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Conserved domains on  [gi|171702395|dbj|BAG16270|]
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AlkB homologue 8 [Homo sapiens]

Protein Classification

DUF1891 and RRM_ALKBH8 domain-containing protein( domain architecture ID 11181630)

protein containing domains DUF1891, RRM_ALKBH8, 2OG-FeII_Oxy, and AdoMet_MTases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
 42-122 1.46e-34

RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and similar proteins; This subfamily corresponds to the RRM of ALKBH8, also termed alpha-ketoglutarate-dependent dioxygenase ABH8, or S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8, expressed in various types of human cancers. It is essential in urothelial carcinoma cell survival mediated by NOX-1-dependent ROS signals. ALKBH8 has also been identified as a tRNA methyltransferase that catalyzes methylation of tRNA to yield 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of the anticodon loop. Thus, ALKBH8 plays a crucial role in the DNA damage survival pathway through a distinct mechanism involving the regulation of tRNA modification. ALKBH8 localizes to the cytoplasm. It contains the characteristic AlkB domain that is composed of a tRNA methyltransferase motif, a motif homologous to the bacterial AlkB DNA/RNA repair enzyme, and a dioxygenase catalytic core domain encompassing cofactor-binding sites for iron and 2-oxoglutarate. In addition, unlike other AlkB homologs, ALKBH8 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal S-adenosylmethionine (SAM)-dependent methyltransferase (MT) domain.


:

Pssm-ID: 409865 [Multi-domain]  Cd Length: 80  Bit Score: 125.77  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  42 TQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEvVDDLGQKITLYLNFVE 121
Cdd:cd12431    1 TQHLVVANGGLGNGVSREQLLEVFEKYGTVEDIVMLPGKPYSFVSFKSVEEAAKAYNALNGKE-LELPQQNVPLYLSFVE 79


                 .
gi 171702395 122 K 122
Cdd:cd12431   80 K 80
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 379-505 5.97e-20

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: 86.59  E-value: 5.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 379 YEEIAGHFSSTRHtpwphIVEFLKALPsGSIVADIGCGNGKYLGI--NKELYMIGCDRSQNLVDICRER------QFQAF 450
Cdd:COG2226    1 FDRVAARYDGREA-----LLAALGLRP-GARVLDLGCGTGRLALAlaERGARVTGVDISPEMLELARERaaeaglNVEFV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 171702395 451 VCDALAVPVRSGSCDACISIAVIHHFataERRVAALQEIVRLLRPGGKALIYVWA 505
Cdd:COG2226   75 VGDAEDLPFPDGSFDLVISSFVLHHL---PDPERALAEIARVLKPGGRLVVVDFS 126
2OG-FeII_Oxy super family cl21496
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 152-334 9.69e-17

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.


The actual alignment was detected with superfamily member pfam13532:

Pssm-ID: 473886  Cd Length: 191  Bit Score: 78.90  E-value: 9.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  152 LLESVDWTEDTDNQNSQKSLKHRRVKHFGYEF---HYENNNVDKDKPLsgGLPDICESFLEKW----LRKGYIKHKPDQM 224
Cdd:pfam13532  21 LLEEGPFRQPTTQGGRPMSVRMTNCGQLGWVTdgpGYRYSGVDPVTGE--PWPPFPEALLQLAerlaAEAGYPGWSPNAC 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  225 TINQYEPGQGIPAHID-THSAFEDEIVSLSLGSEIVMDFKHPDG----IAVPvmLPRRSLLVMTGESRYLWtHGITCRKF 299
Cdd:pfam13532  99 LVNFYRDGARMGLHQDrDESGPGAPIVSLSLGASATFRFGGKSRsdptISLR--LESGDVLVMGGESRLAY-HGVPPIRR 175

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 171702395  300 DTvqaSESLksgiitsdvgdltlskRGLRTSFTFR 334
Cdd:pfam13532 176 GT---HPLL----------------GGGRINLTFR 191
ALKBH8_N pfam09004
Alkylated DNA repair protein alkB homolog 8, N-terminal; This domain is the N-terminal domain ...
 1-37 3.61e-11

Alkylated DNA repair protein alkB homolog 8, N-terminal; This domain is the N-terminal domain of Alkylated DNA repair protein alkB homolog 8 (ALKBH8) and its homologs. This domain corresponds to the basic alpha-helix located at the N-terminal of the RRM domain, which enhances its RNA binding affinity.


