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Conserved domains on  [gi|1002256685|ref|XP_015632648|]
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adenylate isopentenyltransferase 5, chloroplastic [Oryza sativa Japonica Group]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
51-317 5.80e-85

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member PLN02165:

Pssm-ID: 476819  Cd Length: 334  Bit Score: 260.53  E-value: 5.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDD-EFTAADFRRE 129
Cdd:PLN02165   42 KDKVVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDgELTASEFRSL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 130 AARAAAGAVERGRLPIIAGGSNSYVEELV------------EGDGRAFRE-RYECCFLWVDVDLEVLRGFVARRVDEMCR 196
Cdd:PLN02165  122 ASLSISEITSRQKLPIVAGGSNSFIHALLadrfdpeiypfsSGSSLISSDlRYDCCFIWVDVSEPVLFEYLSKRVDEMMD 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 197 RGLVREVAAAFDPRRTDYSR-GIWRAIGVPELDAYLR--SRGDGADEEERARMLA--AAVAEIKLNTFRLACRQHRKIER 271
Cdd:PLN02165  202 SGMFEELAEFYDPVKSGSEPlGIRKAIGVPEFDRYFKkyPPENKMGKWDQARKAAyeEAVREIKENTCQLAKRQIEKIMK 281
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002256685 272 LDRM-WRARRVDATEVFR------RRGHAADDAWQRLVAAPCIDAVRSFLFED 317
Cdd:PLN02165  282 LKSAgWDIKRVDATASFRavmrkkGKKKKWREIWEKDVLEPSVKIVKRFLVED 334
 
Name Accession Description Interval E-value
PLN02165 PLN02165
adenylate isopentenyltransferase
51-317 5.80e-85

adenylate isopentenyltransferase


Pssm-ID: 177823  Cd Length: 334  Bit Score: 260.53  E-value: 5.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDD-EFTAADFRRE 129
Cdd:PLN02165   42 KDKVVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDgELTASEFRSL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 130 AARAAAGAVERGRLPIIAGGSNSYVEELV------------EGDGRAFRE-RYECCFLWVDVDLEVLRGFVARRVDEMCR 196
Cdd:PLN02165  122 ASLSISEITSRQKLPIVAGGSNSFIHALLadrfdpeiypfsSGSSLISSDlRYDCCFIWVDVSEPVLFEYLSKRVDEMMD 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 197 RGLVREVAAAFDPRRTDYSR-GIWRAIGVPELDAYLR--SRGDGADEEERARMLA--AAVAEIKLNTFRLACRQHRKIER 271
Cdd:PLN02165  202 SGMFEELAEFYDPVKSGSEPlGIRKAIGVPEFDRYFKkyPPENKMGKWDQARKAAyeEAVREIKENTCQLAKRQIEKIMK 281
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002256685 272 LDRM-WRARRVDATEVFR------RRGHAADDAWQRLVAAPCIDAVRSFLFED 317
Cdd:PLN02165  282 LKSAgWDIKRVDATASFRavmrkkGKKKKWREIWEKDVLEPSVKIVKRFLVED 334
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
51-265 1.11e-36

tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440093  Cd Length: 306  Bit Score: 134.42  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREA 130
Cdd:COG0324     1 KPPLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 131 ARAAAGAVERGRLPIIAGGSNSYVEELVEG----------------------------------D--------------- 161
Cdd:COG0324    81 RAAIAEILARGKLPILVGGTGLYIKALLEGlsflppadpelraeleaeaeelglealhaelaelDpeaaarihpndpqri 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 162 ----------GRAFRE---------RYECCFLWVDVDLEVLRGFVARRVDEMCRRGLVREVAAAFDprrTDYSRG--IWR 220
Cdd:COG0324   161 iralevyeltGKPLSElqkekkeppPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVRALLA---RGLDPDlpAMR 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002256685 221 AIGVPELDAYLRSRGDgadeeerarmLAAAVAEIKLNTFRLACRQ 265
Cdd:COG0324   238 AIGYRELLAYLDGEIS----------LEEAIERIKRATRQYAKRQ 272
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
54-265 2.71e-30

tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate transferase, IPP transferase, 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. Catalyzes the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladenosine. Understanding of substrate specificity has changed. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 213512  Cd Length: 287  Bit Score: 116.72  E-value: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  54 AVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREAARA 133
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSAADFQTQALNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 134 AAGAVERGRLPIIAGGSNSYVEELVEGDGR------AFRER--------------------------------------- 168
Cdd:TIGR00174  81 IADITARGKIPLLVGGTGLYLKALLEGLSPtpsadkLIREQleilaeeqgwdflynelkkvdpvaaakihpndtrrvqra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 169 -----------------------YECCFLWVDVDLEVLRGFVARRVDEMCRRGLVREVAAAFDpRRTDYSRGIWRAIGVP 225
Cdd:TIGR00174 161 levfyatgkppselfkeqkielfYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYA-QYDLCDLPSIQAIGYK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002256685 226 ELDAYLrsrgdgadeeERARMLAAAVAEIKLNTFRLACRQ 265
Cdd:TIGR00174 240 EFLLYL----------EGTVSLEDAIERIKCNTRQYAKRQ 269
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
87-265 7.48e-25

IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2)-isopentenylpyrophosphate transferase. These enzymes modify both cytoplasmic and mitochondrial tRNAs at A(37) to give isopentenyl A(37).


Pssm-ID: 460304  Cd Length: 242  Bit Score: 100.96  E-value: 7.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  87 QIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREAARAAAGAVERGRLPIIAGGSNSYV------------ 154
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEEYSVADFQRDALAAIEEIHARGKLPILVGGTGLYLkalldglddfpp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 155 ----------------------EELVEGD-------------------------GRAF---------RERYECCFLWVDv 178
Cdd:pfam01715  81 adpelraeleaeaaeeglealhAELAEVDpeaaarihpndrrriiralevyeltGKPLsefqepekpPPPYDTLIIGLS- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 179 DLEVLRGFVARRVDEMCRRGLVREVAAAFDpRRTDYSRGIWRAIGVPELDAYLRSRGDgadeeerarmLAAAVAEIKLNT 258
Cdd:pfam01715 160 DREELYERINARVDAMLEAGLLEEVRALLD-RGYGGDLPAMQAIGYKELLAYLDGEIS----------LEEAIELIKRAT 228

                  ....*..
gi 1002256685 259 FRLACRQ 265
Cdd:pfam01715 229 RQYAKRQ 235
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
55-90 6.61e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 36.85  E-value: 6.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002256685  55 VVVMGATGTGKSRLAVDLALRFGGEVINSDkmQIHS 90
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGD--DLHP 35
 
Name Accession Description Interval E-value
PLN02165 PLN02165
adenylate isopentenyltransferase
51-317 5.80e-85

adenylate isopentenyltransferase


Pssm-ID: 177823  Cd Length: 334  Bit Score: 260.53  E-value: 5.80e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDD-EFTAADFRRE 129
Cdd:PLN02165   42 KDKVVVIMGATGSGKSRLSVDLATRFPSEIINSDKMQVYDGLKITTNQITIQDRRGVPHHLLGELNPDDgELTASEFRSL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 130 AARAAAGAVERGRLPIIAGGSNSYVEELV------------EGDGRAFRE-RYECCFLWVDVDLEVLRGFVARRVDEMCR 196
Cdd:PLN02165  122 ASLSISEITSRQKLPIVAGGSNSFIHALLadrfdpeiypfsSGSSLISSDlRYDCCFIWVDVSEPVLFEYLSKRVDEMMD 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 197 RGLVREVAAAFDPRRTDYSR-GIWRAIGVPELDAYLR--SRGDGADEEERARMLA--AAVAEIKLNTFRLACRQHRKIER 271
Cdd:PLN02165  202 SGMFEELAEFYDPVKSGSEPlGIRKAIGVPEFDRYFKkyPPENKMGKWDQARKAAyeEAVREIKENTCQLAKRQIEKIMK 281
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1002256685 272 LDRM-WRARRVDATEVFR------RRGHAADDAWQRLVAAPCIDAVRSFLFED 317
Cdd:PLN02165  282 LKSAgWDIKRVDATASFRavmrkkGKKKKWREIWEKDVLEPSVKIVKRFLVED 334
PLN02748 PLN02748
tRNA dimethylallyltransferase
51-319 4.24e-62

tRNA dimethylallyltransferase


Pssm-ID: 215399 [Multi-domain]  Cd Length: 468  Bit Score: 205.50  E-value: 4.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREA 130
Cdd:PLN02748   21 KAKVVVVMGPTGSGKSKLAVDLASHFPVEIINADSMQVYSGLDVLTNKVPLHEQKGVPHHLLGVISPSVEFTAKDFRDHA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 131 ARAAAGAVERGRLPIIAGGSNSYVEELV---------------------------------------------------- 158
Cdd:PLN02748  101 VPLIEEILSRNGLPVIVGGTNYYIQALVspfllddmaeetedctfvvasvldehmdvesglgnddedhgyellkeldpva 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 159 -----------------------------------EGDGRAFRERYECCFLWVDVDLEVLRGFVARRVDEMCRRGLVREV 203
Cdd:PLN02748  181 anrihpnnhrkinrylelyattgvlpsklyqgkaaENWGRISNSRFDCCFICVDADTAVLDRYVNQRVDCMIDAGLLDEV 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 204 AAAFDPrRTDYSRGIWRAIGVPELDAYLR-----SRGD---------------------GADEEERARMLAAAVAEIKLN 257
Cdd:PLN02748  261 YDIYDP-GADYTRGLRQAIGVREFEDFLRlylsrNENGeltsssnndkvmkensrkilnFPHDDKLKILLDEAIDQVKLN 339
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002256685 258 TFRLACRQHRKIERLDRM--WRARRVDATEVFRrrgHAADDAWQRLVAAPCIDAVRSFLFEDQE 319
Cdd:PLN02748  340 TRRLVRRQKRRLHRLNTVfgWNIHYIDATEAIL---CKSEESWNAKVVKPAVEIVRRFLSDDTS 400
MiaA COG0324
tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; ...
51-265 1.11e-36

tRNA A37 N6-isopentenylltransferase MiaA [Translation, ribosomal structure and biogenesis]; tRNA A37 N6-isopentenylltransferase MiaA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440093  Cd Length: 306  Bit Score: 134.42  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREA 130
Cdd:COG0324     1 KPPLIVIVGPTASGKTALAIELAKRLGGEIISADSMQVYRGMDIGTAKPTAEERAGVPHHLIDILDPDEEYSVADFQRDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 131 ARAAAGAVERGRLPIIAGGSNSYVEELVEG----------------------------------D--------------- 161
Cdd:COG0324    81 RAAIAEILARGKLPILVGGTGLYIKALLEGlsflppadpelraeleaeaeelglealhaelaelDpeaaarihpndpqri 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 162 ----------GRAFRE---------RYECCFLWVDVDLEVLRGFVARRVDEMCRRGLVREVAAAFDprrTDYSRG--IWR 220
Cdd:COG0324   161 iralevyeltGKPLSElqkekkeppPYDVLKIGLDPDREELYERINRRVDQMLEAGLLDEVRALLA---RGLDPDlpAMR 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1002256685 221 AIGVPELDAYLRSRGDgadeeerarmLAAAVAEIKLNTFRLACRQ 265
Cdd:COG0324   238 AIGYRELLAYLDGEIS----------LEEAIERIKRATRQYAKRQ 272
miaA TIGR00174
tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate ...
54-265 2.71e-30

tRNA dimethylallyltransferase; Alternate names include delta(2)-isopentenylpyrophosphate transferase, IPP transferase, 2-methylthio-N6-isopentyladenosine tRNA modification enzyme. Catalyzes the first step in the modification of an adenosine near the anticodon to 2-methylthio-N6-isopentyladenosine. Understanding of substrate specificity has changed. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 213512  Cd Length: 287  Bit Score: 116.72  E-value: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  54 AVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREAARA 133
Cdd:TIGR00174   1 VIFLMGPTASGKSQLSIQLAQKLNAEIISVDSMQIYKGMDIGTAKPSLQEREGIPHHLIDILDPSESYSAADFQTQALNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 134 AAGAVERGRLPIIAGGSNSYVEELVEGDGR------AFRER--------------------------------------- 168
Cdd:TIGR00174  81 IADITARGKIPLLVGGTGLYLKALLEGLSPtpsadkLIREQleilaeeqgwdflynelkkvdpvaaakihpndtrrvqra 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 169 -----------------------YECCFLWVDVDLEVLRGFVARRVDEMCRRGLVREVAAAFDpRRTDYSRGIWRAIGVP 225
Cdd:TIGR00174 161 levfyatgkppselfkeqkielfYDIVQIGLASSREPLHQRIEQRVHDMLESGLLAEVKALYA-QYDLCDLPSIQAIGYK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1002256685 226 ELDAYLrsrgdgadeeERARMLAAAVAEIKLNTFRLACRQ 265
Cdd:TIGR00174 240 EFLLYL----------EGTVSLEDAIERIKCNTRQYAKRQ 269
IPPT pfam01715
IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2) ...
87-265 7.48e-25

IPP transferase; This is a family of IPP transferases EC:2.5.1.8 also known as tRNA delta(2)-isopentenylpyrophosphate transferase. These enzymes modify both cytoplasmic and mitochondrial tRNAs at A(37) to give isopentenyl A(37).


Pssm-ID: 460304  Cd Length: 242  Bit Score: 100.96  E-value: 7.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  87 QIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREAARAAAGAVERGRLPIIAGGSNSYV------------ 154
Cdd:pfam01715   1 QVYRGMDIGTAKPTPEERAGVPHHLIDILDPDEEYSVADFQRDALAAIEEIHARGKLPILVGGTGLYLkalldglddfpp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 155 ----------------------EELVEGD-------------------------GRAF---------RERYECCFLWVDv 178
Cdd:pfam01715  81 adpelraeleaeaaeeglealhAELAEVDpeaaarihpndrrriiralevyeltGKPLsefqepekpPPPYDTLIIGLS- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 179 DLEVLRGFVARRVDEMCRRGLVREVAAAFDpRRTDYSRGIWRAIGVPELDAYLRSRGDgadeeerarmLAAAVAEIKLNT 258
Cdd:pfam01715 160 DREELYERINARVDAMLEAGLLEEVRALLD-RGYGGDLPAMQAIGYKELLAYLDGEIS----------LEEAIELIKRAT 228

                  ....*..
gi 1002256685 259 FRLACRQ 265
Cdd:pfam01715 229 RQYAKRQ 235
PLN02840 PLN02840
tRNA dimethylallyltransferase
51-160 7.00e-23

tRNA dimethylallyltransferase


Pssm-ID: 215451  Cd Length: 421  Bit Score: 98.74  E-value: 7.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  51 KHKAVVVMGATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPHHLISVARPDDEFTAADFRREA 130
Cdd:PLN02840   20 KEKVIVISGPTGAGKSRLALELAKRLNGEIISADSVQVYRGLDVGSAKPSLSERKEVPHHLIDILHPSDDYSVGAFFDDA 99
                          90       100       110
                  ....*....|....*....|....*....|
gi 1002256685 131 ARAAAGAVERGRLPIIAGGSNSYVEELVEG 160
Cdd:PLN02840  100 RRATQDILNRGRVPIVAGGTGLYLRWYIYG 129
IPT pfam01745
Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes ...
59-207 2.15e-03

Isopentenyl transferase; Isopentenyl transferase / dimethylallyl transferase synthesizes isopentenyladensosine 5'-monophosphate, a cytokinin that induces shoot formation on host plants infected with the Ti plasmid.


Pssm-ID: 366786  Cd Length: 232  Bit Score: 39.30  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685  59 GATGTGKSRLAVDLALRFGGEVINSDKMQIHSGLDVVTNKVTEEECAGVPH-HLISvaRPDDE--FTAADFRREAARAAA 135
Cdd:pfam01745   8 GATCTGKTAEAIALAKETGWPVIVLDRVQCCSQLATGSGRPLPAELQGTRRiYLDN--RPLSEgiIDAEEAHDRLIAEVT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002256685 136 GAVERGRLpIIAGGSNSYVEELVegdgrafRERYECC-FLWVdVDLEVLRG---FVAR---RVDEMCR-----RGLVREV 203
Cdd:pfam01745  86 SHKDEGGV-ILEGGSISLLKRMA-------QSPYWNAgFPWH-VKRMRLPDrdvFLAQakaRVRQMLRpdsggPSLLDEL 156

                  ....
gi 1002256685 204 AAAF 207
Cdd:pfam01745 157 AELW 160
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
55-90 6.61e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 36.85  E-value: 6.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002256685  55 VVVMGATGTGKSRLAVDLALRFGGEVINSDkmQIHS 90
Cdd:cd02021     2 IVVMGVSGSGKSTVGKALAERLGAPFIDGD--DLHP 35
 
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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