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Conserved domains on  [gi|124394810|emb|CAK60329|]
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unnamed protein product (macronuclear) [Paramecium tetraurelia]

Protein Classification

YbaK/prolyl-tRNA synthetase associated domain-containing protein( domain architecture ID 10137858)

uncharaterized YbaK/prolyl-tRNA synthetase associated domain-containing protein may function as an aminoacyl-tRNA deacylase involved in tRNA editing; similar to Escherichia coli YeaK

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 8-159 1.29e-84

YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.


:

Pssm-ID: 239828 [Multi-domain]  Cd Length: 153  Bit Score: 244.95  E-value: 1.29e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   8 FEAIQQLLNTNNIQFKLLIHEPTKTSEESAKVRGVSLDSGAKAMLLQNKKT-QLFILCVMSASKKLSWKLIRKLLDCKQL 86
Cdd:cd04336    1 FERLQELLNTNGARFRVLDHPPEGTSEEVAAIRGTELGQGAKALLCKVKDGsRRFVLAVLPADKKLDLKAVAAAVGGKKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124394810  87 DLANEQQVYEVTKCVTGAVPPFGSIFKVQTYLDPSLITQGDQINFNCGLRTHSVAMSIQDYLKIENPIQLQFC 159
Cdd:cd04336   81 DLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLDRGDEIAFNAGRLDASVVLDTADYLRIARPLVLQFT 153
 
Name Accession Description Interval E-value
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 8-159 1.29e-84

YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.


Pssm-ID: 239828 [Multi-domain]  Cd Length: 153  Bit Score: 244.95  E-value: 1.29e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   8 FEAIQQLLNTNNIQFKLLIHEPTKTSEESAKVRGVSLDSGAKAMLLQNKKT-QLFILCVMSASKKLSWKLIRKLLDCKQL 86
Cdd:cd04336    1 FERLQELLNTNGARFRVLDHPPEGTSEEVAAIRGTELGQGAKALLCKVKDGsRRFVLAVLPADKKLDLKAVAAAVGGKKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124394810  87 DLANEQQVYEVTKCVTGAVPPFGSIFKVQTYLDPSLITQGDQINFNCGLRTHSVAMSIQDYLKIENPIQLQFC 159
Cdd:cd04336   81 DLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLDRGDEIAFNAGRLDASVVLDTADYLRIARPLVLQFT 153
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 9-160 7.44e-36

Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442018 [Multi-domain]  Cd Length: 152  Bit Score: 121.35  E-value: 7.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   9 EAIQQLLNTNNIQFKLLIHE-PTKTSEESAKVRGVSLDSGAKAMLLQNKKTqlFILCVMSASKKLSWKLIRKLLDCKQLD 87
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPePAATAEEAAEALGVPPEQIAKTLVFRGDGG--PVLAVVPGDRRLDLKKLAAALGAKKVE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124394810  88 LANEQQVYEVTKCVTGAVPPFGSIFKVQTYLDPSLITQgDQINFNCGLRTHSVAMSIQDYLKIENPIQLQFCE 160
Cdd:COG2606   79 MADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEF-DEVYVSAGDRGLLVELAPADLARLTGATVADIAR 150
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 27-150 4.44e-33

Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.


Pssm-ID: 427693 [Multi-domain]  Cd Length: 123  Bit Score: 113.47  E-value: 4.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   27 HEPTKTSEESAKVRGVSLDSGAKAMLLQNKKTQlFILCVMSASKKLSWKLIRKLLDCKQLDLANEQQVYEVTKCVTGAVP 106
Cdd:pfam04073   1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK-YVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 124394810  107 PFGSI-FKVQTYLDPSLITQGDqINFNCGLRTHSVAMSIQDYLKI 150
Cdd:pfam04073  80 PFGLKaKGVPVLVDESLKDLPD-VVVGAGENGATLRLSNADLRKL 123
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 25-134 3.82e-03

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 36.60  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810  25 LIHEP-TKTSEESAKVRGVSLDSGAKAMLLQNKKtQLFILCV-------MsasKKLSwklirKLLDCKQLDLANEQQVYE 96
Cdd:PRK09194 252 KVDTPnAKTIEELAEFLNVPAEKTVKTLLVKADG-ELVAVLVrgdhelnE---VKLE-----NLLGAAPLELATEEEIRA 322

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124394810  97 VTKCVTGAVPPFGSIFKVQTYLDPSLItqgDQINFNCG 134
Cdd:PRK09194 323 ALGAVPGFLGPVGLPKDVPIIADRSVA---DMSNFVVG 357
 
Name Accession Description Interval E-value
YeaK cd04336
YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. ...
 8-159 1.29e-84

YeaK is an uncharacterized Echerichia coli protein with a YbaK-like domain of unknown function. The YbaK-like domain family includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, and ProX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express a single-domain INS homolog such as YbaK, ProX, or PrdX which supplies the function of INS in trans.


Pssm-ID: 239828 [Multi-domain]  Cd Length: 153  Bit Score: 244.95  E-value: 1.29e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   8 FEAIQQLLNTNNIQFKLLIHEPTKTSEESAKVRGVSLDSGAKAMLLQNKKT-QLFILCVMSASKKLSWKLIRKLLDCKQL 86
Cdd:cd04336    1 FERLQELLNTNGARFRVLDHPPEGTSEEVAAIRGTELGQGAKALLCKVKDGsRRFVLAVLPADKKLDLKAVAAAVGGKKA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124394810  87 DLANEQQVYEVTKCVTGAVPPFGSIFKVQTYLDPSLITQGDQINFNCGLRTHSVAMSIQDYLKIENPIQLQFC 159
Cdd:cd04336   81 DLASPEEAEELTGCVIGAVPPFSFDPKLKLIADPSLLDRGDEIAFNAGRLDASVVLDTADYLRIARPLVLQFT 153
EbsC COG2606
Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal ...
 9-160 7.44e-36

Cys-tRNA(Pro) deacylase, prolyl-tRNA editing enzyme YbaK/EbsC [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442018 [Multi-domain]  Cd Length: 152  Bit Score: 121.35  E-value: 7.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   9 EAIQQLLNTNNIQFKLLIHE-PTKTSEESAKVRGVSLDSGAKAMLLQNKKTqlFILCVMSASKKLSWKLIRKLLDCKQLD 87
Cdd:COG2606    1 TPVRRALDAAGIPYEVVEHPePAATAEEAAEALGVPPEQIAKTLVFRGDGG--PVLAVVPGDRRLDLKKLAAALGAKKVE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124394810  88 LANEQQVYEVTKCVTGAVPPFGSIFKVQTYLDPSLITQgDQINFNCGLRTHSVAMSIQDYLKIENPIQLQFCE 160
Cdd:COG2606   79 MADPEEVERLTGYEVGGVSPFGLKKGLPVYVDESLLEF-DEVYVSAGDRGLLVELAPADLARLTGATVADIAR 150
YbaK_like cd04332
YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of ...
 21-155 6.50e-34

YbaK-like. The YbaK family of deacylase domains includes the INS amino acid-editing domain of the bacterial class II prolyl tRNA synthetase (ProRS), and it's trans-acting homologs, YbaK, ProX, and PrdX. The primary function of INS is to hydrolyze mischarged cysteinyl-tRNA(Pro)'s, thus helping ensure the fidelity of translation. Organisms whose ProRS lacks the INS domain express an INS homolog in trans (e.g. YbaK, ProX, or PrdX).


Pssm-ID: 239824 [Multi-domain]  Cd Length: 136  Bit Score: 116.10  E-value: 6.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810  21 QFKLLIHEP-TKTSEESAKVRGVSLDSGAKAMLLQNKKTQlFILCVMSASKKLSWKLIRKLLDCKQLDLANEQQVYEVTK 99
Cdd:cd04332    1 EYLEYEHTPgAKTIEEAAEALGVPPGQIAKTLVLKDDKGG-LVLVVVPGDHELDLKKLAKALGAKKLRLASEEELEELTG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 124394810 100 CVTGAVPPFGSIFKVQTYLDPSLiTQGDQINFNCGLRTHSVAMSIQDYLKIENPIQ 155
Cdd:cd04332   80 CEPGGVGPFGLKKGVPVVVDESL-LELEDVYVGAGERGADLHLSPADLLRLLGEAE 134
tRNA_edit pfam04073
Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with ...
 27-150 4.44e-33

Aminoacyl-tRNA editing domain; This domain is found either on its own or in association with the tRNA synthetase class II core domain (pfam00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro). The structure of this domain shows a novel fold.


Pssm-ID: 427693 [Multi-domain]  Cd Length: 123  Bit Score: 113.47  E-value: 4.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   27 HEPTKTSEESAKVRGVSLDSGAKAMLLQNKKTQlFILCVMSASKKLSWKLIRKLLDCKQLDLANEQQVYEVTKCVTGAVP 106
Cdd:pfam04073   1 HPPAATIEELAAALGVPPGRIAKTLVLKDKKGK-YVLVVVPGDREVDLKKLAKLLGVKRLRLASEEELLELTGVEPGGVT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 124394810  107 PFGSI-FKVQTYLDPSLITQGDqINFNCGLRTHSVAMSIQDYLKI 150
Cdd:pfam04073  80 PFGLKaKGVPVLVDESLKDLPD-VVVGAGENGATLRLSNADLRKL 123
ProX COG3760
Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function ...
 7-150 7.86e-18

Predicted aminoacyl-tRNA deacylase, YbaK-like aminoacyl-tRNA editing domain [General function prediction only];


Pssm-ID: 442974  Cd Length: 162  Bit Score: 75.55  E-value: 7.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   7 TFEAIQQLLNTNNIQFKLLIHEPTKTSEESAKVRGVSLDSGAKAMLLQNKKTQLFILCVMSASKKLSWKLIRKLLDCKQL 86
Cdd:COG3760    3 TEQELYALLDELGIPYETVEHPPVFTVEEAEALRGDLPGAHTKNLFLRDKKGTRFYLVVVPEDKRVDLKALSKQLGSGRL 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124394810  87 DLANEQQVYEVTKCVTGAVPPFGSIF----KVQTYLDPSLItQGDQINFNCGLRTHSVAMSIQDYLKI 150
Cdd:COG3760   83 SFASPERLEEYLGVTPGSVTPFGLINdtenRVTVVLDADLL-EAELINCHPLVNTATLKISTDDLLRF 149
PrdX_deacylase cd04335
This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and ...
 8-150 1.59e-14

This CD includes bacterial (Agrobacterium tumefaciens and Caulobacter crescentus ProX, and Clostridium sticklandii PrdX) and eukaryotic (Plasmodium falciparum N-terminal ProRS editing domain) sequences. The C. sticklandii PrdX protein, a homolog of the YbaK and ProX proteins, and the prolyl-tRNA synthetase-editing domain (ProRS-INS), specifically hydrolyzes Ala-tRNA(Pro). In this CD, many of the eukaryotic editing domains are N-terminal and cis-acting, expressed from a multidomain ProRS, however, similar to the bacterial PrdX, the mammalian, amphibian, and echinoderm PrdX-like proteins are trans-acting, single-domain proteins.


Pssm-ID: 239827  Cd Length: 156  Bit Score: 66.77  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810   8 FEAIQQLLNTNNIQFKLLIHEPTKTSEESAKVRGVSLDSGAKAMLLQNKKTQLFILcVMSASKKLSWKLIRKLLDCKQLD 87
Cdd:cd04335    1 EDELLALLDELGIAYETVEHPPVFTVEEADEVLGELPGAHTKNLFLKDKKGRLYLV-TALHDKKVDLKALSKQLGASRLS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124394810  88 LANEQQVYEVTKCVTGAVPPFGSIF----KVQTYLDPSLiTQGDQINFNCGLRTHSVAMSIQDYLKI 150
Cdd:cd04335   80 FASEERLEEKLGVTPGSVTPFALINdkenDVQVVLDKDL-LEEERVGFHPLTNTATVGISTEDLLKF 145
ProX_deacylase cd04333
This CD, composed mainly of bacterial single-domain proteins, includes the Thermus ...
 28-122 7.20e-12

This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain.


Pssm-ID: 239825 [Multi-domain]  Cd Length: 148  Bit Score: 59.44  E-value: 7.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810  28 EPTKTSEESAKVRGVSLDSGAKAMLLQNKKTqlFILCVMSASKKLSWKLIRKLLDCKqLDLANEQQVYEVTKCVTGAVPP 107
Cdd:cd04333   22 ESTRTAALAAEALGCEPGQIAKSLVFRVDDE--PVLVVTSGDARVDNKKFKALFGEK-LKMADAEEVRELTGFAIGGVCP 98

                         90
                 ....*....|....*
gi 124394810 108 FGSIFKVQTYLDPSL 122
Cdd:cd04333   99 FGHPEPLPVYLDESL 113
YbaK_deacylase cd00002
This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia ...
 13-150 6.17e-10

This CD includes cysteinyl-tRNA(Pro) deacylases from Haemophilus influenzae and Escherichia coli and other related bacterial proteins. These trans-acting, single-domain proteins are homologs of ProX and also the cis-acting prolyl-tRNA synthetase (ProRS) inserted (INS) editing domain. The bacterial amino acid trans-editing enzyme YbaK is a deacylase that hydrolyzes cysteinyl-tRNA(Pro)'s mischarged by prolyl-tRNA synthetase. YbaK also hydrolyzes glycyl-tRNA's, alanyl-tRNA's, seryl-tRNA's, and prolyl-tRNA's. YbaK is homologous to the INS domain of prolyl-tRNA synthetase (ProRS) as well as the trans-editing enzyme ProX of Aeropyrum pernix which hydrolyzes alanyl-tRNA's and glycyl-tRNA's.


Pssm-ID: 237976 [Multi-domain]  Cd Length: 152  Bit Score: 54.38  E-value: 6.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810  13 QLLNTNNIQFKLLIHEPTKTS---EESAKVRGVSLDSGAKAMLLQNKKTQLFIlCVMSASKKLSWKLIRKLLDCKQLDLA 89
Cdd:cd00002    6 RLLDKAKIPYELHEYEHDEDAsdgLEAAEKLGLDPEQVFKTLVVEGDKKGLVV-AVVPVDEELDLKKLAKALGAKKVEMA 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124394810  90 NEQQVYEVTKCVTGAVPPFGSIFKVQTYLDPSlITQGDQINFNCGLRTHSVAMSIQDYLKI 150
Cdd:cd00002   85 PPKDAERLTGYIRGGISPLGQKKRLPTVIDES-ALDLDTIYVSAGKRGLQIELAPQDLAKL 144
ProRS-INS cd04334
INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA ...
 25-134 4.22e-05

INS is an amino acid-editing domain inserted (INS) into the bacterial class II prolyl-tRNA synthetase (ProRS) however, this CD is not exclusively bacterial. It is also found at the N-terminus of the eukaryotic/archaea-like ProRS's of yeasts and single-celled parasites. ProRS catalyzes the attachment of proline to tRNA(Pro); proline is first activated by ATP, and then transferred to the acceptor end of tRNA(Pro). ProRS can inadvertently process noncognate amino acids such as alanine and cysteine, and to avoid such errors, in post-transfer editing, the INS domain deacylates mischarged Ala-tRNA(Pro), thus ensuring the fidelity of translation. Misacylated Cys-tRNA(Pro) is not edited by ProRS. In addition to the INS editing domain, the prokaryote-like ProRS protein contains catalytic and anticodon-binding domains which form a dimeric interface.


Pssm-ID: 239826 [Multi-domain]  Cd Length: 160  Bit Score: 41.34  E-value: 4.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810  25 LIHEP-TKTSEESAKVRGVSLDSGAKAMLLQNKKTQLFILCVMSASKKLSWKLIRKLLDCKQLDLANEQQVYEVTKCVTG 103
Cdd:cd04334   29 KVATPgQKTIEELAEFLGVPPSQTVKTLLVKADGEEELVAVLLRGDHELNEVKLENLLGAAPLELASEEEIEAATGAPPG 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 124394810 104 AVPPFGsIFKVQTYLDPSLItqgDQINFNCG 134
Cdd:cd04334  109 FIGPVG-LKKIPIIADRSVA---DLKNFVCG 135
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 25-134 3.82e-03

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 36.60  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124394810  25 LIHEP-TKTSEESAKVRGVSLDSGAKAMLLQNKKtQLFILCV-------MsasKKLSwklirKLLDCKQLDLANEQQVYE 96
Cdd:PRK09194 252 KVDTPnAKTIEELAEFLNVPAEKTVKTLLVKADG-ELVAVLVrgdhelnE---VKLE-----NLLGAAPLELATEEEIRA 322

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 124394810  97 VTKCVTGAVPPFGSIFKVQTYLDPSLItqgDQINFNCG 134
Cdd:PRK09194 323 ALGAVPGFLGPVGLPKDVPIIADRSVA---DMSNFVVG 357
 
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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