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Conserved domains on  [gi|973165478|gb|KUL05251|]
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PUA domain containing protein [Methanomicrobiales archaeon 53_19]

Protein Classification

ArcTGT family protein( domain architecture ID 11443234)

ArcTGT family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ArcTGT COG1370
tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains ...
 7-157 1.55e-77

tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440981 [Multi-domain]  Cd Length: 157  Bit Score: 227.00  E-value: 1.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   7 SLRRVRKIAEFQFGRGSGDALFPEECTFQYSTSQ-RIRYVILDGVRLATVRAQDGRLTLSYDGAARLHAFLAPPTGRVVV 85
Cdd:COG1370    5 DLERLRTIADYQFGRGAGEALFPDDITIERSKKTgRIRQVYLDGKRLATLRATDGRFTLTIEGARRLHEALPFPKYRVVV 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165478  86 HEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQGRDKQ 157
Cdd:COG1370   85 DDESAPFVREGKNVFAKFVIDVDPEIRPGDEVLVVDEDDELLAVGRALLSGEEMKDFKRGVAVKVREGVKKE 156
 
Name Accession Description Interval E-value
ArcTGT COG1370
tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains ...
 7-157 1.55e-77

tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440981 [Multi-domain]  Cd Length: 157  Bit Score: 227.00  E-value: 1.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   7 SLRRVRKIAEFQFGRGSGDALFPEECTFQYSTSQ-RIRYVILDGVRLATVRAQDGRLTLSYDGAARLHAFLAPPTGRVVV 85
Cdd:COG1370    5 DLERLRTIADYQFGRGAGEALFPDDITIERSKKTgRIRQVYLDGKRLATLRATDGRFTLTIEGARRLHEALPFPKYRVVV 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165478  86 HEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQGRDKQ 157
Cdd:COG1370   85 DDESAPFVREGKNVFAKFVIDVDPEIRPGDEVLVVDEDDELLAVGRALLSGEEMKDFKRGVAVKVREGVKKE 156
TGT_C2 pfam14810
Patch-forming domain C2 of tRNA-guanine transglycosylase; Domain C2 of tRNA-guanine ...
 10-79 3.87e-35

Patch-forming domain C2 of tRNA-guanine transglycosylase; Domain C2 of tRNA-guanine transglycosylase is formed by a four-stranded anti-parallel beta-sheet lined with two alpha helices. It has conserved basic residues on the surface of the beta-sheets as does the C-terminal domain PUA, pfam01472. The catalytic domain, TGT has conserved basic residues on the outer surface of the N-terminal three-stranded beta sheet, which closes the barrel, and it is postulated that these basic residues from the three domains form a continuous, positively charged patch to which the tRNA binds.


Pssm-ID: 434230 [Multi-domain]  Cd Length: 70  Bit Score: 116.82  E-value: 3.87e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   10 RVRKIAEFQFGRGSGDALFPEECTFQYSTSQRIRYVILDGVRLATVRAQDGRLTLSYDGAARLHAFLAPP 79
Cdd:pfam14810   1 RLRAIADYQFGRGAGDALFPDDVTIQRSSTGRIRQVLLDGERLATLRAQDGRLTLSIEGAKRLHEALPPP 70
PUA_archaeosine_TGT cd21149
PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA ...
 79-153 2.59e-28

PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this archaeosine tRNA-guanine transglycosylase (TGT) family are responsible for the exchange of a guanine residue in archaeal tRNAs with a preQ0 base (7-cyano-7-deazaguanine), which constitutes the initial step in archaeosine biosynthesis. Archaeosine is a modified RNA base specific to archaea (7-formamidino-7deazaguanosine), found at position 15 in tRNAs. It has been shown that the PUA domain of archaeosine TGT is not required for its specificity for position 15.


