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Conserved domains on  [gi|1831518590|ref|NP_001367002|]
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Serine/threonine-protein phosphatase 5 [Caenorhabditis elegans]

Protein Classification

PP5 family serine/threonine-protein phosphatase( domain architecture ID 13326225)

PP5 (protein phosphatase 5) family serine/threonine-protein phosphatase catalyzes the dephosphorylation of phosphoserine and phosphothreonine residues of specific protein substrates; contains tetratricopeptide repeat(s)

CATH:  3.60.21.10
EC:  3.1.3.16
Gene Ontology:  GO:0005515|GO:0046872|GO:0004722|GO:0006470
PubMed:  10517866|18488168|25837850|30401537|9646865|29925267
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-490 0e+00

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 615.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 176 YDGPRLED-KITKEFVLQLIKTFKNQQKLHKKYAFKMLLEFYNYVKSLPTMVEITVPTGKKFTICGDVHGQFYDLCNIFE 254
Cdd:cd07417     1 YSGPKLEDgKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 255 INGYPSETNPYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETF 334
Cdd:cd07417    81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 335 CWLPLCHLINEKIFVCHGGLFKEDGVTLEDIRKTDRNRQPPDEGIMCDLLWSDPQPINGRSPSKRGVGCQFGPDVTSKWC 414
Cdd:cd07417   161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831518590 415 ETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFITITGDNLTPRFTPFDAVPHPKLPPMAYAN 490
Cdd:cd07417   241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PLN03088 super family cl33632
SGT1, suppressor of G2 allele of SKP1; Provisional
 29-139 1.46e-18

SGT1, suppressor of G2 allele of SKP1; Provisional


The actual alignment was detected with superfamily member PLN03088:

Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 87.15  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  29 AGMIKDEANQFFKDQVYDVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANM 107
Cdd:PLN03088    2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPnNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831518590 108 ALGRFKKALTDYQAVVKVCPNDKDARAKFDEC 139
Cdd:PLN03088   82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKEC 113
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-490 0e+00

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 615.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 176 YDGPRLED-KITKEFVLQLIKTFKNQQKLHKKYAFKMLLEFYNYVKSLPTMVEITVPTGKKFTICGDVHGQFYDLCNIFE 254
Cdd:cd07417     1 YSGPKLEDgKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 255 INGYPSETNPYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETF 334
Cdd:cd07417    81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 335 CWLPLCHLINEKIFVCHGGLFKEDGVTLEDIRKTDRNRQPPDEGIMCDLLWSDPQPINGRSPSKRGVGCQFGPDVTSKWC 414
Cdd:cd07417   161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831518590 415 ETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFITITGDNLTPRFTPFDAVPHPKLPPMAYAN 490
Cdd:cd07417   241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 203-479 1.62e-119

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 351.52  E-value: 1.62e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  203 LHKKYAFKMLLEFYNYVKSLPTMVEITVPTgkkfTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETI 282
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPV----TVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  283 FTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLfKEDGVTL 362
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  363 EDIRKTDRNRQPPDEGIMCDLLWSDP-QPINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQC 441
Cdd:smart00156 155 DDIRKLKRPQEPPDDGLLIDLLWSDPdQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKL 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1831518590  442 FTVFSAPNYCDQMNNKGAFITItGDNLTPRFTPFDAVP 479
Cdd:smart00156 235 VTIFSAPNYCDRFGNKAAVLKV-DKDLKLTFEQFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 221-463 2.49e-69

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 223.63  E-value: 2.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 221 SLPTMVEITVPTgkkfTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSR 300
Cdd:PTZ00244   43 SQPMLLEIRPPV----RVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 301 GNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLfKEDGVTLEDIRKTDRNRQPPDEGIM 380
Cdd:PTZ00244  118 GNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLASVNEIERPCDVPDRGIL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 381 CDLLWSDPQ-PINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGA 459
Cdd:PTZ00244  197 CDLLWADPEdEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAA 276


                  ....
gi 1831518590 460 FITI 463
Cdd:PTZ00244  277 VMNI 280
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-227 2.97e-42

PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats.


