NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|442618365|ref|NP_001262445|]
View 

arginine methyltransferase 4, isoform B [Drosophila melanogaster]

Protein Classification

histone-arginine methyltransferase( domain architecture ID 10351171)

histone-arginine methyltransferase is a type I arginine methyltransferase belonging to the class I SAM-dependent methyltransferase superfamily, similar to Drosophila histone-arginine methyltransferase CARMER that methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins, using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110|2.30.29.30
EC:  2.1.1.319
Gene Ontology:  GO:1904047|GO:0035097|GO:0042054|GO:0018216
PubMed:  12504684|12826405|22728242|15493994
SCOP:  3000118|4002395

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
154-341 4.61e-43

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.88  E-value: 4.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 154 QQNMMQDYVRTSTYQRAIlgNAVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVQHKISV 232
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 233 IPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKW-LKPQGKMYPTHGDLHIAPfsdesLYSEQYnkANFWYQS 311
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRlLKPGGRIIPERITNAAQP-----VESPVD--AEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 442618365 312 AFHGVDLTTLhkeGMKEYFRQPIVDTFDIR 341
Cdd:COG4076  163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 24-134 6.56e-04

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13330:

Pssm-ID: 473070  Cd Length: 107  Bit Score: 39.31  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  24 CQFCGVVISSIADEQKLEFTNKYKGSCTLLCSYDSQgvvlRVVSDDDRSHVLKeYMIAADTDAAQMGRRSYAVSLDADNL 103
Cdd:cd13330    1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSV----LVLSTNEDVCVFK-CSVNRETECSRVGKQSFLITLGCNSV 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442618365 104 VLRFASEQDQQLFRKVVENVKHL-RPKSVFSQ 134
Cdd:cd13330   76 LLQFATPSEFSSFYNALKNCRGQtNEKSVFSQ 107
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
154-341 4.61e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.88  E-value: 4.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 154 QQNMMQDYVRTSTYQRAIlgNAVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVQHKISV 232
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 233 IPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKW-LKPQGKMYPTHGDLHIAPfsdesLYSEQYnkANFWYQS 311
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRlLKPGGRIIPERITNAAQP-----VESPVD--AEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 442618365 312 AFHGVDLTTLhkeGMKEYFRQPIVDTFDIR 341
Cdd:COG4076  163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 183-281 5.91e-13

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 65.14  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQlVESNNVQHKISVIPGKIEEIEL--PEKVDVIISEPMgYMLY 259
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISpVALELARK-AAAALLADNVEVLKGDAEELPPeaDESFDVIISDPP-LHHL 79

                         90       100
                 ....*....|....*....|..
gi 442618365 260 NERMLETYLHARKWLKPQGKMY 281
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 183-278 2.16e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 62.97  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  183 VLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVqhKISVIPGKIEEIELP-EKVDVIISePMGYMLYN 260
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 442618365  261 ERMLETYLH-ARKWLKPQG 278
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
175-250 1.87e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.16  E-value: 1.87e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442618365 175 AVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMA-QYAQQLVESNNVQHKISVIPGKieeielpEKVDVII 250
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAvEAARENAELNGVELNVYLPQGD-------LKADVIV 184
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 182-227 5.31e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 40.37  E-value: 5.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442618365  182 IVLDVGAGSGILSFFAVQAGA-AKVYAIEAS-NMAQYAQQLVESNNVQ 227
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpDAYEILEENVKLNNLP 48
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 24-134 6.56e-04

Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241484  Cd Length: 107  Bit Score: 39.31  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  24 CQFCGVVISSIADEQKLEFTNKYKGSCTLLCSYDSQgvvlRVVSDDDRSHVLKeYMIAADTDAAQMGRRSYAVSLDADNL 103
Cdd:cd13330    1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSV----LVLSTNEDVCVFK-CSVNRETECSRVGKQSFLITLGCNSV 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442618365 104 VLRFASEQDQQLFRKVVENVKHL-RPKSVFSQ 134
Cdd:cd13330   76 LLQFATPSEFSSFYNALKNCRGQtNEKSVFSQ 107
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
154-341 4.61e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.88  E-value: 4.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 154 QQNMMQDYVRTSTYQRAIlgNAVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVQHKISV 232
Cdd:COG4076   12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 233 IPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKW-LKPQGKMYPTHGDLHIAPfsdesLYSEQYnkANFWYQS 311
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRlLKPGGRIIPERITNAAQP-----VESPVD--AEGFEDW 162