Pssm-ID: 409291 [Multi-domain]  Cd Length: 75  Bit Score: 99.61  E-value: 2.59e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973165478  79 PTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQG 153
Cdd:cd21149    1 PENRVVVNKESAPFVRKGGSVFAKGVVDADENIRPGDEVLVVDEDDRLLAVGRAVLSGKEMKEFERGVAVKVRHG 75
PRK13795 PRK13795
hypothetical protein; Provisional
 45-151 4.91e-17

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 76.96  E-value: 4.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478  45 VILDGVRLATVR----AQDGRLTLSYDGAARLHAFLappTGR-VVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFV 119
Cdd:PRK13795  89 IIVDGRVIGHLRfdllELRWRFEPRLEGAKRLLKKR---LKKwVIVDKGALEPIKNGKNVLAPGVVEADLDIKKGDEVVV 165

                         90       100       110
                 ....*....|....*....|....*....|..
gi 973165478 120 VAEDDSLLATGMANLSGSEMLEFKYGGAVKVR 151
Cdd:PRK13795 166 VTEDGEVVGVGRAKMDGDDMIKRFRGRAVKVR 197
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
81-152 6.02e-14

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 63.04  E-value: 6.02e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165478    81 GRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFK-YGGAVKVRQ 152
Cdd:smart00359   1 GKVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKgKGLAVKVRR 73
unchar_dom_2 TIGR00451
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ...
 59-151 6.74e-14

uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and uncharacterized proteins, often at the C-terminus. It is found in some but not all members of a family of related tRNA-guanine transglycosylases (tgt), which exchange a guanine base for some modified base without breaking the phosphodiester backbone of the tRNA. It is also found in rRNA pseudouridine synthase, another enzyme of RNA base modification not otherwise homologous to tgt. It is found, again at the C-terminus, in two putative glutamate 5-kinases. It is also found in a family of small, uncharacterized archaeal proteins consisting mostly of this domain.


Pssm-ID: 129543 [Multi-domain]  Cd Length: 107  Bit Score: 63.61  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   59 DGRLTLSYDGAARLhaflAPPTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAED-DSLLATGMANLSGS 137
Cdd:TIGR00451  13 DDKVIPSLKGALKL----MEDKKIVVVDNGAVKFLKNGADVMRPGIVDADEDIKEGDDVVVVDENkDRPLAVGIALMSGE 88

                          90
                  ....*....|....
gi 973165478  138 EMLEFKYGGAVKVR 151
Cdd:TIGR00451  89 EMKEMDKGKAVKNI 102
 
Name Accession Description Interval E-value
ArcTGT COG1370
tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains ...
 7-157 1.55e-77

tRNA-guanine transglycosylase, archaeosine-15-forming, contains TGT and PUA domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440981 [Multi-domain]  Cd Length: 157  Bit Score: 227.00  E-value: 1.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   7 SLRRVRKIAEFQFGRGSGDALFPEECTFQYSTSQ-RIRYVILDGVRLATVRAQDGRLTLSYDGAARLHAFLAPPTGRVVV 85
Cdd:COG1370    5 DLERLRTIADYQFGRGAGEALFPDDITIERSKKTgRIRQVYLDGKRLATLRATDGRFTLTIEGARRLHEALPFPKYRVVV 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165478  86 HEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQGRDKQ 157
Cdd:COG1370   85 DDESAPFVREGKNVFAKFVIDVDPEIRPGDEVLVVDEDDELLAVGRALLSGEEMKDFKRGVAVKVREGVKKE 156
TGT_C2 pfam14810
Patch-forming domain C2 of tRNA-guanine transglycosylase; Domain C2 of tRNA-guanine ...
 10-79 3.87e-35

Patch-forming domain C2 of tRNA-guanine transglycosylase; Domain C2 of tRNA-guanine transglycosylase is formed by a four-stranded anti-parallel beta-sheet lined with two alpha helices. It has conserved basic residues on the surface of the beta-sheets as does the C-terminal domain PUA, pfam01472. The catalytic domain, TGT has conserved basic residues on the outer surface of the N-terminal three-stranded beta sheet, which closes the barrel, and it is postulated that these basic residues from the three domains form a continuous, positively charged patch to which the tRNA binds.


Pssm-ID: 434230 [Multi-domain]  Cd Length: 70  Bit Score: 116.82  E-value: 3.87e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   10 RVRKIAEFQFGRGSGDALFPEECTFQYSTSQRIRYVILDGVRLATVRAQDGRLTLSYDGAARLHAFLAPP 79
Cdd:pfam14810   1 RLRAIADYQFGRGAGDALFPDDVTIQRSSTGRIRQVLLDGERLATLRAQDGRLTLSIEGAKRLHEALPPP 70
PUA_archaeosine_TGT cd21149
PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA ...
 79-153 2.59e-28

PUA RNA-binding domain of archaeosine tRNA-guanine transglycosylase; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this archaeosine tRNA-guanine transglycosylase (TGT) family are responsible for the exchange of a guanine residue in archaeal tRNAs with a preQ0 base (7-cyano-7-deazaguanine), which constitutes the initial step in archaeosine biosynthesis. Archaeosine is a modified RNA base specific to archaea (7-formamidino-7deazaguanosine), found at position 15 in tRNAs. It has been shown that the PUA domain of archaeosine TGT is not required for its specificity for position 15.


Pssm-ID: 409291 [Multi-domain]  Cd Length: 75  Bit Score: 99.61  E-value: 2.59e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 973165478  79 PTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQG 153
Cdd:cd21149    1 PENRVVVNKESAPFVRKGGSVFAKGVVDADENIRPGDEVLVVDEDDRLLAVGRAVLSGKEMKEFERGVAVKVRHG 75
PUA pfam01472
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ...
 81-153 4.70e-18

PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain.


Pssm-ID: 426278 [Multi-domain]  Cd Length: 74  Bit Score: 73.29  E-value: 4.70e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165478   81 GRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQG 153
Cdd:pfam01472   1 GRVVVDDGAVKAILNGASLLAPGVVRVDGDFRKGDEVVVVTEKGELVAVGLANYSSEELAKIEGGKAVKVRRV 73
PRK13795 PRK13795
hypothetical protein; Provisional
 45-151 4.91e-17

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 76.96  E-value: 4.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478  45 VILDGVRLATVR----AQDGRLTLSYDGAARLHAFLappTGR-VVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFV 119
Cdd:PRK13795  89 IIVDGRVIGHLRfdllELRWRFEPRLEGAKRLLKKR---LKKwVIVDKGALEPIKNGKNVLAPGVVEADLDIKKGDEVVV 165

                         90       100       110
                 ....*....|....*....|....*....|..
gi 973165478 120 VAEDDSLLATGMANLSGSEMLEFKYGGAVKVR 151
Cdd:PRK13795 166 VTEDGEVVGVGRAKMDGDDMIKRFRGRAVKVR 197
PUA COG5270
PUA domain (predicted RNA-binding domain) [Translation, ribosomal structure and biogenesis];
45-151 1.00e-16

PUA domain (predicted RNA-binding domain) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444082 [Multi-domain]  Cd Length: 488  Bit Score: 75.90  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478  45 VILDGVRLATVR----AQDGRLTLSYDGAARLHAflAPPTGRVVVHEEAVPFvAAGKTAMAKHVINADPNIRAEDEVFVV 120
Cdd:COG5270   87 VIVDGEVIGTLRfdpeERRWRFDLRPEGARLLVE--HATKKIVVLDKGAVKF-HKGKNVLAPGVLSADPDIKKGDEVIIL 163

                         90       100       110
                 ....*....|....*....|....*....|.
gi 973165478 121 AEDDSLLATGMANLSGSEMLEFKYGGAVKVR 151
Cdd:COG5270  164 TRDGEVVGVGRARMDGAEMVESERGVVVKVR 194
PUA cd07953
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ...
 81-151 7.71e-16

PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism.


Pssm-ID: 409289 [Multi-domain]  Cd Length: 73  Bit Score: 67.71  E-value: 7.71e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 973165478  81 GRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVR 151
Cdd:cd07953    1 PVVVVDKGAEKAVLNGADLMAPGVVSADGDFKRGDLVRIVSEGGRPLAIGVAEMSSDEMKEELKGIAVRVL 71
PUA smart00359
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;
81-152 6.02e-14

Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase;


Pssm-ID: 214635 [Multi-domain]  Cd Length: 76  Bit Score: 63.04  E-value: 6.02e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165478    81 GRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSLLATGMANLSGSEMLEFK-YGGAVKVRQ 152
Cdd:smart00359   1 GKVVVDDGAEKAILNGASLLAPGVVRVDGDIKEGDVVVIVDEKGEPLGIGLANMSSEEIARIKgKGLAVKVRR 73
unchar_dom_2 TIGR00451
uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and ...
 59-151 6.74e-14

uncharacterized domain 2; This uncharacterized domain is found a number of enzymes and uncharacterized proteins, often at the C-terminus. It is found in some but not all members of a family of related tRNA-guanine transglycosylases (tgt), which exchange a guanine base for some modified base without breaking the phosphodiester backbone of the tRNA. It is also found in rRNA pseudouridine synthase, another enzyme of RNA base modification not otherwise homologous to tgt. It is found, again at the C-terminus, in two putative glutamate 5-kinases. It is also found in a family of small, uncharacterized archaeal proteins consisting mostly of this domain.


Pssm-ID: 129543 [Multi-domain]  Cd Length: 107  Bit Score: 63.61  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478   59 DGRLTLSYDGAARLhaflAPPTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAED-DSLLATGMANLSGS 137
Cdd:TIGR00451  13 DDKVIPSLKGALKL----MEDKKIVVVDNGAVKFLKNGADVMRPGIVDADEDIKEGDDVVVVDENkDRPLAVGIALMSGE 88

                          90
                  ....*....|....
gi 973165478  138 EMLEFKYGGAVKVR 151
Cdd:TIGR00451  89 EMKEMDKGKAVKNI 102
PRK14560 PRK14560
putative RNA-binding protein; Provisional
 78-149 8.33e-12

putative RNA-binding protein; Provisional


Pssm-ID: 237757 [Multi-domain]  Cd Length: 160  Bit Score: 59.48  E-value: 8.33e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165478  78 PPTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAE-DDSLLATGMANLSGSEMLEFKYGGAVK 149
Cdd:PRK14560  74 PEKRRVVVDAGAVKFVSNGADVMAPGIVEADEDIKEGDIVFVVEEtHGKPLAVGRALMDGDEMVEEKKGKAVK 146
PUA_MJ1432-like cd21154
PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA ...
 79-149 2.85e-11

PUA RNA-binding domain of MJ1432, TA1423, PH0734, and similar proteins; The RNA-binding PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in a number of proteins involved in RNA metabolism. Members of this mostly archaeal family have not been characterized functionally; they may bind to RNA. This family includes Pyrococcus horikoshii PH0734 where the N-terminal domain may modulate the binding target of the C-terminal PUA domain using its characteristic electropositive surface.


Pssm-ID: 409296 [Multi-domain]  Cd Length: 84  Bit Score: 56.36  E-value: 2.85e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 973165478  79 PTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAEDDSL-LATGMANLSGSEMLEFKYGGAVK 149
Cdd:cd21154    1 SLPRVVVDMGAVKFVANGADVMRPGIVEADEEIKKGDIVVVVDERHGKpLAVGIALMSGEEMVEMKKGKAVK 72
Tma20 COG2016
Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ...
 78-149 1.43e-09

Predicted ribosome-associated RNA-binding protein Tma20, contains PUA domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441619 [Multi-domain]  Cd Length: 154  Bit Score: 53.25  E-value: 1.43e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 973165478  78 PPTGRVVVHEEAVPFVAAGKTAMAKHVINADPNIRAEDEVFVVAED-DSLLATGMANLSGSEMLEFKYGGAVK 149
Cdd:COG2016   71 PEKPVVTVDMGAVKFVSNGADVMRPGIVEADGEIKEGDIVVIVEEKhGKPLAVGRALVDGEEMVEGKKGKAVK 143
PRK13794 PRK13794
hypothetical protein; Provisional
 45-157 3.30e-08

hypothetical protein; Provisional


Pssm-ID: 237509 [Multi-domain]  Cd Length: 479  Bit Score: 51.21  E-value: 3.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 973165478  45 VILDGVRLATVRAQDGR----LTLSYDGAARLHaflapPTGR---VVVHEEAVPFV-AAGKTAMAKHVINADPNIRAEDE 116
Cdd:PRK13794  87 IIVDGAVVGIIRYNEKKhrwkIIPRPEGARRLI-----PTAKkkfIVVKDDVPKFIrNKGASVLRPGVAEASEDIEEGDD 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 973165478 117 VFVVAEDDSLLATGMANLSGSEMLEFKYGGAVKVRQGRDKQ 157
Cdd:PRK13794 162 VIILDENGDVVGVGRARMSYEEIVNMEKGMVVKVRKSEEPK 202
 
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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