NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|502745998|ref|WP_012980982|]
View 

TIGR00295 family protein [Methanocaldococcus sp. FS406-22]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TIGR00295 TIGR00295
TIGR00295 family protein; This set of orthologs is narrowly defined, comprising proteins found ...
 3-168 1.04e-82

TIGR00295 family protein; This set of orthologs is narrowly defined, comprising proteins found in three Archaea but not in Pyrococcus horikoshii. The closest homologs are other archaeal proteins that appear to be represent distinct orthologous clusters. [Hypothetical proteins, Conserved]


:

Pssm-ID: 129396 [Multi-domain]  Cd Length: 164  Bit Score: 241.30  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998    3 FEKALSILKnlCPENVVEHCIAVSEYAYELALAIKNNGHNVDIELVRLGGLLHDIGRSKTHGIDHGVVGAEILRELGFDE 82
Cdd:TIGR00295   1 VQRLLDKYK--CDESVRRHCLAVARVAMELAENIRKKGHEVDMDLVLKGALLHDIGRARTHGFEHFVKGAEILRKEGVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   83 KLALIAERHIGAGITKEEAIELGLPPKDYLPITLEEKIVAHADNLIFGTKRVEINEVIKKFEKRLGRNHPSIKRIILLND 162
Cdd:TIGR00295  79 KIVRIAERHFGAGINAEEASKLGLPPKDYMPETLEEKIVAHADNLIMGVREVTIDEVIKKLEERLGKNHPSIERARKLKE 158


                  ....*.
gi 502745998  163 EINNLL 168
Cdd:TIGR00295 159 ELERLL 164
 
Name Accession Description Interval E-value
TIGR00295 TIGR00295
TIGR00295 family protein; This set of orthologs is narrowly defined, comprising proteins found ...
 3-168 1.04e-82

TIGR00295 family protein; This set of orthologs is narrowly defined, comprising proteins found in three Archaea but not in Pyrococcus horikoshii. The closest homologs are other archaeal proteins that appear to be represent distinct orthologous clusters. [Hypothetical proteins, Conserved]


Pssm-ID: 129396 [Multi-domain]  Cd Length: 164  Bit Score: 241.30  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998    3 FEKALSILKnlCPENVVEHCIAVSEYAYELALAIKNNGHNVDIELVRLGGLLHDIGRSKTHGIDHGVVGAEILRELGFDE 82
Cdd:TIGR00295   1 VQRLLDKYK--CDESVRRHCLAVARVAMELAENIRKKGHEVDMDLVLKGALLHDIGRARTHGFEHFVKGAEILRKEGVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   83 KLALIAERHIGAGITKEEAIELGLPPKDYLPITLEEKIVAHADNLIFGTKRVEINEVIKKFEKRLGRNHPSIKRIILLND 162
Cdd:TIGR00295  79 KIVRIAERHFGAGINAEEASKLGLPPKDYMPETLEEKIVAHADNLIMGVREVTIDEVIKKLEERLGKNHPSIERARKLKE 158


                  ....*.
gi 502745998  163 EINNLL 168
Cdd:TIGR00295 159 ELERLL 164
PRK12703 PRK12703
tRNA 2'-O-methylase; Reviewed
 7-167 1.17e-42

tRNA 2'-O-methylase; Reviewed


Pssm-ID: 237176 [Multi-domain]  Cd Length: 339  Bit Score: 144.63  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   7 LSILKNlcpENVVEHCIAVSEYAYELALAIKNNGhNVDIELVRLGGLLHDIGRSKTHGIDHGVVGAEILRELGFDEKLAL 86
Cdd:PRK12703 176 LDLLKK---YGASDLLIRHVKTVYKLAMRIADCI-NADRRLVAAGALLHDIGRTKTNGIDHAVAGAEILRKENIDDRVVS 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  87 IAERHIGAGITKEEAIELGLPPKDYLPITLEEKIVAHADNLIFGTKRVEINEVIKKFEKRlgRNHPSIKRIILLNDEINN 166
Cdd:PRK12703 252 IVERHIGAGITSEEAQKLGLPVKDYVPETIEEMIVAHADNLFAGDKRLNLKQVMDKYRKK--GLHDAAERIKKLHEELSS 329


                 .
gi 502745998 167 L 167
Cdd:PRK12703 330 I 330
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 16-127 3.80e-13