                        170       180       190
                 ....*....|....*....|....*....|
gi 442618365 312 AFHGVDLTTLhkeGMKEYFRQPIVDTFDIR 341
Cdd:COG4076  163 QFDGFDFRLF---GFLLYAEPLLHLTRLVR 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 183-281 5.91e-13

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 65.14  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQlVESNNVQHKISVIPGKIEEIEL--PEKVDVIISEPMgYMLY 259
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISpVALELARK-AAAALLADNVEVLKGDAEELPPeaDESFDVIISDPP-LHHL 79

                         90       100
                 ....*....|....*....|..
gi 442618365 260 NERMLETYLHARKWLKPQGKMY 281
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 183-278 2.16e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 62.97  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  183 VLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVqhKISVIPGKIEEIELP-EKVDVIISePMGYMLYN 260
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 442618365  261 ERMLETYLH-ARKWLKPQG 278
Cdd:pfam13649  78 DPDLEAALReIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 183-281 6.16e-12

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 63.80  E-value: 6.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVQHKISVIPGKIEEIELPEKVDVIISEPMgYMLYNE 261
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSIGM-FEHVGP 133

                         90       100
                 ....*....|....*....|.
gi 442618365 262 RMLETYL-HARKWLKPQGKMY 281
Cdd:COG2230  134 ENYPAYFaKVARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 183-281 6.88e-12

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 62.73  E-value: 6.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILSFFAVQAGaAKVYAIEAS-NMAQYAQQLVESNNVQhkisVIPGKIEEIELP-EKVDVIISepMGYMLYN 260
Cdd:COG2227   28 VLDVGCGTGRLALALARRG-ADVTGVDISpEALEIARERAAELNVD----FVQGDLEDLPLEdGSFDLVIC--SEVLEHL 100

                         90       100
                 ....*....|....*....|.
gi 442618365 261 ERMLETYLHARKWLKPQGKMY 281
Cdd:COG2227  101 PDPAALLRELARLLKPGGLLL 121
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 171-281 6.30e-11

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 62.47  E-value: 6.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 171 ILGNAVDFQD-KIVLDVGAGSGILSFFAVQ-AGAAKVYAIEA-SNMAQYAQQLVESNNVQHKISVIPGKIEEIE---LPE 244
Cdd:COG4123   28 LLAAFAPVKKgGRVLDLGTGTGVIALMLAQrSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLKEFAaelPPG 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442618365 245 KVDVIISEPmGYMLYNE------------RM-----LETYLH-ARKWLKPQGKMY 281
Cdd:COG4123  108 SFDLVVSNP-PYFKAGSgrkspdearaiaRHedaltLEDLIRaAARLLKPGGRFA 161
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
175-250 1.30e-10

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 62.11  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 175 AVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAI-------EAsnmaqyAQQLVESNNVQHKISVIPGKIEEielPEKVD 247
Cdd:COG2264  144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVdidpvavEA------ARENAELNGVEDRIEVVLGDLLE---DGPYD 214


                 ...
gi 442618365 248 VII 250
Cdd:COG2264  215 LVV 217
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
177-253 1.71e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 57.61  E-value: 1.71e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442618365 177 DFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVqhKISVIPGKIEEIELPEKVDVIISEP 253
Cdd:COG2263   43 DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDpEALEIARENAERLGV--RVDFIRADVTRIPLGGSVDTVVMNP 118
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
175-250 1.87e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 55.16  E-value: 1.87e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442618365 175 AVDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMA-QYAQQLVESNNVQHKISVIPGKieeielpEKVDVII 250
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAvEAARENAELNGVELNVYLPQGD-------LKADVIV 184
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 169-281 2.64e-08

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 52.69  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 169 RAILGNAVDFQDKIVLDVGAGSGILSFFAVQAGaAKVYAIEAS-NMAQYAQQLVESNNVQhkISVIPGKIEEIELP-EKV 246
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAERG-ARVTGVDISpEMLELARERAAEAGLN--VEFVVGDAEDLPFPdGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442618365 247 DVIISepmGYMLYN----ERMLEtylHARKWLKPQGKMY 281
Cdd:COG2226   89 DLVIS---SFVLHHlpdpERALA---EIARVLKPGGRLV 121
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 179-250 4.34e-08