Pssm-ID: 462427  Cd Length: 92  Bit Score: 145.31  E-value: 2.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 136 FDECSKIVRRQKFEAAISTDhDKKTVAETLDINAMAIEDSYDGPRLED-KITKEFVLQLIKTFKNQQKLHKKYAFKMLLE 214
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVE-EKPSAAETIDLESIVVEDSYDGPRLEDeKITLEFVKDMIERFKKGKKLHKKYAYQILLK 79

                          90
                  ....*....|...
gi 1831518590 215 FYNYVKSLPTMVE 227
Cdd:pfam08321  80 VKEILKKEPSLVE 92
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 29-139 1.46e-18

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 87.15  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  29 AGMIKDEANQFFKDQVYDVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANM 107
Cdd:PLN03088    2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPnNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831518590 108 ALGRFKKALTDYQAVVKVCPNDKDARAKFDEC 139
Cdd:PLN03088   82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKEC 113
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 15-121 3.25e-17

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


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 84.65  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  15 ESIEEKSYEDEKEKAGMIKDEANQFFKDQVYDVAADLYSVAIEIHPTAVLYGNRAQAYLKKELYGSALEDADNAIAIDPS 94
Cdd:TIGR00990 113 SSVANLSEEERKKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDPVYYSNRAACHNALGDWEKVVEDTTAALELDPD 192

                          90       100
                  ....*....|....*....|....*..
gi 1831518590  95 YVKGFYRRATANMALGRFKKALTDYQA 121
Cdd:TIGR00990 193 YSKALNRRANAYDGLGKYADALLDLTA 219
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
45-220 3.41e-16

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 78.12  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG0457    58 YEEALADYEQALELDPDdAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 124 KVCPNDKDARAKFDECSKivRRQKFEAAISTDHDKKTVAETLDINAMAIEDSYDGPRLEDKITKEFVLQLIKTFKNQQKL 203
Cdd:COG0457   138 ELDPDDADALYNLGIALE--KLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILT 215

                         170
                  ....*....|....*..
gi 1831518590 204 HKKYAFKMLLEFYNYVK 220
Cdd:COG0457   216 LAALAELLLLALALLLA 232
TPR_9 pfam13371
Tetratricopeptide repeat;
70-134 1.11e-04

Tetratricopeptide repeat;


Pssm-ID: 463860 [Multi-domain]  Cd Length: 73  Bit Score: 40.28  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831518590  70 QAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDARA 134
Cdd:pfam13371   3 AIYLREEDWERALAVVERLLLLAPDDPEERRDRGLLYAQLGCFQAALEDLEAYLELAPDAPDAEA 67
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 96-129 1.34e-03

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


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 36.27  E-value: 1.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831518590   96 VKGFYRRATANMALGRFKKALTDYQAVVKVCPND 129
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-490 0e+00

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 615.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 176 YDGPRLED-KITKEFVLQLIKTFKNQQKLHKKYAFKMLLEFYNYVKSLPTMVEITVPTGKKFTICGDVHGQFYDLCNIFE 254
Cdd:cd07417     1 YSGPKLEDgKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 255 INGYPSETNPYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETF 334
Cdd:cd07417    81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 335 CWLPLCHLINEKIFVCHGGLFKEDGVTLEDIRKTDRNRQPPDEGIMCDLLWSDPQPINGRSPSKRGVGCQFGPDVTSKWC 414
Cdd:cd07417   161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831518590 415 ETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFITITGDNLTPRFTPFDAVPHPKLPPMAYAN 490
Cdd:cd07417   241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 203-479 1.62e-119

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 351.52  E-value: 1.62e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  203 LHKKYAFKMLLEFYNYVKSLPTMVEITVPTgkkfTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETI 282
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPV----TVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  283 FTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLfKEDGVTL 362
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  363 EDIRKTDRNRQPPDEGIMCDLLWSDP-QPINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQC 441
Cdd:smart00156 155 DDIRKLKRPQEPPDDGLLIDLLWSDPdQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKL 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1831518590  442 FTVFSAPNYCDQMNNKGAFITItGDNLTPRFTPFDAVP 479
Cdd:smart00156 235 VTIFSAPNYCDRFGNKAAVLKV-DKDLKLTFEQFKPGK 271
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 185-472 8.18e-104

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 312.42  E-value: 8.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 185 ITKEFVLQLIKTFKNQQKLHKKYAFKMLLEFYNYVKSLPTMVEITVPTGKKFTICGDVHGQFYDLCNIFEINGYPSETNP 264
Cdd:cd07420     2 LTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPENP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 265 YLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKY---TQQMCDMFTETFCWLPLCH 341
Cdd:cd07420    82 YVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYkdhGKKILRLLEDVFSWLPLAT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 342 LINEKIFVCHGGLfkEDGVTLEDIRKTDRNRQPPDE---GIMCDLLWSDPQPINGRSP-SKRGVGCQFGPDVTSKWCETN 417
Cdd:cd07420   162 IIDNKVLVVHGGI--SDSTDLDLLDKIDRHKYVSTKtewQQVVDILWSDPKATKGCKPnTFRGGGCYFGPDVTSQFLQKH 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1831518590 418 GIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFITITGDnLTPRF 472
Cdd:cd07420   240 GLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQ-LTPHF 293
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 223-479 1.19e-94

PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of phosphoprotein phosphatases (PPP's) including PP4 and PP6. PP2A (Protein phosphatase 2A) is a critical regulator of many cellular activities. PP2A comprises about 1% of total cellular proteins. PP2A, together with protein phosphatase 1 (PP1), accounts for more than 90% of all serine/threonine phosphatase activities in most cells and tissues. The PP2A subunit in addition to having a catalytic domain homologous to PP1, has a unique C-terminal tail, containing a motif that is conserved in the catalytic subunits of all PP2A-like phosphatases including PP4 and PP6, and has an important role in PP2A regulation. The PP2A-like family of phosphatases all share a similar heterotrimeric architecture, that includes: a 65kDa scaffolding subunit (A), a 36kDa catalytic subunit (C), and one of 18 regulatory subunits (B). The PPP (phosphoprotein phosphatase) family, to which PP2A belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277360 [Multi-domain]  Cd Length: 285  Bit Score: 288.33  E-value: 1.19e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 223 PTMVEITVPTgkkfTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGN 302
Cdd:cd07415    35 SNVQRVRSPV----TVCGDIHGQFYDLLELFRIGGDVPDTN-YLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGN 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 303 HESDVMNKMYGFEGEVKAKYTQ-QMCDMFTETFCWLPLCHLINEKIFVCHGGLFKeDGVTLEDIRKTDRNRQPPDEGIMC 381
Cdd:cd07415   110 HESRQITQVYGFYDECLRKYGNaNVWKYFTDLFDYLPLAALIDGQIFCVHGGLSP-SIQTLDQIRALDRFQEVPHEGPMC 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 382 DLLWSDPQPINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFI 461
Cdd:cd07415   189 DLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASIL 268

                         250
                  ....*....|....*...
gi 1831518590 462 TItGDNLTPRFTPFDAVP 479
Cdd:cd07415   269 EL-DEHLNRSFKQFEAAP 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 237-463 2.52e-90

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 275.40  E-value: 2.52e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 237 TICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEG 316
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 317 EV----KAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLFKEdgVTLEDIRKTDRNRQPPDEGIMCDLLWSDPQPIN 392
Cdd:cd00144    80 ERtlrcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPD--LTLLDQIRNIRPIENPDDQLVEDLLWSDPDESV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831518590 393 GRSP-SKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGAFITI 463
Cdd:cd00144   158 GDFEsSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 197-485 1.28e-85

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 266.09  E-value: 1.28e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 197 FKNQQKLHKKYAFKMLLEFYNYVKSLPTMVEITVPTgkkfTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGS 276
Cdd:cd07416    10 FMREGRLSEEDALRIITEGAEILRQEPNLLRIEAPV----TVCGDIHGQFYDLLKLFEVGGSPANTR-YLFLGDYVDRGY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 277 FSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLFK 356
Cdd:cd07416    85 FSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 357 EDGvTLEDIRKTDRNRQPPDEGIMCDLLWSDPQPINGRSP--------SKRGVGCQFGPDVTSKWCETNGIEYVVRSHEV 428
Cdd:cd07416   165 ELK-TLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKtqehfvhnTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEA 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831518590 429 KPEGYEMHHNGQ------CFTVFSAPNYCDQMNNKGAFITITGDNLTPRftPFDAVPHPKLPP 485
Cdd:cd07416   244 QDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVMNIR--QFNCSPHPYWLP 304
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 220-472 3.40e-85

PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 264.20  E-value: 3.40e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 220 KSLPTMVEITVPtgkkFTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMS 299
Cdd:cd07414    40 LSQPILLELEAP----LKICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 300 RGNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLfKEDGVTLEDIRKTDRNRQPPDEGI 379
Cdd:cd07414   115 RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGL-SPDLQSMEQIRRIMRPTDVPDQGL 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 380 MCDLLWSDPQP-INGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKG 458
Cdd:cd07414   194 LCDLLWSDPDKdVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAG 273

                         250
                  ....*....|....
gi 1831518590 459 AFITITgDNLTPRF 472
Cdd:cd07414   274 AMMSVD-ETLMCSF 286
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 184-485 8.50e-70