:

Pssm-ID: 117570  Cd Length: 38  Bit Score: 58.30  E-value: 3.61e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 171702395    1 MDSNHQSNYKLSKTEKKFLRKQIKAKH-TLLRHEGIET 37
Cdd:pfam09004   1 WTTNTTSLLKKAQQRLYFLRKLKKANHpTLFYHEGIES 38
 
Name Accession Description Interval E-value
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
 42-122 1.46e-34

RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and similar proteins; This subfamily corresponds to the RRM of ALKBH8, also termed alpha-ketoglutarate-dependent dioxygenase ABH8, or S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8, expressed in various types of human cancers. It is essential in urothelial carcinoma cell survival mediated by NOX-1-dependent ROS signals. ALKBH8 has also been identified as a tRNA methyltransferase that catalyzes methylation of tRNA to yield 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of the anticodon loop. Thus, ALKBH8 plays a crucial role in the DNA damage survival pathway through a distinct mechanism involving the regulation of tRNA modification. ALKBH8 localizes to the cytoplasm. It contains the characteristic AlkB domain that is composed of a tRNA methyltransferase motif, a motif homologous to the bacterial AlkB DNA/RNA repair enzyme, and a dioxygenase catalytic core domain encompassing cofactor-binding sites for iron and 2-oxoglutarate. In addition, unlike other AlkB homologs, ALKBH8 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal S-adenosylmethionine (SAM)-dependent methyltransferase (MT) domain.


Pssm-ID: 409865 [Multi-domain]  Cd Length: 80  Bit Score: 125.77  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  42 TQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEvVDDLGQKITLYLNFVE 121
Cdd:cd12431    1 TQHLVVANGGLGNGVSREQLLEVFEKYGTVEDIVMLPGKPYSFVSFKSVEEAAKAYNALNGKE-LELPQQNVPLYLSFVE 79


                 .
gi 171702395 122 K 122
Cdd:cd12431   80 K 80
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 379-505 5.97e-20

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: 86.59  E-value: 5.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 379 YEEIAGHFSSTRHtpwphIVEFLKALPsGSIVADIGCGNGKYLGI--NKELYMIGCDRSQNLVDICRER------QFQAF 450
Cdd:COG2226    1 FDRVAARYDGREA-----LLAALGLRP-GARVLDLGCGTGRLALAlaERGARVTGVDISPEMLELARERaaeaglNVEFV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 171702395 451 VCDALAVPVRSGSCDACISIAVIHHFataERRVAALQEIVRLLRPGGKALIYVWA 505
Cdd:COG2226   75 VGDAEDLPFPDGSFDLVISSFVLHHL---PDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 410-497 2.14e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.38  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  410 VADIGCGNGKYLGINKELY---MIGCDRSQNLVDICRER------QFQAFVCDALAVPVRSGSCDACISIAVIHHFATAE 480
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGgarVTGVDLSPEMLERARERaaeaglNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*..
gi 171702395  481 RRvAALQEIVRLLRPGG 497
Cdd:pfam13649  81 LE-AALREIARVLKPGG 96
2OG-FeII_Oxy_2 pfam13532
2OG-Fe(II) oxygenase superfamily;
152-334 9.69e-17

2OG-Fe(II) oxygenase superfamily;


Pssm-ID: 433285  Cd Length: 191  Bit Score: 78.90  E-value: 9.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  152 LLESVDWTEDTDNQNSQKSLKHRRVKHFGYEF---HYENNNVDKDKPLsgGLPDICESFLEKW----LRKGYIKHKPDQM 224
Cdd:pfam13532  21 LLEEGPFRQPTTQGGRPMSVRMTNCGQLGWVTdgpGYRYSGVDPVTGE--PWPPFPEALLQLAerlaAEAGYPGWSPNAC 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  225 TINQYEPGQGIPAHID-THSAFEDEIVSLSLGSEIVMDFKHPDG----IAVPvmLPRRSLLVMTGESRYLWtHGITCRKF 299
Cdd:pfam13532  99 LVNFYRDGARMGLHQDrDESGPGAPIVSLSLGASATFRFGGKSRsdptISLR--LESGDVLVMGGESRLAY-HGVPPIRR 175

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 171702395  300 DTvqaSESLksgiitsdvgdltlskRGLRTSFTFR 334
Cdd:pfam13532 176 GT---HPLL----------------GGGRINLTFR 191
PRK08317 PRK08317
hypothetical protein; Provisional
 407-501 6.86e-15