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 3.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  16 ENVVEHCIAVSEYAYELALAIKNNGhnVDIELVRLGGLLHDIGR----------SKTHGIDHGVVGAEILRELGFDEKLA 85
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLSE--EDIELLRLAALLHDIGKpgtpdaiteeESELEKDHAIVGAEILRELLLEEVIK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502745998  86 LIAERHIGAGITKEEAIELGLPP--KDYLPITLEEKIVAHADNL 127
Cdd:cd00077   79 LIDELILAVDASHHERLDGLGYPdgLKGEEITLEARIVKLADRL 122
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 2-127 8.90e-13

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 62.99  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   2 EFEKALSILKNLCPENVVEHCIAVSEYAYELALAIknnghNVDIELVRLGGLLHDIGRSKTHGI--DHGVVGAEILRELG 79
Cdd:COG1418    3 ELIKLVKYLRTSYGQHDLQHSLRVAKLAGLIAAEE-----GADVEVAKRAALLHDIGKAKDHEVegSHAEIGAELARKYL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502745998  80 FDEKLALIAERHIgagitkEEAIELGLPPKDYLPITLEEKIVAHADNL 127
Cdd:COG1418   78 ESLGFPEEEIEAV------VHAIEAHSFSGGIEPESLEAKIVQDADRL 119
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 18-127 6.76e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 58.79  E-value: 6.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   18 VVEHCIAVSEYAYELALAIKNnghnVDIELVRLGGLLHDIGRSKTH--------GIDHGVVGAEILRELGFDEKL---AL 86
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGE----LDRELLLLAALLHDIGKGPFGdekpefeiFLGHAVVGAEILRELEKRLGLedvLK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 502745998   87 IAERHIGAGITKEEaielglppkdYLPITLEEKIVAHADNL 127
Cdd:pfam01966  77 LILEHHESWEGAGY----------PEEISLEARIVKLADRL 107
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 14-127 1.52e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 58.46  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998    14 CPENVVEHCIAVSEYAYELALAIKNnghnVDIELVRLGGLLHDIGRSKTHGI---------DHGVVGAEILRELGFDEKL 84
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGL----LDIELLLLAALLHDIGKPGTPDSflvktsvleDHHFIGAEILLEEEEPRIL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 502745998    85 ALIAERHIgagitkeEAIELGLPPKDYLPITLEEKIVAHADNL 127
Cdd:smart00471  77 EEILRTAI-------LSHHERPDGLRGEPITLEARIVKVADRL 112
 
Name Accession Description Interval E-value
TIGR00295 TIGR00295
TIGR00295 family protein; This set of orthologs is narrowly defined, comprising proteins found ...
 3-168 1.04e-82

TIGR00295 family protein; This set of orthologs is narrowly defined, comprising proteins found in three Archaea but not in Pyrococcus horikoshii. The closest homologs are other archaeal proteins that appear to be represent distinct orthologous clusters. [Hypothetical proteins, Conserved]


Pssm-ID: 129396 [Multi-domain]  Cd Length: 164  Bit Score: 241.30  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998    3 FEKALSILKnlCPENVVEHCIAVSEYAYELALAIKNNGHNVDIELVRLGGLLHDIGRSKTHGIDHGVVGAEILRELGFDE 82
Cdd:TIGR00295   1 VQRLLDKYK--CDESVRRHCLAVARVAMELAENIRKKGHEVDMDLVLKGALLHDIGRARTHGFEHFVKGAEILRKEGVDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   83 KLALIAERHIGAGITKEEAIELGLPPKDYLPITLEEKIVAHADNLIFGTKRVEINEVIKKFEKRLGRNHPSIKRIILLND 162
Cdd:TIGR00295  79 KIVRIAERHFGAGINAEEASKLGLPPKDYMPETLEEKIVAHADNLIMGVREVTIDEVIKKLEERLGKNHPSIERARKLKE 158


                  ....*.
gi 502745998  163 EINNLL 168
Cdd:TIGR00295 159 ELERLL 164
PRK12703 PRK12703
tRNA 2'-O-methylase; Reviewed
 7-167 1.17e-42

tRNA 2'-O-methylase; Reviewed


Pssm-ID: 237176 [Multi-domain]  Cd Length: 339  Bit Score: 144.63  E-value: 1.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   7 LSILKNlcpENVVEHCIAVSEYAYELALAIKNNGhNVDIELVRLGGLLHDIGRSKTHGIDHGVVGAEILRELGFDEKLAL 86
Cdd:PRK12703 176 LDLLKK---YGASDLLIRHVKTVYKLAMRIADCI-NADRRLVAAGALLHDIGRTKTNGIDHAVAGAEILRKENIDDRVVS 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  87 IAERHIGAGITKEEAIELGLPPKDYLPITLEEKIVAHADNLIFGTKRVEINEVIKKFEKRlgRNHPSIKRIILLNDEINN 166
Cdd:PRK12703 252 IVERHIGAGITSEEAQKLGLPVKDYVPETIEEMIVAHADNLFAGDKRLNLKQVMDKYRKK--GLHDAAERIKKLHEELSS 329


