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Conserved domains on  [gi|384871652|ref|NP_001245190|]
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histone demethylase UTY isoform 16 [Homo sapiens]

Protein Classification

KDM6 family histone demethylase( domain architecture ID 11421451)

KDM6 family histone demethylase, similar to lysine-specific demethylase 6A (KDM6A), also called UTX (ubiquitously-transcribed TPR protein on the X chromosome) that specifically demethylates 'Lys-27' of histone H3, and UTY (ubiquitously-transcribed TPR protein on the Y chromosome) that catalyzes trimethylated 'Lys-27' (H3K27me3) demethylation in histone H3

CATH:  1.25.40.10|2.60.120.10
EC:  1.14.11.-
Gene Ontology:  GO:0005515|GO:0032452|GO:0031490|GO:0046872
PubMed:  26059336|21153002|10517866|30708253|22404999|11165500|14697267|19478949
SCOP:  4001344|3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 1122-1230 2.96e-37

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


:

Pssm-ID: 396791  Cd Length: 114  Bit Score: 135.89  E-value: 2.96e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  1122 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 1194
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 384871652  1195 PVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNV 1230
Cdd:pfam02373   79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 127-408 7.50e-22

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 97.11  E-value: 7.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  127 AAFLYG---LGLVYFYYNAFHWAIKAFQDVLYVDPSfcrAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAE 203
Cdd:COG2956     5 VAAALGwyfKGLNYLLNGQPDKAIDLLEEALELDPE---TVEAHLALGNLYRRRGEYDRAIRIHQ-KLLERDP---DRAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  204 IQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVK-ATVLQQLG-WmhhnmdlvgDKAtkesyaIQYLQKSLEADPN 279
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDpdDAEALRLlAEIYEQEGdW---------EKA------IEVLERLLKLGPE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  280 SGQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKrcSNTSTLAARIK 359
Cdd:COG2956   143 NAHAYCELA-ELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQD--PDYLPALPRLA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 384871652  360 FLQAQLCNLPQ--SSLQNKTKLLPSIEEAWSLpipAELTSRQGAMNTAQQQ 408
Cdd:COG2956   220 ELYEKLGDPEEalELLRKALELDPSDDLLLAL---ADLLERKEGLEAALAL 267
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 1088-1152 6.19e-08

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


:

Pssm-ID: 214721  Cd Length: 58  Bit Score: 50.33  E-value: 6.19e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652   1088 QLHELTKLPafarvvSAGNLLTHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 1152
Cdd:smart00558    1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 72-158 1.18e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


:

Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 44.18  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG5010    72 ESLALLEQALQLDPN--NPELYYNLALLYSRSGDKDEAKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*..
gi 384871652  152 DVLYVDP 158
Cdd:COG5010   147 RALGTSP 153
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 1122-1230 2.96e-37

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 135.89  E-value: 2.96e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  1122 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 1194
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 384871652  1195 PVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNV 1230
Cdd:pfam02373   79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 127-408 7.50e-22

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 97.11  E-value: 7.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  127 AAFLYG---LGLVYFYYNAFHWAIKAFQDVLYVDPSfcrAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAE 203
Cdd:COG2956     5 VAAALGwyfKGLNYLLNGQPDKAIDLLEEALELDPE---TVEAHLALGNLYRRRGEYDRAIRIHQ-KLLERDP---DRAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  204 IQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVK-ATVLQQLG-WmhhnmdlvgDKAtkesyaIQYLQKSLEADPN 279
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDpdDAEALRLlAEIYEQEGdW---------EKA------IEVLERLLKLGPE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  280 SGQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKrcSNTSTLAARIK 359
Cdd:COG2956   143 NAHAYCELA-ELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQD--PDYLPALPRLA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 384871652  360 FLQAQLCNLPQ--SSLQNKTKLLPSIEEAWSLpipAELTSRQGAMNTAQQQ 408
Cdd:COG2956   220 ELYEKLGDPEEalELLRKALELDPSDDLLLAL---ADLLERKEGLEAALAL 267
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 1088-1152 6.19e-08

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 50.33  E-value: 6.19e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652   1088 QLHELTKLPafarvvSAGNLLTHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 1152
Cdd:smart00558    1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 82-296 3.26e-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: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 51.62  E-value: 3.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652    82 LKAEGKVESDFF-CQLGHFNLLLEDySKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSF 160
Cdd:TIGR02917  658 LKRALELKPDNTeAQIGLAQLLLAA-KRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSS 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   161 CRAKEIHLRLGLmfkvNTDYKSSLKHFQLALIDcNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTenlpAQVKA 240
Cdd:TIGR02917  737 QNAIKLHRALLA----SGNTAEAVKTLEAWLKT-HP---NDAVLRTALAELYLAQKDYDKAIKHYQTVVKK----APDNA 804