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 74.59  E-value: 6.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 407 GSIVADIGCGNG---KYLG--INKELYMIGCDRSQNLVDICRERQFQA-----FVC-DALAVPVRSGSCDACISIAVIHH 475
Cdd:PRK08317  20 GDRVLDVGCGPGndaRELArrVGPEGRVVGIDRSEAMLALAKERAAGLgpnveFVRgDADGLPFPDGSFDAVRSDRVLQH 99

                         90       100
                 ....*....|....*....|....*.
gi 171702395 476 FATAERrvaALQEIVRLLRPGGKALI 501
Cdd:PRK08317 100 LEDPAR---ALAEIARVLRPGGRVVV 122
ALKBH8_N pfam09004
Alkylated DNA repair protein alkB homolog 8, N-terminal; This domain is the N-terminal domain ...
 1-37 3.61e-11

Alkylated DNA repair protein alkB homolog 8, N-terminal; This domain is the N-terminal domain of Alkylated DNA repair protein alkB homolog 8 (ALKBH8) and its homologs. This domain corresponds to the basic alpha-helix located at the N-terminal of the RRM domain, which enhances its RNA binding affinity.


Pssm-ID: 117570  Cd Length: 38  Bit Score: 58.30  E-value: 3.61e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 171702395    1 MDSNHQSNYKLSKTEKKFLRKQIKAKH-TLLRHEGIET 37
Cdd:pfam09004   1 WTTNTTSLLKKAQQRLYFLRKLKKANHpTLFYHEGIES 38
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 410-501 4.55e-10

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: 57.05  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 410 VADIGCGNGKY---LGINKELYMIGCDRSQNLVDICRERQFQA-------FVCDALAVP-VRSGSCDACISIAVIHHFAt 478
Cdd:cd02440    2 VLDLGCGTGALalaLASGPGARVTGVDISPVALELARKAAAALladnvevLKGDAEELPpEADESFDVIISDPPLHHLV- 80

                         90       100
                 ....*....|....*....|...
gi 171702395 479 aERRVAALQEIVRLLRPGGKALI 501
Cdd:cd02440   81 -EDLARFLEEARRLLKPGGVLVL 102
AlkB COG3145
Alkylated DNA repair dioxygenase AlkB [Replication, recombination and repair];
226-294 1.98e-08

Alkylated DNA repair dioxygenase AlkB [Replication, recombination and repair];


Pssm-ID: 442379  Cd Length: 200  Bit Score: 54.78  E-value: 1.98e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171702395 226 INQYEPGQgipAHIDTHS------AFEDEIVSLSLGSEIVMDFKHPD--GIAVPVMLPRRSLLVMTGESRYLWTHGI 294
Cdd:COG3145  107 LNLYRDGQ---DRMGWHQddeeelGFNPPIASVSLGATRRFRFGHKErkDPTRSLPLEHGDLLVMGGPTQLAWQHGV 180
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 50-105 9.96e-04

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 37.98  E-value: 9.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171702395   50 GGLGNGVSRNQLLPVLEKCGLV-DALLMPPN----KPYSFARYRTTEESKRAYVTLNGKEV 105
Cdd:pfam00076   4 GNLPPDTTEEDLKDLFSKFGPIkSIRLVRDEtgrsKGFAFVEFEDEEDAEKAIEALNGKEL 64
 
Name Accession Description Interval E-value
RRM_ALKBH8 cd12431
RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and ...
 42-122 1.46e-34

RNA recognition motif (RRM) found in alkylated DNA repair protein alkB homolog 8 (ALKBH8) and similar proteins; This subfamily corresponds to the RRM of ALKBH8, also termed alpha-ketoglutarate-dependent dioxygenase ABH8, or S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8, expressed in various types of human cancers. It is essential in urothelial carcinoma cell survival mediated by NOX-1-dependent ROS signals. ALKBH8 has also been identified as a tRNA methyltransferase that catalyzes methylation of tRNA to yield 5-methylcarboxymethyl uridine (mcm5U) at the wobble position of the anticodon loop. Thus, ALKBH8 plays a crucial role in the DNA damage survival pathway through a distinct mechanism involving the regulation of tRNA modification. ALKBH8 localizes to the cytoplasm. It contains the characteristic AlkB domain that is composed of a tRNA methyltransferase motif, a motif homologous to the bacterial AlkB DNA/RNA repair enzyme, and a dioxygenase catalytic core domain encompassing cofactor-binding sites for iron and 2-oxoglutarate. In addition, unlike other AlkB homologs, ALKBH8 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal S-adenosylmethionine (SAM)-dependent methyltransferase (MT) domain.


Pssm-ID: 409865 [Multi-domain]  Cd Length: 80  Bit Score: 125.77  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  42 TQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEvVDDLGQKITLYLNFVE 121
Cdd:cd12431    1 TQHLVVANGGLGNGVSREQLLEVFEKYGTVEDIVMLPGKPYSFVSFKSVEEAAKAYNALNGKE-LELPQQNVPLYLSFVE 79


                 .
gi 171702395 122 K 122
Cdd:cd12431   80 K 80
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 379-505 5.97e-20

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: 86.59  E-value: 5.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 379 YEEIAGHFSSTRHtpwphIVEFLKALPsGSIVADIGCGNGKYLGI--NKELYMIGCDRSQNLVDICRER------QFQAF 450
Cdd:COG2226    1 FDRVAARYDGREA-----LLAALGLRP-GARVLDLGCGTGRLALAlaERGARVTGVDISPEMLELARERaaeaglNVEFV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 171702395 451 VCDALAVPVRSGSCDACISIAVIHHFataERRVAALQEIVRLLRPGGKALIYVWA 505
Cdd:COG2226   75 VGDAEDLPFPDGSFDLVISSFVLHHL---PDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 410-497 2.14e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 83.38  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  410 VADIGCGNGKYLGINKELY---MIGCDRSQNLVDICRER------QFQAFVCDALAVPVRSGSCDACISIAVIHHFATAE 480
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGgarVTGVDLSPEMLERARERaaeaglNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*..
gi 171702395  481 RRvAALQEIVRLLRPGG 497
Cdd:pfam13649  81 LE-AALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 412-501 2.81e-19

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 83.10  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  412 DIGCGNGKYLGINKELYM--IGCDRSQNLVDICRER----QFQAFVCDALAVPVRSGSCDACISIAVIHHFataERRVAA 485
Cdd:pfam08241   2 DVGCGTGLLTELLARLGArvTGVDISPEMLELAREKapreGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHV---EDPERA 78

                          90
                  ....*....|....*.
gi 171702395  486 LQEIVRLLRPGGKALI 501
Cdd:pfam08241  79 LREIARVLKPGGILII 94
2OG-FeII_Oxy_2 pfam13532
2OG-Fe(II) oxygenase superfamily;
152-334 9.69e-17

2OG-Fe(II) oxygenase superfamily;


Pssm-ID: 433285  Cd Length: 191  Bit Score: 78.90  E-value: 9.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  152 LLESVDWTEDTDNQNSQKSLKHRRVKHFGYEF---HYENNNVDKDKPLsgGLPDICESFLEKW----LRKGYIKHKPDQM 224
Cdd:pfam13532  21 LLEEGPFRQPTTQGGRPMSVRMTNCGQLGWVTdgpGYRYSGVDPVTGE--PWPPFPEALLQLAerlaAEAGYPGWSPNAC 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  225 TINQYEPGQGIPAHID-THSAFEDEIVSLSLGSEIVMDFKHPDG----IAVPvmLPRRSLLVMTGESRYLWtHGITCRKF 299
Cdd:pfam13532  99 LVNFYRDGARMGLHQDrDESGPGAPIVSLSLGASATFRFGGKSRsdptISLR--LESGDVLVMGGESRLAY-HGVPPIRR 175

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 171702395  300 DTvqaSESLksgiitsdvgdltlskRGLRTSFTFR 334
Cdd:pfam13532 176 GT---HPLL----------------GGGRINLTFR 191
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 387-501 1.31e-15

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: 73.51  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 387 SSTRHTPW-PHIVEFL-KALPSGSIVADIGCGNGKYL------GINkelyMIGCDRSQNLVDICRER----QFQAFVCDA 454
Cdd:COG2227    3 DPDARDFWdRRLAALLaRLLPAGGRVLDVGCGTGRLAlalarrGAD----VTGVDISPEALEIARERaaelNVDFVQGDL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 171702395 455 LAVPVRSGSCDACISIAVIHHFATAErrvAALQEIVRLLRPGGKALI 501
Cdd:COG2227   79 EDLPLEDGSFDLVICSEVLEHLPDPA---ALLRELARLLKPGGLLLL 122
PRK08317 PRK08317
hypothetical protein; Provisional
 407-501 6.86e-15

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 74.59  E-value: 6.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 407 GSIVADIGCGNG---KYLG--INKELYMIGCDRSQNLVDICRERQFQA-----FVC-DALAVPVRSGSCDACISIAVIHH 475
Cdd:PRK08317  20 GDRVLDVGCGPGndaRELArrVGPEGRVVGIDRSEAMLALAKERAAGLgpnveFVRgDADGLPFPDGSFDAVRSDRVLQH 99

                         90       100
                 ....*....|....*....|....*.
gi 171702395 476 FATAERrvaALQEIVRLLRPGGKALI 501
Cdd:PRK08317 100 LEDPAR---ALAEIARVLRPGGRVVV 122
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 386-509 1.04e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 70.33  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 386 FSSTRHTP-WPHIVEFLKALPSGSIVADIGCGNGKYLGINKELY---MIGCDRSQNLVDICRERQFQA-------FVCDA 454
Cdd:COG0500    5 YYSDELLPgLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFggrVIGIDLSPEAIALARARAAKAglgnvefLVADL 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 171702395 455 LA-VPVRSGSCDACISIAVIHHFAtAERRVAALQEIVRLLRPGGKALIYVWAMEQE 509
Cdd:COG0500   85 AElDPLPAESFDLVVAFGVLHHLP-PEEREALLRELARALKPGGVLLLSASDAAAA 139
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 396-503 6.29e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.88  E-value: 6.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 396 HIVEFLkALPSGSIVADIGCGNG-------KYLGINkelyMIGCDRSQNLVDICRER--------QFQAFVCDALAVPvR 460
Cdd:COG2230   42 LILRKL-GLKPGMRVLDIGCGWGglalylaRRYGVR----VTGVTLSPEQLEYARERaaeagladRVEVRLADYRDLP-A 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 171702395 461 SGSCDACISIAVIHHFATAERRvAALQEIVRLLRPGGKALIYV 503
Cdd:COG2230  116 DGQFDAIVSIGMFEHVGPENYP-AYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
372-509 2.43e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 65.79  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 372 QEYVHQVYEEIAG----HFSSTRHTPWPHIV--EFLKALPSGSI--VADIGCGNGkYLGI---NKELYMIGCDRSQNLVD 440
Cdd:COG4976    4 DAYVEALFDQYADsydaALVEDLGYEAPALLaeELLARLPPGPFgrVLDLGCGTG-LLGEalrPRGYRLTGVDLSEEMLA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171702395 441 ICRERQFQA--FVCDALAVPVRSGSCDACISIAVIHHFATAERrvaALQEIVRLLRPGGKALIYVWAMEQE 509
Cdd:COG4976   83 KAREKGVYDrlLVADLADLAEPDGRFDLIVAADVLTYLGDLAA---VFAGVARALKPGGLFIFSVEDADGS 150
ALKBH8_N pfam09004
Alkylated DNA repair protein alkB homolog 8, N-terminal; This domain is the N-terminal domain ...
 1-37 3.61e-11

Alkylated DNA repair protein alkB homolog 8, N-terminal; This domain is the N-terminal domain of Alkylated DNA repair protein alkB homolog 8 (ALKBH8) and its homologs. This domain corresponds to the basic alpha-helix located at the N-terminal of the RRM domain, which enhances its RNA binding affinity.


Pssm-ID: 117570  Cd Length: 38  Bit Score: 58.30  E-value: 3.61e-11
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 171702395    1 MDSNHQSNYKLSKTEKKFLRKQIKAKH-TLLRHEGIET 37
Cdd:pfam09004   1 WTTNTTSLLKKAQQRLYFLRKLKKANHpTLFYHEGIES 38
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
410-503 1.72e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.30  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 410 VADIGCGNGKY----LGINKELYMIGCDRSQNLVDICRER--QFQAFVCDALAVPVRsGSCDACISIAVIHHFataERRV 483
Cdd:COG4106    5 VLDLGCGTGRLtallAERFPGARVTGVDLSPEMLARARARlpNVRFVVADLRDLDPP-EPFDLVVSNAALHWL---PDHA 80

                         90       100
                 ....*....|....*....|
gi 171702395 484 AALQEIVRLLRPGGKALIYV 503
Cdd:COG4106   81 ALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 410-501 4.55e-10

