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Conserved domains on  [gi|5453958|ref|NP_006238|]
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serine/threonine-protein phosphatase 5 isoform 1 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-491 0e+00

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


:

Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 699.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  176 YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE 255
Cdd:cd07417   1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  256 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 335
Cdd:cd07417  81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  336 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL 415
Cdd:cd07417 161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453958  416 EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 491
Cdd:cd07417 241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-147 3.49e-19

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


:

Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 86.12  E-value: 3.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   19 PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKG 98
Cdd:COG4785  64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5453958   99 YYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKA 147
Cdd:COG4785 144 YLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLYLAERKLDPEK 192
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-491 0e+00

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


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 699.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  176 YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE 255
Cdd:cd07417   1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  256 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 335
Cdd:cd07417  81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  336 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL 415
Cdd:cd07417 161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453958  416 EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 491
Cdd:cd07417 241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 204-480 8.91e-142

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: 408.14  E-value: 8.91e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     204 LHRKCAYQILVQVKEVLSKLSTLVEttlkETEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVI 283
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVE----VSAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     284 LTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTL 363
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     364 DDIRKIERNRQPPDSGPMCDLLWSDP-QPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRC 442
Cdd:smart00156 155 DDIRKLKRPQEPPDDGLLIDLLWSDPdQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKL 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 5453958     443 VTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQFTAVP 480
Cdd:smart00156 235 VTIFSAPNYCDRFGNKAAVLKV-DKDLKLTFEQFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 211-464 1.27e-72

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 232.10  E-value: 1.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   211 QILVQVKEVLSKLSTLVETTLKE------TEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVIL 284
Cdd:PTZ00244  22 QILIREEDIRAVLTEVREIFMSQpmlleiRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETIT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   285 TLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLD 364
Cdd:PTZ00244 101 LQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   365 DIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCV 443
Cdd:PTZ00244 180 SVNEIERPCDVPDRGILCDLLWADPEDEvRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLV 259

                        250       260
                 ....*....|....*....|.
gi 5453958   444 TVFSAPNYCDQMGNKASYIHL 464
Cdd:PTZ00244 260 TVFSAPNYCGEFDNDAAVMNI 280
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-228 9.93e-44

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: 149.16  E-value: 9.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958    136 YQECNKIVKQKAFERAIAGDEhKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQ 215
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEE-KPSAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQILLK 79

                          90
                  ....*....|...
gi 5453958    216 VKEVLSKLSTLVE 228
Cdd:pfam08321  80 VKEILKKEPSLVE 92
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-147 3.49e-19

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 86.12  E-value: 3.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   19 PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKG 98
Cdd:COG4785  64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5453958   99 YYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKA 147
Cdd:COG4785 144 YLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLYLAERKLDPEK 192
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 28-145 1.08e-16

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 81.37  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958    28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:PLN03088   2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 5453958   108 ALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQ 145
Cdd:PLN03088  82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAE 119
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 26-119 3.88e-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: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPsNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:TIGR00990 125 KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANA 203

                          90
                  ....*....|....
gi 5453958    106 NMALGKFRAALRDY 119
Cdd:TIGR00990 204 YDGLGKYADALLDL 217
TPR_11 pfam13414
TPR repeat;
35-74 1.54e-06

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 44.77  E-value: 1.54e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 5453958     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 7.20e-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: 42.82  E-value: 7.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 5453958      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 1.62e-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: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453958   29 EELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLrtecygyALGDATRAIELDKKYIK 97
Cdd:cd24142   1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILL-------ELGDVEEAREVLLRAIE 62
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
236-307 4.69e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.69e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453958  236 KITVCGDTHGQFYDLLNIFE-LNGLPSETnpYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETD 307
Cdd:COG0622   1 KIAVISDTHGNLPALEAVLEdLEREGVDL--IVHLGDLVGYGPDPPEVL------DLLRELPIVAVRGNHDGA 65
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 176-491 0e+00

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


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 699.01  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  176 YSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFE 255
Cdd:cd07417   1 YSGPKLEDGKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  256 LNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVF 335
Cdd:cd07417  81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  336 EWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFL 415
Cdd:cd07417 161 NWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDPQPQPGRGPSKRGVGCQFGPDVTKRFL 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453958  416 EENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYAN 491
Cdd:cd07417 241 EENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFEAVPHPNVKPMAYAN 316
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 204-480 8.91e-142

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: 408.14  E-value: 8.91e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     204 LHRKCAYQILVQVKEVLSKLSTLVEttlkETEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVI 283
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVE----VSAPVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     284 LTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTL 363
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGL-SPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     364 DDIRKIERNRQPPDSGPMCDLLWSDP-QPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRC 442
Cdd:smart00156 155 DDIRKLKRPQEPPDDGLLIDLLWSDPdQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKL 234

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 5453958     443 VTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQFTAVP 480
Cdd:smart00156 235 VTIFSAPNYCDRFGNKAAVLKV-DKDLKLTFEQFKPGK 271
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 202-480 4.12e-104

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: 312.60  E-value: 4.12e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  202 KKLHRKCAYQILVQVKEVLSKLSTLVETTLKetekITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVE 281
Cdd:cd07415  13 ELLPESEVKSLCEKAKEILVKESNVQRVRSP----VTVCGDIHGQFYDLLELFRIGGDVPDTN-YLFLGDYVDRGYYSVE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  282 VILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDG 360
Cdd:cd07415  88 TFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGL-SPSI 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  361 VTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGG 440
Cdd:cd07415 167 QTLDQIRALDRFQEVPHEGPMCDLLWSDPDDREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNN 246

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 5453958  441 RCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQFTAVP 480
Cdd:cd07415 247 KLVTVWSAPNYCYRCGNVASILEL-DEHLNRSFKQFEAAP 285
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 194-476 1.95e-101

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


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 306.26  E-value: 1.95e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  194 LMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFV 273
Cdd:cd07420  10 LIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  274 DRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKY---TAQMYELFSEVFEWLPLAQCINGKVLI 350
Cdd:cd07420  90 DRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLV 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  351 MHGGLfsEDGVTLDDIRKIERNR---QPPDSGPMCDLLWSDPQPQNG-RSISKRGVSCQFGPDVTKAFLEENNLDYIIRS 426
Cdd:cd07420 170 VHGGI--SDSTDLDLLDKIDRHKyvsTKTEWQQVVDILWSDPKATKGcKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRS 247

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 5453958  427 HEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLqGSDLRPQFHQF 476
Cdd:cd07420 248 HECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKL-GPQLTPHFVQY 296
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 238-464 1.23e-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: 293.89  E-value: 1.23e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  238 TVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEG 317
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDK-YLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  318 EV----KAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEdgVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQN 393
Cdd:cd00144  80 ERtlrcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPD--LTLLDQIRNIRPIENPDDQLVEDLLWSDPDESV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453958  394 GRS-ISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHL 464
Cdd:cd00144 158 GDFeSSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 203-482 7.61e-95

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: 289.59  E-value: 7.61e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  203 KLHRKCAYQILVQVKEVLSKLSTLVETTlketEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEV 282
Cdd:cd07416  15 RLSEEDALRIITEGAEILRQEPNLLRIE----APVTVCGDIHGQFYDLLKLFEVGGSPANTR-YLFLGDYVDRGYFSIEC 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  283 ILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVT 362
Cdd:cd07416  90 VLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGL-SPELKT 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  363 LDDIRKIERNRQPPDSGPMCDLLWSDP--QPQNGRSI------SKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGY 434
Cdd:cd07416 169 LDDIRKLDRFREPPSYGPMCDLLWSDPleDFGNEKTQehfvhnTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGY 248

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 5453958  435 EVAHGGR------CVTVFSAPNYCDQMGNKASYIHLQGSDLRpqFHQFTAVPHP 482
Cdd:cd07416 249 RMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNVMN--IRQFNCSPHP 300
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 211-457 2.23e-85

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


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 264.97  E-value: 2.23e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  211 QILVQVKEVLSKLSTLVEttLKETEKItvCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFK 290
Cdd:cd07414  30 GLCLKSREIFLSQPILLE--LEAPLKI--CGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYK 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  291 LLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIE 370
Cdd:cd07414 105 IKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGL-SPDLQSMEQIRRIM 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  371 RNRQPPDSGPMCDLLWSDPQPQ-NGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAP 449
Cdd:cd07414 184 RPTDVPDQGLLCDLLWSDPDKDvQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAP 263


                ....*...
gi 5453958  450 NYCDQMGN 457
Cdd:cd07414 264 NYCGEFDN 271
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 182-486 4.33e-77

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: 246.64  E-value: 4.33e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  182 EDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKE----------VLSKLSTLVETTLKETEKITVCGDTHGQFYDLL 251
Cdd:cd07418   3 DGGALTNEWVHELMSVFEWSSRNLPPSELPSVLPVNVfdslvltahkILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  252 NIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKY---TAQMY 328
Cdd:cd07418  83 FLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYgdkGKHVY 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  329 ELFSEVFEWLPLAQCINGKVLIMHGGLF--------------------SEDGV------TLDDIRKIERN-RQPPDSGPM 381
Cdd:cd07418 163 RKCLGCFEGLPLASIIAGRVYTAHGGLFrspslpkrkkqkgknrrvllLEPESeslklgTLDDLMKARRSvLDPPGEGSN 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  382 C---DLLWSDPQPQNGRSISK-RGVSCQFGPDVTKAFLEENNLDYIIRSHEVK------------AEGYEVAH---GGRC 442
Cdd:cd07418 243 LipgDVLWSDPSLTPGLSPNKqRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPdarekrpglagmNKGYTVDHdveSGKL 322

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 5453958  443 VTVFSAPNYC------DQMGNKASYIHLQGSDLR-PQFHQFTAV-PHPNVKP 486
Cdd:cd07418 323 ITLFSAPDYPqfqateERYNNKGAYIILQPPDFSdPQFHTFEAVkPRPKANP 374
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 211-464 1.27e-72

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 232.10  E-value: 1.27e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   211 QILVQVKEVLSKLSTLVETTLKE------TEKITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVIL 284
Cdd:PTZ00244  22 QILIREEDIRAVLTEVREIFMSQpmlleiRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETIT 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   285 TLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLD 364
Cdd:PTZ00244 101 LQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL-SPDLTSLA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   365 DIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCV 443
Cdd:PTZ00244 180 SVNEIERPCDVPDRGILCDLLWADPEDEvRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLV 259

                        250       260
                 ....*....|....*....|.
gi 5453958   444 TVFSAPNYCDQMGNKASYIHL 464
Cdd:PTZ00244 260 TVFSAPNYCGEFDNDAAVMNI 280
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 237-480 1.33e-71

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 229.70  E-value: 1.33e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   237 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 316
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGGDIPNAN-YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFY 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   317 GEVKAKY-TAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGR 395
Cdd:PTZ00239 124 EEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGL-SPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   396 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGR-CVTVFSAPNYCDQMGNKASYIHLQgSDLRPQFH 474
Cdd:PTZ00239 203 AVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQnLVTVWSAPNYCYRCGNIASILCLD-ENLQQTWK 281


                 ....*.
gi 5453958   475 QFTAVP 480
Cdd:PTZ00239 282 TFKEVP 287
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 237-467 9.24e-67

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 217.99  E-value: 9.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   237 ITVCGDTHGQFYDLLNIFELNGLPSETNpYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFE 316
Cdd:PTZ00480  61 LKICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   317 GEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLfSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQ-NGR 395
Cdd:PTZ00480 140 DECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGL-SPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDvQGW 218

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5453958   396 SISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGS 467
Cdd:PTZ00480 219 ADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDES 290
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 229-469 2.33e-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: 198.05  E-value: 2.33e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  229 TTLKETEKITVCGDTHGQFYDLLNIFELNGLPS-------ETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLR 301
Cdd:cd07419  42 SVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVteeagdiEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIR 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  302 GNHETDNMNQIYGFEGEVKAKYTAQM------YELFSEVFEWLPLAQCINGKVLIMHGGLfsedGVTLDDIRKIERNRQP 375
Cdd:cd07419 122 GNHEAADINALFGFREECIERLGEDIrdgdsvWQRINRLFNWLPLAALIEDKIICVHGGI----GRSINHIHQIENLKRP 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  376 ---PDSGP-MCDLLWSDP---------QPqNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRC 442
Cdd:cd07419 198 itmEAGSPvVMDLLWSDPtendsvlglRP-NAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHL 276

                       250       260
                ....*....|....*....|....*..
gi 5453958  443 VTVFSAPNYCDQMGNKASYIHLqGSDL 469
Cdd:cd07419 277 ITLFSATNYCGTAGNAGAILVL-GRDL 302
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 136-228 9.93e-44

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: 149.16  E-value: 9.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958    136 YQECNKIVKQKAFERAIAGDEhKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQ 215
Cdd:pfam08321   1 LKECEKLIRRIAFEKAIAVEE-KPSAAETIDLESIVVEDSYDGPRLEDEKITLEFVKDMIERFKKGKKLHKKYAYQILLK 79

                          90
                  ....*....|...
gi 5453958    216 VKEVLSKLSTLVE 228
Cdd:pfam08321  80 VKEILKKEPSLVE 92
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-147 3.49e-19

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 86.12  E-value: 3.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   19 PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKG 98
Cdd:COG4785  64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYA 143

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 5453958   99 YYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKA 147
Cdd:COG4785 144 YLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLYLAERKLDPEK 192
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 236-346 6.74e-18

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


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 79.18  E-value: 6.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958    236 KITVCGDTH--GQFYDLLNIFElnGLPSETNPYIF--NGDFVDRGSFSVEVILTLfgFKLLYPDHFHLLRGNHETDNMNQ 311
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLK--KLLEEGKPDLVlhAGDLVDRGPPSEEVLELL--ERLIKYVPVYLVRGNHDFDYGEC 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 5453958    312 IYGFEGEvkaKYTAQMYELFSEVFEWLPLAQCING 346
Cdd:pfam00149  78 LRLYPYL---GLLARPWKRFLEVFNFLPLAGILSG 109
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
28-132 4.61e-17

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 80.82  E-value: 4.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:COG0457   8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQ 87

                        90       100
                ....*....|....*....|....*
gi 5453958  108 ALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG0457  88 ALGRYEEALEDYDKALELDPDDAEA 112
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
28-153 5.32e-17

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 80.44  E-value: 5.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:COG0457  42 AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALL 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 5453958  108 ALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKivKQKAFERAIA 153
Cdd:COG0457 122 ELGRYDEAIEAYERALELDPDDADALYNLGIALE--KLGRYEEALE 165
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 28-145 1.08e-16

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 81.37  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958    28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNM 107
Cdd:PLN03088   2 AKDLEDKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACM 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 5453958   108 ALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQ 145
Cdd:PLN03088  82 KLEEYQTAKAALEKGASLAPGDSRFTKLIKECDEKIAE 119
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 26-119 3.88e-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: 3.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     26 KRAEELKTQANDYFKAKDYENAIKFYSQAIELNPsNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAAS 105
Cdd:TIGR00990 125 KYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANA 203

                          90
                  ....*....|....
gi 5453958    106 NMALGKFRAALRDY 119
Cdd:TIGR00990 204 YDGLGKYADALLDL 217
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 12-127 2.51e-14

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


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 70.37  E-value: 2.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   12 AEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIEL 91
Cdd:COG5010  38 KEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALAL 117

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5453958   92 DKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKP 127
Cdd:COG5010 118 SPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
38-120 2.54e-13

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 69.65  E-value: 2.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   38 YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:COG0457  86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALE 165


                ...
gi 5453958  118 DYE 120
Cdd:COG0457 166 LLE 168
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 24-134 3.19e-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: 66.57  E-value: 3.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   24 ALKRAEE-LKTQAND----------YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELD 92
Cdd:COG4235   2 AIARLRQaLAANPNDaegwlllgraYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 5453958   93 KKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKM 134
Cdd:COG4235  82 PDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
38-127 4.80e-13

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 64.81  E-value: 4.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   38 YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALgDATRAIELDKKYIKGYYRRAASNMALGKFRAALR 117
Cdd:COG3063   2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAI-ALEKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                        90
                ....*....|
gi 5453958  118 DYETVVKVKP 127
Cdd:COG3063  81 YLERALELDP 90
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 35-129 9.96e-13

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 65.21  E-value: 9.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG4783  45 GEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDE 124

                        90
                ....*....|....*
gi 5453958  115 ALRDYETVVKVKPHD 129
Cdd:COG4783 125 AIAALEKALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 18-132 1.44e-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: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   18 EPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIK 97
Cdd:COG3914  68 AAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAE 147

                        90       100       110
                ....*....|....*....|....*....|....*
gi 5453958   98 GYYRRAASNMALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG3914 148 AYLNLGEALRRLGRLEEAIAALRRALELDPDNAEA 182
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 27-155 3.18e-12

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 64.06  E-value: 3.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   27 RAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASN 106
Cdd:COG4783   3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 5453958  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 8.45e-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: 8.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   23 GALKRAEE-----LKTQAND----------YFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATR 87
Cdd:COG2956  90 GLLDRAEElleklLELDPDDaealrllaeiYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEK 169

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 5453958   88 AIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQEC 139
Cdd:COG2956 170 ALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAEL 221
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 35-132 7.14e-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: 7.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG3914 119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEE 198

                        90
                ....*....|....*...
gi 5453958  115 ALRDYETVVKVKPHDKDA 132
Cdd:COG3914 199 AIAAYRRALELDPDNADA 216
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
55-132 9.73e-11

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.95  E-value: 9.73e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453958   55 IELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG0457   1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEA 78
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
27-132 1.23e-10

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 61.47  E-value: 1.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   27 RAEELKTQANDYFKAKDYENAIkfysQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASN 106
Cdd:COG4785  42 ADLALALAAAALAAAALAAERI----DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAY 117

                        90       100
                ....*....|....*....|....*.
gi 5453958  107 MALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:COG4785 118 LLLGDYDAALEDFDRALELDPDYAYA 143
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 35-153 1.84e-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: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG2956  83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5453958  115 ALRDYETVVKVKPHDKDAKMKYQECNkiVKQKAFERAIA 153
Cdd:COG2956 163 AIEALEKALKLDPDCARALLLLAELY--LEQGDYEEAIA 199
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 24-153 1.46e-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: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   24 ALKRAEELKTQ--------ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKY 95
Cdd:COG2956 132 VLERLLKLGPEnahaycelAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5453958   96 IKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQecnKIVKQKAFERAIA 153
Cdd:COG2956 212 LPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALAD---LLERKEGLEAALA 266
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 37-133 2.46e-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: 49.22  E-value: 2.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   37 DYFKAKDYENAIKFYSQAIELNPSNAiyYGNRSLaYLRTECYgYALGDATRAIELDKKYIKGY----------YRRAASN 106
Cdd:COG1729   2 ALLKAGDYDEAIAAFKAFLKRYPNSP--LAPDAL-YWLGEAY-YALGDYDEAAEAFEKLLKRYpdspkapdalLKLGLSY 77

                        90       100
                ....*....|....*....|....*..
gi 5453958  107 MALGKFRAALRDYETVVKVKPHDKDAK 133
Cdd:COG1729  78 LELGDYDKARATLEELIKKYPDSEAAK 104
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
35-120 7.94e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 7.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYlrtecygYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG0457 117 GLALLELGRYDEAIEAYERALELDPDDADALYNLGIAL-------EKLGRYEEALELLEKLEAAALAALLAAALGEAALA 189


                ....*.
gi 5453958  115 ALRDYE 120
Cdd:COG0457 190 LAAAEV 195
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 35-153 8.40e-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: 8.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRA 114
Cdd:COG2956  49 GNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEK 128

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 5453958  115 ALRDYETVVKVKPHDKDAKMKYQECNkiVKQKAFERAIA 153
Cdd:COG2956 129 AIEVLERLLKLGPENAHAYCELAELY--LEQGDYDEAIE 165
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 28-149 8.80e-07

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


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 49.86  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAiyYGNRS---LAYlrteCYgYALGDATRAIELDKKYIK------- 97
Cdd:TIGR03302  33 AEELYEEAKEALDSGDYTEAIKYFEALESRYPFSP--YAEQAqldLAY----AY-YKSGDYAEAIAAADRFIRlhpnhpd 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5453958     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 1.36e-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: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   28 AEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAiyYGNRS---LAYlrteCYgYALGDATRAIELDKKYIKGY----- 99
Cdd:COG4105  32 AEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSP--YAEQAqlmLAY----AY-YKQGDYEEAIAAADRFIKLYpnspn 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5453958  100 -----YRRAASNMALGK--------FRAALRDYETVVKVKPHDK---DAKMKYQECNKIVKQKAFERA 151
Cdd:COG4105 105 adyayYLRGLSYYEQSPdsdrdqtsTRKAIEAFQELINRYPDSEyaeDAKKRIDELRDKLARKELEVA 172
TPR_11 pfam13414
TPR repeat;
35-74 1.54e-06

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 44.77  E-value: 1.54e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 5453958     35 ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLR 74
Cdd:pfam13414   1 GDAYYEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 241-369 3.91e-06

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


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 47.68  E-value: 3.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  241 GDTHGQFYDLLNIFELNGLPSETNPYIFN-------GDFVDRGSFSVEVIltlFGFKLLYPD------HFHLLRGNHETd 307
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEIL---KLLEKLKRQarkaggKVILLLGNHEL- 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5453958  308 nMNQI----YGFEGEVKAKYT--AQMYELFS---EVFEWL---PLAQCINGkVLIMHGGLfsedGVTLDdiRKI 369
Cdd:cd07425  80 -MNLCgdfrYVHPRGLNEFGGvaKRRYALLSdggYIGRYLrthPVVLVVND-ILFVHGGL----GPLWS--RGY 145
TPR_1 pfam00515
Tetratricopeptide repeat;
28-61 6.84e-06

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.79  E-value: 6.84e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 5453958     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 7.20e-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: 42.82  E-value: 7.20e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 5453958      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 1.62e-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: 1.62e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453958   29 EELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLrtecygyALGDATRAIELDKKYIK 97
Cdd:cd24142   1 DELLEKAEELLDQGNFELALKFLQRALELEPNNVEALELLGEILL-------ELGDVEEAREVLLRAIE 62
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 239-305 2.04e-05

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 44.18  E-value: 2.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  239 VCGDTHGQFYDLLNIFELNgLPSETNP--YIFNGDFVDRGSFSVEVILTLFGFKLL-YPDHFhlLRGNHE 305
Cdd:cd00838   2 VISDIHGNLEALEAVLEAA-LAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLLAgIPVYV--VPGNHD 68
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 41-152 2.44e-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: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     41 AKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYE 120
Cdd:TIGR02917 172 ENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHAD 251

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 5453958    121 TVVKVKP-----HDKDAKMKYQecnkivkQKAFERAI 152
Cdd:TIGR02917 252 ALLKKAPnsplaHYLKALVDFQ-------KKNYEDAR 281
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 21-115 3.41e-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: 3.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   21 ADGALKRAEELK--------TQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELD 92
Cdd:COG3914 131 ALAALRRALALNpdfaeaylNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELD 210

                        90       100
                ....*....|....*....|...
gi 5453958   93 KKYIKgyyrrAASNMALGKFRAA 115
Cdd:COG3914 211 PDNAD-----AHSNLLFALRQAC 228
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 28-59 5.98e-05

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


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 40.20  E-value: 5.98e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 5453958     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 ...
 237-352 1.70e-04

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


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 42.69  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958  237 ITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETDNMNQIYGFE 316
Cdd:cd07424   3 DFVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVL------ELLKQPWFHAVQGNHEQMAIDALRGGD 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5453958  317 GEVKAKY--------TAQMYELFSEVFEWLPLAQCI---NGKVLIMH 352
Cdd:cd07424  77 DVMWRANgggwffdlPDEEAKVLLEKLHHLPIAIEVesrNGKVGIVH 123
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 24-91 4.79e-04

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 42.76  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     24 ALKRAEE-LKTQAND----------YFKAKDYENAIKFYSQAIELNPSNAIYYGNrsLAYLRTECYG-YALGDATRAIEL 91
Cdd:TIGR02917 755 AVKTLEAwLKTHPNDavlrtalaelYLAQKDYDKAIKHYQTVVKKAPDNAVVLNN--LAWLYLELKDpRALEYAERALKL 832
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 33-99 8.30e-04

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: 37.70  E-value: 8.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     33 TQANDYFKAKDYENAIKFYSQAIELN---PSNAIYYGNRSLAYLRtecygyaLGDATRAIELDKKYIKGY 99
Cdd:pfam13432   2 ALARAALRAGDYDDAAAALEAALARFpesPDAAAALLLLGLAALR-------QGRLAEAAAAYRAALRAA 64
PHA02239 PHA02239
putative protein phosphatase
 237-312 8.72e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 41.13  E-value: 8.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453958   237 ITVCGDTHGQFYDLLNIfeLNGLPSETNP---YIFNGDFVDRGSFSVEVILTLFGFkLLYPDHFHLLRGNHETDNMNQI 312
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTI--MDKINNERKPeetIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDDEFYNIM 78
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 236-305 1.09e-03

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


Pssm-ID: 163664  Cd Length: 304  Bit Score: 40.95  E-value: 1.09e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5453958  236 KITVC-GDTHGqFYDLLNIFELNgLPSETNP-------YIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFH-LLRGNHE 305
Cdd:cd07421   2 RVVICvGDIHG-YISKLNNLWLN-LQSALGPsdfasalVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHD 78
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 24-132 1.53e-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: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     24 ALKRAEE----LKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLrtecygyALGDATRAI-------ELD 92
Cdd:TIGR02917 321 ILKYAPNshqaRRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYL-------ALGDFEKAAeylakatELD 393

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5453958     93 KKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDA 132
Cdd:TIGR02917 394 PENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRA 433
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 21-108 2.06e-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: 38.45  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   21 ADGALKRAEELKTQ--------ANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELD 92
Cdd:COG4235  36 ALAAYEKALRLDPDnadalldlAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALL 115

                        90
                ....*....|....*.
gi 5453958   93 KKYIKGYYRRAASNMA 108
Cdd:COG4235 116 PADAPARLLEASIAEA 131
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 81-155 2.06e-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: 38.45  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   81 ALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQEC----NKIVK-QKAFERAIAGD 155
Cdd:COG4235   2 AIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEAllaaGDTEEaEELLERALALD 81
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 35-115 3.63e-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: 37.28  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958   35 ANDYFKAKDYENAIKFYSQAIELNPSNAiyygNRSLAYLRT-ECYgYALGDATRAIELDKKYIKGYYRRAASNMALGKFR 113
Cdd:COG1729  37 GEAYYALGDYDEAAEAFEKLLKRYPDSP----KAPDALLKLgLSY-LELGDYDKARATLEELIKKYPDSEAAKEARARLA 111


                ..
gi 5453958  114 AA 115
Cdd:COG1729 112 RL 113
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 23-152 3.84e-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: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     23 GALKRAEELKTQANDYFK--AKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYY 100
Cdd:TIGR00990 324 GKLGEKEAIALNLRGTFKclKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYY 403

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 5453958    101 RRAASNMALGKFRAALRDYETVVKVKP-----HDKDAKMKYQEcNKIVKQKA-FERAI 152
Cdd:TIGR00990 404 HRAQLHFIKGEFAQAGKDYQKSIDLDPdfifsHIQLGVTQYKE-GSIASSMAtFRRCK 460
TPR_12 pfam13424
Tetratricopeptide repeat;
35-99 4.60e-03

Tetratricopeptide repeat;


Pssm-ID: 315987 [Multi-domain]  Cd Length: 77  Bit Score: 36.21  E-value: 4.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     35 ANDYFKAKDYENAIKFYSQAIELnpsNAIYYGNRSLAYLRT-----ECYgYALGDATRAIELDKKYIKGY 99
Cdd:pfam13424  10 AAVLRRLGRYDEALELLEKALEI---ARRLLGPDHPLTATTllnlgRLY-LELGRYEEALELLERALALA 75
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
236-307 4.69e-03

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 38.36  E-value: 4.69e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5453958  236 KITVCGDTHGQFYDLLNIFE-LNGLPSETnpYIFNGDFVDRGSFSVEVIltlfgfKLLYPDHFHLLRGNHETD 307
Cdd:COG0622   1 KIAVISDTHGNLPALEAVLEdLEREGVDL--IVHLGDLVGYGPDPPEVL------DLLRELPIVAVRGNHDGA 65
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 21-153 6.98e-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: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5453958     21 ADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYY 100
Cdd:TIGR02917 594 ADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQI 673

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 5453958    101 RRAASNMALGKFRAALRDYETVVKVKPhdKDAKMKYQECNKIVKQKAFERAIA 153
Cdd:TIGR02917 674 GLAQLLLAAKRTESAKKIAKSLQKQHP--KAALGFELEGDLYLRQKDYPAAIQ 724
TPR_1 pfam00515
Tetratricopeptide repeat;
96-129 9.86e-03

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 33.93  E-value: 9.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 5453958     96 IKGYYRRAASNMALGKFRAALRDYETVVKVKPHD 129
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPNN 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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