NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|51316479|sp|Q8IZ69|]
View 

RecName: Full=tRNA (uracil-5-)-methyltransferase homolog A; AltName: Full=mRNA (uracil-5-)-methyltransferase TRMT2A

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 178-587 3.99e-68

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 226.21  E-value: 3.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 178 VPYAEQLERKQLECEQVLQKLAKEIGstnrallpwlleqrhkhnkacCPLEGVRPSPQQTEYRNKCEFlvgvGVDGEDNT 257
Cdd:COG2265  81 LSYEAQLELKQRVVREALERIGGLPE---------------------VEVEPIIGSPEPWGYRNRARL----SVRRTDGR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 258 VgcRLGKYKGGTCAVAaPFDTVHI-PEATKQVVKAFQEFIRSTpysaydpETYTGHWKQLTVRtsrrhqamaiayfhpqk 336
Cdd:COG2265 136 L--RLGFYARGSHELV-DIDECPLlDPALNALLPALRELLAEL-------GARRGELRHLVVR----------------- 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 337 lspeelaelktslaqhftagpgrasgvtclyfveegqrktpsqeglplehvAGDRCIHEDLLGLTFRISPHAFFQVNTPA 416
Cdd:COG2265 189 ---------------------------------------------------AGRDYLTERLGGLTFRISPGSFFQVNPEQ 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 417 AEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTL 496
Cdd:COG2265 218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPEL 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 497 VSRLASQhlVAILDPPRAGLHSKVILAIRRAKnLRRLLYVSCNP----RaamgnfvDLCRAPSNRvkgipFRPVKAVAVD 572
Cdd:COG2265 298 LWGGRPD--VVVLDPPRAGAGPEVLEALAALG-PRRIVYVSCNPatlaR-------DLALLVEGG-----YRLEKVQPVD 362

                       410
                ....*....|....*
gi 51316479 573 LFPQTPHCEMLILFE 587
Cdd:COG2265 363 MFPHTHHVESVALLE 377
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
 68-146 4.07e-40

RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and similar proteins; This subfamily corresponds to the RRM of TRMT2A, also known as HpaII tiny fragments locus 9c protein (HTF9C), a novel cell cycle regulated protein. It is an independent biologic factor expressed in tumors associated with clinical outcome in HER2 expressing breast cancer. The function of TRMT2A remains unclear although by sequence homology it has a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), related to RNA methyltransferases.


:

Pssm-ID: 409873 [Multi-domain]  Cd Length: 79  Bit Score: 140.84  E-value: 4.07e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479  68 FTSEIFKLELQNVPRHASFSDVRRFLGRFGLQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLARP 146
Cdd:cd12439   1 FTSEIFKIEIKNLPKYIGFGQLKKFLQKLGLKPHKIKLIGRQTFAFVTFRNEEDRDKALKVLNGHKWKGKVLSAKLAKP 79
 
Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 178-587 3.99e-68

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 226.21  E-value: 3.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 178 VPYAEQLERKQLECEQVLQKLAKEIGstnrallpwlleqrhkhnkacCPLEGVRPSPQQTEYRNKCEFlvgvGVDGEDNT 257
Cdd:COG2265  81 LSYEAQLELKQRVVREALERIGGLPE---------------------VEVEPIIGSPEPWGYRNRARL----SVRRTDGR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 258 VgcRLGKYKGGTCAVAaPFDTVHI-PEATKQVVKAFQEFIRSTpysaydpETYTGHWKQLTVRtsrrhqamaiayfhpqk 336
Cdd:COG2265 136 L--RLGFYARGSHELV-DIDECPLlDPALNALLPALRELLAEL-------GARRGELRHLVVR----------------- 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 337 lspeelaelktslaqhftagpgrasgvtclyfveegqrktpsqeglplehvAGDRCIHEDLLGLTFRISPHAFFQVNTPA 416
Cdd:COG2265 189 ---------------------------------------------------AGRDYLTERLGGLTFRISPGSFFQVNPEQ 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 417 AEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTL 496
Cdd:COG2265 218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPEL 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 497 VSRLASQhlVAILDPPRAGLHSKVILAIRRAKnLRRLLYVSCNP----RaamgnfvDLCRAPSNRvkgipFRPVKAVAVD 572
Cdd:COG2265 298 LWGGRPD--VVVLDPPRAGAGPEVLEALAALG-PRRIVYVSCNPatlaR-------DLALLVEGG-----YRLEKVQPVD 362

                       410
                ....*....|....*
gi 51316479 573 LFPQTPHCEMLILFE 587
Cdd:COG2265 363 MFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 178-581 1.33e-42

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 158.83  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   178 VPYAEQLERKQLECEQVLQklakeigstnrallpwlleqRHKHNKaccpLEGVRPSPQQTE----YRNKCEFLVGvgvdg 253
Cdd:TIGR00479  72 LSYELQLRSKQQQVIALLE--------------------RIGKFV----SEPIEDVPTIGDdpwgYRNKARLSLG----- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   254 EDNTVGCRLGKYKGGT--------CAVAAPfdtvhipeATKQVVKAFQEFIRSTPYSAYDPETYTGHWKQLTVRTSRRHQ 325
Cdd:TIGR00479 123 RSPSGQLQAGFYQKGShdivdvkqCPVQAP--------ALNALLPKVRAILENFGASRYLEHKELGQARHGVLRIGRHTG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   326 AMAIAyFHPQKLSPEELAELKTSLAQHFTAGPGRASGVTclyfveegQRKTPSQEGLPLEHVAGDRCIHEDLLGLTFRIS 405
Cdd:TIGR00479 195 ELSSV-DRTALERFPHKEELDLYLQPDSPDVKSICQNIN--------PEKTNVIFGEETEVIAGEMPIYDKSGDLSFTFS 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   406 PHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFH 485
Cdd:TIGR00479 266 ARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFY 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   486 CGRAEDLVPTLVSRLASQHLVaILDPPRAGLHSKVILAIRRAKNlRRLLYVSCNPRAAMGNFVDLCRApsnrvkgiPFRP 565
Cdd:TIGR00479 346 HGTLETVLPKQPWAGNGFDKV-LLDPPRKGCAAGVLRTIIKLKP-ERIVYVSCNPATLARDLEALCKA--------GYTI 415

                         410
                  ....*....|....*.
gi 51316479   566 VKAVAVDLFPQTPHCE 581
Cdd:TIGR00479 416 ARVQPVDMFPHTGHVE 431
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
 68-146 4.07e-40

RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and similar proteins; This subfamily corresponds to the RRM of TRMT2A, also known as HpaII tiny fragments locus 9c protein (HTF9C), a novel cell cycle regulated protein. It is an independent biologic factor expressed in tumors associated with clinical outcome in HER2 expressing breast cancer. The function of TRMT2A remains unclear although by sequence homology it has a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), related to RNA methyltransferases.


Pssm-ID: 409873 [Multi-domain]  Cd Length: 79  Bit Score: 140.84  E-value: 4.07e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479  68 FTSEIFKLELQNVPRHASFSDVRRFLGRFGLQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLARP 146
Cdd:cd12439   1 FTSEIFKIEIKNLPKYIGFGQLKKFLQKLGLKPHKIKLIGRQTFAFVTFRNEEDRDKALKVLNGHKWKGKVLSAKLAKP 79
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
385-588 2.14e-27

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 113.04  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  385 EHVA---GDRCIH--------EDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDW-AQLDAGSMVlDVCCGTGTIGLALAR 452
Cdd:PRK03522 115 VHMAileGEEEIFlteqqalpERFNGVPLFIRPQSFFQTNPAVAAQLYATARDWvRELPPRSMW-DLFCGVGGFGLHCAT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  453 KVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA------EDLVPTLVsrlasqhlvaILDPPRAGLhSKVILAIRR 526
Cdd:PRK03522 194 PGMQLTGIEISAEAIACAKQSAAELGLTNVQFQALDStqfataQGEVPDLV----------LVNPPRRGI-GKELCDYLS 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51316479  527 AKNLRRLLYVSCNPrAAMGNfvDLCRAPSnrvkgipFRPVKAVAVDLFPQTPHCEMLILFER 588
Cdd:PRK03522 263 QMAPRFILYSSCNA-QTMAK--DLAHLPG-------YRIERVQLFDMFPHTAHYEVLTLLVR 314
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 408-589 5.19e-14

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 74.01  E-value: 5.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   408 AFFQVNTPAAEVLYTVIQDWAQLDAGSMvLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCG 487
Cdd:pfam05958 178 SFTQPNAAVNIKMLEWACDVTQGSKGDL-LELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIRM 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   488 RAEDLVPTLVSRLASQHLVAI-----------LDPPRAGLHSKVilaIRRAKNLRRLLYVSCNPRAAMGNFVDLCRapSN 556
Cdd:pfam05958 257 SAEEFTQAMNGVREFNRLKGIdlksyncstifVDPPRAGLDPET---LKLVQAYPRILYISCNPETLCANLEQLSK--TH 331

                         170       180       190
                  ....*....|....*....|....*....|...
gi 51316479   557 RVKgipfrpvKAVAVDLFPQTPHCEMLILFERV 589
Cdd:pfam05958 332 RVE-------RFALFDQFPYTHHMECGVLLEKK 357
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 436-538 1.07e-12

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: 64.76  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 436 VLDVCCGTGTIGLALAR-KVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLAsqhlVAILDPP-- 512
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFD----VIISDPPlh 77

                        90       100
                ....*....|....*....|....*..
gi 51316479 513 -RAGLHSKVILAIRRAKNLRRLLYVSC 538
Cdd:cd02440  78 hLVEDLARFLEEARRLLKPGGVLVLTL 104
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
112-149 1.20e-07

RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 49.33  E-value: 1.20e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 51316479 112 AFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKAD 149
Cdd:COG0724  46 GFVEMPDDEEAQAAIEALNGAELMGRTLKVNEARPREE 83
RRM smart00360
RNA recognition motif;
79-141 5.12e-06

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.51  E-value: 5.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51316479     79 NVPRHASFSDVRRFLGRFG----LQPHKTKLFGQP-PCAFVTFRSAAERDKALRVLHGALWKGRPLSV 141
Cdd:smart00360   6 NLPPDTTEEELRELFSKFGkvesVRLVRDKETGKSkGFAFVEFESEEDAEKALEALNGKELDGRPLKV 73
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 102-164 6.77e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 6.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316479   102 KTKLFGqppcaFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKADPMARRRRQEGESEPP 164
Cdd:TIGR01628 324 VSRGFG-----FVCFSNPEEANRAVTEMHGRMLGGKPLYVALAQRKEQRRAHLQDQFMQLQPR 381
 
Name Accession Description Interval E-value
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 178-587 3.99e-68

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 226.21  E-value: 3.99e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 178 VPYAEQLERKQLECEQVLQKLAKEIGstnrallpwlleqrhkhnkacCPLEGVRPSPQQTEYRNKCEFlvgvGVDGEDNT 257
Cdd:COG2265  81 LSYEAQLELKQRVVREALERIGGLPE---------------------VEVEPIIGSPEPWGYRNRARL----SVRRTDGR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 258 VgcRLGKYKGGTCAVAaPFDTVHI-PEATKQVVKAFQEFIRSTpysaydpETYTGHWKQLTVRtsrrhqamaiayfhpqk 336
Cdd:COG2265 136 L--RLGFYARGSHELV-DIDECPLlDPALNALLPALRELLAEL-------GARRGELRHLVVR----------------- 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 337 lspeelaelktslaqhftagpgrasgvtclyfveegqrktpsqeglplehvAGDRCIHEDLLGLTFRISPHAFFQVNTPA 416
Cdd:COG2265 189 ---------------------------------------------------AGRDYLTERLGGLTFRISPGSFFQVNPEQ 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 417 AEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTL 496
Cdd:COG2265 218 AEALYAAALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPEL 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 497 VSRLASQhlVAILDPPRAGLHSKVILAIRRAKnLRRLLYVSCNP----RaamgnfvDLCRAPSNRvkgipFRPVKAVAVD 572
Cdd:COG2265 298 LWGGRPD--VVVLDPPRAGAGPEVLEALAALG-PRRIVYVSCNPatlaR-------DLALLVEGG-----YRLEKVQPVD 362

                       410
                ....*....|....*
gi 51316479 573 LFPQTPHCEMLILFE 587
Cdd:COG2265 363 MFPHTHHVESVALLE 377
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 178-581 1.33e-42

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 158.83  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   178 VPYAEQLERKQLECEQVLQklakeigstnrallpwlleqRHKHNKaccpLEGVRPSPQQTE----YRNKCEFLVGvgvdg 253
Cdd:TIGR00479  72 LSYELQLRSKQQQVIALLE--------------------RIGKFV----SEPIEDVPTIGDdpwgYRNKARLSLG----- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   254 EDNTVGCRLGKYKGGT--------CAVAAPfdtvhipeATKQVVKAFQEFIRSTPYSAYDPETYTGHWKQLTVRTSRRHQ 325
Cdd:TIGR00479 123 RSPSGQLQAGFYQKGShdivdvkqCPVQAP--------ALNALLPKVRAILENFGASRYLEHKELGQARHGVLRIGRHTG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   326 AMAIAyFHPQKLSPEELAELKTSLAQHFTAGPGRASGVTclyfveegQRKTPSQEGLPLEHVAGDRCIHEDLLGLTFRIS 405
Cdd:TIGR00479 195 ELSSV-DRTALERFPHKEELDLYLQPDSPDVKSICQNIN--------PEKTNVIFGEETEVIAGEMPIYDKSGDLSFTFS 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   406 PHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFH 485
Cdd:TIGR00479 266 ARDFIQVNSGQNEKLVDRALEWLELQGEERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIANVTFY 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   486 CGRAEDLVPTLVSRLASQHLVaILDPPRAGLHSKVILAIRRAKNlRRLLYVSCNPRAAMGNFVDLCRApsnrvkgiPFRP 565
Cdd:TIGR00479 346 HGTLETVLPKQPWAGNGFDKV-LLDPPRKGCAAGVLRTIIKLKP-ERIVYVSCNPATLARDLEALCKA--------GYTI 415

                         410
                  ....*....|....*.
gi 51316479   566 VKAVAVDLFPQTPHCE 581
Cdd:TIGR00479 416 ARVQPVDMFPHTGHVE 431
RRM_TRMT2A cd12439
RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and ...
 68-146 4.07e-40

RNA recognition motif (RRM) found in tRNA (uracil-5-)-methyltransferase homolog A (TRMT2A) and similar proteins; This subfamily corresponds to the RRM of TRMT2A, also known as HpaII tiny fragments locus 9c protein (HTF9C), a novel cell cycle regulated protein. It is an independent biologic factor expressed in tumors associated with clinical outcome in HER2 expressing breast cancer. The function of TRMT2A remains unclear although by sequence homology it has a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), related to RNA methyltransferases.


