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Conserved domains on  [gi|199559777|ref|NP_035285|]
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serine/threonine-protein phosphatase 5 isoform 1 [Mus musculus]

Protein Classification

serine/threonine-protein phosphatase 5( domain architecture ID 18775429)

serine/threonine-protein phosphatase 5 (PP5) catalyzes the dephosphorylation of phosphoserine and phosphothreonine residues in a variety of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT; contains tetratricopeptide repeats

CATH:  3.60.21.10
EC:  3.1.3.16
Gene Ontology:  GO:0005515|GO:0046872|GO:0004722|GO:0006470
PubMed:  10517866|18488168|25837850|29925267|9646865|30401537
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 ...
 176-491 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: 693.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 176 YSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE 255
Cdd:cd07417    1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 256 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 335
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 336 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFL 415
Cdd:cd07417  161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 199559777 416 EENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 491
Cdd:cd07417  241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
2-129 2.87e-20

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


:

Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 89.59  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   2 AMAEGERTECAETPRDEPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYA 81
Cdd:COG4785   47 ALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAA 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 199559777  82 LGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPND 129
Cdd:COG4785  127 LEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPND 174
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-491 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: 693.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 176 YSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE 255
Cdd:cd07417    1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 256 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 335
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 336 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFL 415
Cdd:cd07417  161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 199559777 416 EENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 491
Cdd:cd07417  241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 204-480 4.67e-141

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: 406.21  E-value: 4.67e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   204 LHRKCAYQILVQVKEVLCKLSTLVEttlkETEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVI 283
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVE----VSAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   284 LTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTL 363
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   364 DDIRKIERNRQPPDSGPMCDLLWSDP-QPQNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRC 442
Cdd:smart00156 155 DDIRKLKRPQEPPDDGLLIDLLWSDPdQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKL 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 199559777   443 VTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQFTAVP 480
Cdd:smart00156 235 VTIFSAPNYCDRFGNKAAVLKV-DKDLKLTFEQFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 211-464 6.65e-72

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 230.18  E-value: 6.65e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 211 QILVQVKEVLCKLSTLVETTLKE------TEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVIL 284
Cdd:PTZ00244  22 QILIREEDIRAVLTEVREIFMSQpmlleiRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETIT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 285 TLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLD 364
Cdd:PTZ00244 101 LQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 365 DIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCV 443
Cdd:PTZ00244 180 SVNEIERPCDVPDRGILCDLLWADPEDEvRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLV 259

                        250       260
                 ....*....|....*....|.
gi 199559777 444 TVFSAPNYCDQMGNKASYIHL 464
Cdd:PTZ00244 260 TVFSAPNYCGEFDNDAAVMNI 280
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-228 3.67e-43

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: 147.62  E-value: 3.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  136 YQECSKIVKQKAFERAIAGDEHRrSVVDSLDIESMTIEDEYSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQ 215
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEEKP-SAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQILLK 79

                          90
                  ....*....|...
gi 199559777  216 VKEVLCKLSTLVE 228
Cdd:pfam08321  80 VKEILKKEPSLVE 92
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
2-129 2.87e-20

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 89.59  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   2 AMAEGERTECAETPRDEPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYA 81
Cdd:COG4785   47 ALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAA 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 199559777  82 LGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPND 129
Cdd:COG4785  127 LEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPND 174
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 28-139 1.41e-16

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 80.99  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:PLN03088   2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 199559777 108 ALGKFRAALRDYETVVKVKPNDKDAKMKYQEC 139
Cdd:PLN03088  82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKEC 113
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 26-119 3.08e-15

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: 78.49  E-value: 3.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPgNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:TIGR00990 125 KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANA 203

                          90
                  ....*....|....
gi 199559777  106 NMALGKFRAALRDY 119
Cdd:TIGR00990 204 YDGLGKYADALLDL 217
TPR_11 pfam13414
TPR repeat;
35-74 9.10e-06

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 42.46  E-value: 9.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 199559777   35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLR 74
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 28-61 1.21e-05

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: 42.05  E-value: 1.21e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 199559777    28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGN 61
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 29-97 1.11e-04