                 .
gi 502745998 167 L 167
Cdd:PRK12703 330 I 330
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 14-94 2.22e-21

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 82.38  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   14 CPENVVEHCIAVSEYAYELALAIknnghNVDIELVRLGGLLHDIGRSKTHG----IDHGVVGAEILRELGFDEKLALIAE 89
Cdd:TIGR00277   1 YGQNVLQHSLEVAKLAEALAREL-----GLDVELARRGALLHDIGKPITREgvifESHVVVGAEIARKYGEPLEVIDIIA 75


                  ....*
gi 502745998   90 RHIGA 94
Cdd:TIGR00277  76 EHHGK 80
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 16-127 3.80e-13

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 63.13  E-value: 3.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  16 ENVVEHCIAVSEYAYELALAIKNNGhnVDIELVRLGGLLHDIGR----------SKTHGIDHGVVGAEILRELGFDEKLA 85
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLSE--EDIELLRLAALLHDIGKpgtpdaiteeESELEKDHAIVGAEILRELLLEEVIK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502745998  86 LIAERHIGAGITKEEAIELGLPP--KDYLPITLEEKIVAHADNL 127
Cdd:cd00077   79 LIDELILAVDASHHERLDGLGYPdgLKGEEITLEARIVKLADRL 122
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
 2-127 8.90e-13

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 62.99  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   2 EFEKALSILKNLCPENVVEHCIAVSEYAYELALAIknnghNVDIELVRLGGLLHDIGRSKTHGI--DHGVVGAEILRELG 79
Cdd:COG1418    3 ELIKLVKYLRTSYGQHDLQHSLRVAKLAGLIAAEE-----GADVEVAKRAALLHDIGKAKDHEVegSHAEIGAELARKYL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502745998  80 FDEKLALIAERHIgagitkEEAIELGLPPKDYLPITLEEKIVAHADNL 127
Cdd:COG1418   78 ESLGFPEEEIEAV------VHAIEAHSFSGGIEPESLEAKIVQDADRL 119
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 18-127 6.76e-12

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 58.79  E-value: 6.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   18 VVEHCIAVSEYAYELALAIKNnghnVDIELVRLGGLLHDIGRSKTH--------GIDHGVVGAEILRELGFDEKL---AL 86
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGE----LDRELLLLAALLHDIGKGPFGdekpefeiFLGHAVVGAEILRELEKRLGLedvLK 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 502745998   87 IAERHIGAGITKEEaielglppkdYLPITLEEKIVAHADNL 127
Cdd:pfam01966  77 LILEHHESWEGAGY----------PEEISLEARIVKLADRL 107
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 14-127 1.52e-11

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 58.46  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998    14 CPENVVEHCIAVSEYAYELALAIKNnghnVDIELVRLGGLLHDIGRSKTHGI---------DHGVVGAEILRELGFDEKL 84
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAALAEELGL----LDIELLLLAALLHDIGKPGTPDSflvktsvleDHHFIGAEILLEEEEPRIL 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 502745998    85 ALIAERHIgagitkeEAIELGLPPKDYLPITLEEKIVAHADNL 127
Cdd:smart00471  77 EEILRTAI-------LSHHERPDGLRGEPITLEARIVKVADRL 112
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
20-91 2.21e-07

HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 48.81  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  20 EHCIAVSEYAYELALAIknngHNVDIELVRLGGLLHDIGR-----------------------------SKTHGIDHGVV 70
Cdd:COG1639  107 RHSLAVAAAARALARRL----GLLDPEEAFLAGLLHDIGKlvllslfpeeyaellalaeadglslaeaeREVLGTDHAEL 182

                         90       100
                 ....*....|....*....|.
gi 502745998  71 GAEILRELGFDEKLALIAERH 91
Cdd:COG1639  183 GAALARKWGLPEELVEAIRYH 203
PRK12705 PRK12705
hypothetical protein; Provisional
 16-81 1.55e-06