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 54.58  E-value: 4.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442618365  179 QDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMA-QYAQQLVESNNVQHKISVI-PGkieeiELP-EKVDVII 250
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVYlPG-----DLPkEKADVVV 230
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 177-265 7.28e-08

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 52.96  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 177 DFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQYAQQL-VESNNVqhKISVIPGKIEEIELPEKVDVIIsepMG 255
Cdd:COG3897   68 EVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLnAALNGV--AITTRLGDWRDPPAAGGFDLIL---GG 142

                         90
                 ....*....|
gi 442618365 256 YMLYNERMLE 265
Cdd:COG3897  143 DVLYERDLAE 152
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
183-278 2.79e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.67  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILS-FFAVQAGAAKVYAIEAS-NMAQYAQQLVESnnvqhkISVIPGKIEEIELPEKVDVIISepmGYML-Y 259
Cdd:COG4106    5 VLDLGCGTGRLTaLLAERFPGARVTGVDLSpEMLARARARLPN------VRFVVADLRDLDPPEPFDLVVS---NAALhW 75

                         90
                 ....*....|....*....
gi 442618365 260 NERMLETYLHARKWLKPQG 278
Cdd:COG4106   76 LPDHAALLARLAAALAPGG 94
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 184-281 2.42e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 45.73  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  184 LDVGAGSGILSFFAVQAGaAKVYAIEAS-NMAQYAQQlvesNNVQHKISVIPGKIEEIELPEK-VDVIISEpmgYMLYNE 261
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDISpEMLELARE----KAPREGLTFVVGDAEDLPFPDNsFDLVLSS---EVLHHV 72

                          90       100
                  ....*....|....*....|.
gi 442618365  262 RMLETYLH-ARKWLKPQGKMY 281
Cdd:pfam08241  73 EDPERALReIARVLKPGGILI 93
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 183-281 4.16e-06

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 47.49  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILS-FFAVQAGAAKVYAIEASNMA-QYAQQLVESNNVQhKISVIPGKIEEIELPEKVDVIISEP------- 253
Cdd:COG2813   53 VLDLGCGYGVIGlALAKRNPEARVTLVDVNARAvELARANAAANGLE-NVEVLWSDGLSGVPDGSFDLILSNPpfhagra 131

                         90       100
                 ....*....|....*....|....*...
gi 442618365 254 MGYMLYnERMLETylhARKWLKPQGKMY 281
Cdd:COG2813  132 VDKEVA-HALIAD---AARHLRPGGELW 155
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 159-278 5.28e-06

PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding protein 1) is PRMT5, an arginine-N-methyltransferase. These proteins appear to be key mitotic regulators. They play a role in Jak signalling in higher eukaryotes.


Pssm-ID: 428356  Cd Length: 171  Bit Score: 46.81  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  159 QDYVRTSTYQRAILGNAVDFQDK--------IVLDVGAGSGIL---SFFAVQ-AGA-AKVYAIEA-SNMAQYAQQLVESN 224
Cdd:pfam05185  35 KDPVKYDLYERAIEKALSDRVPEkkktskllVILVVGAGRGPLvdrALRAAEeTGTkVKIYAVEKnPNAYVTLQKRINFE 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442618365  225 NVQHKISVIPGKIEEIELPEKVDVIISEPMGYMLYNERMLETYLHARKWLKPQG 278
Cdd:pfam05185 115 KWGDKVTIISSDMREWQGPEKADILVSELLGSFGDNELSPECLDGAQKFLKPDG 168
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 171-281 6.32e-06

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 46.61  E-value: 6.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 171 ILGNavDFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEAS-NMAQYAQQLVESNNVQHKISVIPGKIE---EIELPEKV 246
Cdd:COG0742   35 ILGP--DIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDrKAAAVIRKNLEKLGLEDRARVIRGDALrflKRLAGEPF 112