Pssm-ID: 409873 [Multi-domain]  Cd Length: 79  Bit Score: 140.84  E-value: 4.07e-40
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479  68 FTSEIFKLELQNVPRHASFSDVRRFLGRFGLQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLARP 146
Cdd:cd12439   1 FTSEIFKIEIKNLPKYIGFGQLKKFLQKLGLKPHKIKLIGRQTFAFVTFRNEEDRDKALKVLNGHKWKGKVLSAKLAKP 79
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
385-588 2.14e-27

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 113.04  E-value: 2.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  385 EHVA---GDRCIH--------EDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDW-AQLDAGSMVlDVCCGTGTIGLALAR 452
Cdd:PRK03522 115 VHMAileGEEEIFlteqqalpERFNGVPLFIRPQSFFQTNPAVAAQLYATARDWvRELPPRSMW-DLFCGVGGFGLHCAT 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  453 KVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRA------EDLVPTLVsrlasqhlvaILDPPRAGLhSKVILAIRR 526
Cdd:PRK03522 194 PGMQLTGIEISAEAIACAKQSAAELGLTNVQFQALDStqfataQGEVPDLV----------LVNPPRRGI-GKELCDYLS 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51316479  527 AKNLRRLLYVSCNPrAAMGNfvDLCRAPSnrvkgipFRPVKAVAVDLFPQTPHCEMLILFER 588
Cdd:PRK03522 263 QMAPRFILYSSCNA-QTMAK--DLAHLPG-------YRIERVQLFDMFPHTAHYEVLTLLVR 314
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
399-588 2.18e-25

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 109.48  E-value: 2.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  399 GLTFRISPHAFFQVNTPAAEVLytVIQ--DWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQD 476
Cdd:PRK13168 264 GLRLAFSPRDFIQVNAQVNQKM--VARalEWLDPQPGDRVLDLFCGLGNFTLPLARQAAEVVGVEGVEAMVERARENARR 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  477 NELSNVEFHCgraEDLVPTLVSRL-ASQHLVAIL-DPPRAGlhskvilAIRRAKNL-----RRLLYVSCNPraamgnfVD 549
Cdd:PRK13168 342 NGLDNVTFYH---ANLEEDFTDQPwALGGFDKVLlDPPRAG-------AAEVMQALaklgpKRIVYVSCNP-------AT 404

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 51316479  550 LCRAPSNRVKGiPFRPVKAVAVDLFPQTPHCEMLILFER 588
Cdd:PRK13168 405 LARDAGVLVEA-GYRLKRAGMLDMFPHTGHVESMALFER 442
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 408-589 5.19e-14

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 74.01  E-value: 5.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   408 AFFQVNTPAAEVLYTVIQDWAQLDAGSMvLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCG 487
Cdd:pfam05958 178 SFTQPNAAVNIKMLEWACDVTQGSKGDL-LELYCGNGNFSLALARNFRKVLATEIAKPSVAAAQYNIAANNIDNVQIIRM 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   488 RAEDLVPTLVSRLASQHLVAI-----------LDPPRAGLHSKVilaIRRAKNLRRLLYVSCNPRAAMGNFVDLCRapSN 556
Cdd:pfam05958 257 SAEEFTQAMNGVREFNRLKGIdlksyncstifVDPPRAGLDPET---LKLVQAYPRILYISCNPETLCANLEQLSK--TH 331

                         170       180       190
                  ....*....|....*....|....*....|...
gi 51316479   557 RVKgipfrpvKAVAVDLFPQTPHCEMLILFERV 589
Cdd:pfam05958 332 RVE-------RFALFDQFPYTHHMECGVLLEKK 357
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 436-492 8.64e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.20  E-value: 8.64e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 51316479   436 VLDVCCGTGTIGLALARKVK-RVIGVELCPEAVEDARVNAQDNELsNVEFHCGRAEDL 492
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL 57
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 379-487 8.80e-14

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 72.10  E-value: 8.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 379 QEGLPLEHVAGdrciHEDLLGLTFRISPHAFfqV---NTpaaEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVK 455
Cdd:COG2890  65 AAGEPLAYILG----EAEFYGLEFKVDPGVL--IprpET---EELVELALALLPAGAPPRVLDLGTGSGAIALALAKERP 135

                        90       100       110
                ....*....|....*....|....*....|....*
gi 51316479 456 --RVIGVELCPEAVEDARVNAQDNELSN-VEFHCG 487
Cdd:COG2890 136 daRVTAVDISPDALAVARRNAERLGLEDrVRFLQG 170
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 380-487 6.15e-13

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 69.42  E-value: 6.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  380 EGLPLEHVAGdrciHEDLLGLTFRISPHAFfqVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVK--RV 457
Cdd:PRK09328  62 AGEPLQYILG----EAEFWGLDFKVSPGVL--IPRPETEELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPdaEV 135

                         90       100       110
                 ....*....|....*....|....*....|
gi 51316479  458 IGVELCPEAVEDARVNAQDNELSNVEFHCG 487
Cdd:PRK09328 136 TAVDISPEALAVARRNAKHGLGARVEFLQG 165
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 426-496 7.34e-13

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: 68.63  E-value: 7.34e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51316479 426 DWAQLDAGSMVLDVCCGTGTIGLALARKVK--RVIGVELCPEAVEDARVNAQDNELSN-VEFHCGRAEDLVPTL 496
Cdd:COG4123  31 AFAPVKKGGRVLDLGTGTGVIALMLAQRSPgaRITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEFAAEL 104
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 436-538 1.07e-12

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: 64.76  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 436 VLDVCCGTGTIGLALAR-KVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLAsqhlVAILDPP-- 512
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFD----VIISDPPlh 77

                        90       100
                ....*....|....*....|....*..
gi 51316479 513 -RAGLHSKVILAIRRAKNLRRLLYVSC 538
Cdd:cd02440  78 hLVEDLARFLEEARRLLKPGGVLVLTL 104
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 426-492 1.33e-12