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


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 44.16  E-value: 1.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199559777  29 EELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLrtecygyALGDATRAIELDKKYIK 97
Cdd:cd24142    1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILL-------ELGDVEEAREVLLRAIE 62
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
236-307 4.69e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 199559777 236 KITVCGDTHGQFYDLLNIFE-LNGLPSETnpYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETD 307
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEdLEREGVDL--IVHLGDLVGYGPDPPEVL------DLLRELPIVAVRGNHDGA 65
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-491 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: 693.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 176 YSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE 255
Cdd:cd07417    1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 256 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 335
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 336 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFL 415
Cdd:cd07417  161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 199559777 416 EENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 491
Cdd:cd07417  241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 204-480 4.67e-141

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: 406.21  E-value: 4.67e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   204 LHRKCAYQILVQVKEVLCKLSTLVEttlkETEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVI 283
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVE----VSAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   284 LTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTL 363
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   364 DDIRKIERNRQPPDSGPMCDLLWSDP-QPQNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRC 442
Cdd:smart00156 155 DDIRKLKRPQEPPDDGLLIDLLWSDPdQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKL 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 199559777   443 VTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQFTAVP 480
Cdd:smart00156 235 VTIFSAPNYCDRFGNKAAVLKV-DKDLKLTFEQFKPGK 271
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 202-480 3.31e-102

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: 307.98  E-value: 3.31e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 202 KKLHRKCAYQILVQVKEVLCKLSTLVETTLKetekITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVE 281
Cdd:cd07415   13 ELLPESEVKSLCEKAKEILVKESNVQRVRSP----VTVCGDIHGQFYDLLELFRIGGDVPDTN-YLFLGDYVDRGYYSVE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 282 VILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDG 360
Cdd:cd07415   88 TFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGL-SPSI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 361 VTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGG 440
Cdd:cd07415  167 QTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNN 246

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 199559777 441 RCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQFTAVP 480
Cdd:cd07415  247 KLVTVWSAPNYCYRCGNVASILEL-DEHLNRSFKQFEAAP 285
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 194-476 3.04e-101

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: 305.87  E-value: 3.04e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 194 LMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFV 273
Cdd:cd07420   10 LIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 274 DRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKY---TAQMYELFSEVFEWLPLAQCINGKVLI 350
Cdd:cd07420   90 DRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 351 MHGGLfsEDGVTLDDIRKIERNR---QPPDSGPMCDLLWSDPQPQNG-RSVSKRGVSCQFGPDVTKAFLEENQLDYIIRS 426
Cdd:cd07420  170 VHGGI--SDSTDLDLLDKIDRHKyvsTKTEWQQVVDILWSDPKATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRS 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 199559777 427 HEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQF 476
Cdd:cd07420  248 HECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKL-GPQLTPHFVQY 296
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 238-464 6.94e-97

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: 291.97  E-value: 6.94e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 238 TVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEG 317
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 318 EV----KAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEdgVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQN 393
Cdd:cd00144   80 ERtlrcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPD--LTLLDQIRNIRPIENPDDQLVEDLLWSDPDESV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 199559777 394 GRS-VSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHL 464
Cdd:cd00144  158 GDFeSSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 203-482 3.26e-93

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: 285.35  E-value: 3.26e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 203 KLHRKCAYQILVQVKEVLCKLSTLVETTlketEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEV 282
Cdd:cd07416   15 RLSEEDALRIITEGAEILRQEPNLLRIE----APVTVCGDIHGQFYDLLKLFEVGGSPANTR-YLFLGDYVDRGYFSIEC 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 283 ILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVT 362
Cdd:cd07416   90 VLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGL-SPELKT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 363 LDDIRKIERNRQPPDSGPMCDLLWSDP--QPQNGRSV------SKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGY 434
Cdd:cd07416  169 LDDIRKLDRFREPPSYGPMCDLLWSDPleDFGNEKTQehfvhnTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGY 248

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 199559777 435 EVAHGGR------CVTVFSAPNYCDQMGNKASYIHLQGSDLRpqFHQFTAVPHP 482
Cdd:cd07416  249 RMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVMN--IRQFNCSPHP 300
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 211-457 6.98e-86

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: 266.13  E-value: 6.98e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 211 QILVQVKEVLCKLSTLVEttLKETEKItvCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFK 290
Cdd:cd07414   30 GLCLKSREIFLSQPILLE--LEAPLKI--CGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 291 LLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIE 370
Cdd:cd07414  105 IKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGL-SPDLQSMEQIRRIM 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 371 RNRQPPDSGPMCDLLWSDPQPQ-NGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAP 449
Cdd:cd07414  184 RPTDVPDQGLLCDLLWSDPDKDvQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAP 263