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: 57.05  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 410 VADIGCGNGKY---LGINKELYMIGCDRSQNLVDICRERQFQA-------FVCDALAVP-VRSGSCDACISIAVIHHFAt 478
Cdd:cd02440    2 VLDLGCGTGALalaLASGPGARVTGVDISPVALELARKAAAALladnvevLKGDAEELPpEADESFDVIISDPPLHHLV- 80

                         90       100
                 ....*....|....*....|...
gi 171702395 479 aERRVAALQEIVRLLRPGGKALI 501
Cdd:cd02440   81 -EDLARFLEEARRLLKPGGVLVL 102
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 372-501 6.88e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 59.78  E-value: 6.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 372 QEYVHQVYEEIAGHF-------SSTRHTPWPHivEFLKAL--PSGSIVADIGCGNG-------KYLGINKElyMIGCDRS 435
Cdd:PRK00216  10 QEKVAEMFDSIAPKYdlmndllSFGLHRVWRR--KTIKWLgvRPGDKVLDLACGTGdlaialaKAVGKTGE--VVGLDFS 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 171702395 436 QNLVDICRERQFQA-------FV-CDALAVPVRSGSCDaCISIA-----VIHhfataerRVAALQEIVRLLRPGGKALI 501
Cdd:PRK00216  86 EGMLAVGREKLRDLglsgnveFVqGDAEALPFPDNSFD-AVTIAfglrnVPD-------IDKALREMYRVLKPGGRLVI 156
AlkB COG3145
Alkylated DNA repair dioxygenase AlkB [Replication, recombination and repair];
226-294 1.98e-08

Alkylated DNA repair dioxygenase AlkB [Replication, recombination and repair];


Pssm-ID: 442379  Cd Length: 200  Bit Score: 54.78  E-value: 1.98e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171702395 226 INQYEPGQgipAHIDTHS------AFEDEIVSLSLGSEIVMDFKHPD--GIAVPVMLPRRSLLVMTGESRYLWTHGI 294
Cdd:COG3145  107 LNLYRDGQ---DRMGWHQddeeelGFNPPIASVSLGATRRFRFGHKErkDPTRSLPLEHGDLLVMGGPTQLAWQHGV 180
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 412-498 1.07e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.06  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  412 DIGCGNG----KYLGINKELYMIGCDRSQNLVDICRER----------QFQAFVCDALAVPvrSGSCDACISIAVIHHFA 477
Cdd:pfam08242   2 EIGCGTGtllrALLEALPGLEYTGLDISPAALEAARERlaalgllnavRVELFQLDLGELD--PGSFDVVVASNVLHHLA 79

                          90       100
                  ....*....|....*....|.
gi 171702395  478 TaerRVAALQEIVRLLRPGGK 498
Cdd:pfam08242  80 D---PRAVLRNIRRLLKPGGV 97
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 406-530 4.19e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 47.03  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  406 SGSIVADIGCGNG-------KYLGINKElyMIGCDRSQNLVDICRER-------QFQAFVCDALAVP--VRSGSCDACIS 469
Cdd:pfam13847   3 KGMRVLDLGCGTGhlsfelaEELGPNAE--VVGIDISEEAIEKARENaqklgfdNVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 171702395  470 IAVIHHFAtaeRRVAALQEIVRLLRPGGKALI--YVWAMEQEYN-KQKSKYLRGNRNSQGKKEE 530
Cdd:pfam13847  81 NCVLNHIP---DPDKVLQEILRVLKPGGRLIIsdPDSLAELPAHvKEDSTYYAGCVGGAILKKK 141
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 397-512 2.03e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.42  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  397 IVEFLKALPSGSIVADIGCGNGKYLginKELYMIGC-----DRSQNLVDICRE-RQFQAFVCDALAVPvrSGSCDACISI 470
Cdd:pfam13489  13 LLRLLPKLPSPGRVLDFGCGTGIFL---RLLRAQGFsvtgvDPSPIAIERALLnVRFDQFDEQEAAVP--AGKFDVIVAR 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 171702395  471 AVIHHFATAERrvaALQEIVRLLRPGGKALIYVWAMEQEYNK 512
Cdd:pfam13489  88 EVLEHVPDPPA---LLRQIAALLKPGGLLLLSTPLASDEADR 126
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 400-501 2.53e-04

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: 42.48  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395 400 FLKALP--SGSIVADIGCGNGkYLGI-----NKELYMIGCDRSQNLVDICRE-------RQFQAFVCDALAvPVRSGSCD 465
Cdd:COG2813   41 LLEHLPepLGGRVLDLGCGYG-VIGLalakrNPEARVTLVDVNARAVELARAnaaanglENVEVLWSDGLS-GVPDGSFD 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 171702395 466 ACISIAVIHHFATAERRVAA--LQEIVRLLRPGGKALI 501
Cdd:COG2813  119 LILSNPPFHAGRAVDKEVAHalIADAARHLRPGGELWL 156
RRM1_hnRNPR_like cd12249
RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein R (hnRNP R) ...
 50-105 4.59e-04

RNA recognition motif 1 (RRM1) found in heterogeneous nuclear ribonucleoprotein R (hnRNP R) and similar proteins; This subfamily corresponds to the RRM1 in hnRNP R, hnRNP Q, APOBEC-1 complementation factor (ACF), and dead end protein homolog 1 (DND1). hnRNP R is a ubiquitously expressed nuclear RNA-binding protein that specifically binds mRNAs with a preference for poly(U) stretches. It has been implicated in mRNA processing and mRNA transport, and also acts as a regulator to modify binding to ribosomes and RNA translation. hnRNP Q is also a ubiquitously expressed nuclear RNA-binding protein. It has been identified as a component of the spliceosome complex, as well as a component of the apobec-1 editosome, and has been implicated in the regulation of specific mRNA transport. ACF is an RNA-binding subunit of a core complex that interacts with apoB mRNA to facilitate C to U RNA editing. It may also act as an apoB mRNA recognition factor and chaperone, and play a key role in cell growth and differentiation. DND1 is essential for maintaining viable germ cells in vertebrates. It interacts with the 3'-untranslated region (3'-UTR) of multiple messenger RNAs (mRNAs) and prevents micro-RNA (miRNA) mediated repression of mRNA. This family also includes two functionally unknown RNA-binding proteins, RBM46 and RBM47. All members in this family, except for DND1, contain three conserved RNA recognition motifs (RRMs); DND1 harbors only two RRMs.


Pssm-ID: 409695 [Multi-domain]  Cd Length: 78  Bit Score: 39.11  E-value: 4.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171702395  50 GGLGNGVSRNQLLPVLEKCGLVDA--LLMPP---NKPYSFARYRTTEESKRAYVTLNGKEV 105
Cdd:cd12249    7 GKIPRDVFEDELVPLFEKCGKIYElrLMMDFsglNRGYAFVTYTNKEAAQRAVKTLNNYEI 67
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 50-105 9.96e-04

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 37.98  E-value: 9.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 171702395   50 GGLGNGVSRNQLLPVLEKCGLV-DALLMPPN----KPYSFARYRTTEESKRAYVTLNGKEV 105
Cdd:pfam00076   4 GNLPPDTTEEDLKDLFSKFGPIkSIRLVRDEtgrsKGFAFVEFEDEEDAEKAIEALNGKEL 64
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
372-498 1.03e-03

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 41.27  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 171702395  372 QEYVHQVYEEIAGHF-------SSTRHTPWPHIVEFLKALPSGSIVADIGCGNGKYL-----GINKELYMIGCDRSQNLV 439
Cdd:pfam01209   1 EQRVGDVFSSVASKYdlmndviSFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTfglsdSAGSSGKVVGLDINENML 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 171702395  440 DICRER-------QFQAFVCDALAVPVRSGSCDaCISIAV-IHHFATaerRVAALQEIVRLLRPGGK 498
Cdd:pfam01209  81 KEGEKKakeegkyNIEFLQGNAEELPFEDDSFD-IVTISFgLRNFPD---YLKVLKEAFRVLKPGGR 143
RRM_RBM18 cd12355
RNA recognition motif (RRM) found in eukaryotic RNA-binding protein 18 and similar proteins; ...
 50-113 5.89e-03

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: 36.12  E-value: 5.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 171702395  50 GGLGNGVSRNQLLPVLEKCGLVDALLM-----PPNK----PYSFARYRTTEESKRAYVTLNGKEVvddLGQKI 113
Cdd:cd12355    5 GNLDPRLTEYHLLKLLSKYGKIKKFDFlfhktGPLKgqprGYCFVTFETKEEAEKAIECLNGKLA---LGKKL 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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