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 227.38  E-value: 8.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 184 KITKEFVLQLIKTFKNQQKLHKKYAFKMLLEFyNYVKSL-----------PTMVEITVPTGKKFTICGDVHGQFYDLCNI 252
Cdd:cd07418     6 ALTNEWVHELMSVFEWSSRNLPPSELPSVLPV-NVFDSLvltahkilhrePNCVRIDVEDVCEVVVVGDVHGQLHDVLFL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 253 FEINGYPSETNPYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQ---MCDM 329
Cdd:cd07418    85 LEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 330 FTETFCWLPLCHLINEKIFVCHGGLFKEDGVTLEDIRKTDRNRQ---------------------------PPDEG---I 379
Cdd:cd07418   165 CLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNRRVlllepeseslklgtlddlmkarrsvldPPGEGsnlI 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 380 MCDLLWSDPQPINGRSPSK-RGVGCQFGPDVTSKWCETNGIEYVVRSHEV------KPE------GYEMHHN---GQCFT 443
Cdd:cd07418   245 PGDVLWSDPSLTPGLSPNKqRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGpdarekRPGlagmnkGYTVDHDvesGKLIT 324

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1831518590 444 VFSAPNYC------DQMNNKGAFITITG-DNLTPRFTPFDAV-PHPKLPP 485
Cdd:cd07418   325 LFSAPDYPqfqateERYNNKGAYIILQPpDFSDPQFHTFEAVkPRPKANP 374
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 221-463 2.49e-69

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 223.63  E-value: 2.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 221 SLPTMVEITVPTgkkfTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSR 300
Cdd:PTZ00244   43 SQPMLLEIRPPV----RVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 301 GNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLfKEDGVTLEDIRKTDRNRQPPDEGIM 380
Cdd:PTZ00244  118 GNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLASVNEIERPCDVPDRGIL 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 381 CDLLWSDPQ-PINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGA 459
Cdd:PTZ00244  197 CDLLWADPEdEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAA 276


                  ....
gi 1831518590 460 FITI 463
Cdd:PTZ00244  277 VMNI 280
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 221-463 1.14e-66

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 217.60  E-value: 1.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 221 SLPTMVEITVPtgkkFTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSR 300
Cdd:PTZ00480   50 SQPILLELEAP----LKICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 301 GNHESDVMNKMYGFEGEVKAKYTQQMCDMFTETFCWLPLCHLINEKIFVCHGGLFKEDGvTLEDIRKTDRNRQPPDEGIM 380
Cdd:PTZ00480  125 GNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELS-NLEQIRRIMRPTDVPDTGLL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 381 CDLLWSDP-QPINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCFTVFSAPNYCDQMNNKGA 459
Cdd:PTZ00480  204 CDLLWSDPdKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGS 283


                  ....
gi 1831518590 460 FITI 463
Cdd:PTZ00480  284 MMTI 287
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 231-479 2.58e-60

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 200.43  E-value: 2.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 231 PTGKKFTICGDVHGQFYDLCNIFEINGYPSETNpYLFNGDFVDRGSFSVETIFTMIGFKLLYPNHFFMSRGNHESDVMNK 310
Cdd:PTZ00239   40 PVRAPVNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQ 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 311 MYGFEGEVKAKY-TQQMCDMFTETFCWLPLCHLINEKIFVCHGGLfKEDGVTLEDIRKTDRNRQPPDEGIMCDLLWSDPQ 389
Cdd:PTZ00239  119 VYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGL-SPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 390 PINGRSPSKRGVGCQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEMHHNGQCF-TVFSAPNYCDQMNNKGAFITITgDNL 468
Cdd:PTZ00239  198 EVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQNLvTVWSAPNYCYRCGNIASILCLD-ENL 276

                         250
                  ....*....|.
gi 1831518590 469 TPRFTPFDAVP 479
Cdd:PTZ00239  277 QQTWKTFKEVP 287
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 219-469 7.06e-53