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652   241 TVLQQLGWMHHNMdlvgdkatKESYAIQYLQKSLEADPNSGQSWYFLGSVLYQQQN 296
Cdd:TIGR02917  805 VVLNNLAWLYLEL--------KDPRALEYAERALKLAPNIPAILDTLGWLLVEKGE 852
TPR_15 pfam13429
Tetratricopeptide repeat;
168-324 2.69e-05

Tetratricopeptide repeat;


Pssm-ID: 433199 [Multi-domain]  Cd Length: 279  Bit Score: 47.74  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   168 LRLGLMFKVNTDYKSSLKhfqlALI-DCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQ-- 244
Cdd:pfam13429   12 YALATLLYGQGDPRKALA----ALKeGAQTAPASDTEFWRTLADLAWALQQDDDARRAYRQLLASGKARADDYERLILll 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   245 ------------QLGWMH-HNMDL------VGDKAtKESYAIQYLQKSLEADPNSGQSWYFLG--SVLYQQQNQPMDALQ 303
Cdd:pfam13429   88 ydarpkdaarlsELGWRRfRSPRHlysalyLYERA-GDYDRLARLLASLEELPAAEQSPAFWLarAEYYRQTGEPDAALR 166

                          170       180
                   ....*....|....*....|....*...
gi 384871652   304 AYICAVQLDHGHAAA-----WM--DLGT 324
Cdd:pfam13429  167 DYRRALALAPASTELraallWFliDLGR 194
Mgr3-like cd24145
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ...
 167-407 3.53e-05

Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; Mgr3 (also called mitochondrial genome-required protein 3) is a component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. The supercomplex is composed of Mgr1, Mgr3, and Yme1. Mgr3, together with Mgr1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation.


Pssm-ID: 467945 [Multi-domain]  Cd Length: 307  Bit Score: 47.34  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  167 HLRLGLMFK-VNTDYKSSLKHFQLALIDCNPCTLS--NAE---IQFHIAHLYEtqrKYHSAKEAYEQLLQtenlpaqvka 240
Cdd:cd24145    10 ILRKALYYEsDKPDPQKALKYYKEALEQADELGMDpfSDEvtgIRIKIAEMLE---KLGMYKAAYEVLER---------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  241 TVLQQLGWmhhnmdlvgDKATKESYAIQYLQKSLEADPNSGQswyflgsvLYQQQNQPMDAL--QAYICAVQLDHGHAAA 318
Cdd:cd24145    77 LYLDCLRW---------TLKDDESERGHLIKRDLRISIKLGE--------LNKDSELGKWELreRLLKKAVEILLKLGEL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  319 WM----------DLGTLYESCNQPQDAIKCYLNAARSKR--CSNTSTLAarikflQAQLCNLPQSSLQnKTKLLPSIEEA 386
Cdd:cd24145   140 WMspsevgafleELATAYDLYGRFCLALPLYMQALSLKGqiLLSQANCH------SLVLMNNEAAELA-LHALRKPLSST 212

                         250       260
                  ....*....|....*....|.
gi 384871652  387 WSLPIPAELTSRQGAMNTAQQ 407
Cdd:cd24145   213 LIEASRLPQKSRDQLLEAALK 233
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 72-158 1.18e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 44.18  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG5010    72 ESLALLEQALQLDPN--NPELYYNLALLYSRSGDKDEAKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*..
gi 384871652  152 DVLYVDP 158
Cdd:COG5010   147 RALGTSP 153
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
 1122-1230 2.96e-37

JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain proteins may be protein hydroxylases that catalyze a novel histone modification. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation.


Pssm-ID: 396791  Cd Length: 114  Bit Score: 135.89  E-value: 2.96e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  1122 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 1194
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 384871652  1195 PVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNV 1230
Cdd:pfam02373   79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 127-408 7.50e-22

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 97.11  E-value: 7.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  127 AAFLYG---LGLVYFYYNAFHWAIKAFQDVLYVDPSfcrAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAE 203
Cdd:COG2956     5 VAAALGwyfKGLNYLLNGQPDKAIDLLEEALELDPE---TVEAHLALGNLYRRRGEYDRAIRIHQ-KLLERDP---DRAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  204 IQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVK-ATVLQQLG-WmhhnmdlvgDKAtkesyaIQYLQKSLEADPN 279
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDpdDAEALRLlAEIYEQEGdW---------EKA------IEVLERLLKLGPE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  280 SGQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARSKrcSNTSTLAARIK 359
Cdd:COG2956   143 NAHAYCELA-ELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQD--PDYLPALPRLA 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 384871652  360 FLQAQLCNLPQ--SSLQNKTKLLPSIEEAWSLpipAELTSRQGAMNTAQQQ 408
Cdd:COG2956   220 ELYEKLGDPEEalELLRKALELDPSDDLLLAL---ADLLERKEGLEAALAL 267
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
165-412 1.72e-18

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 86.60  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  165 EIHLRLGLMFKVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQvkATVLQ 244
Cdd:COG0457     9 EAYNNLGLAYRRLGRYEEAIEDYEKAL-ELDP---DDAEALYNLGLAYLRLGRYEEALADYEQALELD--PDD--AEALN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  245 QLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSGQSWYFLGSVLYQQQNQPmDALQAYICAVQLDHGHAAAWMDLGT 324
Cdd:COG0457    81 NLGLALQAL---GRYEE----ALEDYDKALELDPDDAEALYNLGLALLELGRYD-EAIEAYERALELDPDDADALYNLGI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  325 LYESCNQPQDAIKCYlNAARSKRCSNTSTLAARIKFLQAQLCNLPQSSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNT 404
Cdd:COG0457   153 ALEKLGRYEEALELL-EKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLL 231


                  ....*...
gi 384871652  405 AQQQSLSL 412
Cdd:COG0457   232 ALRLAALA 239
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 72-344 1.45e-17

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 84.40  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGKVESDFfcQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG2956    26 KAIDLLEEALELDPETVEAHL--ALGNLYRRRGEYDRAIRIHQKLLERDPD---RAEALLELAQDYLKAGLLDRAEELLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  152 DVLYVDPsfcRAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQT 231
Cdd:COG2956   101 KLLELDP---DDAEALRLLAEIYEQEGDWEKAIEVLE-RLLKLGP---ENAHAYCELAELYLEQGDYDEAIEALEKALKL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  232 EnlPAQVKATVLqqLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSGQSWYFLGSvLYQQQNQPMDALQAYICAVQL 311
Cdd:COG2956   174 D--PDCARALLL--LAELYLEQ---GDYEE----AIAALERALEQDPDYLPALPRLAE-LYEKLGDPEEALELLRKALEL 241

                         250       260       270
                  ....*....|....*....|....*....|...
gi 384871652  312 DHGhAAAWMDLGTLYESCNQPQDAIKCYLNAAR 344
Cdd:COG2956   242 DPS-DDLLLALADLLERKEGLEAALALLERQLR 273
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
201-342 6.79e-17

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 81.98  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  201 NAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNS 280
Cdd:COG0457     7 DAEAYNNLGLAYRRLGRYEEAIEDYEKALELD--PDDAEA--LYNLGLAYLRL---GRYEE----ALADYEQALELDPDD 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384871652  281 GQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNA 342
Cdd:COG0457    76 AEALNNLG-LALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERA 136
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
125-305 5.13e-16

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 79.28  E-value: 5.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  125 KNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDYKSSLKHFQLALiDCNPctlSNAEI 204
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEA---LYNLGLAYLRLGRYEEALADYEQAL-ELDP---DDAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  205 QFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSGQSW 284
Cdd:COG0457    79 LNNLGLALQALGRYEEALEDYDKALELD--PDDAEA--LYNLGLALLEL---GRYDE----AIEAYERALELDPDDADAL 147

                         170       180
                  ....*....|....*....|.
gi 384871652  285 YFLGsVLYQQQNQPMDALQAY 305
Cdd:COG0457   148 YNLG-IALEKLGRYEEALELL 167
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 186-393 4.46e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 73.87  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  186 HFQLALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVK--------ATVLQQLGWMHHNMDLVG 257
Cdd:COG3914     6 LLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALlalaageaAAAAAALLLLAALLELAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  258 DKATKESY---AIQYLQKSLEADPNSGQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQD 334
Cdd:COG3914    86 LLLQALGRyeeALALYRRALALNPDNAEALFNLG-NLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEE 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384871652  335 AIKCYLNAARsKRCSNTSTLAARIKFLQaQLCNLPQS--SLQNKTKLLPSIEEAWSLPIPA 393
Cdd:COG3914   165 AIAALRRALE-LDPDNAEALNNLGNALQ-DLGRLEEAiaAYRRALELDPDNADAHSNLLFA 223
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 266-344 5.36e-13

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 67.34  E-value: 5.36e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384871652  266 AIQYLQKSLEADPNSGQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAAR 344
Cdd:COG4235     2 AIARLRQALAANPNDAEGWLLLG-RAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALA 79
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 202-344 9.94e-13

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 66.75  E-value: 9.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  202 AEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSG 281
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELD--PDNPEA--FALLGEILLQL---GDLDE----AIVLLHEALELDPDEP 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384871652  282 QSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAAR 344
Cdd:COG4783    73 EARLNLG-LALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALE 134
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
72-303 3.56e-12

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 68.11  E-value: 3.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGKVESdfFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG0457    26 EAIEDYEKALELDPDDAEA--LYNLGLAYLRLGRYEEALADYEQALELDPD---DAEALNNLGLALQALGRYEEALEDYD 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  152 DVLYVDPSFCRAK----EIHLRLGlmfkvntDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQ 227
Cdd:COG0457   101 KALELDPDDAEALynlgLALLELG-------RYDEAIEAYERAL-ELDP---DDADALYNLGIALEKLGRYEEALELLEK 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652  228 LLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAIQYLQKSLEADPNSGQSWYFLGSVLYQQQNQPMDALQ 303
Cdd:COG0457   170 LEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYRA 245
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 72-277 5.59e-11

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 64.75  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGKVESdfFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG2956    94 RAEELLEKLLELDPDDAEA--LRLLAEIYEQEGDWEKAIEVLERLLKLGPE---NAHAYCELAELYLEQGDYDEAIEALE 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  152 DVLYVDPSFCRAK----EIHLRLGlmfkvntDYKSSLKHFQlALIDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQ 227
Cdd:COG2956   169 KALKLDPDCARALlllaELYLEQG-------DYEEAIAALE-RALEQDP---DYLPALPRLAELYEKLGDPEEALELLRK 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 384871652  228 LLQTENLPAQV--KATVLQQLGwmhhnmdlvGDKAtkesyAIQYLQKSLEAD 277
Cdd:COG2956   238 ALELDPSDDLLlaLADLLERKE---------GLEA-----ALALLERQLRRH 275
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 221-339 2.21e-10

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 59.63  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  221 AKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMDLVGDkatkesyAIQYLQKSLEADPNSGQSWYFLGSVLYQQQNQPmD 300
Cdd:COG4235     2 AIARLRQALAAN--PNDAEG--WLLLGRAYLRLGRYDE-------ALAAYEKALRLDPDNADALLDLAEALLAAGDTE-E 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 384871652  301 ALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCY 339
Cdd:COG4235    70 AEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAW 108
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 95-230 4.08e-10

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 59.44  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   95 QLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFcraKEIHLRLGLMF 174
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPD---NPEAFALLGEILLQLGDLDEAIVLLHEALELDPDE---PEARLNLGLAL 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652  175 KVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQ 230
Cdd:COG4783    83 LKAGDYDEALALLEKAL-KLDP---EHPEAYLRLARAYRALGRPDEAIAALEKALE 134
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 95-356 6.09e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 63.86  E-value: 6.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   95 QLGHFNLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMF 174
Cdd:COG3914    46 LLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEA---LFNLGNLL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  175 KVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMD 254
Cdd:COG3914   123 LALGRLEEALAALRRAL-ALNP---DFAEAYLNLGEALRRLGRLEEAIAALRRALELD--PDNAEA--LNNLGNALQDLG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  255 LVGDkatkesyAIQYLQKSLEADPNSGQSWYFLGSVLYQQ-QNQPMDALQAYICAVQLDhghAAAWMDLGTLYESCNQPQ 333
Cdd:COG3914   195 RLEE-------AIAAYRRALELDPDNADAHSNLLFALRQAcDWEVYDRFEELLAALARG---PSELSPFALLYLPDDDPA 264

                         250       260
                  ....*....|....*....|...
gi 384871652  334 DAIKCYLNAARSKRCSNTSTLAA 356
Cdd:COG3914   265 ELLALARAWAQLVAAAAAPELPP 287
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 266-345 1.05e-09

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 58.82  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  266 AIQYLQKSLEADPNSGQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAARS 345
Cdd:COG5010    73 SLALLEQALQLDPNNPELYYNLA-LLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGT 151
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 95-191 5.07e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 55.78  E-value: 5.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   95 QLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMF 174
Cdd:COG4235    22 LLGRAYLRLGRYDEALAAYEKALRLDPD---NADALLDLAEALLAAGDTEEAEELLERALALDPDNPEA---LYLLGLAA 95

                          90
                  ....*....|....*..
gi 384871652  175 KVNTDYKSSLKHFQLAL 191
Cdd:COG4235    96 FQQGDYAEAIAAWQKLL 112
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
266-344 6.49e-09

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 54.41  E-value: 6.49e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384871652  266 AIQYLQKSLEADPNSGQSWYFLGSVLYqQQNQPMDALQaYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAAR 344
Cdd:COG3063    11 AEEYYEKALELDPDNADALNNLGLLLL-EQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALE 87
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
274-344 3.03e-08

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.17  E-value: 3.03e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384871652  274 LEADPNSGQSWYFLGSVlYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAAR 344
Cdd:COG0457     1 LELDPDDAEAYNNLGLA-YRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALE 70
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
 1088-1152 6.19e-08

A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).


Pssm-ID: 214721  Cd Length: 58  Bit Score: 50.33  E-value: 6.19e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652   1088 QLHELTKLPafarvvSAGNLLTHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 1152
Cdd:smart00558    1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 201-305 1.21e-07

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 51.93  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  201 NAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAqvKATVLQQLGWMhhnmdLVGDKATKEsyAIQYLQKSLEADPNS 280
Cdd:COG4235    16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLD--PD--NADALLDLAEA-----LLAAGDTEE--AEELLERALALDPDN 84

                          90       100
                  ....*....|....*....|....*
gi 384871652  281 GQSWYFLGSVLYQQQnQPMDALQAY 305
Cdd:COG4235    85 PEALYLLGLAAFQQG-DYAEAIAAW 108
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 72-191 4.60e-07

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 50.58  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLIlkAEGKVESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG4783    22 EAEALLEKAL--ELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPD---EPEARLNLGLALLKAGDYDEALALLE 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 384871652  152 DVLYVDPSFcraKEIHLRLGLMFKVNTDYKSSLKHFQLAL 191
Cdd:COG4783    97 KALKLDPEH---PEAYLRLARAYRALGRPDEAIAALEKAL 133
TPR COG0790
TPR repeat [General function prediction only];
109-344 1.21e-06

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 51.47  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  109 ALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSfcrakEIHLRLGLMFK----VNTDYKSSL 184
Cdd:COG0790    13 AAAAALAAAAAAAGAAAAAAAAAAAAAALAAAAGAAAAAAAAAAAAAAGGA-----EAQYNLGLMYAegrgVPKDYEKAL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  185 KHFQLAlidcnpCTLSNAEIQFHIAHLYE----TQRKYHSAKEAYEQLLQTENLPAQVkatvlqQLGWMHHNMDLV-GDK 259
Cdd:COG0790    88 EWFEKA------AEQGDAEAQYNLGLMYEeglgVPQDYAKALEWYEKAAEQGDADAQY------NLGLLYLNGEGVpKDP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  260 ATkesyAIQYLQKSLEAdpNSGQSWYFLGSVLYQQQNQPMD---ALQAYICAVqlDHGHAAAWMDLGTLYESCNQ-PQD- 334
Cdd:COG0790   156 AK----AAEWYRKAAEQ--GDADAQYNLGVLYENGRGVPKDpakALEWYRKAA--EQGDADAQYNLGRLYLNGEGvEKDl 227

                         250
                  ....*....|..
gi 384871652  335 --AIKCYLNAAR 344
Cdd:COG0790   228 ekALRWLRKAAE 239
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 82-296 3.26e-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: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 51.62  E-value: 3.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652    82 LKAEGKVESDFF-CQLGHFNLLLEDySKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSF 160
Cdd:TIGR02917  658 LKRALELKPDNTeAQIGLAQLLLAA-KRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSS 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   161 CRAKEIHLRLGLmfkvNTDYKSSLKHFQLALIDcNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTenlpAQVKA 240
Cdd:TIGR02917  737 QNAIKLHRALLA----SGNTAEAVKTLEAWLKT-HP---NDAVLRTALAELYLAQKDYDKAIKHYQTVVKK----APDNA 804

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 384871652   241 TVLQQLGWMHHNMdlvgdkatKESYAIQYLQKSLEADPNSGQSWYFLGSVLYQQQN 296
Cdd:TIGR02917  805 VVLNNLAWLYLEL--------KDPRALEYAERALKLAPNIPAILDTLGWLLVEKGE 852
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 127-280 5.14e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 47.49  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  127 AAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDYKSSLKHFQLALIDcNPctlSNAEIQF 206
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEA---FALLGEILLQLGDLDEAIVLLHEALEL-DP---DEPEARL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384871652  207 HIAHLYETQRKYHSAKEAYEQLLQTEnlPAQvkATVLQQLGWMHHNMdlvGDKAtkesYAIQYLQKSLEADPNS 280
Cdd:COG4783    77 NLGLALLKAGDYDEALALLEKALKLD--PEH--PEAYLRLARAYRAL---GRPD----EAIAALEKALELDPDD 139
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
258-337 6.21e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 48.76  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  258 DKATKESYAIQYLQKSLEADPNSGQSWYFLGSVLYQQQNQPmDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIK 337
Cdd:COG4785    84 DSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYD-AALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIA 162
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 263-344 8.45e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 47.26  E-value: 8.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  263 ESYAIQYLQKSLEADPNSGQSWYFLGSVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNA 342
Cdd:COG5010    35 NNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKA 114


                  ..
gi 384871652  343 AR 344
Cdd:COG5010   115 LA 116
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 108-278 8.69e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 47.26  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  108 KALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGlmfkvntDYKSSLKHF 187
Cdd:COG5010     5 EGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLG-------DFEESLALL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  188 QLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvlqqlgwmHHNMDLVGDKATKESYAI 267
Cdd:COG5010    78 EQAL-QLDP---NNPELYYNLALLYSRSGDKDEAKEYYEKALALS--PDNPNA---------YSNLAALLLSLGQDDEAK 142

                         170
                  ....*....|.
gi 384871652  268 QYLQKSLEADP 278
Cdd:COG5010   143 AALQRALGTSP 153
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 100-234 1.76e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 46.49  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  100 NLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHW------AIKAFQDVLYVDPSFcraKEIHLRLGLM 173
Cdd:COG5010    21 RTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKlgdfeeSLALLEQALQLDPNN---PELYYNLALL 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384871652  174 FKVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENL 234
Cdd:COG5010    98 YSRSGDKDEAKEYYEKAL-ALSP---DNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPL 154
TPR_15 pfam13429
Tetratricopeptide repeat;
168-324 2.69e-05

Tetratricopeptide repeat;


Pssm-ID: 433199 [Multi-domain]  Cd Length: 279  Bit Score: 47.74  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   168 LRLGLMFKVNTDYKSSLKhfqlALI-DCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQ-- 244
Cdd:pfam13429   12 YALATLLYGQGDPRKALA----ALKeGAQTAPASDTEFWRTLADLAWALQQDDDARRAYRQLLASGKARADDYERLILll 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   245 ------------QLGWMH-HNMDL------VGDKAtKESYAIQYLQKSLEADPNSGQSWYFLG--SVLYQQQNQPMDALQ 303
Cdd:pfam13429   88 ydarpkdaarlsELGWRRfRSPRHlysalyLYERA-GDYDRLARLLASLEELPAAEQSPAFWLarAEYYRQTGEPDAALR 166

                          170       180
                   ....*....|....*....|....*...
gi 384871652   304 AYICAVQLDHGHAAA-----WM--DLGT 324
Cdd:pfam13429  167 DYRRALALAPASTELraallWFliDLGR 194
Mgr3-like cd24145
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ...
 167-407 3.53e-05

Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; Mgr3 (also called mitochondrial genome-required protein 3) is a component of the mitochondrial inner membrane i-AAA protease supercomplex, which degrades misfolded mitochondrial proteins. The supercomplex is composed of Mgr1, Mgr3, and Yme1. Mgr3, together with Mgr1, functions in an adapter complex that targets substrates to the i-AAA protease for degradation.


Pssm-ID: 467945 [Multi-domain]  Cd Length: 307  Bit Score: 47.34  E-value: 3.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  167 HLRLGLMFK-VNTDYKSSLKHFQLALIDCNPCTLS--NAE---IQFHIAHLYEtqrKYHSAKEAYEQLLQtenlpaqvka 240
Cdd:cd24145    10 ILRKALYYEsDKPDPQKALKYYKEALEQADELGMDpfSDEvtgIRIKIAEMLE---KLGMYKAAYEVLER---------- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  241 TVLQQLGWmhhnmdlvgDKATKESYAIQYLQKSLEADPNSGQswyflgsvLYQQQNQPMDAL--QAYICAVQLDHGHAAA 318
Cdd:cd24145    77 LYLDCLRW---------TLKDDESERGHLIKRDLRISIKLGE--------LNKDSELGKWELreRLLKKAVEILLKLGEL 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  319 WM----------DLGTLYESCNQPQDAIKCYLNAARSKR--CSNTSTLAarikflQAQLCNLPQSSLQnKTKLLPSIEEA 386
Cdd:cd24145   140 WMspsevgafleELATAYDLYGRFCLALPLYMQALSLKGqiLLSQANCH------SLVLMNNEAAELA-LHALRKPLSST 212

                         250       260
                  ....*....|....*....|.
gi 384871652  387 WSLPIPAELTSRQGAMNTAQQ 407
Cdd:cd24145   213 LIEASRLPQKSRDQLLEAALK 233
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 84-346 7.83e-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: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 47.39  E-value: 7.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652    84 AEGKVESD--FFCQLGHFNLLLEDYSKALSAYQRYYSLQAdywKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFC 161
Cdd:TIGR02917  355 ALGLDPDDpaALSLLGEAYLALGDFEKAAEYLAKATELDP---ENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELG 431

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   162 RAKEI----HLRLGLMFKVNTDYKSSLKHfqlalidcnpcTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQ 237
Cdd:TIGR02917  432 RADLLlilsYLRSGQFDKALAAAKKLEKK-----------QPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIE--PDF 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   238 VKATVLQQlgwmhhNMDLVGDKATKesyAIQYLQKSLEADPNSGQSWYFLGSvLYQQQNQPMDALQAYICAVQLDHGHAA 317
Cdd:TIGR02917  499 FPAAANLA------RIDIQEGNPDD---AIQRFEKVLTIDPKNLRAILALAG-LYLRTGNEEEAVAWLEKAAELNPQEIE 568

                          250       260       270
                   ....*....|....*....|....*....|..
gi 384871652   318 AWMDLGTLYESCNQPQDAI---KCYLNAARSK 346
Cdd:TIGR02917  569 PALALAQYYLGKGQLKKALailNEAADAAPDS 600
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 72-158 1.18e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 44.18  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG5010    72 ESLALLEQALQLDPN--NPELYYNLALLYSRSGDKDEAKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQ 146


                  ....*..
gi 384871652  152 DVLYVDP 158
Cdd:COG5010   147 RALGTSP 153
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 162-337 1.24e-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: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 46.62  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   162 RAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVk 239
Cdd:TIGR02917  599 DSPEAWLMLGRAQLAAGDLNKAVSSFK-KLLALQP---DSALALLLLADAYAVMKNYAKAITSLKRALELKpdNTEAQI- 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   240 atVLQQLgwmhhnmdLVGDKATKESYAI-QYLQKsleADPNSGQSWYFLGSvLYQQQNQPMDALQAYICAVQLDHGHAAA 318
Cdd:TIGR02917  674 --GLAQL--------LLAAKRTESAKKIaKSLQK---QHPKAALGFELEGD-LYLRQKDYPAAIQAYRKALKRAPSSQNA 739

                          170
                   ....*....|....*....
gi 384871652   319 wMDLGTLYESCNQPQDAIK 337
Cdd:TIGR02917  740 -IKLHRALLASGNTAEAVK 757
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
136-230 1.31e-04

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.08  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  136 VYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDYKSSLKhFQLALiDCNPctlSNAEIQFHIAHLYETQ 215
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADA---LNNLGLLLLEQGRYDEAIA-LEKAL-KLDP---NNAEALLNLAELLLEL 72

                          90
                  ....*....|....*
gi 384871652  216 RKYHSAKEAYEQLLQ 230
Cdd:COG3063    73 GDYDEALAYLERALE 87
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 105-191 2.65e-04

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 41.90  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  105 DYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSL 184
Cdd:COG1729     8 DYDEAIAAFKAFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGDYDKAR 87


                  ....*..
gi 384871652  185 KHFQLAL 191
Cdd:COG1729    88 ATLEELI 94
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 266-365 4.10e-04

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 41.52  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  266 AIQYLQKSLEADPNS---GQSWYFLGSVLYQQQNQPmDALQAYICAVQL--DHGHAA-AWMDLGTLYESCNQPQDAIKCY 339
Cdd:COG1729    12 AIAAFKAFLKRYPNSplaPDALYWLGEAYYALGDYD-EAAEAFEKLLKRypDSPKAPdALLKLGLSYLELGDYDKARATL 90

                          90       100
                  ....*....|....*....|....*.
gi 384871652  340 LNAArsKRCSNTStLAARIKFLQAQL 365
Cdd:COG1729    91 EELI--KKYPDSE-AAKEARARLARL 113
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 146-231 4.39e-04

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 41.13  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  146 AIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAY 225
Cdd:COG1729    12 AIAAFKAFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFE-KLLKRYPDSPKAPDALLKLGLSYLELGDYDKARATL 90


                  ....*.
gi 384871652  226 EQLLQT 231
Cdd:COG1729    91 EELIKK 96
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
93-163 5.11e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 42.98  E-value: 5.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384871652   93 FCQLGHFNLLLEDYSKALSAYQRYYSLQADYwknAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRA 163
Cdd:COG4785   110 YNNRGLAYLLLGDYDAALEDFDRALELDPDY---AYAYLNRGIALYYLGRYELAIADLEKALELDPNDPER 177
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 146-280 5.63e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  146 AIKAFQDVLYVDPSFcraKEIHLRLGLMFKVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAY 225
Cdd:COG4235     2 AIARLRQALAANPND---AEGWLLLGRAYLRLGRYDEALAAYEKAL-RLDP---DNADALLDLAEALLAAGDTEEAEELL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 384871652  226 EQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNS 280
Cdd:COG4235    75 ERALALD--PDNPEA--LYLLGLAAFQQ---GDYAE----AIAAWQKLLALLPAD 118
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 179-280 1.25e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 39.97  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  179 DYKSSLKHFQlALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKA-TVLQQLGWMHHNMdlvG 257
Cdd:COG1729     8 DYDEAIAAFK-AFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRY--PDSPKApDALLKLGLSYLEL---G 81

                          90       100
                  ....*....|....*....|...
gi 384871652  258 DKATkesyAIQYLQKSLEADPNS 280
Cdd:COG1729    82 DYDK----ARATLEELIKKYPDS 100
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
101-191 1.56e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.00  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  101 LLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIkAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDY 180
Cdd:COG3063     3 LKLGDLEEAEEYYEKALELDPD---NADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEA---LLNLAELLLELGDY 75

                          90
                  ....*....|.
gi 384871652  181 KSSLKHFQLAL 191
Cdd:COG3063    76 DEALAYLERAL 86
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 201-344 1.82e-03

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 42.20  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  201 NAEIQFHIAHLYETQRKYHSAKEAYEQLLQtenlpAQVKATVLQQLGwmhhnmDLVGDKATKesyAIQYLQKSLEADPNS 280
Cdd:COG3071   192 DPELAAAYARALIALGDHDEAERLLREALK-----RQWDPRLVRLYG------RLQGGDPAK---QLKRAEKWLKKHPND 257

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384871652  281 GQSWYFLGsVLYQQQNQPMDALQAYICAVQLDHGhAAAWMDLGTLYESCNQPQDAIKCYLNAAR 344
Cdd:COG3071   258 PDLLLALG-RLCLRNQLWGKAREYLEAALALRPS-AEAYAELARLLEQLGDPEEAAEHYRKALA 319
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 266-367 1.97e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 41.85  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  266 AIQYLQKSLEADPNSGQSWYFLGSvLYQQQNQPMDALQAYICAVQLD-HGHAAAWMDLGTLyescNQPQDAIKCY----- 339
Cdd:cd24142    19 ALKFLQRALELEPNNVEALELLGE-ILLELGDVEEAREVLLRAIELDpDGGYEKYLYLGQL----SGGEEALQYYekgie 93

                          90       100
                  ....*....|....*....|....*....
gi 384871652  340 -LNAARSKRCSNTSTLAARIKFLQAQLCN 367
Cdd:cd24142    94 iLEEELQALQAASAEAEEEAEELKRKLSS 122
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
291-337 2.18e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.61  E-value: 2.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 384871652  291 LYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIK 337
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA 47
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
166-279 2.89e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.61  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  166 IHLRLGlmfkvntDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAkEAYEQLLQTEnlPAQVKAtvLQQ 245
Cdd:COG3063     1 LYLKLG-------DLEEAEEYYEKAL-ELDP---DNADALNNLGLLLLEQGRYDEA-IALEKALKLD--PNNAEA--LLN 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 384871652  246 LGWMHHNMdlvGDKATkesyAIQYLQKSLEADPN 279
Cdd:COG3063    65 LAELLLEL---GDYDE----ALAYLERALELDPS 91
TPR_17 pfam13431
Tetratricopeptide repeat;
269-303 3.97e-03

Tetratricopeptide repeat;


Pssm-ID: 433201 [Multi-domain]  Cd Length: 34  Bit Score: 36.37  E-value: 3.97e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 384871652   269 YLQKSLEADPNSGQSWYFLGsVLYQQQNQPMDALQ 303
Cdd:pfam13431    1 LYLKALELDPNNADAYYNLA-VLLLELGQSETALQ 34
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 95-295 3.99e-03

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: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.61  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652    95 QLGHFNLLLEDYSKALSAYQRyySLQADYWKNAAFLYgLGLVYFYYNAFHWAIKAFQDVlYVDPSFCRAkEIHLRLGLMF 174
Cdd:TIGR02917   61 LLGKIYLALGDYAAAEKELRK--ALSLGYPKNQVLPL-LARAYLLQGKFQQVLDELPGK-TLLDDEGAA-ELLALRGLAY 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   175 KVNTDYKSSLKHFQLALIDcNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKATVLQ-QLGWMHHNM 253
Cdd:TIGR02917  136 LGLGQLELAQKSYEQALAI-DP---RSLYAKLGLAQLALAENRFDEARALIDEVLTAD--PGNVDALLLKgDLLLSLGNI 209

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 384871652   254 DLvgdkatkesyAIQYLQKSLEADPNSGQSWYFLGSVLYQQQ 295
Cdd:TIGR02917  210 EL----------ALAAYRKAIALRPNNIAVLLALATILIEAG 241
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
72-162 4.57e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.84  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALsAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG3063    10 EAEEYYEKALELDPD--NADALNNLGLLLLEQGRYDEAI-ALEKALKLDPN---NAEALLNLAELLLELGDYDEALAYLE 83

                          90
                  ....*....|.
gi 384871652  152 DVLYVDPSFCR 162
Cdd:COG3063    84 RALELDPSALR 94
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 70-238 4.97e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 41.13  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652   70 LGKAVRCYESLILKAEGKVEsdFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKA 149
Cdd:COG3914   128 LEEALAALRRALALNPDFAE--AYLNLGEALRRLGRLEEAIAALRRALELDPD---NAEALNNLGNALQDLGRLEEAIAA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871652  150 FQDVLYVDPSFCRAkeIHLRLGLMFKVNTDYKSSLKHFQLALIDCNPCTLSNaeiqFHIAHLY----ETQRKYHsakEAY 225
Cdd:COG3914   203 YRRALELDPDNADA--HSNLLFALRQACDWEVYDRFEELLAALARGPSELSP----FALLYLPdddpAELLALA---RAW 273

                         170
                  ....*....|...
gi 384871652  226 EQLLQTENLPAQV 238
Cdd:COG3914   274 AQLVAAAAAPELP 286
TPR_1 pfam00515
Tetratricopeptide repeat;
127-160 6.10e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.47  E-value: 6.10e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 384871652   127 AAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSF 160
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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