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Conserved domains on  [gi|446631144|ref|WP_000708490|]
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MULTISPECIES: fused tRNA nucleotidyltransferase/2',3'-cyclic phosphodiesterase/2' nucleotidase/phosphatase Cca [Enterobacteriaceae]

Protein Classification

multifunctional CCA addition/repair protein( domain architecture ID 11485063)

multifunctional CCA addition/repair protein catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template

CATH:  1.10.3090.10|1.10.1300.10
EC:  2.7.7.72|3.1.3.-|3.1.4.-
Gene Ontology:  GO:0004810|GO:0005524|GO:0000049|GO:0000287|GO:0004112|GO:0016791|GO:0001680
PubMed:  3009457|15210699
SCOP:  4003222|3000943

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-409 0e+00

multifunctional CCA addition/repair protein;


:

Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 829.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALM 160
Cdd:PRK10885  81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWHPEIDTGIHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 241 MLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 321 KLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGAEIREELTRRRIAAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                 ....*....
gi 446631144 401 ASWKEQRCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
 
Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-409 0e+00

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 829.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALM 160
Cdd:PRK10885  81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWHPEIDTGIHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 241 MLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 321 KLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGAEIREELTRRRIAAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                 ....*....
gi 446631144 401 ASWKEQRCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-403 4.26e-128

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 374.54  E-value: 4.26e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGsTPQEMLDAG-----YQQVGRDFPVFLHP--QTHEEYALARTERKSGSGYTG 73
Cdd:COG0617   18 FEAYLVGGAVRDLLLGRPPKDIDIVTVA-TPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  74 FTCYAApdvTLEDDLKRRDLTINALAQDDN-GEIIDPYNGLGDLQNRLLRHVS---PAFGEDPLRVLRVARFAARyahLG 149
Cdd:COG0617   97 FVEFGD---TLEEDLARRDFTINALAYDLNdGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 150 FRIADETLALMREMthAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLfpeidalfgvpaparwhpeidtg 229
Cdd:COG0617  171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 230 ihtlmtlsmaamlspqvDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIH 309
Cdd:COG0617  226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 310 TFPMLNPKTIVKLFDsidawRKPQRVEQLALTSEAdvrgrtGFESADYPQ--GRWLREAWEVAQ-SVPTKAVVEAGFK-G 385
Cdd:COG0617  289 GLGELRDSAVRRLLE-----RGPEALEDLLLLREN------GLEYPELQErlAELLEAAWRRFQpPVDGEDLMALGLKpG 357

                        410
                 ....*....|....*...
gi 446631144 386 AEIREELTRRRIAAVASW 403
Cdd:COG0617  358 PEIGEILRALREAVLDGG 375
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-118 7.58e-31

Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily.


Pssm-ID: 143388 [Multi-domain]  Cd Length: 139  Bit Score: 115.00  E-value: 7.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHE--------EYALARTERKSGSGyt 72
Cdd:cd05398   17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGLGEEFGTATvvingltiDVATLRTETYTDPG-- 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446631144  73 gfTCYAAPDVTLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQN 118
Cdd:cd05398   95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 4-324 8.58e-28

poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca).


Pssm-ID: 130997 [Multi-domain]  Cd Length: 410  Bit Score: 113.74  E-value: 8.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144    4 YLVGGAVRDALLGLPVKDRDwVVVGSTPQEM--LDAGYQQVGRDFPVfLH---PQTHEEYALARTERKSGSGYTGFTCYA 78
Cdd:TIGR01942  33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRILKD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   79 APDVTLEDDLKRRDLTINALAQDDNGE-IIDPYNGLGDLQNRLLRHVSPA---FGEDPLRVLRVARFAARYahlGFRIAD 154
Cdd:TIGR01942 111 NVYGTLEEDAWRRDFTVNALYYDPSREvIIDYVGGMEDLKNRRLRLIGDPrsrYQEDPVRMLRALRFSVKL---EFTIDE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  155 ETLALMREMTHagELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGvpaparwhpEIDTGIHTLM 234
Cdd:TIGR01942 188 STARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYALR---------ESPKFESAFT 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  235 TLSMAAMLSPQVDVRFATLCHDLGKGLTPPELwPRHHGHGPA-GVK-----------LVEQLCQRLRVPNEIRDLARLVA 302
Cdd:TIGR01942 257 VQALVNDTDFRVKRDKPVTPAFLYAALLWPGL-VFRVADAPDqGVMpypavfdairdFVEEQCAPISIPKRFSIPTREIW 335

                         330       340
                  ....*....|....*....|..
gi 446631144  303 EFHdliHTFPMLNPKTIVKLFD 324
Cdd:TIGR01942 336 QMQ---LRLERRSGMRARKLLG 354
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 3-122 2.65e-20

Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.


Pssm-ID: 396348 [Multi-domain]  Cd Length: 126  Bit Score: 85.79  E-value: 2.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144    3 IYLVGGAVRDALLGLPVKDRDwVVVGSTPQEMLDAGYQQVGRDFPVFLHPQT------HEEYALARTerKSGSGYTGFtc 76
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQVATLFRRRRIVHLLSGIEFGTihvifgNQILEVATF--RIEFDESDF-- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446631144   77 yAAPDV-----TLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQNRLLR 122
Cdd:pfam01743  76 -RNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 228-328 1.66e-05

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: 43.82  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   228 TGIHTLMTLSMAAMLSPQVD------VRFATLCHDLGKGLTPPELWPR---HHGHGPAGVKLVEQlcqrLRVPNEIRDLA 298
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVKtsvLEDHHFIGAEILLE----EEEPRILEEIL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 446631144   299 RLVAEFHDLIHTF----PMLNPKTIVKLFDSIDA 328
Cdd:smart00471  81 RTAILSHHERPDGlrgePITLEARIVKVADRLDA 114
 
Name Accession Description Interval E-value
cca PRK10885
multifunctional CCA addition/repair protein;
1-409 0e+00

multifunctional CCA addition/repair protein;


Pssm-ID: 182810 [Multi-domain]  Cd Length: 409  Bit Score: 829.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK10885   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGATPEEMLAQGYQQVGKDFPVFLHPKTHEEYALARTERKSGRGYTGFTCYAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALM 160
Cdd:PRK10885  81 DVTLEEDLIRRDLTINAMAQDDDGELIDPYGGQRDLEARLLRHVSPAFAEDPLRVLRVARFAARFAHLGFRIAPETLALM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWHPEIDTGIHTLMTLSMAA 240
Cdd:PRK10885 161 REMVASGELDALTPERVWKETERALMERNPQVFFQVLRDCGALAVLLPEIDALFGVPQPAKWHPEIDTGIHTLMVLDQAA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 241 MLSPQVDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPKTIV 320
Cdd:PRK10885 241 KLSPSLDVRFAALCHDLGKGLTPPEEWPRHHGHEPRGVKLVEQLCQRLRVPNECRDLALLVAEEHDNIHRAPELRPKTLV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 321 KLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGAEIREELTRRRIAAV 400
Cdd:PRK10885 321 KLLDRIDAWRKPQRFEQFLLACEADARGRLGFEDRPYPQAEYLREALQAARSVDAKAVVAAGFKGAAIREELTRRRIAAV 400


                 ....*....
gi 446631144 401 ASWKEQRCP 409
Cdd:PRK10885 401 AAWKEQRCP 409
PRK13298 PRK13298
tRNA CCA-pyrophosphorylase; Provisional
 1-406 0e+00

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237338 [Multi-domain]  Cd Length: 417  Bit Score: 543.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13298   1 MKIYLVGGAVRDSLLNLPVKDKDWVVVGGTPKILLSINFQQVGKDFPVFLHPETHEEYALARTERKSGVGYTGFITDTSS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALM 160
Cdd:PRK13298  81 DVTLEEDLIRRDLTINAIAQDENGNYIDPFQGKKDIQLRLLRHVSESFIEDPLRVLRVARFAALLVHLGFKIAKETMILM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVPAPARWH-PEIDTGIHTLMTLSMA 239
Cdd:PRK13298 161 CIMVKKHELLYLTPERIWNETEKALKTDNPHVYFQVLYECNALKFLFPEIDFLYEKPYFLNSFfKKFNLGNYILMGLSKI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 240 AMLSPQVDVRFATLCHDLGKGLTPPELWP--RHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMLNPK 317
Cdd:PRK13298 241 SKLTKDIDIRFSYLCQFLGSMIPINQIKRnyKKIFFDKYAASLIKNLCKRFKIPSYIRNIAVLNTGFYFFLYNIHYQSSK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 318 TIVKLFDSIDAWRKPQRVEQLALTSEADVRGRTGFESADYPQGRWLREAWEVAQSVPTKAVVEAGFKGAEIREELTRRRI 397
Cdd:PRK13298 321 NIITLFSKIDAWRKPDRIKKLIFLSNFNLLRNKKSINFLIKQGNFLKKAFSVTKKISIKDILKKGFKGYEIKQELYRLRI 400


                 ....*....
gi 446631144 398 AAVASWKEQ 406
Cdd:PRK13298 401 HKLKFWRNK 409
PcnB COG0617
tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and ...
 1-403 4.26e-128

tRNA nucleotidyltransferase/poly(A) polymerase [Translation, ribosomal structure and biogenesis]; tRNA nucleotidyltransferase/poly(A) polymerase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440382 [Multi-domain]  Cd Length: 391  Bit Score: 374.54  E-value: 4.26e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGsTPQEMLDAG-----YQQVGRDFPVFLHP--QTHEEYALARTERKSGSGYTG 73
Cdd:COG0617   18 FEAYLVGGAVRDLLLGRPPKDIDIVTVA-TPEEVAALFrkalrTVPVGRDFGTVTVVfgGEKIEVATARTERYYGDGRRP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  74 FTCYAApdvTLEDDLKRRDLTINALAQDDN-GEIIDPYNGLGDLQNRLLRHVS---PAFGEDPLRVLRVARFAARyahLG 149
Cdd:COG0617   97 FVEFGD---TLEEDLARRDFTINALAYDLNdGELIDPFGGLADLEARVIRTVGdpeERFREDPLRILRAVRFAAR---LG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 150 FRIADETLALMREMthAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLfpeidalfgvpaparwhpeidtg 229
Cdd:COG0617  171 FTIEPETLAAIREM--AGLLDRLSAERVWDELLKLLLSPHPSRGLELLRETGLLEVL----------------------- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 230 ihtlmtlsmaamlspqvDVRFATLCHDLGKGLTPPELWPRHHGHGPAGVKLVEQLCQRLRVPNEIRDLARLVAEFHDLIH 309
Cdd:COG0617  226 -----------------ALRLAALLHDLGKPATREDGLPTFHGHEEAGAELAEALLKRLRLPNRERKLVRELVELHLRFH 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 310 TFPMLNPKTIVKLFDsidawRKPQRVEQLALTSEAdvrgrtGFESADYPQ--GRWLREAWEVAQ-SVPTKAVVEAGFK-G 385
Cdd:COG0617  289 GLGELRDSAVRRLLE-----RGPEALEDLLLLREN------GLEYPELQErlAELLEAAWRRFQpPVDGEDLMALGLKpG 357

                        410
                 ....*....|....*...
gi 446631144 386 AEIREELTRRRIAAVASW 403
Cdd:COG0617  358 PEIGEILRALREAVLDGG 375
PRK13297 PRK13297
tRNA CCA-pyrophosphorylase; Provisional
 1-339 2.15e-95

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 139469 [Multi-domain]  Cd Length: 364  Bit Score: 290.36  E-value: 2.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13297  12 LQVYIVGGAVRDALLGLPAGDRDWVVVGATPEDMARRGFIPVGGDFPVFLHPRTKEEYALARTERKSGRGYKGFTFYTGA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHlgFRIADETLALM 160
Cdd:PRK13297  92 DVTLEQDLQRRDLTVNAIARTPQGELVDPLDGVADVRARVLRHVGEAFAEDPVRILRLGRFAARFGD--FSIAPETMQLC 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 161 REMTHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGVpaparwHPEIDTgihtlmtlsmAA 240
Cdd:PRK13297 170 RRMVEAGEADALVPERVWKEVSRGLMAQAPSRMLDVLARAGALARVMPELHDDAAV------RAEIDR----------AA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 241 MLSPQVDVRFATLCHdlgkgLTPPELwprhhghgpagvklveQLCQRLRVPNEIRDLARLVAEFHDLIHTFPMlnPKTIV 320
Cdd:PRK13297 234 AAGLPLAGRYALLCR-----HTPERD----------------ALGRRLRAPVECMDQARLLPLAVDALAASAT--PAAQL 290

                        330
                 ....*....|....*....
gi 446631144 321 KLFDSIDAWRKPQRVEQLA 339
Cdd:PRK13297 291 DLIERCDALRKPERFDALL 309
PRK13296 PRK13296
CCA tRNA nucleotidyltransferase;
1-217 6.60e-91

CCA tRNA nucleotidyltransferase;


Pssm-ID: 106256 [Multi-domain]  Cd Length: 360  Bit Score: 278.79  E-value: 6.60e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHEEYALARTERKSGSGYTGFTCYAAP 80
Cdd:PRK13296   1 MKFYLVGGAVRDMLLGITPKDKDWVVVGATEDEMLANGFIKIAANFPVFIHPQTKQEYALARSEKKTASGYHGFEVNFSK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  81 DVTLEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHVSPAFGEDPLRVLRVARFAARYAHLGFRIADETLALM 160
Cdd:PRK13296  81 YITLEDDLKRRDLTINSIAIDQNNKVIDPFNGQADLQNRILRHTSIAFIEDPLRVVRLARFKAQLSNFNFSIAQEMLALI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446631144 161 REMTHAGELEHLTPERVWKETESALttRNPQVFFQVLRDCGALRVLFPEID-ALFGVP 217
Cdd:PRK13296 161 KELVKTGELNHLTRERLHIEFVKAL--NNPKIFFTTLKELEALKIIFPNIScILPLIP 216
PRK13299 PRK13299
tRNA CCA-pyrophosphorylase; Provisional
 4-238 2.20e-40

tRNA CCA-pyrophosphorylase; Provisional


Pssm-ID: 237339 [Multi-domain]  Cd Length: 394  Bit Score: 147.68  E-value: 2.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   4 YLVGGAVRDALLGLPVKDRDwVVVGSTPQEMLDAgYQ---QVGRDFPVFLHPQTHEEYALA--RTErksgSGYTGftcYA 78
Cdd:PRK13299  24 YFVGGSVRDYLLGRPIHDVD-IATSAYPEEVKAI-FPrtvDVGIEHGTVLVLENGEEYEVTtfRTE----SEYVD---YR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  79 APD-VT----LEDDLKRRDLTINALAQDDNGEIIDPYNGLGDLQNRLLRHV-SPA--FGEDPLRVLRVARFAARyahLGF 150
Cdd:PRK13299  95 RPSeVTfvrsLEEDLKRRDFTINAIAMDENGEIIDLFDGLEDLKNRLIRAVgNAEerFQEDALRMMRAVRFASQ---LGF 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 151 RIADETLALMREmtHAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGalrvLFPEI-------DALFGVPAPARWH 223
Cdd:PRK13299 172 DLETETFEAMKT--QAPLLEKISVERIFVEFEKLLLGPFWRKGLKLLIETG----LYNYLpglkgkeENLLKLTQLLWFS 245

                        250
                 ....*....|....*
gi 446631144 224 PEIDTGIHTLMTLSM 238
Cdd:PRK13299 246 FETSEQAWAALLISL 260
NT_ClassII-CCAase cd05398
Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the ...
 1-118 7.58e-31

Nucleotidyltransferase (NT) domain of ClassII CCA-adding enzymes; CCA-adding enzymes add the sequence [cytidine(C)-cytidine-adenosine (A)], one nucleotide at a time, onto the 3' end of tRNA, in a template-independent reaction. This Class II group is comprised mainly of eubacterial and eukaryotic enzymes and includes Bacillus stearothermophilus CCAase, Escherichia coli poly(A) polymerase I, human mitochondrial CCAase, and Saccharomyces cerevisiae CCAase (CCA1). CCA-adding enzymes have a single catalytic pocket, which recognizes both ATP and CTP substrates. Included in this subgroup are CC- and A-adding enzymes from various ancient species of bacteria such as Aquifex aeolicus; these enzymes collaborate to add CCA to tRNAs. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are fairly well conserved in this family. Escherichia coli CCAase is related to this group but has not been included in this alignment as this enzyme lacks the N-terminal helix conserved in the remainder of the NT superfamily.


Pssm-ID: 143388 [Multi-domain]  Cd Length: 139  Bit Score: 115.00  E-value: 7.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   1 MKIYLVGGAVRDALLGLPVKDRDWVVVGSTPQEMLDAGYQQVGRDFPVFLHPQTHE--------EYALARTERKSGSGyt 72
Cdd:cd05398   17 YEAYLVGGAVRDLLLGRPPKDIDIATDADGPEFAEALFKKIGGRVVGLGEEFGTATvvingltiDVATLRTETYTDPG-- 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446631144  73 gfTCYAAPDVTLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQN 118
Cdd:cd05398   95 --RRPPVVGFTIEEDLLRRDFTINAMAYDlDDGELIDPFGGLKDLEN 139
pcnB TIGR01942
poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as ...
 4-324 8.58e-28

poly(A) polymerase; This model describes the pcnB family of poly(A) polymerases (also known as plasmid copy number protein). These enzymes sequentially add adenosine nucleotides to the 3' end of RNAs, targeting them for degradation by the cell. This was originally described for anti-sense RNAs, but was later demonstrated for mRNAs as well. Members of this family are as yet limited to the gamma- and beta-proteobacteria, with putative members in the Chlamydiacae and spirochetes. This family has homology to tRNA nucleotidyltransferase (cca).


Pssm-ID: 130997 [Multi-domain]  Cd Length: 410  Bit Score: 113.74  E-value: 8.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144    4 YLVGGAVRDALLGLPVKDRDwVVVGSTPQEM--LDAGYQQVGRDFPVfLH---PQTHEEYALARTERKSGSGYTGFTCYA 78
Cdd:TIGR01942  33 YIVGGAVRDLLLGIEPKDFD-VVTSATPEEVrkLFRNSRIVGRRFRL-VHvsfGRQIIEVATFRSGHKSSVNAEGRILKD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   79 APDVTLEDDLKRRDLTINALAQDDNGE-IIDPYNGLGDLQNRLLRHVSPA---FGEDPLRVLRVARFAARYahlGFRIAD 154
Cdd:TIGR01942 111 NVYGTLEEDAWRRDFTVNALYYDPSREvIIDYVGGMEDLKNRRLRLIGDPrsrYQEDPVRMLRALRFSVKL---EFTIDE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  155 ETLALMREMTHagELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALFGvpaparwhpEIDTGIHTLM 234
Cdd:TIGR01942 188 STARPIRESAP--LLKGIPPARLFEEILKLLFSGRSAALFRMLCGYQLLEPLFPSVAYALR---------ESPKFESAFT 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  235 TLSMAAMLSPQVDVRFATLCHDLGKGLTPPELwPRHHGHGPA-GVK-----------LVEQLCQRLRVPNEIRDLARLVA 302
Cdd:TIGR01942 257 VQALVNDTDFRVKRDKPVTPAFLYAALLWPGL-VFRVADAPDqGVMpypavfdairdFVEEQCAPISIPKRFSIPTREIW 335

                         330       340
                  ....*....|....*....|..
gi 446631144  303 EFHdliHTFPMLNPKTIVKLFD 324
Cdd:TIGR01942 336 QMQ---LRLERRSGMRARKLLG 354
PolyA_pol pfam01743
Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, ...
 3-122 2.65e-20

Poly A polymerase head domain; This family includes nucleic acid independent RNA polymerases, such as Poly(A) polymerase, which adds the poly (A) tail to mRNA EC:2.7.7.19. This family also includes the tRNA nucleotidyltransferase that adds the CCA to the 3' of the tRNA EC:2.7.7.25. This family is part of the nucleotidyltransferase superfamily.


Pssm-ID: 396348 [Multi-domain]  Cd Length: 126  Bit Score: 85.79  E-value: 2.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144    3 IYLVGGAVRDALLGLPVKDRDwVVVGSTPQEMLDAGYQQVGRDFPVFLHPQT------HEEYALARTerKSGSGYTGFtc 76
Cdd:pfam01743   1 LYIVGGAVRDLLLGKTPKDVD-IATDATPEQVATLFRRRRIVHLLSGIEFGTihvifgNQILEVATF--RIEFDESDF-- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446631144   77 yAAPDV-----TLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQNRLLR 122
Cdd:pfam01743  76 -RNPRSeeytgTLEEDAKRRDFTINALAYNpNSGEVIDYFGGIKDLKSGVIR 126
pcnB PRK11623
poly(A) polymerase I; Provisional
 4-214 2.45e-15

poly(A) polymerase I; Provisional


Pssm-ID: 236939 [Multi-domain]  Cd Length: 472  Bit Score: 77.48  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   4 YLVGGAVRDALLGLPVKDRDwVVVGSTPQEM--LDAGYQQVGRDFP---VFLHPQT---------HEEYALARTErkSGS 69
Cdd:PRK11623  70 YLVGGGVRDLLLGKKPKDFD-VTTNATPEQVrkLFRNCRLVGRRFRlahVMFGPEIievatfrghHEGNESDRNT--SQR 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  70 GYTGFTCYAAPDVTLEDDLKRRDLTINALAQD-DNGEIIDPYNGLGDLQN---RLLRHVSPAFGEDPLRVLRVARFAARy 145
Cdd:PRK11623 147 GQNGMLLRDNIFGSIEEDAQRRDFTINSLYYSvADFTVRDYVGGMKDLKEgviRLIGNPETRYREDPVRMLRAVRFAAK- 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631144 146 ahLGFRIADETLALMREMthAGELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALF 214
Cdd:PRK11623 226 --LDMRISPETAEPIPRL--ATLLNDIPPARLFEESLKLLQAGYGYETYKLLCEYHLFQPLFPTITRYF 290
PolyA_pol_RNAbd pfam12627
Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA ...
 149-214 8.42e-14

Probable RNA and SrmB- binding site of polymerase A; This region encompasses much of the RNA and SrmB binding motifs on polymerase A.


Pssm-ID: 463648 [Multi-domain]  Cd Length: 64  Bit Score: 65.58  E-value: 8.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631144  149 GFRIADETLALMREMTHagELEHLTPERVWKETESALTTRNPQVFFQVLRDCGALRVLFPEIDALF 214
Cdd:pfam12627   1 GFTIEPETREAIRKLAP--LLKKISPERIFEELLKLLLSGHPERGLELLRETGLLEYLFPELAAAL 64
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
 228-329 1.88e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 57.63  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144  228 TGIHTLMTLSMAAMLSPQVD------VRFATLCHDLGKGLTPPE--LWPRHHGHGPAGVKLVEQLCQRLRVpneiRDLAR 299
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGeldrelLLLAALLHDIGKGPFGDEkpEFEIFLGHAVVGAEILRELEKRLGL----EDVLK 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 446631144  300 LVAEFHDLIHTFPMLNPKT----IVKLFDSIDAW 329
Cdd:pfam01966  77 LILEHHESWEGAGYPEEISlearIVKLADRLDAL 110
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 227-343 6.73e-07

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.49  E-value: 6.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144 227 DTGIHTLMTLSMAAMLSPQVD--------VRFATLCHDLGKGLTP----PELWPRHHGHGPAGVKLVEQLcQRLRVPNEI 294
Cdd:cd00077    2 HRFEHSLRVAQLARRLAEELGlseedielLRLAALLHDIGKPGTPdaitEEESELEKDHAIVGAEILREL-LLEEVIKLI 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446631144 295 RDLARLVAEFH----------DLIHTFPMLNPKTIVKLFDSIDAWRKPQRVEQLALTSE 343
Cdd:cd00077   81 DELILAVDASHherldglgypDGLKGEEITLEARIVKLADRLDALRRDSREKRRRIAEE 139
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 228-328 1.66e-05

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: 43.82  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631144   228 TGIHTLMTLSMAAMLSPQVD------VRFATLCHDLGKGLTPPELWPR---HHGHGPAGVKLVEQlcqrLRVPNEIRDLA 298
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGlldielLLLAALLHDIGKPGTPDSFLVKtsvLEDHHFIGAEILLE----EEEPRILEEIL 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 446631144   299 RLVAEFHDLIHTF----PMLNPKTIVKLFDSIDA 328
Cdd:smart00471  81 RTAILSHHERPDGlrgePITLEARIVKVADRLDA 114
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
 231-296 1.32e-03

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: 37.32  E-value: 1.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631144  231 HTLMT----LSMAAMLSPQVD-VRFATLCHDLGKGLTPpeLWPRHHGHGPAGVKLVEQLCQRLRVPNEIRD 296
Cdd:TIGR00277   8 HSLEVaklaEALARELGLDVElARRGALLHDIGKPITR--EGVIFESHVVVGAEIARKYGEPLEVIDIIAE 76
 
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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