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 181.10  E-value: 7.06e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 219 VKSLPTMVEITVPtgkkFTICGDVHGQFYDLCNIFEINGYPS-------ETNPYLFNGDFVDRGSFSVETIFTMIGFKLL 291
Cdd:cd07419    37 FRQEPSVLRLRAP----IKIFGDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDRGSHSLETICLLLALKVK 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 292 YPNHFFMSRGNHESDVMNKMYGFEGEVKAKYTQQMCD------MFTETFCWLPLCHLINEKIFVCHGGLFKEdgVT-LED 364
Cdd:cd07419   113 YPNQIHLIRGNHEAADINALFGFREECIERLGEDIRDgdsvwqRINRLFNWLPLAALIEDKIICVHGGIGRS--INhIHQ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 365 IRKTDRN-RQPPDEGIMCDLLWSDP---QPINGRSPS---KRGVG--CQFGPDVTSKWCETNGIEYVVRSHEVKPEGYEM 435
Cdd:cd07419   191 IENLKRPiTMEAGSPVVMDLLWSDPtenDSVLGLRPNaidPRGTGliVKFGPDRVMEFLEENDLQMIIRAHECVMDGFER 270

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1831518590 436 HHNGQCFTVFSAPNYCDQMNNKGAFITItGDNLT 469
Cdd:cd07419   271 FAQGHLITLFSATNYCGTAGNAGAILVL-GRDLV 303
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-227 2.97e-42

PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats.


Pssm-ID: 462427  Cd Length: 92  Bit Score: 145.31  E-value: 2.97e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 136 FDECSKIVRRQKFEAAISTDhDKKTVAETLDINAMAIEDSYDGPRLED-KITKEFVLQLIKTFKNQQKLHKKYAFKMLLE 214
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVE-EKPSAAETIDLESIVVEDSYDGPRLEDeKITLEFVKDMIERFKKGKKLHKKYAYQILLK 79

                          90
                  ....*....|...
gi 1831518590 215 FYNYVKSLPTMVE 227
Cdd:pfam08321  80 VKEILKKEPSLVE 92
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 29-139 1.46e-18

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 87.15  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  29 AGMIKDEANQFFKDQVYDVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANM 107
Cdd:PLN03088    2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPnNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1831518590 108 ALGRFKKALTDYQAVVKVCPNDKDARAKFDEC 139
Cdd:PLN03088   82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKEC 113
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 15-121 3.25e-17

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


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 84.65  E-value: 3.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  15 ESIEEKSYEDEKEKAGMIKDEANQFFKDQVYDVAADLYSVAIEIHPTAVLYGNRAQAYLKKELYGSALEDADNAIAIDPS 94
Cdd:TIGR00990 113 SSVANLSEEERKKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPDPVYYSNRAACHNALGDWEKVVEDTTAALELDPD 192

                          90       100
                  ....*....|....*....|....*..
gi 1831518590  95 YVKGFYRRATANMALGRFKKALTDYQA 121
Cdd:TIGR00990 193 YSKALNRRANAYDGLGKYADALLDLTA 219
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
45-220 3.41e-16

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 78.12  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG0457    58 YEEALADYEQALELDPDdAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 124 KVCPNDKDARAKFDECSKivRRQKFEAAISTDHDKKTVAETLDINAMAIEDSYDGPRLEDKITKEFVLQLIKTFKNQQKL 203
Cdd:COG0457   138 ELDPDDADALYNLGIALE--KLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILT 215

                         170
                  ....*....|....*..
gi 1831518590 204 HKKYAFKMLLEFYNYVK 220
Cdd:COG0457   216 LAALAELLLLALALLLA 232
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
45-133 8.15e-16

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 76.97  E-value: 8.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG0457    24 YEEAIEDYEKALELDPDdAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKAL 103

                          90
                  ....*....|
gi 1831518590 124 KVCPNDKDAR 133
Cdd:COG0457   104 ELDPDDAEAL 113
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
30-129 8.31e-15

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 73.41  E-value: 8.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  30 GMIKDEANQffkdqvYDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMA 108
Cdd:COG4785    80 GVAYDSLGD------YDLAIADFDQALELDPDlAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYY 153

                          90       100
                  ....*....|....*....|.
gi 1831518590 109 LGRFKKALTDYQAVVKVCPND 129
Cdd:COG4785   154 LGRYELAIADLEKALELDPND 174
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 235-343 2.90e-13

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 66.08  E-value: 2.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590 235 KFTICGDVH--GQFYDLCNIFEIngYPSETNPYLF--NGDFVDRGSFSVETIFTMigFKLLYPNHFFMSRGNHESDV--M 308
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKK--LLEEGKPDLVlhAGDLVDRGPPSEEVLELL--ERLIKYVPVYLVRGNHDFDYgeC 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1831518590 309 NKMYGFEGEVKAKYtqqmcDMFTETFCWLPLCHLI 343
Cdd:pfam00149  78 LRLYPYLGLLARPW-----KRFLEVFNFLPLAGIL 107
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
46-133 2.99e-13