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 47.01  E-value: 1.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502745998  16 ENVVEHCIAVSEYAYELALAIknnghNVDIELVRLGGLLHDIGRSKTHGID--HGVVGAEILRELGFD 81
Cdd:PRK12705 322 QNVLSHSLEVAHLAGIIAAEI-----GLDPALAKRAGLLHDIGKSIDRESDgnHVEIGAELARKFNEP 384
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
 20-91 4.59e-06

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 45.35  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  20 EHCIAVSEYAYELALAIKNNGHnvDIELVRLGGLLHDIGRSkthGID--------------------HGVVGAEILRELG 79
Cdd:COG2206  146 GHSVRVAVLALALARELGLSEE--ELEDLGLAALLHDIGKI---GIPdeilnkpgkltdeefeiikkHPEYGYEILKKLP 220

                         90
                 ....*....|..
gi 502745998  80 FDEKLALIAERH 91
Cdd:COG2206  221 GLSEVAEIVLQH 232
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
 47-123 8.01e-06

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 44.98  E-value: 8.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502745998  47 LVRLGGLLHDIGrsKTHGIDHGVVGAEILRElgfdeklalIAERhigagitkeeaieLGLPPKDylpITLEEKIVAH 123
Cdd:PRK03381 444 LLLLGALLHDIG--KGRGGDHSVVGAELARQ---------IGAR-------------LGLSPAD---VALLSALVRH 493
HDOD pfam08668
HDOD domain;
20-91 5.17e-05

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 41.83  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   20 EHCIAVSEYAYELALAIKNNghnvDIELVRLGGLLHDIGR-----------------------------SKTHGIDHGVV 70
Cdd:pfam08668  97 EHSLACALAARLLARRLGLD----DPEEAFLAGLLHDIGKlillsllpdkyeellekaaeegislleaeRELLGTDHAEV 172

                          90       100
                  ....*....|....*....|.
gi 502745998   71 GAEILRELGFDEKLALIAERH 91
Cdd:pfam08668 173 GAALLERWNLPEELVEAIAYH 193
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
6-76 7.31e-05

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 41.86  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   6 ALSILKNLCPENVVEHCIAVSEYAYELALAiknngHNVDIELVRLGGLLHDIGRS----------KTHGID--------- 66
Cdd:PRK07152 185 LEDILKSFLDEYRYKHCLRVAQLAAELAKK-----NNLDPKKAYYAGLYHDITKEwdeekhrkflKKYLKDvknlpwyvl 259

                         90
                 ....*....|
gi 502745998  67 HGVVGAEILR 76
Cdd:PRK07152 260 HQYVGALWLK 269
GlnD COG2844
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ...
 23-101 1.25e-04

UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];


Pssm-ID: 442092 [Multi-domain]  Cd Length: 864  Bit Score: 41.28  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  23 IAVSEYAYELALAIK--NNGHNvdIELVRLGGLLHDIGrsKTHGIDHGVVGAEILRElgfdeklalIAERHigaGITKEE 100
Cdd:COG2844  454 FERGELAEEFPLASEliAELPK--PELLYLAALFHDIA--KGRGGDHSELGAEDARR---------FCPRH---GLSPED 517


                 .
gi 502745998 101 A 101
Cdd:COG2844  518 T 518
glnD PRK00227
[protein-PII] uridylyltransferase;
46-116 2.75e-04

[protein-PII] uridylyltransferase;


Pssm-ID: 178937 [Multi-domain]  Cd Length: 693  Bit Score: 40.52  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  46 ELVRLGGLLHDIGrsKTHGIDHGVVGAEIL----RELGFDEKLA-----LIAERHIGAGI------TKEEAIELGLPPKD 110
Cdd:PRK00227 403 DLLLLGALYHDIG--KGYPRPHEQVGAEMVaraaRRMGLNLRDRavvqtLVAEHTTLARIagrldpTSEEAVDKLLDAVR 480


                 ....*.
gi 502745998 111 YLPITL 116
Cdd:PRK00227 481 YDLLTL 486
YdhJ COG1078
HD superfamily phosphohydrolase [General function prediction only];
20-104 2.94e-04

HD superfamily phosphohydrolase [General function prediction only];


Pssm-ID: 440696 [Multi-domain]  Cd Length: 340  Bit Score: 40.16  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  20 EHCIAVSEYAYELALAIKNNGHNVD---IELVRLGGLLHDIGrsktHG-------------IDHGVVGAEILRELGFDEK 83
Cdd:COG1078   52 EHSLGVMHLARRALDRLRRKGVEIDeeeRELVRAAALLHDIG----HGpfshafeevlltgVDHEEITLRIIEENEINGI 127

                         90       100
                 ....*....|....*....|.
gi 502745998  84 LaliaERHigaGITKEEAIEL 104
Cdd:COG1078  128 L----EKH---GIDPELVADI 141
COG4341 COG4341
Predicted HD phosphohydrolase [General function prediction only];
44-91 7.39e-04

Predicted HD phosphohydrolase [General function prediction only];


Pssm-ID: 443482  Cd Length: 182  Bit Score: 38.34  E-value: 7.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502745998  44 DIELVrLGGLLHDIG------RSKTHGID--HGVVGAEILRElGFDEKLALIAERH 91
Cdd:COG4341   42 DEELV-VAALLHDIGhllhdlGEDLDGGDdnHEEIAAAILRP-FFSEEVTWPVRLH 95
Cas10_III cd09680
CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short ...
 50-138 9.94e-04

CRISPR/Cas system-associated protein Cas10; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Multidomain protein with permuted HD nuclease domain, palm domain and Zn-ribbon; signature gene for type III; also known as Csm1 family


Pssm-ID: 187811 [Multi-domain]  Cd Length: 650  Bit Score: 38.84  E-value: 9.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  50 LGGLLHDIG----RSKTHGID--HGVVGAEILRE-LGFDEKLALIAERHIgagitKEEAIELGLPPKDylpitLEEKIVA 122
Cdd:cd09680    3 LGALLHDIGkvvqRAGLGFYSktHSKFGAEFLKEfSKNKDDLGDCISYHH-----TKELAKALLENHH-----PLAYIVY 72

                         90
                 ....*....|....*.
gi 502745998 123 HADNLIFGTKRVEINE 138
Cdd:cd09680   73 IADNIAASVERREGEE 88
cas3_HD TIGR01596
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ...
 19-88 1.04e-03

CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.


Pssm-ID: 273711 [Multi-domain]  Cd Length: 176  Bit Score: 37.95  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   19 VEHCIAVSEYAYELALAIKNNGHNVDIELVRLG---GLLHDIG---------------RSKTHGIDHGVVGA----EILR 76
Cdd:TIGR01596   2 KEHLLDVAAVAEALPALRPRLAEKLGLELRELLklaGLLHDLGkaspafqkklrkaeeRGDRGEVRHSTLSAallyDLLE 81

                          90
                  ....*....|..
gi 502745998   77 ELGFDEKLALIA 88
Cdd:TIGR01596  82 ELGLEEELALLL 93
UTase_glnD TIGR01693
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ...
 18-92 1.97e-03

[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]


Pssm-ID: 273761 [Multi-domain]  Cd Length: 850  Bit Score: 37.78  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998   18 VVEHCIAVSEYAYELALAIKNNGHNVDIELVRLGGLLHDIGrsKTHGIDHGVVGAEILRE----LGFD----EKLALIAE 89
Cdd:TIGR01693 438 VHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIG--KGRGGDHSVLGAEDARDvcprLGLDrpdtELVAWLVR 515


                  ...
gi 502745998   90 RHI 92
Cdd:TIGR01693 516 NHL 518
Cas3''_I cd09641
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ...
 19-160 3.35e-03

CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I


Pssm-ID: 193608 [Multi-domain]  Cd Length: 200  Bit Score: 36.48  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  19 VEHCIAVSEYAYELALAIKNN---GHNVDIELVRLGGLLHDIG------------------RSKTHGIDHGVVGAEILRE 77
Cdd:cd09641   10 LEHLLDVAAWDAELAEEFARKlglELGLSRELLALAGLLHDLGkatpafqkylrggkealrEGKRKEVRHSLLGALLLYE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502745998  78 LGFDEKLALIAERHIGAGIT------KEEAIELGLPPKDYLPITLEEkivAHADNLIFGTKRVEINEVIKKFEKRLGRNH 151
Cdd:cd09641   90 LLKELGLDEELALLLAYAIAghhgglPDVLLLLDEDDESALKERLEE---LDEEKLLLELWEEELEELLDELLKELLLLL 166


                 ....*....
gi 502745998 152 PSIKRIILL 160
Cdd:cd09641  167 LPELLSFEL 175
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH