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Conserved domains on  [gi|50593215|ref|NP_011304|]
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Ncs6p [Saccharomyces cerevisiae S288C]

Protein Classification

tRNA 2-thiolation protein( domain architecture ID 18932641)

tRNA 2-thiolation protein is a nucleotide alpha hydrolase (AANH) superfamily protein that directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation; such as cytoplasmic tRNA 2-thiolation protein 1

CATH:  3.40.50.620
EC:  2.7.7.-
Gene Ontology:  GO:0000049|GO:0034227|GO:0016779
PubMed:  12012333|18391219
SCOP:  3001593

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 50-256 2.19e-115

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


:

Pssm-ID: 467486  Cd Length: 208  Bit Score: 333.40  E-value: 2.19e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  50 FETEIHNTIVANNLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGL 129
Cdd:cd01713   1 IERRVHRTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDYGVELIAVTIDEGIKGYRDDSLEAARKLAEEYGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 130 PLEIFSFKDLYDWTMDEIVSVA-GIRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVARLEKS 208
Cdd:cd01713  81 PLEIVSFEDEFGFTLDELIVGKgGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGDVARLLRT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 50593215 209 TAIITQSSGSPIKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEA 256
Cdd:cd01713 161 GPEPRSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA 208
TIGR00269 super family cl42867
TIGR00269 family protein; [Hypothetical proteins, Conserved]
 220-329 7.76e-17

TIGR00269 family protein; [Hypothetical proteins, Conserved]


The actual alignment was detected with superfamily member TIGR00269:

Pssm-ID: 129370 [Multi-domain]  Cd Length: 104  Bit Score: 75.23  E-value: 7.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   220 IKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEAFRGTAREYMKNLEAVRPSCIIDIIQSGENLALKAKKSNAGKRV 299
Cdd:TIGR00269   1 VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPLLKELSEQEDL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 50593215   300 vkfvdgNRCARCGYLSSNNICKACMLLEGL 329
Cdd:TIGR00269  81 ------RRCERCGEPTSGRICKACKFLEEL 104
 
Name Accession Description Interval E-value
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 50-256 2.19e-115

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 333.40  E-value: 2.19e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  50 FETEIHNTIVANNLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGL 129
Cdd:cd01713   1 IERRVHRTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDYGVELIAVTIDEGIKGYRDDSLEAARKLAEEYGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 130 PLEIFSFKDLYDWTMDEIVSVA-GIRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVARLEKS 208
Cdd:cd01713  81 PLEIVSFEDEFGFTLDELIVGKgGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGDVARLLRT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 50593215 209 TAIITQSSGSPIKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEA 256
Cdd:cd01713 161 GPEPRSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA 208
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 53-287 1.15e-51

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 171.55  E-value: 1.15e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  53 EIHNTIVANNLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYdyGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGLPLE 132
Cdd:COG0037   1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRL--GFELVAVHVDHGLREESDEDAEFVAELCEELGIPLH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 133 IFSFKDLYDWTMDEivsvagiRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGD-VARLekstAI 211
Cdd:COG0037  79 VVRVDVPAIAKKEG-------KSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSgLAGL----AG 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50593215 212 ITQSSGSPIKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEAFRGTAR-EYMKNLEAVRPSCIIDIIQSGENLA 287
Cdd:COG0037 148 MPPSRGGGVRLIRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRhLVLPELEERNPGFKENLARSAENLA 224
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 69-246 2.78e-23

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 95.39  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215    69 KVAVGASGGKDSTVLAHMLKLLNDRYdyGIEIVLLSIDEGIigyRDDSLAT---VKRNQQQYGLPLEIFSFkdlyDWTMD 145
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKI--KIKLIAAHVDHGL---RPESDEEaefVQQFCRKLNIPLEIKKV----DVKAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   146 EIVSVAGI----RNsctycgvFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVAR-LEKSTAIITQSSGSPI 220
Cdd:TIGR02432  72 AKGKKKNLeeaaRE-------ARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRgLSGMKPIRILGSGIQI 144

                         170       180
                  ....*....|....*....|....*.
gi 50593215   221 KRskPFKYSYQKEIVLYAHYMKLDYF 246
Cdd:TIGR02432 145 IR--PLLGISKSEIEEYLKENGLPWF 168
TIGR00269 TIGR00269
TIGR00269 family protein; [Hypothetical proteins, Conserved]
 220-329 7.76e-17

TIGR00269 family protein; [Hypothetical proteins, Conserved]


Pssm-ID: 129370 [Multi-domain]  Cd Length: 104  Bit Score: 75.23  E-value: 7.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   220 IKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEAFRGTAREYMKNLEAVRPSCIIDIIQSGENLALKAKKSNAGKRV 299
Cdd:TIGR00269   1 VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPLLKELSEQEDL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 50593215   300 vkfvdgNRCARCGYLSSNNICKACMLLEGL 329
Cdd:TIGR00269  81 ------RRCERCGEPTSGRICKACKFLEEL 104
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 72-246 7.83e-17

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 77.28  E-value: 7.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215    72 VGASGGKDSTVLAHMLKllNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGLPLEIFSFkdlyDWTMDEIVSV- 150
Cdd:pfam01171   1 VAVSGGPDSMALLYLLA--KLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRV----DVAKKSGENLe 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   151 AGIRNsctycgvFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVARLEKSTAIITQSSGSPIKRskPFKYSY 230
Cdd:pfam01171  75 AAARE-------ARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIR--PLLKVS 145

                         170
                  ....*....|....*.
gi 50593215   231 QKEIVLYAHYMKLDYF 246
Cdd:pfam01171 146 KAEIEAYAKEHKIPWF 161
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 62-200 8.33e-15

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 73.35  E-value: 8.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   62 NLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRnqqQYGLPLEIfSFKDLYD 141
Cdd:PRK10696  24 NMIEEGDRVMVCLSGGKDSYTLLDILLNLQKRAPINFELVAVNLDQKQPGFPEHVLPEYLE---SLGVPYHI-EEQDTYS 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50593215  142 WTMDEivsvagIRNSCTYCGV---FRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRG 200
Cdd:PRK10696 100 IVKEK------IPEGKTTCSLcsrLRRGILYRTARELGATKIALGHHRDDILETLFLNMFYG 155
zn-ribbon_14 pfam16503
Zinc-ribbon; This is a family of zinc-ribbons largely from eukaryotes that lie at the ...
 306-337 1.40e-12

Zinc-ribbon; This is a family of zinc-ribbons largely from eukaryotes that lie at the C-terminus of cytoplasmic tRNA adenylyltransferase 1 proteins. Most of these proteins carry an ATP-binding domain towards the N-terminus.


Pssm-ID: 465147  Cd Length: 32  Bit Score: 61.02  E-value: 1.40e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 50593215   306 NRCARCGYLSSNNICKACMLLEGLEKSRAQVA 337
Cdd:pfam16503   1 GRCERCGYISSQKICKACVLLEGLNKGRPKIA 32
 
Name Accession Description Interval E-value
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 50-256 2.19e-115

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 333.40  E-value: 2.19e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  50 FETEIHNTIVANNLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGL 129
Cdd:cd01713   1 IERRVHRTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDYGVELIAVTIDEGIKGYRDDSLEAARKLAEEYGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 130 PLEIFSFKDLYDWTMDEIVSVA-GIRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVARLEKS 208
Cdd:cd01713  81 PLEIVSFEDEFGFTLDELIVGKgGKKNACTYCGVFRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGDVARLLRT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 50593215 209 TAIITQSSGSPIKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEA 256
Cdd:cd01713 161 GPEPRSEGEGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTECPYAPEA 208
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 53-287 1.15e-51

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 171.55  E-value: 1.15e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  53 EIHNTIVANNLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYdyGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGLPLE 132
Cdd:COG0037   1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRL--GFELVAVHVDHGLREESDEDAEFVAELCEELGIPLH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 133 IFSFKDLYDWTMDEivsvagiRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGD-VARLekstAI 211
Cdd:COG0037  79 VVRVDVPAIAKKEG-------KSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSgLAGL----AG 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50593215 212 ITQSSGSPIKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEAFRGTAR-EYMKNLEAVRPSCIIDIIQSGENLA 287
Cdd:COG0037 148 MPPSRGGGVRLIRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRhLVLPELEERNPGFKENLARSAENLA 224
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 61-256 1.79e-43

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 149.01  E-value: 1.79e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  61 NNLFQRGEKVAVGASGGKDSTVLAHMLKllndryDYGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGLPLEIFSFKDLY 140
Cdd:cd01993   2 YKMFEKDDKILVAVSGGKDSLALLAVLK------KLGYNVEALYINLGIGEYSEKSEEVVKKLAEKLNLPLHVVDLKEEY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 141 DWTMDEIvSVAGIRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVARLEKSTAIITQSSGSPI 220
Cdd:cd01993  76 GLGIPEL-AKKSRRPPCSVCGLVKRYIMNKFAVENGFDVVATGHNLDDEAAFLLGNILNWNEEYLAKQGPFLLPEHGGLV 154

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 50593215 221 KRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEA 256
Cdd:cd01993 155 TRVKPLYEITEEEIALYALLNGIPYLEEECPYAEGA 190
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 62-253 3.23e-30

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 113.91  E-value: 3.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  62 NLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYDYGIEIVLLSIDEGIIGYRDDSlATVKRNQQQYGLPLEIFSFKDLyd 141
Cdd:cd24138   3 KMIEPGDRILVGLSGGKDSLTLLHLLEELKRRAPIKFELVAVTVDPGYPGYRPPR-EELAEILEELGEILEDEESEII-- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 142 wtmdEIVSVAGIRNSCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGdvARLEKSTAIITQSSGSPIK 221
Cdd:cd24138  80 ----IIEKEREEKSPCSLCSRLRRGILYSLAKELGCNKLALGHHLDDAVETLLMNLLYG--GRLKTMPPKVTMDRGGLTV 153

                       170       180       190
                ....*....|....*....|....*....|..
gi 50593215 222 rSKPFKYSYQKEIVLYAHYMKLDYFSTECTYA 253
Cdd:cd24138 154 -IRPLIYVREKDIRAFAEENGLPKIECPCPYC 184
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 69-246 2.78e-23

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 95.39  E-value: 2.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215    69 KVAVGASGGKDSTVLAHMLKLLNDRYdyGIEIVLLSIDEGIigyRDDSLAT---VKRNQQQYGLPLEIFSFkdlyDWTMD 145
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKI--KIKLIAAHVDHGL---RPESDEEaefVQQFCRKLNIPLEIKKV----DVKAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   146 EIVSVAGI----RNsctycgvFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVAR-LEKSTAIITQSSGSPI 220
Cdd:TIGR02432  72 AKGKKKNLeeaaRE-------ARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRgLSGMKPIRILGSGIQI 144

                         170       180
                  ....*....|....*....|....*.
gi 50593215   221 KRskPFKYSYQKEIVLYAHYMKLDYF 246
Cdd:TIGR02432 145 IR--PLLGISKSEIEEYLKENGLPWF 168
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 69-246 6.04e-21

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 88.81  E-value: 6.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  69 KVAVGASGGKDSTVLAHMLKLLndRYDYGIEIVLLSIDEGIigyRDDSLA---TVKRNQQQYGLPLEIFSFKDLYDWTMD 145
Cdd:cd01992   1 KILVAVSGGPDSMALLHLLKEL--RPKLGLKLVAVHVDHGL---REESAEeaqFVAKLCKKLGIPLHILTVTEAPKSGGN 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215 146 eIVSVAgiRNsctycgvFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGdvARLEKSTAIITQSSGSPIKRSKP 225
Cdd:cd01992  76 -LEAAA--RE-------ARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRG--SGLSGLAGMAARSKAGGIRLIRP 143

                       170       180
                ....*....|....*....|.
gi 50593215 226 FKYSYQKEIVLYAHYMKLDYF 246
Cdd:cd01992 144 LLGISKAELLAYCRENGLPWV 164
TIGR00269 TIGR00269
TIGR00269 family protein; [Hypothetical proteins, Conserved]
 220-329 7.76e-17

TIGR00269 family protein; [Hypothetical proteins, Conserved]


Pssm-ID: 129370 [Multi-domain]  Cd Length: 104  Bit Score: 75.23  E-value: 7.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   220 IKRSKPFKYSYQKEIVLYAHYMKLDYFSTECTYAPEAFRGTAREYMKNLEAVRPSCIIDIIQSGENLALKAKKSNAGKRV 299
Cdd:TIGR00269   1 VPRIKPLRYIPEKEVVLYAFLNELKVHLDECPYSSLSVRARIRDFLYDLENKKPGVKFSVLRGFEKLIPLLKELSEQEDL 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 50593215   300 vkfvdgNRCARCGYLSSNNICKACMLLEGL 329
Cdd:TIGR00269  81 ------RRCERCGEPTSGRICKACKFLEEL 104
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 72-246 7.83e-17

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 77.28  E-value: 7.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215    72 VGASGGKDSTVLAHMLKllNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRNQQQYGLPLEIFSFkdlyDWTMDEIVSV- 150
Cdd:pfam01171   1 VAVSGGPDSMALLYLLA--KLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRV----DVAKKSGENLe 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   151 AGIRNsctycgvFRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRGDVARLEKSTAIITQSSGSPIKRskPFKYSY 230
Cdd:pfam01171  75 AAARE-------ARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIR--PLLKVS 145

                         170
                  ....*....|....*.
gi 50593215   231 QKEIVLYAHYMKLDYF 246
Cdd:pfam01171 146 KAEIEAYAKEHKIPWF 161
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 62-200 8.33e-15

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 73.35  E-value: 8.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215   62 NLFQRGEKVAVGASGGKDSTVLAHMLKLLNDRYDYGIEIVLLSIDEGIIGYRDDSLATVKRnqqQYGLPLEIfSFKDLYD 141
Cdd:PRK10696  24 NMIEEGDRVMVCLSGGKDSYTLLDILLNLQKRAPINFELVAVNLDQKQPGFPEHVLPEYLE---SLGVPYHI-EEQDTYS 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50593215  142 WTMDEivsvagIRNSCTYCGV---FRRQSLDRGAAKLGISHVVTGHNADDMAETVLMNILRG 200
Cdd:PRK10696 100 IVKEK------IPEGKTTCSLcsrLRRGILYRTARELGATKIALGHHRDDILETLFLNMFYG 155
zn-ribbon_14 pfam16503
Zinc-ribbon; This is a family of zinc-ribbons largely from eukaryotes that lie at the ...
 306-337 1.40e-12

Zinc-ribbon; This is a family of zinc-ribbons largely from eukaryotes that lie at the C-terminus of cytoplasmic tRNA adenylyltransferase 1 proteins. Most of these proteins carry an ATP-binding domain towards the N-terminus.


Pssm-ID: 465147  Cd Length: 32  Bit Score: 61.02  E-value: 1.40e-12
                          10        20        30
                  ....*....|....*....|....*....|..
gi 50593215   306 NRCARCGYLSSNNICKACMLLEGLEKSRAQVA 337
Cdd:pfam16503   1 GRCERCGYISSQKICKACVLLEGLNKGRPKIA 32
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 68-186 6.12e-06

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 46.48  E-value: 6.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215    68 EKVAVGASGGKDSTVLAHMLKllndryDYGIEIV---------LLSIDEGIIGYRDDSLATVKRNQQQYGLPLEIFSFKD 138
Cdd:pfam03054   1 MKVVVAMSGGVDSSVAAYLLK------EQGHNVIgvfmknwdeEQSLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEK 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50593215   139 LYdWtmDEIVS--VAGIR-----NSCTYC------GVFrrqsLDRGAAKLGISHVVTGHNA 186
Cdd:pfam03054  75 EY-W--EDVFEpfLDEYKngrtpNPDVLCnkeikfGAL----LDYALENLGADYVATGHYA 128
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 67-183 1.37e-05

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 45.61  E-value: 1.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  67 GEKVAVGASGGKDSTVLAHMLKLLNdrydygIEIVLLSIDEGI-----IGYRDdslATVKRnqqqYGLPLEIFSFKDLYD 141
Cdd:COG0175  33 GGRVVVSSSGGKDSTVLLHLAAKFK------PPIPVLFLDTGYefpetYEFRD---RLAER----LGLDLIVVRPEDAFA 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 50593215 142 WTMDE--IVSVAGIRNSCTYcgvfRRQS--LDRGAAKLGISHVVTG 183
Cdd:COG0175 100 EQLAEfgPPLFYRDPRWCCK----IRKVepLKRALAGYDFDAWITG 141
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 69-184 2.46e-05