                 ....*...
gi 199559777 450 NYCDQMGN 457
Cdd:cd07414  264 NYCGEFDN 271
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 219-486 1.26e-75

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: 242.78  E-value: 1.26e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 219 VLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFH 298
Cdd:cd07418   50 ILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 299 LLRGNHETDNMNQIYGFEGEVKAKY---TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLF------------------- 356
Cdd:cd07418  130 LLRGNHESKFCTSMYGFEQEVLTKYgdkGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFrspslpkrkkqkgknrrvl 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 357 -SEDGV------TLDDIRKIERN-RQPPDSGPMC---DLLWSDPQPQNGRSVSK-RGVSCQFGPDVTKAFLEENQLDYII 424
Cdd:cd07418  210 lLEPESeslklgTLDDLMKARRSvLDPPGEGSNLipgDVLWSDPSLTPGLSPNKqRGIGLLWGPDCTEEFLEKNNLKLII 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 425 RSHEVK------------AEGYEVAH---GGRCVTVFSAPNYC------DQMGNKASYIHLQGSDLR-PQFHQFTAV-PH 481
Cdd:cd07418  290 RSHEGPdarekrpglagmNKGYTVDHdveSGKLITLFSAPDYPqfqateERYNNKGAYIILQPPDFSdPQFHTFEAVkPR 369


                 ....*
gi 199559777 482 PNVKP 486
Cdd:cd07418  370 PKANP 374
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 211-464 6.65e-72

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 230.18  E-value: 6.65e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 211 QILVQVKEVLCKLSTLVETTLKE------TEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVIL 284
Cdd:PTZ00244  22 QILIREEDIRAVLTEVREIFMSQpmlleiRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETIT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 285 TLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLD 364
Cdd:PTZ00244 101 LQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 365 DIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCV 443
Cdd:PTZ00244 180 SVNEIERPCDVPDRGILCDLLWADPEDEvRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLV 259

                        250       260
                 ....*....|....*....|.
gi 199559777 444 TVFSAPNYCDQMGNKASYIHL 464
Cdd:PTZ00244 260 TVFSAPNYCGEFDNDAAVMNI 280
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 237-480 2.92e-71

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 228.93  E-value: 2.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 237 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 316
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 317 GEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGR 395
Cdd:PTZ00239 124 EEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGL-SPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 396 SVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGR-CVTVFSAPNYCDQMGNKASYIHLQgSDLRPQFH 474
Cdd:PTZ00239 203 AVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQnLVTVWSAPNYCYRCGNIASILCLD-ENLQQTWK 281


                 ....*.
gi 199559777 475 QFTAVP 480
Cdd:PTZ00239 282 TFKEVP 287
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 237-467 4.53e-67

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 218.76  E-value: 4.53e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 237 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 316
Cdd:PTZ00480  61 LKICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 317 GEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGR 395
Cdd:PTZ00480 140 DECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGL-SPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDvQGW 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 199559777 396 SVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGS 467
Cdd:PTZ00480 219 ADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDES 290
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 229-469 1.21e-58

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: 196.12  E-value: 1.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 229 TTLKETEKITVCGDTHGQFYDLLNIFELNGLPS-------ETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLR 301
Cdd:cd07419   42 SVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIR 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 302 GNHETDNMNQIYGFEGEVKAKYTAQM------YELFSEVFEWLPLAQCINGKVLIMHGGLfsedGVTLDDIRKIERNRQP 375
Cdd:cd07419  122 GNHEAADINALFGFREECIERLGEDIrdgdsvWQRINRLFNWLPLAALIEDKIICVHGGI----GRSINHIHQIENLKRP 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 376 ---PDSGP-MCDLLWSDP---------QPQNGRSVSKrGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRC 442
Cdd:cd07419  198 itmEAGSPvVMDLLWSDPtendsvlglRPNAIDPRGT-GLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHL 276

                        250       260
                 ....*....|....*....|....*..
gi 199559777 443 VTVFSAPNYCDQMGNKASYIHLqGSDL 469
Cdd:cd07419  277 ITLFSATNYCGTAGNAGAILVL-GRDL 302
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-228 3.67e-43