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: 65.40  E-value: 1.33e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51316479 426 DWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELsNVEFHCGRAEDL 492
Cdd:COG2226  16 AALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDL 81
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 430-539 2.85e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 64.75  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   430 LDAGSMVLDVCCGTGTIGLALARKV---KRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLvPTLVSR------L 500
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELgpnAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEEL-PELLEDdkfdvvI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 51316479   501 ASQHLVAILDPPRA------GLHSKVILAIRRAKNLRRLLYVSCN 539
Cdd:pfam13847  80 SNCVLNHIPDPDKVlqeilrVLKPGGRLIISDPDSLAELPAHVKE 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 415-494 3.32e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.71  E-value: 3.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 415 PAAEVLYTVIQDwaqLDAGSMVLDVCCGTGTIGLALA-RKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLV 493
Cdd:COG0500  12 PGLAALLALLER---LPKGGRVLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELD 88


                .
gi 51316479 494 P 494
Cdd:COG0500  89 P 89
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
 441-588 5.84e-12

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 67.55  E-value: 5.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  441 CGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTL-----VSRLASQHLVA-----IL- 509
Cdd:PRK05031 215 CGNGNFTLALARNFRRVLATEISKPSVAAAQYNIAANGIDNVQIIRMSAEEFTQAMngvreFNRLKGIDLKSynfstIFv 294

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479  510 DPPRAGLHSKVIlaiRRAKNLRRLLYVSCNPRAAMGNFVDLCRapSNRVKgipfrpvKAVAVDLFPQTPHCEMLILFER 588
Cdd:PRK05031 295 DPPRAGLDDETL---KLVQAYERILYISCNPETLCENLETLSQ--THKVE-------RFALFDQFPYTHHMECGVLLEK 361
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 420-492 3.45e-11

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: 60.80  E-value: 3.45e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316479 420 LYTVIQDWaqLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDnelSNVEFHCGRAEDL 492
Cdd:COG2227  14 LAALLARL--LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDL 81
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 427-533 1.62e-10

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: 60.59  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 427 WAQLDAGSM-------------VLDVCCGTGTIGLALARK--VKRVIGVELCPEAVEDARVNAQDNELSNVEFHcgraed 491
Cdd:COG2813  31 RDRLDIGTRlllehlpeplggrVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAANGLENVEVL------ 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51316479 492 lVPTLVSRLASQHLVAIL-DPP-RAGL--HSKVILA-IRRAKnlRRL 533
Cdd:COG2813 105 -WSDGLSGVPDGSFDLILsNPPfHAGRavDKEVAHAlIADAA--RHL 148
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
436-505 7.28e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 7.28e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51316479 436 VLDVCCGTGTIGLALARKVK--RVIGVELCPEAVEDARvnaqdNELSNVEFHCGRAEDLVPT-----LVSRLASQHL 505
Cdd:COG4106   5 VLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARAR-----ARLPNVRFVVADLRDLDPPepfdlVVSNAALHWL 76
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
426-487 2.23e-08

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 54.68  E-value: 2.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316479   426 DWAQLDAGSMVLDVCCGTGTIGLALARKVK---RVIGVELCPEAVEDARVNAQDNELSNVEFHCG 487
Cdd:pfam01135  67 ELLELKPGMRVLEIGSGSGYLTACFARMVGevgRVVSIEHIPELVEIARRNLEKLGLENVIVVVG 131
PRK14968 PRK14968
putative methyltransferase; Provisional
 428-484 5.18e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 53.36  E-value: 5.18e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479  428 AQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSN--VEF 484
Cdd:PRK14968  19 AVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNngVEV 77
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
416-492 6.48e-08

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 52.69  E-value: 6.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 416 AAEVLYTVIQDWAQ-------LDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDnelsnVEFHCGR 488
Cdd:COG4976  23 VEDLGYEAPALLAEellarlpPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVY-----DRLLVAD 97


                ....
gi 51316479 489 AEDL 492
Cdd:COG4976  98 LADL 101
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
112-149 1.20e-07

RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 49.33  E-value: 1.20e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 51316479 112 AFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKAD 149
Cdd:COG0724  46 GFVEMPDDEEAQAAIEALNGAELMGRTLKVNEARPREE 83
RRM1_RBM40_like cd12238
RNA recognition motif 1 (RRM1) found in RNA-binding protein 40 (RBM40) and similar proteins; ...
 79-141 1.42e-07

RNA recognition motif 1 (RRM1) found in RNA-binding protein 40 (RBM40) and similar proteins; This subfamily corresponds to the RRM1 of RBM40, also known as RNA-binding region-containing protein 3 (RNPC3) or U11/U12 small nuclear ribonucleoprotein 65 kDa protein (U11/U12-65K protein), It serves as a bridging factor between the U11 and U12 snRNPs. It contains two repeats of RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), connected by a linker that includes a proline-rich region. It binds to the U11-associated 59K protein via its RRM1 and employs the RRM2 to bind hairpin III of the U12 small nuclear RNA (snRNA). The proline-rich region might be involved in protein-protein interactions.


Pssm-ID: 409684 [Multi-domain]  Cd Length: 73  Bit Score: 48.79  E-value: 1.42e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51316479  79 NVPRHASFSDVRRFLGRFGLqpHKTKLFGQPP----CAFVTFRSAAERDKALRVLHGALWKGRPLSV 141
Cdd:cd12238   6 HLPPELSEDDKEDLLKHFGA--TSVRVMKRRGklkhTAFATFDNEQAASKALSRLHQLKILGKRLVV 70
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 79-142 1.58e-07

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 48.82  E-value: 1.58e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51316479  79 NVPRHASFSDVRRFLGRFG----LQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVR 142
Cdd:cd00590   5 NLPPDTTEEDLRELFSKFGevvsVRIVRDRDGKSKGFAFVEFESPEDAEKALEALNGTELGGRPLKVS 72
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 428-512 1.65e-07

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 51.49  E-value: 1.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 428 AQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLvptlvsRLASQHL-V 506
Cdd:COG1041  22 AGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDL------PLADESVdA 95


                ....*.
gi 51316479 507 AILDPP 512
Cdd:COG1041  96 IVTDPP 101
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 437-492 1.96e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.20  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51316479   437 LDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNelsNVEFHCGRAEDL 492
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPRE---GLTFVVGDAEDL 53
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 415-495 2.21e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.70  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 415 PAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVK-RVIGVELCPEAVEDARVNAQDNELSN-VEFHCGRAEDL 492
Cdd:COG2230  34 EAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDL 113


                ...
gi 51316479 493 VPT 495
Cdd:COG2230 114 PAD 116
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 426-492 2.51e-07

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 51.88  E-value: 2.51e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   426 DWAQLDAGSMVLDVCCGTGTIGLALARKV---KRVIGVELCPEAVEDARvnAQDNELSNVEFHCGRAEDL 492
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAK--KKSELPLNIEFIQADAEAL 100
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 426-492 2.63e-07

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 52.08  E-value: 2.63e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51316479  426 DWAQLDAGSMVLDVCCGTGTIGLALARKVKR---VIGVELCPEAVEDARVNAQDNELS-NVEFHCGRAEDL 492
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgeVVGLDFSEGMLAVGREKLRDLGLSgNVEFVQGDAEAL 115
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 436-512 5.88e-07

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 51.59  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   436 VLDVCCGTGTIGLALA--RKVKRVIGVELCPEAVEDARVNAQDNELS-NVEFHCGRaedlvptLVSRLASQHLVAIL-DP 511
Cdd:TIGR00536 118 ILDLGTGSGCIALALAyeFPNAEVIAVDISPDALAVAEENAEKNQLEhRVEFIQSN-------LFEPLAGQKIDIIVsNP 190


                  .
gi 51316479   512 P 512
Cdd:TIGR00536 191 P 191
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
411-492 1.31e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 1.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 411 QVNTP---AAEVLYTVIqdwAQLD-AGSMVLDVCCGTGTIGLALA-RKVKRVIGVELCPEAVEDARVNAqDNELSNVEFH 485
Cdd:COG2263  23 QYPTPaelAAELLHLAY---LRGDiEGKTVLDLGCGTGMLAIGAAlLGAKKVVGVDIDPEALEIARENA-ERLGVRVDFI 98


                ....*..
gi 51316479 486 CGRAEDL 492
Cdd:COG2263  99 RADVTRI 105
PRK08317 PRK08317
hypothetical protein; Provisional
 414-514 1.43e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.94  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  414 TPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVK---RVIGVELCPEAVEDARvNAQDNELSNVEFHCGRAE 490
Cdd:PRK08317   1 LPDFRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRVGpegRVVGIDRSEAMLALAK-ERAAGLGPNVEFVRGDAD 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 51316479  491 DL------VPTLVSRLASQHlvaILDPPRA 514
Cdd:PRK08317  80 GLpfpdgsFDAVRSDRVLQH---LEDPARA 106
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 427-485 2.17e-06

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: 47.97  E-value: 2.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51316479   427 WAQLDAGS-------------MVLDVCCGTGTIGLALARKVKRVI--GVELCPEAVEDARVNAQDNELSNVEFH 485
Cdd:pfam05175  13 HGRLDIGSrlllehlpkdlsgKVLDLGCGAGVLGAALAKESPDAEltMVDINARALESARENLAANGLENGEVV 86
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
427-531 2.31e-06

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 48.39  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479   427 WAQLDAGSMVLDVCCGTGTIGL-ALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLvPTLVSRLASQHL 505
Cdd:pfam03602  36 LAPYIEGARVLDLFAGSGALGLeALSRGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALLAL-LRLAGKGPVFDI 114

                          90       100
                  ....*....|....*....|....*..
gi 51316479   506 VaILDPP-RAGLHSKVILAIRRAKNLR 531
Cdd:pfam03602 115 V-FLDPPyAKGLIEEVLDLLAEKGWLK 140
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 432-536 3.41e-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: 47.77  E-value: 3.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 432 AGSMVLDVCCGTGTIGL-ALARKVKRVIGVELCPEAVEDARVNAQD-NELSNVEFHCGRAEDLVPTLVSRlaSQHLVaIL 509
Cdd:COG0742  41 EGARVLDLFAGSGALGLeALSRGAASVVFVEKDRKAAAVIRKNLEKlGLEDRARVIRGDALRFLKRLAGE--PFDLV-FL 117

                        90       100       110
                ....*....|....*....|....*....|
gi 51316479 510 DPP-RAGLHSKVILAIRRAKNLRR--LLYV 536
Cdd:COG0742 118 DPPyAKGLLEKALELLAENGLLAPggLIVV 147
arsM PRK11873
arsenite methyltransferase;
428-492 3.97e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 48.79  E-value: 3.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51316479  428 AQLDAGSMVLDVCCGTGTIGLALARKVK---RVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDL 492
Cdd:PRK11873  73 AELKPGETVLDLGSGGGFDCFLAARRVGptgKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEAL 140
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 379-512 5.07e-06

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 49.02  E-value: 5.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 379 QEGLPLE--HVAGDRC----IHEDllGLTFRISPHA-----FF--QVNTPAAevlytvIQDWAqldAGSMVLDVCCGTGT 445
Cdd:COG1092 161 LEGLPQYegVLYGEAPeeveVEEN--GLKFLVDLTDgqktgLFldQRENRAR------VAELA---KGKRVLNLFSYTGG 229

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479 446 IGL-ALARKVKRVIGVELCPEAVEDARVNAQDNELS-NVEFHCGRAEDLVPTLVSRLASQHLVaILDPP 512
Cdd:COG1092 230 FSVhAAAGGAKSVTSVDLSATALEWAKENAALNGLDdRHEFVQADAFDWLRELAREGERFDLI-ILDPP 297
RRM smart00360
RNA recognition motif;
79-141 5.12e-06

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.51  E-value: 5.12e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51316479     79 NVPRHASFSDVRRFLGRFG----LQPHKTKLFGQP-PCAFVTFRSAAERDKALRVLHGALWKGRPLSV 141
Cdd:smart00360   6 NLPPDTTEEELRELFSKFGkvesVRLVRDKETGKSkGFAFVEFESEEDAEKALEALNGKELDGRPLKV 73
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 429-491 7.41e-06

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 48.62  E-value: 7.41e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316479 429 QLDAGSMVLDVCCGTGTIGLALARKVK--RVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAED 491
Cdd:COG2242 244 ALRPGDVLWDIGAGSGSVSIEAARLAPggRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPE 308
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
433-492 8.27e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 47.43  E-value: 8.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316479   433 GSMVLDVCCGTGTIGLALARKVK---RVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDL 492
Cdd:pfam01209  43 GNKFLDVAGGTGDWTFGLSDSAGssgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEEL 105
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
433-516 9.25e-06

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 47.98  E-value: 9.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479 433 GSMVLDVCCGTG--TIGlALARKVKRVIGVELCPEAVEDARVNAQDNELSN--VEFHCGRAEDLVPtlvsRLASQHLVAI 508
Cdd:COG2521 133 GDRVLDTCTGLGytAIE-ALKRGAREVITVEKDPNVLELAELNPWSRELANerIKIILGDASEVIK----TFPDESFDAI 207


                ....*....
gi 51316479 509 L-DPPRAGL 516
Cdd:COG2521 208 IhDPPRFSL 216
RRM_RBM18 cd12355
RNA recognition motif (RRM) found in eukaryotic RNA-binding protein 18 and similar proteins; ...
 101-145 1.80e-05

RNA recognition motif (RRM) found in eukaryotic RNA-binding protein 18 and similar proteins; This subfamily corresponds to the RRM of RBM18, a putative RNA-binding protein containing a well-conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The biological role of RBM18 remains unclear.


Pssm-ID: 409791 [Multi-domain]  Cd Length: 80  Bit Score: 43.06  E-value: 1.80e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 51316479 101 HKT-KLFGQP-PCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLAR 145
Cdd:cd12355  34 HKTgPLKGQPrGYCFVTFETKEEAEKAIECLNGKLALGKKLVVRWAH 80
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
428-493 3.32e-05

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 45.93  E-value: 3.32e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316479 428 AQLDAGSMVLDVCCGTGtIgLA-LARK--VKRVIGVELCPEAVEDARVNAQDNELSN-VEFHCGRAE-----DLV 493
Cdd:COG2264 144 KLLKPGKTVLDVGCGSG-I-LAiAAAKlgAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLedgpyDLV 216
PRK14967 PRK14967
putative methyltransferase; Provisional
 430-474 4.48e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.04  E-value: 4.48e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 51316479  430 LDAGSMVLDVCCGTGTIGLALARK-VKRVIGVELCPEAVEDARVNA 474
Cdd:PRK14967  34 LGPGRRVLDLCTGSGALAVAAAAAgAGSVTAVDISRRAVRSARLNA 79
RRM2_RBM40_like cd12239
RNA recognition motif 2 (RRM2) found in RNA-binding protein 40 (RBM40) and similar proteins; ...
 74-144 9.54e-05

RNA recognition motif 2 (RRM2) found in RNA-binding protein 40 (RBM40) and similar proteins; This subfamily corresponds to the RRM2 of RBM40 and the RRM of RBM41. RBM40, also known as RNA-binding region-containing protein 3 (RNPC3) or U11/U12 small nuclear ribonucleoprotein 65 kDa protein (U11/U12-65K protein). It serves as a bridging factor between the U11 and U12 snRNPs. It contains two RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), connected by a linker that includes a proline-rich region. It binds to the U11-associated 59K protein via its RRM1 and employs the RRM2 to bind hairpin III of the U12 small nuclear RNA (snRNA). The proline-rich region might be involved in protein-protein interactions. RBM41 contains only one RRM. Its biological function remains unclear.


Pssm-ID: 409685 [Multi-domain]  Cd Length: 82  Bit Score: 41.06  E-value: 9.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  74 KLELQNVPRHASFSDVRRFLGRFgLQPHKT-------------KLFGQppcAFVTFRSAAERDKALRVLHGALWKGRPLS 140
Cdd:cd12239   3 RLYVKNLSKRVSEKDLKYIFGRF-VDSSSEeknmfdirlmtegRMKGQ---AFITFPSEELAEKALNLTNGYVLHGKPMV 78


                ....
gi 51316479 141 VRLA 144
Cdd:cd12239  79 VQFA 82
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 428-500 1.93e-04

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 42.86  E-value: 1.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51316479  428 AQLDAGSMVLDVCCGTGTI----GLALARKvKRVIGVELCPEAVEDARVNAQD-NELSNVEFHCGRAEDLVPTLVSRL 500
Cdd:PRK00377  36 LRLRKGDMILDIGCGTGSVtveaSLLVGET-GKVYAVDKDEKAINLTRRNAEKfGVLNNIVLIKGEAPEILFTINEKF 112
RRM1_2_CELF1-6_like cd12361
RNA recognition motif 1 (RRM1) and 2 (RRM2) found in CELF/Bruno-like family of RNA binding ...
 74-131 4.23e-04

RNA recognition motif 1 (RRM1) and 2 (RRM2) found in CELF/Bruno-like family of RNA binding proteins and plant flowering time control protein FCA; This subfamily corresponds to the RRM1 and RRM2 domains of the CUGBP1 and ETR-3-like factors (CELF) as well as plant flowering time control protein FCA. CELF, also termed BRUNOL (Bruno-like) proteins, is a family of structurally related RNA-binding proteins involved in regulation of pre-mRNA splicing in the nucleus, and control of mRNA translation and deadenylation in the cytoplasm. The family contains six members: CELF-1 (also known as BRUNOL-2, CUG-BP1, NAPOR, EDEN-BP), CELF-2 (also known as BRUNOL-3, ETR-3, CUG-BP2, NAPOR-2), CELF-3 (also known as BRUNOL-1, TNRC4, ETR-1, CAGH4, ER DA4), CELF-4 (BRUNOL-4), CELF-5 (BRUNOL-5) and CELF-6 (BRUNOL-6). They all contain three highly conserved RNA recognition motifs (RRMs), also known as RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains): two consecutive RRMs (RRM1 and RRM2) situated in the N-terminal region followed by a linker region and the third RRM (RRM3) close to the C-terminus of the protein. The low sequence conservation of the linker region is highly suggestive of a large variety in the co-factors that associate with the various CELF family members. Based on both, sequence similarity and function, the CELF family can be divided into two subfamilies, the first containing CELFs 1 and 2, and the second containing CELFs 3, 4, 5, and 6. The different CELF proteins may act through different sites on at least some substrates. Furthermore, CELF proteins may interact with each other in varying combinations to influence alternative splicing in different contexts. This subfamily also includes plant flowering time control protein FCA that functions in the posttranscriptional regulation of transcripts involved in the flowering process. FCA contains two RRMs, and a WW protein interaction domain.


Pssm-ID: 409796 [Multi-domain]  Cd Length: 77  Bit Score: 39.14  E-value: 4.23e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316479  74 KLELQNVPRHASFSDVRRFLGRFG----LQPHKTKLFGQPP-CAFVTFRSAAERDKALRVLHG 131
Cdd:cd12361   1 KLFVGMIPKTASEEDVRPLFEQFGnieeVQILRDKQTGQSKgCAFVTFSTREEALRAIEALHN 63
MenG_heptapren TIGR02752
demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that ...
 432-492 5.40e-04

demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that catalyzes the last step in menaquinone biosynthesis; the exact enzymatic activity differs for different MenG because the menaquinone differ in their prenoid side chains in different species. Members of this MenG protein family are 2-heptaprenyl-1,4-naphthoquinone methyltransferase, and are found together in operons with the two subunits of the heptaprenyl diphosphate synthase in Bacillus subtilis and related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131799  Cd Length: 231  Bit Score: 42.10  E-value: 5.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51316479   432 AGSMVLDVCCGTGTIGLALARKV---KRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDL 492
Cdd:TIGR02752  45 AGTSALDVCCGTADWSIALAEAVgpeGHVIGLDFSENMLSVGRQKVKDAGLHNVELVHGNAMEL 108
RRM2_NsCP33_like cd21608
RNA recognition motif 2 (RRM2) found in Nicotiana sylvestris chloroplastic 33 kDa ...
 112-144 5.43e-04

RNA recognition motif 2 (RRM2) found in Nicotiana sylvestris chloroplastic 33 kDa ribonucleoprotein (NsCP33) and similar proteins; The family includes NsCP33, Arabidopsis thaliana chloroplastic 31 kDa ribonucleoprotein (CP31A) and mitochondrial glycine-rich RNA-binding protein 2 (AtGR-RBP2). NsCP33 may be involved in splicing and/or processing of chloroplast RNA's. AtCP31A, also called RNA-binding protein 1/2/3 (AtRBP33), or RNA-binding protein CP31A, or RNA-binding protein RNP-T, or RNA-binding protein cp31, is required for specific RNA editing events in chloroplasts and stabilizes specific chloroplast mRNAs, as well as for normal chloroplast development under cold stress conditions by stabilizing transcripts of numerous mRNAs under these conditions. CP31A may modulate telomere replication through RNA binding domains. AtGR-RBP2, also called AtRBG2, or glycine-rich protein 2 (AtGRP2), or mitochondrial RNA-binding protein 1a (At-mRBP1a), plays a role in RNA transcription or processing during stress. It binds RNAs and DNAs sequence with a preference to single-stranded nucleic acids. AtGR-RBP2 displays strong affinity to poly(U) sequence. It exerts cold and freezing tolerance, probably by exhibiting an RNA chaperone activity during the cold and freezing adaptation process. Some members in this family contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The model corresponds to the second RRM motif.


Pssm-ID: 410187 [Multi-domain]  Cd Length: 76  Bit Score: 39.07  E-value: 5.43e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 51316479 112 AFVTFRSAAERDKALRVLHGALWKGRPLSVRLA 144
Cdd:cd21608  44 GFVTFSTAEAAEAAIDALNGKELDGRSIVVNEA 76
RRM_hnRNPH_ESRPs_RBM12_like cd12254
RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein (hnRNP) H protein ...
 75-142 6.17e-04

RNA recognition motif (RRM) found in heterogeneous nuclear ribonucleoprotein (hnRNP) H protein family, epithelial splicing regulatory proteins (ESRPs), Drosophila RNA-binding protein Fusilli, RNA-binding protein 12 (RBM12) and similar proteins; The family includes RRM domains in the hnRNP H protein family, G-rich sequence factor 1 (GRSF-1), ESRPs (also termed RBM35), Drosophila Fusilli, RBM12 (also termed SWAN), RBM12B, RBM19 (also termed RBD-1) and similar proteins. The hnRNP H protein family includes hnRNP H (also termed mcs94-1), hnRNP H2 (also termed FTP-3 or hnRNP H'), hnRNP F and hnRNP H3 (also termed hnRNP 2H9), which represent a group of nuclear RNA binding proteins that are involved in pre-mRNA processing. GRSF-1 is a cytoplasmic poly(A)+ mRNA binding protein which interacts with RNA in a G-rich element-dependent manner. It may function in RNA packaging, stabilization of RNA secondary structure, or other macromolecular interactions. ESRP1 (also termed RBM35A) and ESRP2 (also termed RBM35B) are epithelial-specific RNA binding proteins that promote splicing of the epithelial variant of fibroblast growth factor receptor 2 (FGFR2), ENAH (also termed hMena), CD44 and CTNND1 (also termed p120-Catenin) transcripts. Fusilli shows high sequence homology to ESRPs. It can regulate endogenous FGFR2 splicing and functions as a splicing factor. The biological roles of both, RBM12 and RBM12B, remain unclear. RBM19 is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. Members in this family contain 2~6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains).


Pssm-ID: 409699 [Multi-domain]  Cd Length: 73  Bit Score: 38.70  E-value: 6.17e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51316479  75 LELQNVPRHASFSDVRRFLGRFGLQP--------HKTKLFGQppcAFVTFRSAAERDKALRvLHGALWKGRPLSVR 142
Cdd:cd12254   2 VRLRGLPFSATEEDIRDFFSGLDIPPdgihivydDDGRPTGE---AYVEFASEEDAQRALR-RHKGKMGGRYIEVF 73
RRM3_Prp24 cd12298
RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar ...
 111-143 6.25e-04

RNA recognition motif 3 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins; This subfamily corresponds to the RRM3 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation.


Pssm-ID: 409739 [Multi-domain]  Cd Length: 78  Bit Score: 38.78  E-value: 6.25e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 51316479 111 CAFVTFRSAAERDKALRvLHGALWKGRPLSVRL 143
Cdd:cd12298  47 FAFVTFEDADSAESALQ-LNGTLLDNRKISVSL 78
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 102-164 6.77e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.49  E-value: 6.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316479   102 KTKLFGqppcaFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKADPMARRRRQEGESEPP 164
Cdd:TIGR01628 324 VSRGFG-----FVCFSNPEEANRAVTEMHGRMLGGKPLYVALAQRKEQRRAHLQDQFMQLQPR 381
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 426-487 9.57e-04

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 40.84  E-value: 9.57e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316479 426 DWAQLDAGSMVLDVccGTGTiG-LA--LARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCG 487
Cdd:COG2518  60 EALDLKPGDRVLEI--GTGS-GyQAavLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVG 121
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
433-494 1.31e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.79  E-value: 1.31e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51316479 433 GSMVLDVCCGTGTIG-LALARKVKRVIGVELCPEAVEDARVNAQDNELS-NVEFHCGRAEDLVP 494
Cdd:COG4076  36 GDVVLDIGTGSGLLSmLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDLDL 99
RRM1_RBM28_like cd12413
RNA recognition motif 1 (RRM1) found in RNA-binding protein 28 (RBM28) and similar proteins; ...
 107-147 1.37e-03

RNA recognition motif 1 (RRM1) found in RNA-binding protein 28 (RBM28) and similar proteins; This subfamily corresponds to the RRM1 of RBM28 and Nop4p. RBM28 is a specific nucleolar component of the spliceosomal small nuclear ribonucleoproteins (snRNPs), possibly coordinating their transition through the nucleolus. It specifically associates with U1, U2, U4, U5, and U6 small nuclear RNAs (snRNAs), and may play a role in the maturation of both small nuclear and ribosomal RNAs. RBM28 has four RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and an extremely acidic region between RRM2 and RRM3. The family also includes nucleolar protein 4 (Nop4p or Nop77p) encoded by YPL043W from Saccharomyces cerevisiae. It is an essential nucleolar protein involved in processing and maturation of 27S pre-rRNA and biogenesis of 60S ribosomal subunits. Nop4p also contains four RRMs.


Pssm-ID: 409847 [Multi-domain]  Cd Length: 79  Bit Score: 37.96  E-value: 1.37e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 51316479 107 GQPPC---AFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPK 147
Cdd:cd12413  36 GKDKCrgfGYVTFALAEDAQRALEEVKGKKFGGRKIKVELAKKK 79
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 433-493 1.84e-03

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 40.87  E-value: 1.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51316479  433 GSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQ-DNELSNVEFHCGRAEDLV 493
Cdd:PLN02396 132 GLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADmDPVTSTIEYLCTTAEKLA 193
RRM_FOX1_like cd12407
RNA recognition motif (RRM) found in vertebrate RNA binding protein fox-1 homologs and similar ...
 74-144 2.02e-03

RNA recognition motif (RRM) found in vertebrate RNA binding protein fox-1 homologs and similar proteins; This subfamily corresponds to the RRM of several tissue-specific alternative splicing isoforms of vertebrate RNA binding protein Fox-1 homologs, which show high sequence similarity to the Caenorhabditis elegans feminizing locus on X (Fox-1) gene encoding Fox-1 protein. RNA binding protein Fox-1 homolog 1 (RBFOX1), also termed ataxin-2-binding protein 1 (A2BP1), or Fox-1 homolog A, or hexaribonucleotide-binding protein 1 (HRNBP1), is predominantly expressed in neurons, skeletal muscle and heart. It regulates alternative splicing of tissue-specific exons by binding to UGCAUG elements. Moreover, RBFOX1 binds to the C-terminus of ataxin-2 and forms an ataxin-2/A2BP1 complex involved in RNA processing. RNA binding protein fox-1 homolog 2 (RBFOX2), also termed Fox-1 homolog B, or hexaribonucleotide-binding protein 2 (HRNBP2), or RNA-binding motif protein 9 (RBM9), or repressor of tamoxifen transcriptional activity, is expressed in ovary, whole embryo, and human embryonic cell lines in addition to neurons and muscle. RBFOX2 activates splicing of neuron-specific exons through binding to downstream UGCAUG elements. RBFOX2 also functions as a repressor of tamoxifen activation of the estrogen receptor. RNA binding protein Fox-1 homolog 3 (RBFOX3 or NeuN or HRNBP3), also termed Fox-1 homolog C, is a nuclear RNA-binding protein that regulates alternative splicing of the RBFOX2 pre-mRNA, producing a message encoding a dominant negative form of the RBFOX2 protein. Its message is detected exclusively in post-mitotic regions of embryonic brain. Like RBFOX1, both RBFOX2 and RBFOX3 bind to the hexanucleotide UGCAUG elements and modulate brain and muscle-specific splicing of exon EIIIB of fibronectin, exon N1 of c-src, and calcitonin/CGRP. Members in this family also harbor one RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains).


Pssm-ID: 409841 [Multi-domain]  Cd Length: 76  Bit Score: 37.38  E-value: 2.02e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51316479  74 KLELQNVPRHASFSDVRRFLGRFGLQPHKTKLF---GQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLA 144
Cdd:cd12407   2 RLHVSNIPFRFRDPDLRQMFGQFGTILDVEIIFnerGSKGFGFVTFANSADADRAREKLNGTVVEGRKIEVNNA 75
RRM_NOL8 cd12226
RNA recognition motif (RRM) found in nucleolar protein 8 (NOL8) and similar proteins; This ...
 84-145 3.11e-03

RNA recognition motif (RRM) found in nucleolar protein 8 (NOL8) and similar proteins; This model corresponds to the RRM of NOL8 (also termed Nop132) encoded by a novel NOL8 gene that is up-regulated in the majority of diffuse-type, but not intestinal-type, gastric cancers. Thus, NOL8 may be a good molecular target for treatment of diffuse-type gastric cancer. Also, NOL8 is a phosphorylated protein that contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), suggesting NOL8 is likely to function as a novel RNA-binding protein. It may be involved in regulation of gene expression at the post-transcriptional level or in ribosome biogenesis in cancer cells.


Pssm-ID: 409673 [Multi-domain]  Cd Length: 77  Bit Score: 36.79  E-value: 3.11e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51316479  84 ASFSDVRRFLGRFG----LQPHKTKLFGQPPCAFVTFR-SAAERDKALRVLHGALWKGRPLSVRLAR 145
Cdd:cd12226  11 ITEDDLERRFSRFGtvsdVEIIRKKDAPDRGFAYIDLRtSEAALQKCLSTLNGVKWKGSRLKIQLAK 77
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
418-471 3.39e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 39.52  E-value: 3.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 51316479 418 EVLYTVIQDWaqLDAGSMVLDVCCGTGTIGLAlARKVKR-VIGVELCPEAVEDAR 471
Cdd:COG0863 170 ELLERLILAS--SNPGDIVLDPFAGSGTTLVA-AERLGRrFIGIEIDPEYVEVAR 221
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 403-493 4.40e-03

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 38.99  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  403 RISPHAFFQVNTPAAEVLYTVIqDWAQL--DAGSMVLDVCCGTG--TIGLALARKVKRVIGVELCPEAVEDARVNAQDNE 478
Cdd:PRK00121  10 RLTKGQQRAIEELWPRLSPAPL-DWAELfgNDAPIHLEIGFGKGefLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEG 88

                         90
                 ....*....|....*
gi 51316479  479 LSNVEFHCGRAEDLV 493
Cdd:PRK00121  89 LTNLRLLCGDAVEVL 103
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
429-496 5.58e-03

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 38.44  E-value: 5.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  429 QLDAGSMVLDVCCGTGTIGLALARKVK--RVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTL 496
Cdd:PRK07402  37 RLEPDSVLWDIGAGTGTIPVEAGLLCPkgRVIAIERDEEVVNLIRRNCDRFGVKNVEVIEGSAPECLAQL 106
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 436-486 5.68e-03

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: 37.68  E-value: 5.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 51316479   436 VLDVCCGTGTIGLALARKVK--RVIGVELCPEAVEDARVNAQDNELSNVEFHC 486
Cdd:TIGR01444   2 VIDVGANIGDTSLYFARKGAegRVIAFEPLPDAYEILEENVKLNNLPNVVLLN 54
PRK06202 PRK06202
hypothetical protein; Provisional
 436-512 5.91e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 38.83  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  436 VLDVCCGTGTIGLALARKVKR------VIGVELCPEAVEDARVNAQDnelSNVEFHCGRAEDLV--PTLVSRLASQHLVA 507
Cdd:PRK06202  64 LLDIGCGGGDLAIDLARWARRdglrleVTAIDPDPRAVAFARANPRR---PGVTFRQAVSDELVaeGERFDVVTSNHFLH 140


                 ....*
gi 51316479  508 ILDPP 512
Cdd:PRK06202 141 HLDDA 145
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 436-514 6.24e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.79  E-value: 6.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316479   436 VLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDnelSNVEFHCGRAEDLVPTLVSrlASQHLVAILDPPRA 514
Cdd:pfam13489  26 VLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRF---DQFDEQEAAVPAGKFDVIV--AREVLEHVPDPPAL 99
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 428-481 7.14e-03

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: 38.79  E-value: 7.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 51316479   428 AQLDAGSMVLDVCCGTGTIGLALAR-KVKRVIGVELCPEAVEDARVNAQDNELSN 481
Cdd:pfam06325 157 RLVKPGESVLDVGCGSGILAIAALKlGAKKVVGVDIDPVAVRAAKENAELNGVEA 211
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 424-492 7.42e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.28  E-value: 7.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316479  424 IQDWAQLdAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELS-NVEFHCGRAEDL 492
Cdd:PRK07580  56 LPADGDL-TGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgNITFEVGDLESL 124
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
436-485 9.32e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 38.21  E-value: 9.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 51316479  436 VLDVCCGTGTIGLAlARK--VKRVIGVELCPEAVEDARVNAQDNelsNVEFH 485
Cdd:PRK00517 123 VLDVGCGSGILAIA-AAKlgAKKVLAVDIDPQAVEAARENAELN---GVELN 170
 
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