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Conserved domains on  [gi|384871658|ref|NP_001245193|]
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histone demethylase UTY isoform 19 [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

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 ...
1109-1217 3.62e-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: 3.62e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  1109 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 1181
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 384871658  1182 PVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNV 1217
Cdd:pfam02373   79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
127-424 1.50e-20

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: 93.26  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  127 AAFLYG---LGLVYFYYNAFHWAIKAFQDVLYVDPSfcrAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAE 203
Cdd:COG2956     5 VAAALGwyfKGLNYLLNGQPDKAIDLLEEALELDPE---TVEAHLALGNLYRRRGEYDRAIRIHQ-KLLERDP---DRAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  204 IQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVK-ATVLQQLG-WmhhnmdlvgDKAtkesyaIQYLQKSLEADPN 279
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDpdDAEALRLlAEIYEQEGdW---------EKA------IEVLERLLKLGPE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  280 SgqswyflgrqsidkseasADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNA 359
Cdd:COG2956   143 N------------------AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERA 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384871658  360 ARSKrcSNTSTLAARIKFLQAQLCNLPQ--SSLQNKTKLLPSIEEAWSLpipAELTSRQGAMNTAQQ 424
Cdd:COG2956   205 LEQD--PDYLPALPRLAELYEKLGDPEEalELLRKALELDPSDDLLLAL---ADLLERKEGLEAALA 266
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
1075-1139 6.50e-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: 6.50e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871658   1075 QLHELTKLPafarvvSAGNLLTHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 1139
Cdd:smart00558    1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
72-158 1.17e-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: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG5010    72 ESLALLEQALQLDPN--NPELYYNLALLYSRSGDKDEAKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQ 146

                  ....*..
gi 384871658  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 ...
1109-1217 3.62e-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: 3.62e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  1109 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 1181
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 384871658  1182 PVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNV 1217
Cdd:pfam02373   79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
127-424 1.50e-20

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: 93.26  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  127 AAFLYG---LGLVYFYYNAFHWAIKAFQDVLYVDPSfcrAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAE 203
Cdd:COG2956     5 VAAALGwyfKGLNYLLNGQPDKAIDLLEEALELDPE---TVEAHLALGNLYRRRGEYDRAIRIHQ-KLLERDP---DRAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  204 IQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVK-ATVLQQLG-WmhhnmdlvgDKAtkesyaIQYLQKSLEADPN 279
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDpdDAEALRLlAEIYEQEGdW---------EKA------IEVLERLLKLGPE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  280 SgqswyflgrqsidkseasADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNA 359
Cdd:COG2956   143 N------------------AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERA 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384871658  360 ARSKrcSNTSTLAARIKFLQAQLCNLPQ--SSLQNKTKLLPSIEEAWSLpipAELTSRQGAMNTAQQ 424
Cdd:COG2956   205 LEQD--PDYLPALPRLAELYEKLGDPEEalELLRKALELDPSDDLLLAL---ADLLERKEGLEAALA 266
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
1075-1139 6.50e-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: 6.50e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871658   1075 QLHELTKLPafarvvSAGNLLTHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 1139
Cdd:smart00558    1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
82-283 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658    82 LKAEGKVESDFF-CQLGHFNLLLEDySKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSF 160
Cdd:TIGR02917  658 LKRALELKPDNTeAQIGLAQLLLAA-KRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSS 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   161 CRAKEIHLRLGLmfkvNTDYKSSLKHFQLALIDcNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTenlpAQVKA 240
Cdd:TIGR02917  737 QNAIKLHRALLA----SGNTAEAVKTLEAWLKT-HP---NDAVLRTALAELYLAQKDYDKAIKHYQTVVKK----APDNA 804
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 384871658   241 TVLQQLGWMHHNMdlvgdkatKESYAIQYLQKSLEADPNSGQS 283
Cdd:TIGR02917  805 VVLNNLAWLYLEL--------KDPRALEYAERALKLAPNIPAI 839
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
72-158 1.17e-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: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG5010    72 ESLALLEQALQLDPN--NPELYYNLALLYSRSGDKDEAKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQ 146

                  ....*..
gi 384871658  152 DVLYVDP 158
Cdd:COG5010   147 RALGTSP 153
Mgr3-like cd24145
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ...
167-426 3.83e-04

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: 44.26  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  167 HLRLGLMFK-VNTDYKSSLKHFQLALIDCNPCTLS--NAE---IQFHIAHLYEtqrKYHSAKEAYEQLLQtenlpaqvka 240
Cdd:cd24145    10 ILRKALYYEsDKPDPQKALKYYKEALEQADELGMDpfSDEvtgIRIKIAEMLE---KLGMYKAAYEVLER---------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  241 TVLQQLGWmhhnmdlvgDKATKESYAIQYLQKSLeadpnsgqswyflgRQSIdkseasadtwcSIGVLYQQQNQPMDAL- 319
Cdd:cd24145    77 LYLDCLRW---------TLKDDESERGHLIKRDL--------------RISI-----------KLGELNKDSELGKWELr 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  320 -QAYICAVQLDHGHAAAWM----------DLGTLYESCNQPQDAIKCYLNAARSKR--CSNTSTLAarikflQAQLCNLP 386
Cdd:cd24145   123 eRLLKKAVEILLKLGELWMspsevgafleELATAYDLYGRFCLALPLYMQALSLKGqiLLSQANCH------SLVLMNNE 196
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 384871658  387 QSSLQnKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNG 426
Cdd:cd24145   197 AAELA-LHALRKPLSSTLIEASRLPQKSRDQLLEAALKWA 235
TPR_1 pfam00515
Tetratricopeptide repeat;
127-160 6.05e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.47  E-value: 6.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 384871658   127 AAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSF 160
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
 
Name Accession Description Interval E-value
JmjC pfam02373
JmjC domain, hydroxylase; The JmjC domain belongs to the Cupin superfamily. JmjC-domain ...
1109-1217 3.62e-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: 3.62e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  1109 QLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEDYWGVLNDFCEKNN-------LNFLMSSWWPnlEDLYEANV 1181
Cdd:pfam02373    1 WLYLGMPFSTTPWHIEDQGLYSINYLHFGAPKVWYIIPPEYAEKFEKVLSDHFggeqpddLLHLNTIISP--KQLRENGI 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 384871658  1182 PVYRFIQRPGDLVWINAGTVHWVQAVGWCNNIAWNV 1217
Cdd:pfam02373   79 PVYRFVQKPGEFVFTFPGWYHQVFNLGFNIAEAVNF 114
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
127-424 1.50e-20

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: 93.26  E-value: 1.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  127 AAFLYG---LGLVYFYYNAFHWAIKAFQDVLYVDPSfcrAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAE 203
Cdd:COG2956     5 VAAALGwyfKGLNYLLNGQPDKAIDLLEEALELDPE---TVEAHLALGNLYRRRGEYDRAIRIHQ-KLLERDP---DRAE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  204 IQFHIAHLYETQRKYHSAKEAYEQLLQTE--NLPAQVK-ATVLQQLG-WmhhnmdlvgDKAtkesyaIQYLQKSLEADPN 279
Cdd:COG2956    78 ALLELAQDYLKAGLLDRAEELLEKLLELDpdDAEALRLlAEIYEQEGdW---------EKA------IEVLERLLKLGPE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  280 SgqswyflgrqsidkseasADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNA 359
Cdd:COG2956   143 N------------------AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERA 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384871658  360 ARSKrcSNTSTLAARIKFLQAQLCNLPQ--SSLQNKTKLLPSIEEAWSLpipAELTSRQGAMNTAQQ 424
Cdd:COG2956   205 LEQD--PDYLPALPRLAELYEKLGDPEEalELLRKALELDPSDDLLLAL---ADLLERKEGLEAALA 266
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
201-423 6.29e-17

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 81.98  E-value: 6.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  201 NAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNS 280
Cdd:COG0457     7 DAEAYNNLGLAYRRLGRYEEAIEDYEKALELD--PDDAEA--LYNLGLAYLRL---GRYEE----ALADYEQALELDPDD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  281 GQSWYFLG----------------RQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYE 344
Cdd:COG0457    76 AEALNNLGlalqalgryeealedyDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384871658  345 SCNQPQDAIKCYlNAARSKRCSNTSTLAARIKFLQAQLCNLPQSSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQ 423
Cdd:COG0457   156 KLGRYEEALELL-EKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
72-361 5.76e-16

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: 79.77  E-value: 5.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGKVESDFfcQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG2956    26 KAIDLLEEALELDPETVEAHL--ALGNLYRRRGEYDRAIRIHQKLLERDPD---RAEALLELAQDYLKAGLLDRAEELLE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  152 DVLYVDPsfcRAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQT 231
Cdd:COG2956   101 KLLELDP---DDAEALRLLAEIYEQEGDWEKAIEVLE-RLLKLGP---ENAHAYCELAELYLEQGDYDEAIEALEKALKL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  232 EnlPAQVKATVLqqLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSGQSWYFLGRqsidkseasadtwcsigvLYQQ 311
Cdd:COG2956   174 D--PDCARALLL--LAELYLEQ---GDYEE----AIAALERALEQDPDYLPALPRLAE------------------LYEK 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 384871658  312 QNQPMDALQAYICAVQLDHGhAAAWMDLGTLYESCNQPQDAIKCYLNAAR 361
Cdd:COG2956   225 LGDPEEALELLRKALELDPS-DDLLLALADLLERKEGLEAALALLERQLR 273
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
125-344 1.07e-14

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 75.43  E-value: 1.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  125 KNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDYKSSLKHFQLALiDCNPctlSNAEI 204
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEA---LYNLGLAYLRLGRYEEALADYEQAL-ELDP---DDAEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  205 QFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSGQSW 284
Cdd:COG0457    79 LNNLGLALQALGRYEEALEDYDKALELD--PDDAEA--LYNLGLALLEL---GRYDE----AIEAYERALELDPDDADAL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384871658  285 YFLG---RQSIDKSEASADtwcsigvlYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYE 344
Cdd:COG0457   148 YNLGialEKLGRYEEALEL--------LEKLEAAALAALLAAALGEAALALAAAEVLLALLLA 202
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
202-410 1.26e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 72.33  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  202 AEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAI-QYLQKSLEADPNS 280
Cdd:COG3914    15 AALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALlELAALLLQALGRY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  281 GQSWYFLgRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAA 360
Cdd:COG3914    95 EEALALY-RRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRAL 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 384871658  361 RsKRCSNTSTLAARIKFLQaQLCNLPQS--SLQNKTKLLPSIEEAWSLPIPA 410
Cdd:COG3914   174 E-LDPDNAEALNNLGNALQ-DLGRLEEAiaAYRRALELDPDNADAHSNLLFA 223
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
266-356 4.87e-12

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: 64.64  E-value: 4.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  266 AIQYLQKSLEADPNSGQSWYFLGR----------------QSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLD 329
Cdd:COG4235     2 AIARLRQALAANPNDAEGWLLLGRaylrlgrydealaayeKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD 81
                          90       100
                  ....*....|....*....|....*..
gi 384871658  330 HGHAAAWMDLGTLYESCNQPQDAIKCY 356
Cdd:COG4235    82 PDNPEALYLLGLAAFQQGDYAEAIAAW 108
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
72-277 1.23e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.18  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGKVESdfFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG0457    26 EAIEDYEKALELDPDDAEA--LYNLGLAYLRLGRYEEALADYEQALELDPD---DAEALNNLGLALQALGRYEEALEDYD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  152 DVLYVDPSFCRAK----EIHLRLGlmfkvntDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQ 227
Cdd:COG0457   101 KALELDPDDAEALynlgLALLELG-------RYDEAIEAYERAL-ELDP---DDADALYNLGIALEKLGRYEEALELLEK 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 384871658  228 LLQTENLPAQVKATVLQQLGWMHHNMDLVGDKATKESYAIQYLQKSLEAD 277
Cdd:COG0457   170 LEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAAL 219
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
72-277 5.53e-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: 5.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGKVESdfFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG2956    94 RAEELLEKLLELDPDDAEA--LRLLAEIYEQEGDWEKAIEVLERLLKLGPE---NAHAYCELAELYLEQGDYDEAIEALE 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  152 DVLYVDPSFCRAK----EIHLRLGlmfkvntDYKSSLKHFQlALIDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQ 227
Cdd:COG2956   169 KALKLDPDCARALlllaELYLEQG-------DYEEAIAALE-RALEQDP---DYLPALPRLAELYEKLGDPEEALELLRK 237
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 384871658  228 LLQTENLPAQV--KATVLQQLGwmhhnmdlvGDKAtkesyAIQYLQKSLEAD 277
Cdd:COG2956   238 ALELDPSDDLLlaLADLLERKE---------GLEA-----ALALLERQLRRH 275
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
202-361 1.47e-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: 60.59  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  202 AEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSG 281
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELD--PDNPEA--FALLGEILLQL---GDLDE----AIVLLHEALELDPDEP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  282 QSWYFLGRqsidkseasadtwcsigvLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNAAR 361
Cdd:COG4783    73 EARLNLGL------------------ALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALE 134
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
95-230 4.04e-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: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   95 QLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFcraKEIHLRLGLMF 174
Cdd:COG4783     9 ALAQALLLAGDYDEAEALLEKALELDPD---NPEAFALLGEILLQLGDLDEAIVLLHEALELDPDE---PEARLNLGLAL 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 384871658  175 KVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQ 230
Cdd:COG4783    83 LKAGDYDEALALLEKAL-KLDP---EHPEAYLRLARAYRALGRPDEAIAALEKALE 134
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
95-191 5.02e-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: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   95 QLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMF 174
Cdd:COG4235    22 LLGRAYLRLGRYDEALAAYEKALRLDPD---NADALLDLAEALLAAGDTEEAEELLERALALDPDNPEA---LYLLGLAA 95
                          90
                  ....*....|....*..
gi 384871658  175 KVNTDYKSSLKHFQLAL 191
Cdd:COG4235    96 FQQGDYAEAIAAWQKLL 112
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
162-329 4.35e-08

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: 53.66  E-value: 4.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  162 RAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAt 241
Cdd:COG4783     2 ACAEALYALAQALLLAGDYDEAEALLE-KALELDP---DNPEAFALLGEILLQLGDLDEAIVLLHEALELD--PDEPEA- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  242 vLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNSGQSWYFLGRqsidkseasadtwcsigvLYQQQNQPMDALQA 321
Cdd:COG4783    75 -RLNLGLALLKA---GDYDE----ALALLEKALKLDPEHPEAYLRLAR------------------AYRALGRPDEAIAA 128

                  ....*...
gi 384871658  322 YICAVQLD 329
Cdd:COG4783   129 LEKALELD 136
JmjC smart00558
A domain family that is part of the cupin metalloenzyme superfamily; Probable enzymes, but of ...
1075-1139 6.50e-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: 6.50e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384871658   1075 QLHELTKLPafarvvSAGNLLTHVGHTILGMNT-VQLYMKVPGSRTPGHQENNNfcSVNINIGPGD 1139
Cdd:smart00558    1 QLWNLAKLP------FKLNLLSDLPEDIPGPDVgPYLYMGMAGSTTPWHIDDYD--LVNYLHQGAG 58
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
266-362 1.91e-07

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: 52.27  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  266 AIQYLQKSLEADPNSGQSWYFLGrqsidkseasadtwcsigVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYES 345
Cdd:COG5010    73 SLALLEQALQLDPNNPELYYNLA------------------LLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS 134
                          90
                  ....*....|....*..
gi 384871658  346 CNQPQDAIKCYLNAARS 362
Cdd:COG5010   135 LGQDDEAKAALQRALGT 151
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
72-191 4.55e-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: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLIlkAEGKVESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG4783    22 EAEALLEKAL--ELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPD---EPEARLNLGLALLKAGDYDEALALLE 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 384871658  152 DVLYVDPSFcraKEIHLRLGLMFKVNTDYKSSLKHFQLAL 191
Cdd:COG4783    97 KALKLDPEH---PEAYLRLARAYRALGRPDEAIAALEKAL 133
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
266-361 7.43e-07

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 48.63  E-value: 7.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  266 AIQYLQKSLEADPNSGQSWYFLGRqsidkseasadtwcsigvLYQQQNQPMDALQaYICAVQLDHGHAAAWMDLGTLYES 345
Cdd:COG3063    11 AEEYYEKALELDPDNADALNNLGL------------------LLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLE 71
                          90
                  ....*....|....*.
gi 384871658  346 CNQPQDAIKCYLNAAR 361
Cdd:COG3063    72 LGDYDEALAYLERALE 87
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
127-280 5.09e-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: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  127 AAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDYKSSLKHFQlALIDCNPctlSNAEIQF 206
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEA---FALLGEILLQLGDLDEAIVLLH-EALELDP---DEPEARL 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384871658  207 HIAHLYETQRKYHSAKEAYEQLLQTEnlPAQvkATVLQQLGWMHHNMdlvGDKAtkesYAIQYLQKSLEADPNS 280
Cdd:COG4783    77 NLGLALLKAGDYDEALALLEKALKLD--PEH--PEAYLRLARAYRAL---GRPD----EAIAALEKALELDPDD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
250-361 5.93e-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: 47.65  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  250 HHNMDLVGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLD 329
Cdd:COG5010     5 EGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLD 84
                          90       100       110
                  ....*....|....*....|....*....|..
gi 384871658  330 HGHAAAWMDLGTLYESCNQPQDAIKCYLNAAR 361
Cdd:COG5010    85 PNNPELYYNLALLYSRSGDKDEAKEYYEKALA 116
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
108-278 8.61e-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: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  108 KALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGlmfkvntDYKSSLKHF 187
Cdd:COG5010     5 EGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLG-------DFEESLALL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  188 QLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKAtvlqqlgwmHHNMDLVGDKATKESYAI 267
Cdd:COG5010    78 EQAL-QLDP---NNPELYYNLALLYSRSGDKDEAKEYYEKALALS--PDNPNA---------YSNLAALLLSLGQDDEAK 142
                         170
                  ....*....|.
gi 384871658  268 QYLQKSLEADP 278
Cdd:COG5010   143 AALQRALGTSP 153
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
100-234 1.74e-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: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  100 NLLLEDYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHW------AIKAFQDVLYVDPSFcraKEIHLRLGLM 173
Cdd:COG5010    21 RTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKlgdfeeSLALLEQALQLDPNN---PELYYNLALL 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384871658  174 FKVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENL 234
Cdd:COG5010    98 YSRSGDKDEAKEYYEKAL-ALSP---DNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPL 154
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
201-322 2.20e-05

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: 45.38  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  201 NAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAqvKATVLQQLGWMhhnmdLVGDKATKEsyAIQYLQKSLEADPNS 280
Cdd:COG4235    16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLD--PD--NADALLDLAEA-----LLAAGDTEE--AEELLERALALDPDN 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 384871658  281 GQSWYFLGRqsidkseasadtwcsigvLYQQQNQPMDALQAY 322
Cdd:COG4235    85 PEALYLLGL------------------AAFQQGDYAEAIAAW 108
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
82-283 1.12e-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: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658    82 LKAEGKVESDFF-CQLGHFNLLLEDySKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSF 160
Cdd:TIGR02917  658 LKRALELKPDNTeAQIGLAQLLLAA-KRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSS 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   161 CRAKEIHLRLGLmfkvNTDYKSSLKHFQLALIDcNPctlSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTenlpAQVKA 240
Cdd:TIGR02917  737 QNAIKLHRALLA----SGNTAEAVKTLEAWLKT-HP---NDAVLRTALAELYLAQKDYDKAIKHYQTVVKK----APDNA 804
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 384871658   241 TVLQQLGWMHHNMdlvgdkatKESYAIQYLQKSLEADPNSGQS 283
Cdd:TIGR02917  805 VVLNNLAWLYLEL--------KDPRALEYAERALKLAPNIPAI 839
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
72-158 1.17e-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: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG5010    72 ESLALLEQALQLDPN--NPELYYNLALLYSRSGDKDEAKEYYEKALALSPD---NPNAYSNLAALLLSLGQDDEAKAALQ 146

                  ....*..
gi 384871658  152 DVLYVDP 158
Cdd:COG5010   147 RALGTSP 153
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
136-230 1.30e-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: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  136 VYFYYNAFHWAIKAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDYKSSLKhFQLALiDCNPctlSNAEIQFHIAHLYETQ 215
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADA---LNNLGLLLLEQGRYDEAIA-LEKAL-KLDP---NNAEALLNLAELLLEL 72
                          90
                  ....*....|....*
gi 384871658  216 RKYHSAKEAYEQLLQ 230
Cdd:COG3063    73 GDYDEALAYLERALE 87
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
146-294 1.76e-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: 42.69  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  146 AIKAFQDVLYVDPSFcraKEIHLRLGLMFKVNTDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAKEAY 225
Cdd:COG4235     2 AIARLRQALAANPND---AEGWLLLGRAYLRLGRYDEALAAYEKAL-RLDP---DNADALLDLAEALLAAGDTEEAEELL 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384871658  226 EQLLQTEnlPAQVKAtvLQQLGWMHHNMdlvGDKATkesyAIQYLQKSLEADPNsGQSWYFLgRQSIDK 294
Cdd:COG4235    75 ERALALD--PDNPEA--LYLLGLAAFQQ---GDYAE----AIAAWQKLLALLPA-DAPARLL-EASIAE 130
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
105-356 2.49e-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: 45.46  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   105 DYSKALSAYQRYYSLQADYWkNAAFLygLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKE----IHLRLGLMfkvnTDY 180
Cdd:TIGR02917  276 NYEDARETLQDALKSAPEYL-PALLL--AGASEYQLGNLEQAYQYLNQILKYAPNSHQARRllasIQLRLGRV----DEA 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   181 KSSLKHFqLALIDCNPCTLSNAEIqfhiAHLyeTQRKYHSAKEAYEQLlqTENLPAQVKATVLQQLGWMHHNmdlvgdka 260
Cdd:TIGR02917  349 IATLSPA-LGLDPDDPAALSLLGE----AYL--ALGDFEKAAEYLAKA--TELDPENAAARTQLGISKLSQG-------- 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   261 tKESYAIQYLQKSLEADPNSGQS-----WYFLGRQSIDKSEASADTWCS-----------IGVLYQQQNQPMDALQAYIC 324
Cdd:TIGR02917  412 -DPSEAIADLETAAQLDPELGRAdllliLSYLRSGQFDKALAAAKKLEKkqpdnaslhnlLGAIYLGKGDLAKAREAFEK 490
                          250       260       270
                   ....*....|....*....|....*....|..
gi 384871658   325 AVQLDHGHAAAWMDLGTLYESCNQPQDAIKCY 356
Cdd:TIGR02917  491 ALSIEPDFFPAAANLARIDIQEGNPDDAIQRF 522
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
105-191 2.63e-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: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  105 DYSKALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSL 184
Cdd:COG1729     8 DYDEAIAAFKAFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLKLGLSYLELGDYDKAR 87

                  ....*..
gi 384871658  185 KHFQLAL 191
Cdd:COG1729    88 ATLEELI 94
Mgr3-like cd24145
Mitochondrial inner membrane i-AAA protease supercomplex subunit Mgr3 and similar proteins; ...
167-426 3.83e-04

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: 44.26  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  167 HLRLGLMFK-VNTDYKSSLKHFQLALIDCNPCTLS--NAE---IQFHIAHLYEtqrKYHSAKEAYEQLLQtenlpaqvka 240
Cdd:cd24145    10 ILRKALYYEsDKPDPQKALKYYKEALEQADELGMDpfSDEvtgIRIKIAEMLE---KLGMYKAAYEVLER---------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  241 TVLQQLGWmhhnmdlvgDKATKESYAIQYLQKSLeadpnsgqswyflgRQSIdkseasadtwcSIGVLYQQQNQPMDAL- 319
Cdd:cd24145    77 LYLDCLRW---------TLKDDESERGHLIKRDL--------------RISI-----------KLGELNKDSELGKWELr 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  320 -QAYICAVQLDHGHAAAWM----------DLGTLYESCNQPQDAIKCYLNAARSKR--CSNTSTLAarikflQAQLCNLP 386
Cdd:cd24145   123 eRLLKKAVEILLKLGELWMspsevgafleELATAYDLYGRFCLALPLYMQALSLKGqiLLSQANCH------SLVLMNNE 196
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 384871658  387 QSSLQnKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNG 426
Cdd:cd24145   197 AAELA-LHALRKPLSSTLIEASRLPQKSRDQLLEAALKWA 235
TPR COG0790
TPR repeat [General function prediction only];
109-361 4.06e-04

TPR repeat [General function prediction only];


Pssm-ID: 440553 [Multi-domain]  Cd Length: 241  Bit Score: 43.76  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  109 ALSAYQRYYSLQADYWKNAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSfcrakEIHLRLGLMFK----VNTDYKSSL 184
Cdd:COG0790    13 AAAAALAAAAAAAGAAAAAAAAAAAAAALAAAAGAAAAAAAAAAAAAAGGA-----EAQYNLGLMYAegrgVPKDYEKAL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  185 KHFQLAlidcnpCTLSNAEIQFHIAHLYE----TQRKYHSAKEAYEQLLQTENLPAQVkatvlqQLGWMHHNMDLV-GDK 259
Cdd:COG0790    88 EWFEKA------AEQGDAEAQYNLGLMYEeglgVPQDYAKALEWYEKAAEQGDADAQY------NLGLLYLNGEGVpKDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  260 ATkesyAIQYLQKSLEAdpNSGQSWYFLGR-----QSIDKSEASADTWcsigvlYQQqnqpmdalqayicAVqlDHGHAA 334
Cdd:COG0790   156 AK----AAEWYRKAAEQ--GDADAQYNLGVlyengRGVPKDPAKALEW------YRK-------------AA--EQGDAD 208
                         250       260       270
                  ....*....|....*....|....*....|.
gi 384871658  335 AWMDLGTLYESCNQ-PQD---AIKCYLNAAR 361
Cdd:COG0790   209 AQYNLGRLYLNGEGvEKDlekALRWLRKAAE 239
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
146-231 4.34e-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: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  146 AIKAFQDVLYVDPSFCRAKEIHLRLGLMFKVNTDYKSSLKHFQlALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAY 225
Cdd:COG1729    12 AIAAFKAFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFE-KLLKRYPDSPKAPDALLKLGLSYLELGDYDKARATL 90

                  ....*.
gi 384871658  226 EQLLQT 231
Cdd:COG1729    91 EELIKK 96
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
93-163 5.05e-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: 5.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384871658   93 FCQLGHFNLLLEDYSKALSAYQRYYSLQADYwknAAFLYGLGLVYFYYNAFHWAIKAFQDVLYVDPSFCRA 163
Cdd:COG4785   110 YNNRGLAYLLLGDYDAALEDFDRALELDPDY---AYAYLNRGIALYYLGRYELAIADLEKALELDPNDPER 177
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
179-280 1.24e-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: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  179 DYKSSLKHFQlALIDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTEnlPAQVKA-TVLQQLGWMHHNMdlvG 257
Cdd:COG1729     8 DYDEAIAAFK-AFLKRYPNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRY--PDSPKApDALLKLGLSYLEL---G 81
                          90       100
                  ....*....|....*....|...
gi 384871658  258 DKATkesyAIQYLQKSLEADPNS 280
Cdd:COG1729    82 DYDK----ARATLEELIKKYPDS 100
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
101-191 1.55e-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: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  101 LLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIkAFQDVLYVDPSFCRAkeiHLRLGLMFKVNTDY 180
Cdd:COG3063     3 LKLGDLEEAEEYYEKALELDPD---NADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEA---LLNLAELLLELGDY 75
                          90
                  ....*....|.
gi 384871658  181 KSSLKHFQLAL 191
Cdd:COG3063    76 DEALAYLERAL 86
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
308-354 2.15e-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: 2.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 384871658  308 LYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIK 354
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA 47
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
166-279 2.86e-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: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  166 IHLRLGlmfkvntDYKSSLKHFQLALiDCNPctlSNAEIQFHIAHLYETQRKYHSAkEAYEQLLQTEnlPAQVKAtvLQQ 245
Cdd:COG3063     1 LYLKLG-------DLEEAEEYYEKAL-ELDP---DNADALNNLGLLLLEQGRYDEA-IALEKALKLD--PNNAEA--LLN 64
                          90       100       110
                  ....*....|....*....|....*....|....
gi 384871658  246 LGWMHHNMdlvGDKATkesyAIQYLQKSLEADPN 279
Cdd:COG3063    65 LAELLLEL---GDYDE----ALAYLERALELDPS 91
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
258-354 3.14e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 40.67  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  258 DKATKESYAIQYLQKSLEADPNSgqswyflgrqsidkseasADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWM 337
Cdd:COG4785    84 DSLGDYDLAIADFDQALELDPDL------------------AEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYL 145
                          90
                  ....*....|....*..
gi 384871658  338 DLGTLYESCNQPQDAIK 354
Cdd:COG4785   146 NRGIALYYLGRYELAIA 162
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
72-162 4.52e-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: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   72 KAVRCYESLILKAEGkvESDFFCQLGHFNLLLEDYSKALsAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKAFQ 151
Cdd:COG3063    10 EAEEYYEKALELDPD--NADALNNLGLLLLEQGRYDEAI-ALEKALKLDPN---NAEALLNLAELLLELGDYDEALAYLE 83
                          90
                  ....*....|.
gi 384871658  152 DVLYVDPSFCR 162
Cdd:COG3063    84 RALELDPSALR 94
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
70-238 4.92e-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: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658   70 LGKAVRCYESLILKAEGKVEsdFFCQLGHFNLLLEDYSKALSAYQRYYSLQADywkNAAFLYGLGLVYFYYNAFHWAIKA 149
Cdd:COG3914   128 LEEALAALRRALALNPDFAE--AYLNLGEALRRLGRLEEAIAALRRALELDPD---NAEALNNLGNALQDLGRLEEAIAA 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384871658  150 FQDVLYVDPSFCRAkeIHLRLGLMFKVNTDYKSSLKHFQLALIDCNPCTLSNaeiqFHIAHLY----ETQRKYHsakEAY 225
Cdd:COG3914   203 YRRALELDPDNADA--HSNLLFALRQACDWEVYDRFEELLAALARGPSELSP----FALLYLPdddpAELLALA---RAW 273
                         170
                  ....*....|...
gi 384871658  226 EQLLQTENLPAQV 238
Cdd:COG3914   274 AQLVAAAAAPELP 286
TPR_1 pfam00515
Tetratricopeptide repeat;
127-160 6.05e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.47  E-value: 6.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 384871658   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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