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Conserved domains on  [gi|324021716|ref|NP_001191213|]
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serine/threonine-protein phosphatase 5 isoform 2 [Homo sapiens]

Protein Classification

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 ...
 176-469 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: 655.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 176 YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQ----------------------TEKITVCGDTHGQFYDLLNIFE 233
Cdd:cd07417    1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQillqvkeilkklpslveitipeGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 234 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 313
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 314 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL 393
Cdd:cd07417  161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716 394 EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 469
Cdd:cd07417  241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-211 1.26e-35

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: 127.20  E-value: 1.26e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716  136 YQECNKIVKQKAFERAIAGDEhKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQ 211
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEE-KPSAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQ 75
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-129 6.73e-19

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


:

Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 85.35  E-value: 6.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  19 PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKG 98
Cdd:COG4785   64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 324021716  99 YYRRAASNMALGKFRAALRDYETVVKVKPHD 129
Cdd:COG4785  144 YLNRGIALYYLGRYELAIADLEKALELDPND 174
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-469 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: 655.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 176 YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQ----------------------TEKITVCGDTHGQFYDLLNIFE 233
Cdd:cd07417    1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQillqvkeilkklpslveitipeGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 234 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 313
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 314 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL 393
Cdd:cd07417  161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716 394 EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 469
Cdd:cd07417  241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 212-458 3.31e-134

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: 388.11  E-value: 3.31e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   212 TEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIY 291
Cdd:smart00156  27 SAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIY 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   292 GFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDP-QPQ 370
Cdd:smart00156 106 GFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPdQPV 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   371 NGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQ 450
Cdd:smart00156 185 NGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKV-DKDLKLT 263


                   ....*...
gi 324021716   451 FHQFTAVP 458
Cdd:smart00156 264 FEQFKPGK 271
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 215-458 1.27e-71

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 229.32  E-value: 1.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGR 373
Cdd:PTZ00239 124 EEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGL-SPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 374 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGR-CVTVFSAPNYCDQMGNKASYIHLQgSDLRPQFH 452
Cdd:PTZ00239 203 AVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQnLVTVWSAPNYCYRCGNIASILCLD-ENLQQTWK 281


                 ....*.
gi 324021716 453 QFTAVP 458
Cdd:PTZ00239 282 TFKEVP 287
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-211 1.26e-35

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: 127.20  E-value: 1.26e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716  136 YQECNKIVKQKAFERAIAGDEhKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQ 211
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEE-KPSAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQ 75
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-129 6.73e-19

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 85.35  E-value: 6.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  19 PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKG 98
Cdd:COG4785   64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 324021716  99 YYRRAASNMALGKFRAALRDYETVVKVKPHD 129
Cdd:COG4785  144 YLNRGIALYYLGRYELAIADLEKALELDPND 174
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 214-324 9.98e-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: 78.79  E-value: 9.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  214 KITVCGDTH--GQFYDLLNIFElnGLPSETNPYIF--NGDFVDRGSFSVEVILTLfgFKLLYPDHFHLLRGNHETDNMNQ 289
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK--KLLEEGKPDLVlhAGDLVDRGPPSEEVLELL--ERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 324021716  290 IYGFEGEvkaKYTAQMYELFSEVFEWLPLAQCING 324
Cdd:pfam00149  78 LRLYPYL---GLLARPWKRFLEVFNFLPLAGILSG 109
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 28-145 9.02e-17

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 81.37  E-value: 9.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:PLN03088   2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 324021716 108 ALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQ 145
Cdd:PLN03088  82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAE 119
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 26-119 3.31e-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: 78.10  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPsNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:TIGR00990 125 KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANA 203

                          90
                  ....*....|....
gi 324021716  106 NMALGKFRAALRDY 119
Cdd:TIGR00990 204 YDGLGKYADALLDL 217
TPR_11 pfam13414
TPR repeat;
35-74 1.88e-06

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 44.38  E-value: 1.88e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 324021716   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLR 74
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 28-61 8.38e-06

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: 42.43  E-value: 8.38e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 324021716    28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSN 61
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 29-97 1.24e-05

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: 46.85  E-value: 1.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 324021716  29 EELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLrtecygyALGDATRAIELDKKYIK 97
Cdd:cd24142    1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILL-------ELGDVEEAREVLLRAIE 62
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
214-285 4.44e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 324021716 214 KITVCGDTHGQFYDLLNIFE-LNGLPSETnpYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETD 285
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 ...
 176-469 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: 655.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 176 YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQ----------------------TEKITVCGDTHGQFYDLLNIFE 233
Cdd:cd07417    1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQillqvkeilkklpslveitipeGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 234 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 313
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 314 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL 393
Cdd:cd07417  161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716 394 EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 469
Cdd:cd07417  241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 212-458 3.31e-134