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 45.57  E-value: 2.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  69 KVAVGASGGKDSTVLAHMLKllNDRYDY-GIEIVLLSIDEGIIGY--RDDSLATVKRNQQQYGLPLEIFSFKDLYdWtmD 145
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLK--EQGYDViGVFMKNWDDEDNEKGGccSEEDIEDARRVADQLGIPLYVVDFSEEY-W--E 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 50593215 146 EIVS--VAGIR-----NSCTYC------GVFRRQsldrgAAKLGISHVVTGH 184
Cdd:cd01998  76 RVFDpfLEEYKagrtpNPDVLCnreikfGALLDA-----AKKLGADYIATGH 122
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 69-189 4.35e-05

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 44.17  E-value: 4.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  69 KVAVGASGGKDSTVLAHMLK-LLNDrydygiEIVLLSIDEGIIGyrDDSLATVKRNQQQYGLPLEIFsfkdlydwTMDEI 147
Cdd:cd01990   1 KVVVAFSGGVDSSLLAKLAKeVLGD------NVVAVTADSPLVP--REELEEAKRIAEEIGIRHEII--------KTDEL 64

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 50593215 148 VSVAGIRN---SCTYCGVFRRQSLDRGAAKLGISHVVTGHNADDM 189
Cdd:cd01990  65 DDEEYVANdpdRCYHCKKALYSTLKEIAKERGYDVVLDGTNADDL 109
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 70-109 4.83e-04

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 38.20  E-value: 4.83e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 50593215  70 VAVGASGGKDSTVLAHMLKLLndRYDYGIEIVLlsIDEGI 109
Cdd:cd01986   1 VVVGYSGGKDSSVALHLASRL--GRKAEVAVVH--IDHGI 36
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
 71-186 6.32e-04

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 40.05  E-value: 6.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  71 AVGASGGKDSTVLAHMLKllndrYDYGIEIVLLSIDEGIigYRDDSLATVKRNQQQYGLPLEIFSFkdlyDW-TMDEIVS 149
Cdd:cd01996   9 IIGVSGGKDSTYAAHKAK-----EKYGLRPLLVTVDAGW--NSPEAVKNIEKLVRALGVDLITFVP----NWkEMRDLQR 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 50593215 150 VAGIR--NSCTYC--GVFrrQSLDRGAAKLGISHVVTGHNA 186
Cdd:cd01996  78 LAFKSngDQDWPQdhGIF--TSLYKMAVKFGIPLIIWGENP 116
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 69-187 1.86e-03

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 39.18  E-value: 1.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  69 KVAVGASGGKDSTVLAHMLKllndRYDYGIEIVLLSIdeGIIGYRDDSLATVKRNQQQYGLPLEIFSF--KDLYDW---- 142
Cdd:cd01991   4 PVGVLLSGGLDSSLIAALAA----RLLPETPIDLFTV--GFEGSPTPDRAAARRVAEELGTEHHEVEVtiEELLDAlpdv 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 50593215 143 -TMDEIVSVAGIRNSCTYCGVFrrqsldRGAAKLGISHVVTGHNAD 187
Cdd:cd01991  78 iLIYPTDTPMDLSIAIPLYFAS------RLAGKLGAKVVLSGEGAD 117
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 68-188 5.59e-03

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 37.59  E-value: 5.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50593215  68 EKVAVGASGGKDSTVLAHMLKllnDRYDygiEIVLLSIDegiIGYR--DDSLATVKRNQQQYGLPLEI---FSFKDLY-D 141
Cdd:cd01995   1 MKAVVLLSGGLDSTTLLYWAL---KEGY---EVHALTFD---YGQRhaKEELEAAKLIAKLLGIEHKVidlSFLGELGgS 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50593215 142 WTMDEIVSVAGI--------------RNsctycGVFrrQSLDRG-AAKLGISHVVTGHNADD 188
Cdd:cd01995  72 SLTDEGEEVPDGeydeesipstwvpnRN-----LIF--LSIAAAyAESLGASAIVIGVNAED 126
 
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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