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: 147.62  E-value: 3.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  136 YQECSKIVKQKAFERAIAGDEHRrSVVDSLDIESMTIEDEYSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQ 215
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEEKP-SAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQILLK 79

                          90
                  ....*....|...
gi 199559777  216 VKEVLCKLSTLVE 228
Cdd:pfam08321  80 VKEILKKEPSLVE 92
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
2-129 2.87e-20

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 89.59  E-value: 2.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   2 AMAEGERTECAETPRDEPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYA 81
Cdd:COG4785   47 ALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAA 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 199559777  82 LGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPND 129
Cdd:COG4785  127 LEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPND 174
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 236-346 4.14e-18

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: 79.95  E-value: 4.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  236 KITVCGDTH--GQFYDLLNIFElnGLPSETNPYIF--NGDFVDRGSFSVEVILTLfgFKLLYPDHFHLLRGNHETDNMNQ 311
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK--KLLEEGKPDLVlhAGDLVDRGPPSEEVLELL--ERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 199559777  312 IYGFEGEvkaKYTAQMYELFSEVFEWLPLAQCING 346
Cdd:pfam00149  78 LRLYPYL---GLLARPWKRFLEVFNFLPLAGILSG 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
28-132 5.58e-18

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 83.52  E-value: 5.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:COG0457    8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQ 87

                         90       100
                 ....*....|....*....|....*
gi 199559777 108 ALGKFRAALRDYETVVKVKPNDKDA 132
Cdd:COG0457   88 ALGRYEEALEDYDKALELDPDDAEA 112
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
28-153 1.49e-17

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 81.98  E-value: 1.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:COG0457   42 AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALL 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 199559777 108 ALGKFRAALRDYETVVKVKPNDKDAKMKYQECSKivKQKAFERAIA 153
Cdd:COG0457  122 ELGRYDEAIEAYERALELDPDDADALYNLGIALE--KLGRYEEALE 165
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 28-139 1.41e-16

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 80.99  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:PLN03088   2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                         90       100       110
                 ....*....|....*....|....*....|..
gi 199559777 108 ALGKFRAALRDYETVVKVKPNDKDAKMKYQEC 139
Cdd:PLN03088  82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKEC 113
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 26-119 3.08e-15

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: 78.49  E-value: 3.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPgNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:TIGR00990 125 KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANA 203

                          90
                  ....*....|....
gi 199559777  106 NMALGKFRAALRDY 119
Cdd:TIGR00990 204 YDGLGKYADALLDL 217
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 12-127 2.46e-14

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: 70.37  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  12 AETPRDEPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIEL 91
Cdd:COG5010   38 KEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL 117

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 199559777  92 DKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKP 127
Cdd:COG5010  118 SPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 35-134 1.41e-13

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 67.72  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG4235   24 GRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAE 103

                         90       100
                 ....*....|....*....|
gi 199559777 115 ALRDYETVVKVKPNDKDAKM 134
Cdd:COG4235  104 AIAAWQKLLALLPADAPARL 123
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
38-120 2.54e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 69.65  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  38 YFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                 ...
gi 199559777 118 DYE 120
Cdd:COG0457  166 LLE 168
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
38-128 2.76e-13

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 65.58  E-value: 2.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  38 YFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALgDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                         90
                 ....*....|.
gi 199559777 118 DYETVVKVKPN 128
Cdd:COG3063   81 YLERALELDPS 91
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 35-129 3.34e-13

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 66.75  E-value: 3.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG4783   45 GEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDE 124

                         90
                 ....*....|....*
gi 199559777 115 ALRDYETVVKVKPND 129
Cdd:COG4783  125 AIAALEKALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 18-132 6.78e-13

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 71.18  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  18 EPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIK 97
Cdd:COG3914   68 AAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 199559777  98 GYYRRAASNMALGKFRAALRDYETVVKVKPNDKDA 132
Cdd:COG3914  148 AYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA 182
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 27-155 1.18e-12

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: 65.21  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  27 RAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASN 106
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 199559777 107 MALGKFRAALRDYETVVKVKPNDKDAKMKYQECSKIVKQ-----KAFERAIAGD 155
Cdd:COG4783   83 LKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRpdeaiAALEKALELD 136
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 26-153 1.69e-12

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: 67.83  E-value: 1.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:COG2956  108 DDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAEL 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 199559777 106 NMALGKFRAALRDYETVVKVKPNDKDAKMKYQECSKivKQKAFERAIA 153
Cdd:COG2956  188 YLEQGDYEEAIAALERALEQDPDYLPALPRLAELYE--KLGDPEEALE 233
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
27-132 2.84e-11

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 63.40  E-value: 2.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  27 RAEELKTQANDYFKAKDYENAIkfysQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASN 106
Cdd:COG4785   42 ADLALALAAAALAAAALAAERI----DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAY 117

                         90       100
                 ....*....|....*....|....*.
gi 199559777 107 MALGKFRAALRDYETVVKVKPNDKDA 132
Cdd:COG4785  118 LLLGDYDAALEDFDRALELDPDYAYA 143
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
55-132 3.62e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 63.49  E-value: 3.62e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 199559777  55 IELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPNDKDA 132
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA 78
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 35-132 5.35e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 65.01  E-value: 5.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG3914  119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEE 198

                         90
                 ....*....|....*...
gi 199559777 115 ALRDYETVVKVKPNDKDA 132
Cdd:COG3914  199 AIAAYRRALELDPDNADA 216
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 35-153 6.22e-11

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 63.21  E-value: 6.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG2956   83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 199559777 115 ALRDYETVVKVKPNDKDAKMKYQECSkiVKQKAFERAIA 153
Cdd:COG2956  163 AIEALEKALKLDPDCARALLLLAELY--LEQGDYEEAIA 199
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 24-153 3.61e-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: 60.90  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  24 TLKRAEELKTQ--------ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKY 95
Cdd:COG2956  132 VLERLLKLGPEnahaycelAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 199559777  96 IKGYYRRAASNMALGKFRAALRDYETVVKVKPNDKDAKMKYQecsKIVKQKAFERAIA 153
Cdd:COG2956  212 LPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD---LLERKEGLEAALA 266
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 37-133 3.47e-08

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: 51.53  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  37 DYFKAKDYENAIKFYSQAIELNPGNAiyYGNRSLaYLRTECYgYALGDATRAIELDKKYIKGY----------YRRAASN 106
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSP--LAPDAL-YWLGEAY-YALGDYDEAAEAFEKLLKRYpdspkapdalLKLGLSY 77

                         90       100
                 ....*....|....*....|....*..
gi 199559777 107 MALGKFRAALRDYETVVKVKPNDKDAK 133
Cdd:COG1729   78 LELGDYDKARATLEELIKKYPDSEAAK 104
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 11-151 5.93e-08

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 53.73  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  11 CAETPRDEPPADgtlkrAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAiyYGNRS---LAYlrteCYgYALGDATR 87
Cdd:COG4105   20 CSSFKKALKSWD-----AEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSP--YAEQAqlmLAY----AY-YKQGDYEE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  88 AIELDKKYIKGY----------YRRAASNMALGK--------FRAALRDYETVVKVKPNDK---DAKMKYQECSKIVKQK 146
Cdd:COG4105   88 AIAAADRFIKLYpnspnadyayYLRGLSYYEQSPdsdrdqtsTRKAIEAFQELINRYPDSEyaeDAKKRIDELRDKLARK 167


                 ....*
gi 199559777 147 AFERA 151
Cdd:COG4105  168 ELEVA 172
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 11-139 1.55e-07

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 52.17  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   11 CA--ETPRDEPPADGTlkrAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAiyYGNRS---LAYlrteCYgYALGDA 85
Cdd:TIGR03302  17 CSskKKKEADPVEEWP---AEELYEEAKEALDSGDYTEAIKYFEALESRYPFSP--YAEQAqldLAY----AY-YKSGDY 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 199559777   86 TRAIELDKKYIK----------GYYRRAASNMAL--------GKFRAALRDYETVVKVKPNDK---DAKMKYQEC 139
Cdd:TIGR03302  87 AEAIAAADRFIRlhpnhpdadyAYYLRGLSNYNQidrvdrdqTAAREAFEAFQELIRRYPNSEyapDAKKRMDYL 161
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
35-120 3.85e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.16  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYlrtecygYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG0457  117 GLALLELGRYDEAIEAYERALELDPDDADALYNLGIAL-------EKLGRYEEALELLEKLEAAALAALLAAALGEAALA 189


                 ....*.
gi 199559777 115 ALRDYE 120
Cdd:COG0457  190 LAAAEV 195
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 35-153 4.03e-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: 51.65  E-value: 4.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG2956   49 GNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEK 128

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 199559777 115 ALRDYETVVKVKPNDKDAKMKYQECSkiVKQKAFERAIA 153
Cdd:COG2956  129 AIEVLERLLKLGPENAHAYCELAELY--LEQGDYDEAIE 165
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 47-134 6.31e-07

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 48.46  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  47 AIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVK 126
Cdd:COG4235    2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD 81


                 ....*...
gi 199559777 127 PNDKDAKM 134
Cdd:COG4235   82 PDNPEALY 89
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 241-369 3.91e-06

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 47.68  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 241 GDTHGQFYDLLNIFELNGLPSETNPYIFN-------GDFVDRGSFSVEVIltlFGFKLLYPD------HFHLLRGNHETd 307
Cdd:cd07425    4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEIL---KLLEKLKRQarkaggKVILLLGNHEL- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 199559777 308 nMNQI----YGFEGEVKAKYT--AQMYELFS---EVFEWL---PLAQCINGkVLIMHGGLfsedGVTLDdiRKI 369
Cdd:cd07425   80 -MNLCgdfrYVHPRGLNEFGGvaKRRYALLSdggYIGRYLrthPVVLVVND-ILFVHGGL----GPLWS--RGY 145
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 41-152 4.11e-06

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 49.70  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   41 AKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYE 120
Cdd:TIGR02917 172 ENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHAD 251

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 199559777  121 TVVKVKPNDK-----DAKMKYQecskivkQKAFERAI 152
Cdd:TIGR02917 252 ALLKKAPNSPlahylKALVDFQ-------KKNYEDAR 281
TPR_11 pfam13414
TPR repeat;
35-74 9.10e-06

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 42.46  E-value: 9.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 199559777   35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLR 74
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 28-61 1.21e-05

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: 42.05  E-value: 1.21e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 199559777    28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGN 61
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
TPR_1 pfam00515
Tetratricopeptide repeat;
28-61 1.29e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.02  E-value: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 199559777   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGN 61
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 239-305 1.70e-05

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: 44.57  E-value: 1.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 239 VCGDTHGQFYDLLNIFELNgLPSETNP--YIFNGDFVDRGSFSVEVILTLFGFKLL-YPDHFhlLRGNHE 305
Cdd:cd00838    2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLLAgIPVYV--VPGNHD 68
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 28-115 3.56e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.52  E-value: 3.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKgyyrrAASNM 107
Cdd:COG3914  146 AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNAD-----AHSNL 220


                 ....*...
gi 199559777 108 ALGKFRAA 115
Cdd:COG3914  221 LFALRQAC 228
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 28-60 4.82e-05

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: 40.20  E-value: 4.82e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 199559777   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPG 60
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 29-97 1.11e-04

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


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 44.16  E-value: 1.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199559777  29 EELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLrtecygyALGDATRAIELDKKYIK 97
Cdd:cd24142    1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILL-------ELGDVEEAREVLLRAIE 62
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 237-352 1.70e-04

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, 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: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 42.69  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777 237 ITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETDNMNQIYGFE 316
Cdd:cd07424    3 DFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVL------ELLKQPWFHAVQGNHEQMAIDALRGGD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 199559777 317 GEVKAKY--------TAQMYELFSEVFEWLPLAQCI---NGKVLIMH 352
Cdd:cd07424   77 DVMWRANgggwffdlPDEEAKVLLEKLHHLPIAIEVesrNGKVGIVH 123
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 81-153 3.43e-04

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 40.76  E-value: 3.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 199559777  81 ALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPNDKDAKMKYQECskIVKQKAFERAIA 153
Cdd:COG4235    2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEA--LLAAGDTEEAEE 72
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 29-155 6.01e-04

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


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 42.28  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   29 EELKTQANDYFKAKD------YENAIKFYSQAIELN---PGNAIYYGNR-SLAYLRTECYGyALGDATRAIELDKKYIKG 98
Cdd:TIGR00990 289 ETGNGQLQLGLKSPEskadesYEEAARAFEKALDLGklgEKEAIALNLRgTFKCLKGKHLE-ALADLSKSIELDPRVTQS 367

