437-566 2.43e-03

poly-beta-1,6 N-acetyl-D-glucosamine export porin PgaA; Members of this protein family are the poly-beta-1,6 N-acetyl-D-glucosamine (PGA) export porin PgaA of Gram-negative bacteria. There is no counterpart in the poly-beta-1,6 N-acetyl-D-glucosamine biosynthesis systems of Gram-positive bacteria such as Staphylococcus epidermidis. The PGA polysaccharide adhesin is a critical determinant of biofilm formation. The conserved C-terminal domain of this outer membrane protein is preceded by a variable number of TPR repeats.


Pssm-ID: 234406 [Multi-domain]  Cd Length: 800  Bit Score: 39.26  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   437 RHDGAIDEAERAIVLNPNfAEGHVILGEALYYSGRPEEALESFARAKTLNPYFPDVLLHfQALAAFQLGRYEEAVDLLLQ 516
Cdd:TIGR03939  68 RDKEAIDVCERYSPVGLP-ARVLEALAKAYRNEKQWDKALELYRKLLQRDPNNPDGLLG-LALTLADAGKDAEALKYLKE 145
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13472852   517 RLARNAvTDVSRAL-LAACYGHLGRFAEARAAWQEVLRLNPDYSLEYRRKV 566
Cdd:TIGR03939 146 YVARFP-TDAARYEaLAYVLRAAEDHLDALQAWQQALTLEPDNPEAALELY 195
TPR_12 pfam13424
Tetratricopeptide repeat;
452-520 3.34e-03

Tetratricopeptide repeat;


Pssm-ID: 257749 [Multi-domain]  Cd Length: 78  Bit Score: 36.20  E-value: 3.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13472852   452 NPNFAEGHVILGEALYYSGRPEEALESFARA----KTLNPYFPDVLLHFQALA--AFQLGRYEEAVDLLLQRLAR 520
Cdd:pfam13424   1 HPDLAAALNNLALVLRRLGDYDEALELLEKAleiaRELGEDHPETATALNNLArlYLALGDYDEALELLEKALEI 75
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking and secretion]
405-533 4.05e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking and secretion]


Pssm-ID: 227343 [Multi-domain]  Cd Length: 257  Bit Score: 37.80  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852 405 AQAEEVATRAVALDDSDPWAHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKt 484
Cdd:COG5010 117 GEAVSVLRKAARLAPTDWEAWNLLGAALDQLGRFDEARRAYRQALELAPNEPSIANNLGMSLLLRGDLEDAETLLLPAY- 195
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13472852 485 LNPYFPDVLLHFQALAAFQLGRYEEAVDLLLQRLARNAVTDVSRALLAA 533
Cdd:COG5010 196 LSPAADSRVRQNLALVVGLQGDFREAEDIAVQELLSEQAANNVAALRAA 244
BTAD smart01043
Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. ...
424-485 5.59e-03

Bacterial transcriptional activator domain; Found in the DNRI/REDD/AFSR family of regulators. This region of AFSR along with the C terminal region is capable of independently directing actinorhodin production. This family contains TPR repeats.


Pssm-ID: 198111 [Multi-domain]  Cd Length: 145  Bit Score: 36.51  E-value: 5.59e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13472852    424 AHWALAIAKLYTRRHDGAIDEAERAIVLNPNFAEGHVILGEALYYSGRPEEALESFARAKTL 485
Cdd:smart01043  63 ALEALAEALLALGRHEEALALLERLLALDPLRERLHRLLMRALYRAGRRAEALRAYRRLRRL 124
NARP1 pfam12569
NMDA receptor-regulated protein 1; This domain family is found in eukaryotes, and is ...
505-574 6.74e-03

NMDA receptor-regulated protein 1; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam07719, pfam00515. There is a single completely conserved residue L that may be functionally important. NARP1 is the mammalian homologue of a yeast N-terminal acetyltransferase that regulates entry into the G(0) phase of the cell cycle.


Pssm-ID: 257134 [Multi-domain]  Cd Length: 516  Bit Score: 38.00  E-value: 6.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13472852   505 GRYEEAVDLLLQrlARNAVTDVsRALL---AACYGHLGRFAEARAAWQEVLRLNPDYSLEYR--RKVLPYKNPAD 574
Cdd:pfam12569  18 GDLEEALEHLEE--KEKQIVDR-LAVMetrADYLLKLGRKEEAEATYRALLERNPENYDYYEglQKALGLEISSG 89
propeller_TolB TIGR02800
tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB ...
190-292 7.62e-03

tol-pal system beta propeller repeat protein TolB; Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear [Transport and binding proteins, Other, Cellular processes, Pathogenesis].


Pssm-ID: 234019 [Multi-domain]  Cd Length: 417  Bit Score: 37.63  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13472852   190 PATAAPPklsIAVLPFANMSGDAEQDYFADGISEdIITALSKLSQLFVIARNSSFTfkGQNVQVQEVG----TKLGVRHV 265
Cdd:TIGR02800  18 GGASALP---IAVAPFSNDGGGSPDANLGEDIAE-VIANDLRRSGLFSPVDKAGLP--SNPISESQVNpaawQALGADAL 91
                          90       100
                  ....*....|....*....|....*...
gi 13472852   266 LEGSVRKSGN-RVRITAQLIDAISGGHL 292
Cdd:TIGR02800  92 VVGSVTPNGNgRYTVRFRLYDVVSGQLQ 119
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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