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 69.17  E-value: 2.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  46 DVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVK 124
Cdd:COG4785    56 AALAAERIDRALALPdLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALE 135


                  ....*....
gi 1831518590 125 VCPNDKDAR 133
Cdd:COG4785   136 LDPDYAYAY 144
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
56-132 2.05e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.95  E-value: 2.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1831518590  56 IEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDA 132
Cdd:COG0457     1 LELDPDdAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA 78
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 45-134 2.26e-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: 64.26  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG4235    33 YDEALAAYEKALRLDPdNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLL 112

                          90
                  ....*....|.
gi 1831518590 124 KVCPNDKDARA 134
Cdd:COG4235   113 ALLPADAPARL 123
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 33-133 2.47e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 62.70  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  33 KDEANQFFKDQVYDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGR 111
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDnAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGR 161

                          90       100
                  ....*....|....*....|..
gi 1831518590 112 FKKALTDYQAVVKVCPNDKDAR 133
Cdd:COG3914   162 LEEAIAALRRALELDPDNAEAL 183
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 36-153 4.42e-10

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: 60.51  E-value: 4.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  36 ANQFFKDQVYDVAADLYSVAIEIHPTAV-LYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKK 114
Cdd:COG2956   151 AELYLEQGDYDEAIEALEKALKLDPDCArALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEE 230

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1831518590 115 ALTDYQAVVKVCPNDKDARAKFDecsKIVRRQKFEAAIS 153
Cdd:COG2956   231 ALELLRKALELDPSDDLLLALAD---LLERKEGLEAALA 266
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
45-128 9.19e-10

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 55.56  E-value: 9.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEdADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG3063     8 LEEAEEYYEKALELDPdNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERAL 86


                  ....*
gi 1831518590 124 KVCPN 128
Cdd:COG3063    87 ELDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 45-129 1.40e-09

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: 56.35  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG4783    54 LDEAIVLLHEALELDPDePEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKAL 133


                  ....*.
gi 1831518590 124 KVCPND 129
Cdd:COG4783   134 ELDPDD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 2-127 6.99e-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: 54.97  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590   2 AATITDDIVATVLESIEEKSYEDEKEKAGMIKDEANQFFKdqvydvAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGS 80
Cdd:COG5010    33 GANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEE------SLALLEQALQLDPNnPELYYNLALLYSRSGDKDE 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1831518590  81 ALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCP 127
Cdd:COG5010   107 AKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 36-133 6.99e-09

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: 54.43  E-value: 6.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  36 ANQFFKDQVYDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKK 114
Cdd:COG4783    11 AQALLLAGDYDEAEALLEKALELDPDnPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDE 90

                          90
                  ....*....|....*....
gi 1831518590 115 ALTDYQAVVKVCPNDKDAR 133
Cdd:COG4783    91 ALALLEKALKLDPEHPEAY 109
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 45-152 1.33e-08

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: 55.89  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG2956   126 WEKAIEVLERLLKLGPEnAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERAL 205

                          90       100
                  ....*....|....*....|....*....
gi 1831518590 124 KVCPNDKDARAKFDECSKivRRQKFEAAI 152
Cdd:COG2956   206 EQDPDYLPALPRLAELYE--KLGDPEEAL 232
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 48-134 4.45e-08

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 55.77  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  48 AADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVC 126
Cdd:COG3914   131 ALAALRRALALNPdFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELD 210


                  ....*...
gi 1831518590 127 PNDKDARA 134
Cdd:COG3914   211 PDNADAHS 218
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 37-154 1.69e-07

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: 52.81  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  37 NQFFKDQvYDVAADLYSVAIEIHP-TAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKA 115
Cdd:COG2956    17 NYLLNGQ-PDKAIDLLEEALELDPeTVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRA 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1831518590 116 LTDYQAVVKVCPNDKDARAKfdeCSKIVRRQK-FEAAIST 154
Cdd:COG2956    96 EELLEKLLELDPDDAEALRL---LAEIYEQEGdWEKAIEV 132
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 22-154 2.24e-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: 50.34  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  22 YEDEKEKAGMIKDEANQFFKDQVYDVAADLYSVAIEIHPTAVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYR 101
Cdd:COG5010    14 LLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYN 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1831518590 102 RATANMALGRFKKALTDYQAVVKVCPNDKDARAKFDECskIVRRQKFEAAIST 154
Cdd:COG5010    94 LALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAAL--LLSLGQDDEAKAA 144
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 68-133 9.14e-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: 48.26  E-value: 9.14e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831518590  68 RAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDAR 133
Cdd:COG4783    10 LAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEAR 75
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 39-154 2.00e-06

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: 49.34  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  39 FFKDQVYDVAADLYSVAIEIHPTAV-LYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALT 117
Cdd:COG2956    86 YLKAGLLDRAEELLEKLLELDPDDAeALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIE 165

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1831518590 118 DYQAVVKVCPNdkDARAKFDECSKIVRRQKFEAAIST 154
Cdd:COG2956   166 ALEKALKLDPD--CARALLLLAELYLEQGDYEEAIAA 200
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 38-134 2.88e-06

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: 46.14  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  38 QFFKDQVYDVAADLYSVAIEIHPTAVLYGN----RAQAYLKKELYGSALEDADNAIAIDPSYVK---GFYRRATANMALG 110
Cdd:COG1729     2 ALLKAGDYDEAIAAFKAFLKRYPNSPLAPDalywLGEAYYALGDYDEAAEAFEKLLKRYPDSPKapdALLKLGLSYLELG 81

                          90       100
                  ....*....|....*....|....
gi 1831518590 111 RFKKALTDYQAVVKVCPNDKDARA 134
Cdd:COG1729    82 DYDKARATLEELIKKYPDSEAAKE 105
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 48-133 3.05e-06

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: 46.54  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  48 AADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVC 126
Cdd:COG4235     2 AIARLRQALAANPNdAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD 81


                  ....*..
gi 1831518590 127 PNDKDAR 133
Cdd:COG4235    82 PDNPEAL 88
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
71-133 3.81e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 45.16  E-value: 3.81e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1831518590  71 AYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALtDYQAVVKVCPNDKDAR 133
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEAL 62
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 68-154 5.25e-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: 45.84  E-value: 5.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  68 RAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDA---RAKFDecskiVR 144
Cdd:TIGR02917 199 KGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAhylKALVD-----FQ 273

                          90
                  ....*....|
gi 1831518590 145 RQKFEAAIST 154
Cdd:TIGR02917 274 KKNYEDARET 283
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 81-152 7.24e-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: 42.69  E-value: 7.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831518590  81 ALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDARAKFDECskIVRRQKFEAAI 152
Cdd:COG4235     2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA--LLAAGDTEEAE 71
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 45-152 8.44e-05

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: 44.33  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHPT-AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVV 123
Cdd:COG2956    58 YDRAIRIHQKLLERDPDrAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLL 137

                          90       100       110
                  ....*....|....*....|....*....|
gi 1831518590 124 KVCPNDKDARAkfdECSKIVRRQK-FEAAI 152
Cdd:COG2956   138 KLGPENAHAYC---ELAELYLEQGdYDEAI 164
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 34-152 1.03e-04

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 44.10  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  34 DEANQFFKDQVYDVAADLYSVAIEIHPTAVlYGNRAQ-----AYLKKELYGSALEDADNAIAIDPS-----YVkgFYRRA 103
Cdd:COG4105    37 EEAKEALEKGDYEKAIKLFEELEPRYPGSP-YAEQAQlmlayAYYKQGDYEEAIAAADRFIKLYPNspnadYA--YYLRG 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831518590 104 TANMALGR--------FKKALTDYQAVVKVCPNDK---DARAKFDECSKI------------VRRQKFEAAI 152
Cdd:COG4105   114 LSYYEQSPdsdrdqtsTRKAIEAFQELINRYPDSEyaeDAKKRIDELRDKlarkelevaryyLKRGAYVAAI 185
TPR_9 pfam13371
Tetratricopeptide repeat;
70-134 1.11e-04

Tetratricopeptide repeat;


Pssm-ID: 463860 [Multi-domain]  Cd Length: 73  Bit Score: 40.28  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1831518590  70 QAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDARA 134
Cdd:pfam13371   3 AIYLREEDWERALAVVERLLLLAPDDPEERRDRGLLYAQLGCFQAALEDLEAYLELAPDAPDAEA 67
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 238-304 2.43e-04