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 199559777   99 YYRRAASNMALGKFRAALRDYETVVKVKPNDKD-----AKMKYQECSKIVKQKAFERAIAGD 155
Cdd:TIGR00990 368 YIKRASMNLELGDPDKAEEDFDKALKLNSEDPDiyyhrAQLHFIKGEFAQAGKDYQKSIDLD 429
PHA02239 PHA02239
putative protein phosphatase
 237-312 8.72e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 41.13  E-value: 8.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199559777 237 ITVCGDTHGQFYDLLNIfeLNGLPSETNP---YIFNGDFVDRGSFSVEVILTLFGFkLLYPDHFHLLRGNHETDNMNQI 312
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTI--MDKINNERKPeetIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDDEFYNIM 78
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 24-132 9.44e-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: 41.99  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   24 TLKRAEE----LKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLrtecygyALGDATRAI-------ELD 92
Cdd:TIGR02917 321 ILKYAPNshqaRRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYL-------ALGDFEKAAeylakatELD 393

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 199559777   93 KKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPNDKDA 132
Cdd:TIGR02917 394 PENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRA 433
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 236-305 1.09e-03

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, 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: 163664  Cd Length: 304  Bit Score: 40.95  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 199559777 236 KITVC-GDTHGqFYDLLNIFELNgLPSETNP-------YIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFH-LLRGNHE 305
Cdd:cd07421    2 RVVICvGDIHG-YISKLNNLWLN-LQSALGPsdfasalVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHD 78
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 33-99 1.19e-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: 37.32  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   33 TQANDYFKAKDYENAIKFYSQAIELN---PGNAIYYGNRSLAYLRtecygyaLGDATRAIELDKKYIKGY 99
Cdd:pfam13432   2 ALARAALRAGDYDDAAAALEAALARFpesPDAAAALLLLGLAALR-------QGRLAEAAAAYRAALRAA 64
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 23-128 1.91e-03

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: 40.74  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   23 GTLKRAEELKTQANDYFK--AKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYY 100
Cdd:TIGR00990 324 GKLGEKEAIALNLRGTFKclKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYY 403

                          90       100
                  ....*....|....*....|....*...
gi 199559777  101 RRAASNMALGKFRAALRDYETVVKVKPN 128
Cdd:TIGR00990 404 HRAQLHFIKGEFAQAGKDYQKSIDLDPD 431
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 34-91 3.06e-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: 3.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 199559777   34 QANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNrsLAYLRTECYG-YALGDATRAIEL 91
Cdd:TIGR02917 776 LAELYLAQKDYDKAIKHYQTVVKKAPDNAVVLNN--LAWLYLELKDpRALEYAERALKL 832
TPR_1 pfam00515
Tetratricopeptide repeat;
96-129 3.27e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 35.09  E-value: 3.27e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 199559777   96 IKGYYRRAASNMALGKFRAALRDYETVVKVKPND 129
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR_12 pfam13424
Tetratricopeptide repeat;
35-99 3.90e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 36.21  E-value: 3.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   35 ANDYFKAKDYENAIKFYSQAIELnpgNAIYYGNRSLAYLRT-----ECYgYALGDATRAIELDKKYIKGY 99
Cdd:pfam13424  10 AAVLRRLGRYDEALELLEKALEI---ARRLLGPDHPLTATTllnlgRLY-LELGRYEEALELLERALALA 75
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
236-307 4.69e-03

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 199559777 236 KITVCGDTHGQFYDLLNIFE-LNGLPSETnpYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETD 307
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEdLEREGVDL--IVHLGDLVGYGPDPPEVL------DLLRELPIVAVRGNHDGA 65
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 38-129 5.21e-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: 39.68  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 199559777   38 YFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:TIGR02917 373 YLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFDKALA 452

                          90
                  ....*....|..
gi 199559777  118 DYETVVKVKPND 129
Cdd:TIGR02917 453 AAKKLEKKQPDN 464
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 27-76 8.46e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 38.82  E-value: 8.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 199559777  27 RAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTE 76
Cdd:COG3914  179 NAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQAC 228
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 35-108 9.64e-03

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: 36.52  E-value: 9.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 199559777  35 ANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMA 108
Cdd:COG4235   58 AEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLLEASIAEA 131
 
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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