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: 388.11  E-value: 3.31e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   212 TEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIY 291
Cdd:smart00156  27 SAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIY 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   292 GFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDP-QPQ 370
Cdd:smart00156 106 GFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPdQPV 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   371 NGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQ 450
Cdd:smart00156 185 NGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKV-DKDLKLT 263


                   ....*...
gi 324021716   451 FHQFTAVP 458
Cdd:smart00156 264 FEQFKPGK 271
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 215-458 1.23e-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: 308.36  E-value: 1.23e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:cd07415   44 VTVCGDIHGQFYDLLELFRIGGDVPDTN-YLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFY 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGR 373
Cdd:cd07415  123 DECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGL-SPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGW 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 374 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQ 453
Cdd:cd07415  202 GISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILEL-DEHLNRSFKQ 280


                 ....*
gi 324021716 454 FTAVP 458
Cdd:cd07415  281 FEAAP 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 216-442 1.36e-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: 293.12  E-value: 1.36e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 216 TVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEG 295
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 296 EV----KAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEdgVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQN 371
Cdd:cd00144   80 ERtlrcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPD--LTLLDQIRNIRPIENPDDQLVEDLLWSDPDESV 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 324021716 372 GRS-ISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHL 442
Cdd:cd00144  158 GDFeSSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 212-454 2.09e-95

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: 290.08  E-value: 2.09e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 212 TEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIY 291
Cdd:cd07420   50 SKEVTICGDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 292 GFEGEVKAKY---TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfsEDGVTLDDIRKIERNR---QPPDSGPMCDLLWS 365
Cdd:cd07420  130 GFTKEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGI--SDSTDLDLLDKIDRHKyvsTKTEWQQVVDILWS 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 366 DPQPQNG-RSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLqG 444
Cdd:cd07420  208 DPKATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKL-G 286

                        250
                 ....*....|
gi 324021716 445 SDLRPQFHQF 454
Cdd:cd07420  287 PQLTPHFVQY 296
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 215-460 3.70e-92

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: 282.27  E-value: 3.70e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:cd07416   45 VTVCGDIHGQFYDLLKLFEVGGSPANTR-YLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFK 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDP--QPQNG 372
Cdd:cd07416  124 QECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGL-SPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPleDFGNE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 373 RSI------SKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGR------CVTVFSAPNYCDQMGNKASYI 440
Cdd:cd07416  203 KTQehfvhnTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVL 282

                        250       260
                 ....*....|....*....|
gi 324021716 441 HLQGSDLRpqFHQFTAVPHP 460
Cdd:cd07416  283 KYENNVMN--IRQFNCSPHP 300
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 215-435 8.42e-85

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


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 262.66  E-value: 8.42e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:cd07414   52 LKICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGR 373
Cdd:cd07414  131 DECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGL-SPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDvQGW 209

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 324021716 374 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGN 435
Cdd:cd07414  210 GENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDN 271
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 211-464 6.85e-74

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: 237.39  E-value: 6.85e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 211 QTEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQI 290
Cdd:cd07418   64 DVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSM 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 291 YGFEGEVKAKY---TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLF--------------------SEDGV------TL 341
Cdd:cd07418  144 YGFEQEVLTKYgdkGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFrspslpkrkkqkgknrrvllLEPESeslklgTL 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 342 DDIRKIERN-RQPPDSGPMC---DLLWSDPQPQNGRSISK-RGVSCQFGPDVTKAFLEENNLDYIIRSHEVK-------- 408
Cdd:cd07418  224 DDLMKARRSvLDPPGEGSNLipgDVLWSDPSLTPGLSPNKqRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPdarekrpg 303

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 324021716 409 ----AEGYEVAH---GGRCVTVFSAPNYC------DQMGNKASYIHLQGSDLR-PQFHQFTAV-PHPNVKP 464
Cdd:cd07418  304 lagmNKGYTVDHdveSGKLITLFSAPDYPqfqateERYNNKGAYIILQPPDFSdPQFHTFEAVkPRPKANP 374
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 215-458 1.27e-71

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 229.32  E-value: 1.27e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGR 373
Cdd:PTZ00239 124 EEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGL-SPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 374 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGR-CVTVFSAPNYCDQMGNKASYIHLQgSDLRPQFH 452
Cdd:PTZ00239 203 AVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQnLVTVWSAPNYCYRCGNIASILCLD-ENLQQTWK 281


                 ....*.
gi 324021716 453 QFTAVP 458
Cdd:PTZ00239 282 TFKEVP 287
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 215-442 5.29e-71

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 227.10  E-value: 5.29e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGR 373
Cdd:PTZ00244 133 DDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEvRGF 211

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 324021716 374 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHL 442
Cdd:PTZ00244 212 LESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNI 280
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 215-445 8.35e-67

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 217.22  E-value: 8.35e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:PTZ00480  61 LKICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 295 GEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGR 373
Cdd:PTZ00480 140 DECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGL-SPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDvQGW 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 324021716 374 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGS 445
Cdd:PTZ00480 219 ADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDES 290
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 215-447 2.62e-59

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: 197.28  E-value: 2.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPS-------ETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNM 287
Cdd:cd07419   50 IKIFGDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 288 NQIYGFEGEVKAKYTAQM------YELFSEVFEWLPLAQCINGKVLIMHGGLfsedGVTLDDIRKIERNRQP---PDSGP 358
Cdd:cd07419  130 NALFGFREECIERLGEDIrdgdsvWQRINRLFNWLPLAALIEDKIICVHGGI----GRSINHIHQIENLKRPitmEAGSP 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 359 -MCDLLWSDP---------QPqNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPN 428
Cdd:cd07419  206 vVMDLLWSDPtendsvlglRP-NAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATN 284

                        250
                 ....*....|....*....
gi 324021716 429 YCDQMGNKASYIHLqGSDL 447
Cdd:cd07419  285 YCGTAGNAGAILVL-GRDL 302
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-211 1.26e-35

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: 127.20  E-value: 1.26e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716  136 YQECNKIVKQKAFERAIAGDEhKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQ 211
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEE-KPSAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQ 75
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-129 6.73e-19

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 85.35  E-value: 6.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  19 PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKG 98
Cdd:COG4785   64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143

                         90       100       110
                 ....*....|....*....|....*....|.
gi 324021716  99 YYRRAASNMALGKFRAALRDYETVVKVKPHD 129
Cdd:COG4785  144 YLNRGIALYYLGRYELAIADLEKALELDPND 174
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 214-324 9.98e-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: 78.79  E-value: 9.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  214 KITVCGDTH--GQFYDLLNIFElnGLPSETNPYIF--NGDFVDRGSFSVEVILTLfgFKLLYPDHFHLLRGNHETDNMNQ 289
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK--KLLEEGKPDLVlhAGDLVDRGPPSEEVLELL--ERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 324021716  290 IYGFEGEvkaKYTAQMYELFSEVFEWLPLAQCING 324
Cdd:pfam00149  78 LRLYPYL---GLLARPWKRFLEVFNFLPLAGILSG 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
28-132 7.65e-17

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 80.05  E-value: 7.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:COG0457    8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQ 87

                         90       100
                 ....*....|....*....|....*
gi 324021716 108 ALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG0457   88 ALGRYEEALEDYDKALELDPDDAEA 112
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
28-153 8.91e-17

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 79.67  E-value: 8.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:COG0457   42 AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALL 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 324021716 108 ALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKivKQKAFERAIA 153
Cdd:COG0457  122 ELGRYDEAIEAYERALELDPDDADALYNLGIALE--KLGRYEEALE 165
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 28-145 9.02e-17

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 81.37  E-value: 9.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:PLN03088   2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 324021716 108 ALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQ 145
Cdd:PLN03088  82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAE 119
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 26-119 3.31e-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: 78.10  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPsNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:TIGR00990 125 KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANA 203

                          90
                  ....*....|....
gi 324021716  106 NMALGKFRAALRDY 119
Cdd:TIGR00990 204 YDGLGKYADALLDL 217
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 12-127 3.62e-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: 69.99  E-value: 3.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  12 AEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIEL 91
Cdd:COG5010   38 KEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL 117

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 324021716  92 DKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKP 127
Cdd:COG5010  118 SPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
38-120 3.51e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 69.27  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  38 YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:COG0457   86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                 ...
gi 324021716 118 DYE 120
Cdd:COG0457  166 LLE 168
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 24-134 3.93e-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: 66.18  E-value: 3.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  24 ALKRAEE-LKTQAND----------YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELD 92
Cdd:COG4235    2 AIARLRQaLAANPNDaegwlllgraYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 324021716  93 KKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKM 134
Cdd:COG4235   82 PDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
38-127 6.55e-13

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 64.42  E-value: 6.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  38 YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALgDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                         90
                 ....*....|
gi 324021716 118 DYETVVKVKP 127
Cdd:COG3063   81 YLERALELDP 90
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 18-132 1.29e-12

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 70.02  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  18 EPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIK 97
Cdd:COG3914   68 AAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 324021716  98 GYYRRAASNMALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG3914  148 AYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA 182
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 35-129 1.33e-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: 64.83  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG4783   45 GEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDE 124

                         90
                 ....*....|....*
gi 324021716 115 ALRDYETVVKVKPHD 129
Cdd:COG4783  125 AIAALEKALELDPDD 139
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 27-155 4.26e-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: 63.67  E-value: 4.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  27 RAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASN 106
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 324021716 107 MALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQ-----KAFERAIAGD 155
Cdd:COG4783   83 LKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRpdeaiAALEKALELD 136
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 23-139 7.80e-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: 65.52  E-value: 7.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  23 GALKRAEE-----LKTQAND----------YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATR 87
Cdd:COG2956   90 GLLDRAEElleklLELDPDDaealrllaeiYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 324021716  88 AIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQEC 139
Cdd:COG2956  170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAEL 221
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 35-132 6.49e-11

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 64.63  E-value: 6.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG3914  119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEE 198

                         90
                 ....*....|....*...
gi 324021716 115 ALRDYETVVKVKPHDKDA 132
Cdd:COG3914  199 AIAAYRRALELDPDNADA 216
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
55-132 1.35e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.56  E-value: 1.35e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 324021716  55 IELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA 78
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 35-153 1.66e-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: 61.67  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG2956   83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 324021716 115 ALRDYETVVKVKPHDKDAKMKYQECNkiVKQKAFERAIA 153
Cdd:COG2956  163 AIEALEKALKLDPDCARALLLLAELY--LEQGDYEEAIA 199
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
27-132 1.96e-10

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 60.70  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  27 RAEELKTQANDYFKAKDYENAIkfysQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASN 106
Cdd:COG4785   42 ADLALALAAAALAAAALAAERI----DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAY 117

                         90       100
                 ....*....|....*....|....*.
gi 324021716 107 MALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG4785  118 LLLGDYDAALEDFDRALELDPDYAYA 143
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 24-153 1.35e-09

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: 58.97  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  24 ALKRAEELKTQ--------ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKY 95
Cdd:COG2956  132 VLERLLKLGPEnahaycelAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 324021716  96 IKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQecnKIVKQKAFERAIA 153
Cdd:COG2956  212 LPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD---LLERKEGLEAALA 266
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 37-133 3.19e-07

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: 48.83  E-value: 3.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  37 DYFKAKDYENAIKFYSQAIELNPSNAiyYGNRSLaYLRTECYgYALGDATRAIELDKKYIKGY----------YRRAASN 106
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSP--LAPDAL-YWLGEAY-YALGDYDEAAEAFEKLLKRYpdspkapdalLKLGLSY 77

                         90       100
                 ....*....|....*....|....*..
gi 324021716 107 MALGKFRAALRDYETVVKVKPHDKDAK 133
Cdd:COG1729   78 LELGDYDKARATLEELIKKYPDSEAAK 104
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 35-153 7.59e-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: 50.50  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG2956   49 GNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEK 128

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 324021716 115 ALRDYETVVKVKPHDKDAKMKYQECNkiVKQKAFERAIA 153
Cdd:COG2956  129 AIEVLERLLKLGPENAHAYCELAELY--LEQGDYDEAIE 165
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
35-120 1.06e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.01  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYlrtecygYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG0457  117 GLALLELGRYDEAIEAYERALELDPDDADALYNLGIAL-------EKLGRYEEALELLEKLEAAALAALLAAALGEAALA 189


                 ....*.
gi 324021716 115 ALRDYE 120
Cdd:COG0457  190 LAAAEV 195
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 28-149 1.13e-06

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: 49.47  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAiyYGNRS---LAYlrteCYgYALGDATRAIELDKKYIK------- 97
Cdd:TIGR03302  33 AEELYEEAKEALDSGDYTEAIKYFEALESRYPFSP--YAEQAqldLAY----AY-YKSGDYAEAIAAADRFIRlhpnhpd 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 324021716   98 ---GYYRRAASNMAL--------GKFRAALRDYETVVKVKPHDK---DAKMKYQECNKIVKQKAFE 149
Cdd:TIGR03302 106 adyAYYLRGLSNYNQidrvdrdqTAAREAFEAFQELIRRYPNSEyapDAKKRMDYLRNRLAGKELY 171
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 28-151 1.65e-06

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


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 49.49  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAiyYGNRS---LAYlrteCYgYALGDATRAIELDKKYIKGY----- 99
Cdd:COG4105   32 AEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSP--YAEQAqlmLAY----AY-YKQGDYEEAIAAADRFIKLYpnspn 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 324021716 100 -----YRRAASNMALGK--------FRAALRDYETVVKVKPHDK---DAKMKYQECNKIVKQKAFERA 151
Cdd:COG4105  105 adyayYLRGLSYYEQSPdsdrdqtsTRKAIEAFQELINRYPDSEyaeDAKKRIDELRDKLARKELEVA 172
TPR_11 pfam13414
TPR repeat;
35-74 1.88e-06

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 44.38  E-value: 1.88e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 324021716   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLR 74
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 219-347 3.68e-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: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 219 GDTHGQFYDLLNIFELNGLPSETNPYIFN-------GDFVDRGSFSVEVIltlFGFKLLYPD------HFHLLRGNHETd 285
Cdd:cd07425    4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEIL---KLLEKLKRQarkaggKVILLLGNHEL- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 324021716 286 nMNQI----YGFEGEVKAKYT--AQMYELFS---EVFEWL---PLAQCINGkVLIMHGGLfsedGVTLDdiRKI 347
Cdd:cd07425   80 -MNLCgdfrYVHPRGLNEFGGvaKRRYALLSdggYIGRYLrthPVVLVVND-ILFVHGGL----GPLWS--RGY 145
TPR_1 pfam00515
Tetratricopeptide repeat;
28-61 7.58e-06

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.41  E-value: 7.58e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 324021716   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSN 61
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 28-61 8.38e-06

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: 42.43  E-value: 8.38e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 324021716    28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSN 61
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPNN 34
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 29-97 1.24e-05

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: 46.85  E-value: 1.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 324021716  29 EELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLrtecygyALGDATRAIELDKKYIK 97
Cdd:cd24142    1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILL-------ELGDVEEAREVLLRAIE 62
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 41-152 2.07e-05

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 47.00  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   41 AKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYE 120
Cdd:TIGR02917 172 ENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHAD 251

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 324021716  121 TVVKVKP-----HDKDAKMKYQecnkivkQKAFERAI 152
Cdd:TIGR02917 252 ALLKKAPnsplaHYLKALVDFQ-------KKNYEDAR 281
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 217-283 2.64e-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: 43.80  E-value: 2.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 217 VCGDTHGQFYDLLNIFELNgLPSETNP--YIFNGDFVDRGSFSVEVILTLFGFKLL-YPDHFhlLRGNHE 283
Cdd:cd00838    2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLLAgIPVYV--VPGNHD 68
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 21-115 3.18e-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: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  21 ADGALKRAEELK--------TQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELD 92
Cdd:COG3914  131 ALAALRRALALNpdfaeaylNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELD 210

                         90       100
                 ....*....|....*....|...
gi 324021716  93 KKYIKgyyrrAASNMALGKFRAA 115
Cdd:COG3914  211 PDNAD-----AHSNLLFALRQAC 228
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 28-59 7.03e-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: 39.81  E-value: 7.03e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 324021716   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNP 59
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDP 32
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 215-330 1.60e-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: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716 215 ITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETDNMNQIYGFE 294
Cdd:cd07424    3 DFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVL------ELLKQPWFHAVQGNHEQMAIDALRGGD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 324021716 295 GEVKAKY--------TAQMYELFSEVFEWLPLAQCI---NGKVLIMH 330
Cdd:cd07424   77 DVMWRANgggwffdlPDEEAKVLLEKLHHLPIAIEVesrNGKVGIVH 123
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 24-91 3.87e-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: 43.15  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   24 ALKRAEE-LKTQAND----------YFKAKDYENAIKFYSQAIELNPSNAIYYGNrsLAYLRTECYG-YALGDATRAIEL 91
Cdd:TIGR02917 755 AVKTLEAwLKTHPNDavlrtalaelYLAQKDYDKAIKHYQTVVKKAPDNAVVLNN--LAWLYLELKDpRALEYAERALKL 832
PHA02239 PHA02239
putative protein phosphatase
 215-290 8.22e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 41.13  E-value: 8.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 324021716 215 ITVCGDTHGQFYDLLNIfeLNGLPSETNP---YIFNGDFVDRGSFSVEVILTLFGFkLLYPDHFHLLRGNHETDNMNQI 290
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTI--MDKINNERKPeetIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDDEFYNIM 78
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 214-283 1.03e-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: 1.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 324021716 214 KITVC-GDTHGqFYDLLNIFELNgLPSETNP-------YIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFH-LLRGNHE 283
Cdd:cd07421    2 RVVICvGDIHG-YISKLNNLWLN-LQSALGPsdfasalVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHD 78
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 33-99 1.27e-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: 1.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   33 TQANDYFKAKDYENAIKFYSQAIELN---PSNAIYYGNRSLAYLRtecygyaLGDATRAIELDKKYIKGY 99
Cdd:pfam13432   2 ALARAALRAGDYDDAAAALEAALARFpesPDAAAALLLLGLAALR-------QGRLAEAAAAYRAALRAA 64
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 24-132 1.43e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.22  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   24 ALKRAEE----LKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLrtecygyALGDATRAI-------ELD 92
Cdd:TIGR02917 321 ILKYAPNshqaRRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYL-------ALGDFEKAAeylakatELD 393

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 324021716   93 KKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:TIGR02917 394 PENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRA 433
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 81-155 2.24e-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: 38.06  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  81 ALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQEC----NKIVK-QKAFERAIAGD 155
Cdd:COG4235    2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEAllaaGDTEEaEELLERALALD 81
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 21-108 2.26e-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: 38.06  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  21 ADGALKRAEELKTQ--------ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELD 92
Cdd:COG4235   36 ALAAYEKALRLDPDnadalldlAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALL 115

                         90
                 ....*....|....*.
gi 324021716  93 KKYIKGYYRRAASNMA 108
Cdd:COG4235  116 PADAPARLLEASIAEA 131
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 23-152 3.45e-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: 39.97  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   23 GALKRAEELKTQANDYFK--AKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYY 100
Cdd:TIGR00990 324 GKLGEKEAIALNLRGTFKclKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYY 403

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 324021716  101 RRAASNMALGKFRAALRDYETVVKVKP-----HDKDAKMKYQEcNKIVKQKA-FERAI 152
Cdd:TIGR00990 404 HRAQLHFIKGEFAQAGKDYQKSIDLDPdfifsHIQLGVTQYKE-GSIASSMAtFRRCK 460
TPR_12 pfam13424
Tetratricopeptide repeat;
35-99 4.39e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 36.21  E-value: 4.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   35 ANDYFKAKDYENAIKFYSQAIELnpsNAIYYGNRSLAYLRT-----ECYgYALGDATRAIELDKKYIKGY 99
Cdd:pfam13424  10 AAVLRRLGRYDEALELLEKALEI---ARRLLGPDHPLTATTllnlgRLY-LELGRYEEALELLERALALA 75
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
214-285 4.44e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 324021716 214 KITVCGDTHGQFYDLLNIFE-LNGLPSETnpYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETD 285
Cdd:COG0622    1 KIAVISDTHGNLPALEAVLEdLEREGVDL--IVHLGDLVGYGPDPPEVL------DLLRELPIVAVRGNHDGA 65
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 35-115 4.71e-03

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 36.89  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716  35 ANDYFKAKDYENAIKFYSQAIELNPSNAiyygNRSLAYLRT-ECYgYALGDATRAIELDKKYIKGYYRRAASNMALGKFR 113
Cdd:COG1729   37 GEAYYALGDYDEAAEAFEKLLKRYPDSP----KAPDALLKLgLSY-LELGDYDKARATLEELIKKYPDSEAAKEARARLA 111


                 ..
gi 324021716 114 AA 115
Cdd:COG1729  112 RL 113
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 21-153 5.81e-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: 39.30  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 324021716   21 ADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYY 100
Cdd:TIGR02917 594 ADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQI 673

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 324021716  101 RRAASNMALGKFRAALRDYETVVKVKPhdKDAKMKYQECNKIVKQKAFERAIA 153
Cdd:TIGR02917 674 GLAQLLLAAKRTESAKKIAKSLQKQHP--KAALGFELEGDLYLRQKDYPAAIQ 724
 
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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