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 41.10  E-value: 2.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1831518590 238 ICGDVHGQFYDLCNIFEINgYPSETNP--YLFNGDFVDRGSFSVETIFTMIGFKLLYPNhFFMSRGNHE 304
Cdd:cd00838     2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLLAGIP-VYVVPGNHD 68
TPR_1 pfam00515
Tetratricopeptide repeat;
96-129 5.43e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.40  E-value: 5.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1831518590  96 VKGFYRRATANMALGRFKKALTDYQAVVKVCPND 129
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 12-151 5.45e-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: 42.76  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  12 TVLESIEEKSYEDEKEKAGMIKDEANQFFKDQVYDVAADLYSVAIEIHPTAvLYGNRAQAYLKKEL--YGSALEDADNAI 89
Cdd:TIGR02917 108 QVLDELPGKTLLDDEGAAELLALRGLAYLGLGQLELAQKSYEQALAIDPRS-LYAKLGLAQLALAEnrFDEARALIDEVL 186

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1831518590  90 AIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDARakFDECSKIVRRQKFEAA 151
Cdd:TIGR02917 187 TADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVL--LALATILIEAGEFEEA 246
TPR_1 pfam00515
Tetratricopeptide repeat;
62-95 5.93e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 37.40  E-value: 5.93e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1831518590  62 AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSY 95
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
45-128 1.00e-03

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 41.02  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIE-IHPT--AVLYGnRAQAYLKKELYGSALEDADNAIAIDPSYVKG----FYRRATAnmALGRFKKALT 117
Cdd:COG4700   105 YDEAIELYEEALTgIFADdpHILLG-LAQALFELGRYAEALETLEKLIAKNPDFKSSdahlLYARALE--ALGDLEAAEA 181

                          90
                  ....*....|.
gi 1831518590 118 DYQAVVKVCPN 128
Cdd:COG4700   182 ELEALARRYSG 192
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 96-129 1.34e-03

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


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 36.27  E-value: 1.34e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831518590   96 VKGFYRRATANMALGRFKKALTDYQAVVKVCPND 129
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 62-95 2.26e-03

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


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 35.50  E-value: 2.26e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1831518590   62 AVLYGNRAQAYLKKELYGSALEDADNAIAIDPSY 95
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 60-133 2.50e-03

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: 39.71  E-value: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831518590  60 PTAVLYGN--RAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDAR 133
Cdd:COG2956     4 PVAAALGWyfKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEAL 79
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 96-128 2.56e-03

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


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 35.58  E-value: 2.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1831518590  96 VKGFYRRATANMALGRFKKALTDYQAVVKVCPN 128
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 67-129 2.71e-03

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 36.55  E-value: 2.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1831518590  67 NRAQAYLKKELYGSALEDADNAIAID---PSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPND 129
Cdd:pfam13432   2 ALARAALRAGDYDDAAAALEAALARFpesPDAAAALLLLGLAALRQGRLAEAAAAYRAALRAAPGD 67
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 45-128 2.74e-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: 40.45  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  45 YDVAADLYSVAIEIHP--TAVLYgNRAQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAV 122
Cdd:TIGR02917 209 IELALAAYRKAIALRPnnIAVLL-ALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDA 287


                  ....*.
gi 1831518590 123 VKVCPN 128
Cdd:TIGR02917 288 LKSAPE 293
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
48-133 4.19e-03

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 38.74  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  48 AADLYSVAIEIHPTAVLYgNRAQAYLKKELYGSALEDADNAIAI--------DPSYVKGFYRRATANMALGRFKKALTDY 119
Cdd:COG4785    18 AASKAAILLAALLFAAVL-ALAIALADLALALAAAALAAAALAAeridralaLPDLAQLYYERGVAYDSLGDYDLAIADF 96

                          90
                  ....*....|....
gi 1831518590 120 QAVVKVCPNDKDAR 133
Cdd:COG4785    97 DQALELDPDLAEAY 110
type_IV_pilW TIGR02521
type IV pilus biogenesis/stability protein PilW; Members of this family are designated PilF ...
 69-154 7.60e-03

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


Pssm-ID: 131573 [Multi-domain]  Cd Length: 234  Bit Score: 38.09  E-value: 7.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1831518590  69 AQAYLKKELYGSALEDADNAIAIDPSYVKGFYRRATANMALGRFKKALTDYQAVVKVCPNDKDA----------RAKFDE 138
Cdd:TIGR02521  38 ALGYLEQGDLEVAKENLDKALEHDPDDYLAYLALALYYQQLGELEKAEDSFRRALTLNPNNGDVlnnygtflcqQGKYEQ 117

                          90
                  ....*....|....*.
gi 1831518590 139 CskivrRQKFEAAIST 154
Cdd:TIGR02521 118 A-----MQQFEQAIED 128
 
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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