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 442618365 247 DVIISEP---MGYMlynERMLETyLHARKWLKPQGKMY 281
Cdd:COG0742  113 DLVFLDPpyaKGLL---EKALEL-LAENGLLAPGGLIV 146
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
171-244 2.24e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 46.05  E-value: 2.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442618365 171 ILGNAVDFQDKIVLDVGAGSGILSFFaVQAGAAKVYAIEA-SNMAQYA-QQLVESNNVQhkisVIPGKIEEIELPE 244
Cdd:PRK14896  21 IVEYAEDTDGDPVLEIGPGKGALTDE-LAKRAKKVYAIELdPRLAEFLrDDEIAAGNVE----IIEGDALKVDLPE 91
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
171-281 9.21e-05

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 43.38  E-value: 9.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  171 ILGNAVdfQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQyaQQLVEsnNVQHKisvipgKIEEIEL-------- 242
Cdd:pfam03602  35 WLAPYI--EGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAV--QILKE--NLQLL------GLPGAVLvmdallal 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 442618365  243 ------PEKVDVIISEPmGYM--LYNERMleTYLHARKWLKPQGKMY 281
Cdd:pfam03602 103 lrlagkGPVFDIVFLDP-PYAkgLIEEVL--DLLAEKGWLKPNALIY 146
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 184-279 1.03e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.20  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  184 LDVGAGSGILSFFAVQAGA-AKVYAIEAS--NMAQYAQQLVESNNVQHKISVIPGKIEEIELPEKVDVIISEpmGYMLYN 260
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISpaALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVAS--NVLHHL 78

                          90
                  ....*....|....*....
gi 442618365  261 ERMLETYLHARKWLKPQGK 279
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGV 97
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 177-280 1.41e-04

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 43.93  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  177 DFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAQYAQQLVE--SNNVQHKIsVIPGKIEEIELPEKVDVIISepM 254
Cdd:pfam08003 113 PLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFLCQFEAVRklLGNDQRAH-LLPLGIEQLPALAAFDTVFS--M 189

                          90       100
                  ....*....|....*....|....*..
gi 442618365  255 GyMLYNERM-LETYLHARKWLKPQGKM 280
Cdd:pfam08003 190 G-VLYHRRSpLDHLLQLKDQLVKGGEL 215
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 169-281 2.49e-04

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.21  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 169 RAILGNAVDFQDKIVLDVGAGSGILSF-FAVQAGAAKVYAIEASNMA-QYAQQLVESNNVQHKISVIPGKI-EEIELPEK 245
Cdd:COG2890  102 ELALALLPAGAPPRVLDLGTGSGAIALaLAKERPDARVTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDGR 181

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442618365 246 VDVIIS--------------------EPM--------GYMLYnERMLEtylHARKWLKPQGKMY 281
Cdd:COG2890  182 FDLIVSnppyipedeiallppevrdhEPRlaldggedGLDFY-RRIIA---QAPRLLKPGGWLL 241
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 183-281 3.13e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 41.42  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  183 VLDVGAGSGILSFFAVQAGA-AKVYAIEASNMA-QYAQQLVESNNVqHKISVIPGKIEEIELPEKVDVIISEP------- 253
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPdAELTMVDINARAlESARENLAANGL-ENGEVVASDVYSGVEDGKFDLIISNPpfhagla 113

                          90       100
                  ....*....|....*....|....*...
gi 442618365  254 MGYMLyNERMLEtylHARKWLKPQGKMY 281
Cdd:pfam05175 114 TTYNV-AQRFIA---DAKRHLRPGGELW 137
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
177-278 3.34e-04

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 42.92  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 177 DFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASN--MAQYA--QQLVESNnvqHKISVIPGKIEEIELPEKVDVIISe 252
Cdd:PRK15068 120 PLKGRTVLDVGCGNGYHMWRMLGAGAKLVVGIDPSQlfLCQFEavRKLLGND---QRAHLLPLGIEQLPALKAFDTVFS- 195

                         90       100
                 ....*....|....*....|....*..
gi 442618365 253 pMGyMLYNERM-LETYLHARKWLKPQG 278
Cdd:PRK15068 196 -MG-VLYHRRSpLDHLKQLKDQLVPGG 220
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 182-227 5.31e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 40.37  E-value: 5.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 442618365  182 IVLDVGAGSGILSFFAVQAGA-AKVYAIEAS-NMAQYAQQLVESNNVQ 227
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpDAYEILEENVKLNNLP 48
PRK14968 PRK14968
putative methyltransferase; Provisional
 164-250 6.41e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.04  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 164 TSTYQRA-----ILGNAVDFQDKIVLDVGAGSGILSFFAVQAGaAKVYAIEASNMA-QYAQQLVESNNVQH-KISVIPGK 236
Cdd:PRK14968   3 DEVYEPAedsflLAENAVDKKGDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAvECAKCNAKLNNIRNnGVEVIRSD 81

                         90
                 ....*....|....
gi 442618365 237 IEEIELPEKVDVII 250
Cdd:PRK14968  82 LFEPFRGDKFDVIL 95
PH_CARM1 cd13330
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ...
 24-134 6.56e-04

Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 241484  Cd Length: 107  Bit Score: 39.31  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  24 CQFCGVVISSIADEQKLEFTNKYKGSCTLLCSYDSQgvvlRVVSDDDRSHVLKeYMIAADTDAAQMGRRSYAVSLDADNL 103
Cdd:cd13330    1 SVFPGVRLLSIGDANGEIQRHAEQQPLRLEVKAGSV----LVLSTNEDVCVFK-CSVNRETECSRVGKQSFLITLGCNSV 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 442618365 104 VLRFASEQDQQLFRKVVENVKHL-RPKSVFSQ 134
Cdd:cd13330   76 LLQFATPSEFSSFYNALKNCRGQtNEKSVFSQ 107
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 177-291 9.21e-04

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 40.47  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  177 DFQDKIVLDVGAGSGILSFFAVQAGAAKVYAIEASNMAqyAQQLVEsnNVQ------HKISVIPGKIE-EIELPEK---V 246
Cdd:TIGR00095  48 DIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKV--AQTLKE--NLStlkksgEQATVLNDAVRaLLFLAKKqtpF 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 442618365  247 DVI-ISEPMGYMLYNErmLETYLHARKWLKPQGKM---YPTHGDLHIAP 291
Cdd:TIGR00095 124 DIIyLDPPFNRGLLEA--LLELLGENKWLNPKGLIvveYDRENELPTVP 170
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 180-280 1.50e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.32  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365  180 DKIVLDVGAGSGILSFFA--VQAGAAKVYAIEAS-NMAQYAQQLVESNNVQhKISVIPGKIEEIEL---PEKVDVIISEp 253
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELaeELGPNAEVVGIDISeEAIEKARENAQKLGFD-NVEFEQGDIEELPElleDDKFDVVISN- 81

                          90       100
                  ....*....|....*....|....*..
gi 442618365  254 mGYMLYNERMLETYLHARKWLKPQGKM 280
Cdd:pfam13847  82 -CVLNHIPDPDKVLQEILRVLKPGGRL 107
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 183-278 2.98e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.13  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 183 VLDVGAGSGILSFFAVQAGAAKVYAIEASN-MAQYAQQLVESNNVqHKISVIPGKIEEIE--LPEKVDVIISepMGYM-L 258
Cdd:COG0500   30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPeAIALARARAAKAGL-GNVEFLVADLAELDplPAESFDLVVA--FGVLhH 106

                         90       100
                 ....*....|....*....|.
gi 442618365 259 YNERMLETYLH-ARKWLKPQG 278
Cdd:COG0500  107 LPPEEREALLReLARALKPGG 127
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 176-208 3.77e-03

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 39.27  E-value: 3.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 442618365 176 VDFQDKIVLDVGAGSGilSF--FAVQAGAAKVYAI 208
Cdd:COG1189   74 IDVAGKVCLDIGASTG--GFtdCLLQRGAAKVYAV 106
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
157-249 8.62e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 37.67  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442618365 157 MMQDYVRTSTYQRAILGNAvdfqdKIVLDVGAGSGILSF-FAVQAGAAKVYAIEASNMaqyAQQLVESNNVQ---HKISV 232
Cdd:PRK08287  14 MTKEEVRALALSKLELHRA-----KHLIDVGAGTGSVSIeAALQFPSLQVTAIERNPD---ALRLIKENRQRfgcGNIDI 85

                         90
                 ....*....|....*..
gi 442618365 233 IPGkIEEIELPEKVDVI 249
Cdd:PRK08287  86 IPG-EAPIELPGKADAI 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH