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Conserved domains on  [gi|2092989885|gb|KAG9953302|]
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FAD/NAD(P)-binding domain-containing protein, partial [Aureobasidium melanogenum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 855-951 6.45e-56

RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins; This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


:

Pssm-ID: 409707 [Multi-domain]  Cd Length: 98  Bit Score: 188.18  E-value: 6.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  855 GVIYISRIPPFMKPATLKHYLSPYGEIGRVFLTPEDPVAQKQRVRNGGNKKKSFTDGWVEFIDKKDAKAAAETLNGNIIG 934
Cdd:cd12263      1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRVAESLNNTPIG 80

                           90
                   ....*....|....*..
gi 2092989885  935 GKKGNFYHDDMWNMKYL 951
Cdd:cd12263     81 GKKRSRFRDDLWNIKYL 97
PRK08163 super family cl32270
3-hydroxybenzoate 6-monooxygenase;
7-388 2.69e-46

3-hydroxybenzoate 6-monooxygenase;


The actual alignment was detected with superfamily member PRK08163:

Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 171.37  E-value: 2.69e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    7 QRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDVrpsevgGTLLRQ-------M 79
Cdd:PRK08163     2 TKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGEIGAGIQLGPNAFSALDALGV------GEAARQravftdhL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   80 RRFDA-NGNLLHTKEFGPEDRSRWQTEWYLVHRVDLHNKLKSEATSTTRagvpVQLHLACKVTDIDLHNASVTLED--GR 156
Cdd:PRK08163    76 TMMDAvDAEEVVRIPTGQAFRARFGNPYAVIHRADIHLSLLEAVLDHPL----VEFRTSTHVVGIEQDGDGVTVFDqqGN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  157 TFNGDLLLGADGLHSFTRKRMVGEiQPYAVGKSCMRWLVSKETLLADPRTDRVSIetpgafveWSAPDRRLVAYPCGDDK 236
Cdd:PRK08163   152 RWTGDALIGCDGVKSVVRQSLVGD-APRVTGHVVYRAVIDVDDMPEDLRINAPVL--------WAGPHCHLVHYPLRGGE 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  237 IMNMCAFAPSSEFqdpenttvDEY-NTSGNMSLMLRAFKNFCPAVQaAMENSGDSLKIWDMYDMKTLPKWCEGSTAIIGD 315
Cdd:PRK08163   223 QYNLVVTFHSREQ--------EEWgVKDGSKEEVLSYFEGIHPRPR-QMLDKPTSWKRWATADREPVAKWSTGRVTLLGD 293

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092989885  316 AAHPFQPYMGQGGAMAIEDAVSVAVLLPlgTSKQEIPERLRLYEKCRKQRNETVLMYTRMNGRDEGDDSVKRM 388
Cdd:PRK08163   294 AAHPMTQYMAQGACMALEDAVTLGKALE--GCDGDAEAAFALYESVRIPRTARVVLSAREMGRIYHAKGVERQ 364
eIF3_subunit super family cl07276
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 774-853 3.77e-05

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


The actual alignment was detected with superfamily member pfam08597:

Pssm-ID: 462530  Cd Length: 239  Bit Score: 46.52  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  774 DFDDEDEEAldktsaiVKKPAPVAPKGRFelDDEDADDFVPEDDEDDNDTLEPATTSTKEKTVKPLTQKQLLKaQKAAKK 853
Cdd:pfam08597    3 DWDDEDFEP-------SSPAPPPARRDKW--DDEDEDEDVKDSWDAEEEEEEEKEKAAKAAAAKAKKKKKSKK-QKIAEK 72
 
Name Accession Description Interval E-value
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 855-951 6.45e-56

RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins; This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409707 [Multi-domain]  Cd Length: 98  Bit Score: 188.18  E-value: 6.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  855 GVIYISRIPPFMKPATLKHYLSPYGEIGRVFLTPEDPVAQKQRVRNGGNKKKSFTDGWVEFIDKKDAKAAAETLNGNIIG 934
Cdd:cd12263      1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRVAESLNNTPIG 80

                           90
                   ....*....|....*..
gi 2092989885  935 GKKGNFYHDDMWNMKYL 951
Cdd:cd12263     81 GKKRSRFRDDLWNIKYL 97
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
7-388 2.69e-46

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 171.37  E-value: 2.69e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    7 QRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDVrpsevgGTLLRQ-------M 79
Cdd:PRK08163     2 TKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGEIGAGIQLGPNAFSALDALGV------GEAARQravftdhL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   80 RRFDA-NGNLLHTKEFGPEDRSRWQTEWYLVHRVDLHNKLKSEATSTTRagvpVQLHLACKVTDIDLHNASVTLED--GR 156
Cdd:PRK08163    76 TMMDAvDAEEVVRIPTGQAFRARFGNPYAVIHRADIHLSLLEAVLDHPL----VEFRTSTHVVGIEQDGDGVTVFDqqGN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  157 TFNGDLLLGADGLHSFTRKRMVGEiQPYAVGKSCMRWLVSKETLLADPRTDRVSIetpgafveWSAPDRRLVAYPCGDDK 236
Cdd:PRK08163   152 RWTGDALIGCDGVKSVVRQSLVGD-APRVTGHVVYRAVIDVDDMPEDLRINAPVL--------WAGPHCHLVHYPLRGGE 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  237 IMNMCAFAPSSEFqdpenttvDEY-NTSGNMSLMLRAFKNFCPAVQaAMENSGDSLKIWDMYDMKTLPKWCEGSTAIIGD 315
Cdd:PRK08163   223 QYNLVVTFHSREQ--------EEWgVKDGSKEEVLSYFEGIHPRPR-QMLDKPTSWKRWATADREPVAKWSTGRVTLLGD 293

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092989885  316 AAHPFQPYMGQGGAMAIEDAVSVAVLLPlgTSKQEIPERLRLYEKCRKQRNETVLMYTRMNGRDEGDDSVKRM 388
Cdd:PRK08163   294 AAHPMTQYMAQGACMALEDAVTLGKALE--GCDGDAEAAFALYESVRIPRTARVVLSAREMGRIYHAKGVERQ 364
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 11-378 3.97e-41

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 154.33  E-value: 3.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDVRPS-EVGGTLLRQMR-RFDANGNL 88
Cdd:COG0654      5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRlLARGAPIRGIRvRDGSDGRV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   89 LHTKEFGPEDRSrwqtEWYLVHRVDLHNKLKSEAtsttrAGVPVQLHLACKVTDIDLHN--ASVTLEDGRTFNGDLLLGA 166
Cdd:COG0654     85 LARFDAAETGLP----AGLVVPRADLERALLEAA-----RALGVELRFGTEVTGLEQDAdgVTVTLADGRTLRADLVVGA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  167 DGLHSFTRKRMvgeiqpyavgkscmrwlvsketlladprtdrvsietPGAFVEWSAPDRRLVAypcgddkimnmcafaps 246
Cdd:COG0654    156 DGARSAVRRLL------------------------------------GIGFTGRDYPQRALWA----------------- 182

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  247 sefqdpeNTTVDeyntsgnmslMLRAFKNFCPAVQAAMENSGDSlkIWdMYDMKTLPKWCEGSTAIIGDAAHPFQPYMGQ 326
Cdd:COG0654    183 -------GVRTE----------LRARLAAAGPRLGELLELSPRS--AF-PLRRRRAERWRRGRVVLLGDAAHTMHPLGGQ 242

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092989885  327 GGAMAIEDAVSVAVLLPLGTSKQEIPERLRLYEKCRKQRNETVLMYTRMNGR 378
Cdd:COG0654    243 GANLALRDAAALAWKLAAALRGRDDEAALARYERERRPRAARVQRAADALGR 294
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 11-373 1.74e-08

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 57.72  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDV--------RPSEVGGTLLRQMRRF 82
Cdd:pfam01494    3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLedrilaegVPHEGMGLAFYNTRRR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   83 dangnLLHTKEFGPEDrsrwqteWYLVHRVDLHNKLKSEATSTtragvPVQLHLACKVTDIDLHNASVT-----LEDG-- 155
Cdd:pfam01494   83 -----ADLDFLTSPPR-------VTVYPQTELEPILVEHAEAR-----GAQVRFGTEVLSLEQDGDGVTavvrdRRDGee 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  156 RTFNGDLLLGADGLHSFTRKRmVGeIQPYAVGKSCMRWL--VSKETLLADPRTDRVSIETPGAfvewsAPDRRLVAYPCG 233
Cdd:pfam01494  146 YTVRAKYLVGCDGGRSPVRKT-LG-IEFEGFEGVPFGSLdvLFDAPDLSDPVERAFVHYLIYA-----PHSRGFMVGPWR 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  234 DDKIMNMCAFAPSSEFQD--PENTTVDEYNTsgnmsLMLRAFknfcpaVQAAMENSGDSLKIWDMYDMkTLPKWCEGSTA 311
Cdd:pfam01494  219 SAGRERYYVQVPWDEEVEerPEEFTDEELKQ-----RLRSIV------GIDLALVEILWKSIWGVASR-VATRYRKGRVF 286

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092989885  312 IIGDAAHPFQPYMGQGGAMAIEDAVSVAVLLPLGTSKQEIPERLRLYEKCRKQRNETVLMYT 373
Cdd:pfam01494  287 LAGDAAHIHPPTGGQGLNTAIQDAFNLAWKLAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
RRM smart00360
RNA recognition motif;
856-937 6.23e-08

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 50.67  E-value: 6.23e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   856 VIYISRIPPFMKPATLKHYLSPYGEIGRVfltpedpvaqkqRVRNGGNKKKSFTDGWVEFIDKKDAKAAAETLNGNIIGG 935
Cdd:smart00360    1 TLFVGNLPPDTTEEELRELFSKFGKVESV------------RLVRDKETGKSKGFAFVEFESEEDAEKALEALNGKELDG 68


                    ..
gi 2092989885   936 KK 937
Cdd:smart00360   69 RP 70
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 857-937 2.41e-07

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: 48.77  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtpedpvaqkqrVRNGGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:pfam00076    1 LFVGNLPPDTTEEDLKDLFSKFGPIKSIRL-----------VRDETGRSKGF--AFVEFEDEEDAEKAIEALNGKELGGR 67


                   .
gi 2092989885  937 K 937
Cdd:pfam00076   68 E 68
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 8-41 1.51e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 45.96  E-value: 1.51e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2092989885     8 RPLKVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:smart01002   19 PPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVR 52
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 774-853 3.77e-05

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 46.52  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  774 DFDDEDEEAldktsaiVKKPAPVAPKGRFelDDEDADDFVPEDDEDDNDTLEPATTSTKEKTVKPLTQKQLLKaQKAAKK 853
Cdd:pfam08597    3 DWDDEDFEP-------SSPAPPPARRDKW--DDEDEDEDVKDSWDAEEEEEEEKEKAAKAAAAKAKKKKKSKK-QKIAEK 72
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 802-987 1.67e-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: 45.57  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  802 FElDDEDADDFVpeddeddnDTLEPATTSTKEKTVKPLTQKQLLKAQKAAKKTGViYISRIPPFMKPATLKHYLSPYGEI 881
Cdd:TIGR01628  136 FE-KEESAKAAI--------QKVNGMLLNDKEVYVGRFIKKHEREAAPLKKFTNL-YVKNLDPSVNEDKLRELFAKFGEI 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  882 grvfltpedpVAQKQRvRNGGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGKKgnfyhddmwnmkylTGFKwshLTE 961
Cdd:TIGR01628  206 ----------TSAAVM-KDGSGRSRGF--AFVNFEKHEDAAKAVEEMNGKKIGLAK--------------EGKK---LYV 255

                          170       180
                   ....*....|....*....|....*.
gi 2092989885  962 QIANENAERAARLRAEVARTRRENKS 987
Cdd:TIGR01628  256 GRAQKRAEREAELRRKFEELQQERKM 281
COG5644 COG5644
U3 small nucleolar RNA-associated protein 14 [Function unknown];
736-841 5.06e-03

U3 small nucleolar RNA-associated protein 14 [Function unknown];


Pssm-ID: 227931 [Multi-domain]  Cd Length: 869  Bit Score: 40.84  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  736 LSDEEEDAGYNSEEQEESR------GARSIKRRRVEQDSDndsqdFDDEDEE-----ALDKTSAIVKKPAPVAPKGRFEL 804
Cdd:COG5644     22 HSYEEESAGFDSEELEDNDeqgysfGVNSEDDEEIDSDEA-----FDEEDEKrfadwSFNASKSGKSNKDHKNLNNTKEI 96

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2092989885  805 DDEDADDFVPEDDEDDndtlEPATTSTKEKTVKPLTQ 841
Cdd:COG5644     97 SLNDSDDSVNSDKLEN----EGSVSSIDENELVDLDT 129
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 11-50 5.10e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 40.25  E-value: 5.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVL----ERSRFAVETGAA 50
Cdd:cd08261    162 TVLVVGAGPIGLGVIQVAKARGARVIVVdiddERLEFARELGAD 205
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 11-39 8.97e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 39.90  E-value: 8.97e-03
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLE 39
Cdd:TIGR03026    2 KIAVIGLGYVGLPLAALLADLGHDVTGVD 30
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
857-937 9.38e-03

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


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 36.23  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtPEDpvaqkqrvRNGGnKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:COG0724      4 IYVGNLPYSVTEEDLRELFSEYGEVTSVKL-ITD--------RETG-RSRGF--GFVEMPDDEEAQAAIEALNGAELMGR 71


                   .
gi 2092989885  937 K 937
Cdd:COG0724     72 T 72
 
Name Accession Description Interval E-value
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 855-951 6.45e-56

RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar proteins; This subfamily corresponds to the RRM of novel nuclear proteins termed ABT1 and its homologous counterpart, pre-rRNA-processing protein ESF2 (eighteen S factor 2), from yeast. ABT1 associates with the TATA-binding protein (TBP) and enhances basal transcription activity of class II promoters. Meanwhile, ABT1 could be a transcription cofactor that can bind to DNA in a sequence-independent manner. The yeast ABT1 homolog, ESF2, is a component of 90S preribosomes and 5' ETS-based RNPs. It is previously identified as a putative partner of the TATA-element binding protein. However, it is primarily localized to the nucleolus and physically associates with pre-rRNA processing factors. ESF2 may play a role in ribosome biogenesis. It is required for normal pre-rRNA processing, as well as for SSU processome assembly and function. Both ABT1 and ESF2 contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409707 [Multi-domain]  Cd Length: 98  Bit Score: 188.18  E-value: 6.45e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  855 GVIYISRIPPFMKPATLKHYLSPYGEIGRVFLTPEDPVAQKQRVRNGGNKKKSFTDGWVEFIDKKDAKAAAETLNGNIIG 934
Cdd:cd12263      1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRVAESLNNTPIG 80

                           90
                   ....*....|....*..
gi 2092989885  935 GKKGNFYHDDMWNMKYL 951
Cdd:cd12263     81 GKKRSRFRDDLWNIKYL 97
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
7-388 2.69e-46

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 171.37  E-value: 2.69e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    7 QRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDVrpsevgGTLLRQ-------M 79
Cdd:PRK08163     2 TKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIGEIGAGIQLGPNAFSALDALGV------GEAARQravftdhL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   80 RRFDA-NGNLLHTKEFGPEDRSRWQTEWYLVHRVDLHNKLKSEATSTTRagvpVQLHLACKVTDIDLHNASVTLED--GR 156
Cdd:PRK08163    76 TMMDAvDAEEVVRIPTGQAFRARFGNPYAVIHRADIHLSLLEAVLDHPL----VEFRTSTHVVGIEQDGDGVTVFDqqGN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  157 TFNGDLLLGADGLHSFTRKRMVGEiQPYAVGKSCMRWLVSKETLLADPRTDRVSIetpgafveWSAPDRRLVAYPCGDDK 236
Cdd:PRK08163   152 RWTGDALIGCDGVKSVVRQSLVGD-APRVTGHVVYRAVIDVDDMPEDLRINAPVL--------WAGPHCHLVHYPLRGGE 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  237 IMNMCAFAPSSEFqdpenttvDEY-NTSGNMSLMLRAFKNFCPAVQaAMENSGDSLKIWDMYDMKTLPKWCEGSTAIIGD 315
Cdd:PRK08163   223 QYNLVVTFHSREQ--------EEWgVKDGSKEEVLSYFEGIHPRPR-QMLDKPTSWKRWATADREPVAKWSTGRVTLLGD 293

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2092989885  316 AAHPFQPYMGQGGAMAIEDAVSVAVLLPlgTSKQEIPERLRLYEKCRKQRNETVLMYTRMNGRDEGDDSVKRM 388
Cdd:PRK08163   294 AAHPMTQYMAQGACMALEDAVTLGKALE--GCDGDAEAAFALYESVRIPRTARVVLSAREMGRIYHAKGVERQ 364
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 11-378 3.97e-41

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 154.33  E-value: 3.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDVRPS-EVGGTLLRQMR-RFDANGNL 88
Cdd:COG0654      5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWDRlLARGAPIRGIRvRDGSDGRV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   89 LHTKEFGPEDRSrwqtEWYLVHRVDLHNKLKSEAtsttrAGVPVQLHLACKVTDIDLHN--ASVTLEDGRTFNGDLLLGA 166
Cdd:COG0654     85 LARFDAAETGLP----AGLVVPRADLERALLEAA-----RALGVELRFGTEVTGLEQDAdgVTVTLADGRTLRADLVVGA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  167 DGLHSFTRKRMvgeiqpyavgkscmrwlvsketlladprtdrvsietPGAFVEWSAPDRRLVAypcgddkimnmcafaps 246
Cdd:COG0654    156 DGARSAVRRLL------------------------------------GIGFTGRDYPQRALWA----------------- 182

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  247 sefqdpeNTTVDeyntsgnmslMLRAFKNFCPAVQAAMENSGDSlkIWdMYDMKTLPKWCEGSTAIIGDAAHPFQPYMGQ 326
Cdd:COG0654    183 -------GVRTE----------LRARLAAAGPRLGELLELSPRS--AF-PLRRRRAERWRRGRVVLLGDAAHTMHPLGGQ 242

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092989885  327 GGAMAIEDAVSVAVLLPLGTSKQEIPERLRLYEKCRKQRNETVLMYTRMNGR 378
Cdd:COG0654    243 GANLALRDAAALAWKLAAALRGRDDEAALARYERERRPRAARVQRAADALGR 294
PRK06753 PRK06753
hypothetical protein; Provisional
 10-378 3.61e-38

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 147.14  E-value: 3.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDVRPS-EVGGTLLRQMRRFDANGNL 88
Cdd:PRK06753     1 MKIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVKEVGAGIGIGDNVIKKLGNHDLAKGiKNAGQILSTMNLLDDKGTL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   89 LHTKEFgpedrsRWQTEWYLVHRVDLHNKLKSEATSTTragvpvqLHLACKVTDIDLHNASVTL--EDGRTFNGDLLLGA 166
Cdd:PRK06753    81 LNKVKL------KSNTLNVTLHRQTLIDIIKSYVKEDA-------IFTGKEVTKIENETDKVTIhfADGESEAFDLCIGA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  167 DGLHSFTRKRMVGEIQPYAVGKSCMRWLVsketlladprtDRVSIETPGAFVEWSAPDRRLVAYPCGDDKIMnmcAFAP- 245
Cdd:PRK06753   148 DGIHSKVRQSVNADSKVRYQGYTCFRGLI-----------DDIDLKLPDCAKEYWGTKGRFGIVPLLNNQAY---WFITi 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  246 SSEFQDPenttvdEYNTSGNMSLMLRaFKNFCPAVQAAMEN-SGDSLKIWDMYDMKTLPKWCEGSTAIIGDAAHPFQPYM 324
Cdd:PRK06753   214 NAKERDP------KYSSFGKPHLQAY-FNHYPNEVREILDKqSETGILHHDIYDLKPLKSFVYGRIVLLGDAAHATTPNM 286

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2092989885  325 GQGGAMAIEDAVSVAVLLplgtSKQEIPERLRLYEKCRKQRNETVLMYTRMNGR 378
Cdd:PRK06753   287 GQGAGQAMEDAIVLANCL----NAYDFEKALQRYDKIRVKHTAKVIKRSRKIGK 336
PRK06475 PRK06475
FAD-binding protein;
5-365 3.71e-28

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 118.39  E-value: 3.71e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    5 IEQRPLkvtIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDV--RPSEVGGT--LLRQMR 80
Cdd:PRK06475     1 TRGSPL---IAGAGVAGLSAALELAARGWAVTIIEKAQELSEVGAGLQLAPNAMRHLERLGVadRLSGTGVTpkALYLMD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   81 RFDANgNLLHTKeFGPEDRSRWQTEWYLVHRVDLHNKLkseaTSTTRAGVPVQLHLACKVTDIDLHNASVTLEDGRT--- 157
Cdd:PRK06475    78 GRKAR-PLLAMQ-LGDLARKRWHHPYIVCHRADLQSAL----LDACRNNPGIEIKLGAEMTSQRQTGNSITATIIRTnsv 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  158 --FNGDLLLGADGLHS-------FTRKRMVGEIQpyavgkscmrWlvsKETLLAD--PRTDRVSIETPGAFVEWSAPDRR 226
Cdd:PRK06475   152 etVSAAYLIACDGVWSmlrakagFSKARFSGHIA----------W---RTTLAADalPASFLSAMPEHKAVSAWLGNKAH 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  227 LVAYPCGDDKIMNMCAFAPSsefqdpENTTvDEYNTSGNMSLMLRAFKNFCPAVQAAMEnSGDSLKIWDMYDMKTLPKWC 306
Cdd:PRK06475   219 FIAYPVKGGKFFNFVAITGG------ENPG-EVWSKTGDKAHLKSIYADWNKPVLQILA-AIDEWTYWPLFEMADAQFVG 290

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2092989885  307 EGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVAVLLPLGtskqEIPERLRLYEKCRKQR 365
Cdd:PRK06475   291 PDRTIFLGDASHAVTPFAAQGAAMAIEDAAALAEALDSD----DQSAGLKRFDSVRKER 345
PRK06847 PRK06847
hypothetical protein; Provisional
 11-395 5.36e-28

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 117.28  E-value: 5.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDV--RPSEVGGTlLRQMRRFDANGNL 88
Cdd:PRK06847     6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYGAGITLQGNALRALRELGVldECLEAGFG-FDGVDLFDPDGTL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   89 LHTKEfgpedrsrwqTEWYL---------VHRVDLHNKLkseATSTTRAGVPVqlHLACKVTDIDLHNASVT--LEDGRT 157
Cdd:PRK06847    85 LAELP----------TPRLAgddlpggggIMRPALARIL---ADAARAAGADV--RLGTTVTAIEQDDDGVTvtFSDGTT 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  158 FNGDLLLGADGLHSFTRKRMVG-EIQPYAVGKSCMRWLVsketlladPRTDRVSietpgAFVEWSAPDRRLVAYPCGDDK 236
Cdd:PRK06847   150 GRYDLVVGADGLYSKVRSLVFPdEPEPEYTGQGVWRAVL--------PRPAEVD-----RSLMYLGPTTKAGVVPLSEDL 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  237 imnMCAFAPSSEfqdPENTTVDEYNTSGNMSLMLRAFKNfcPAVQAAMENSGDSLKIwdMYD-MKTL---PKWCEGSTAI 312
Cdd:PRK06847   217 ---MYLFVTEPR---PDNPRIEPDTLAALLRELLAPFGG--PVLQELREQITDDAQV--VYRpLETLlvpAPWHRGRVVL 286

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  313 IGDAAHPFQPYMGQGGAMAIEDAVSVAVLL----PLGTSKQEIPERlRlYEKCRK-QRNETVLMYTRMNGRDEGDDS--V 385
Cdd:PRK06847   287 IGDAAHATTPHLAQGAGMAIEDAIVLAEELarhdSLEAALQAYYAR-R-WERCRMvVEASARIGRIEIEGGDKAEHAglM 364

                          410
                   ....*....|
gi 2092989885  386 KRMTDTLTQP 395
Cdd:PRK06847   365 RESMELLAQP 374
PRK07538 PRK07538
hypothetical protein; Provisional
 10-379 7.24e-25

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 108.44  E-value: 7.24e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATA------LLEWMD---VRPSEvggtllrqMR 80
Cdd:PRK07538     1 MKVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPELRPLGVGINLLPHAVRelaelgLLDALDaigIRTRE--------LA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   81 RFDANGNLLHTKEFGPEDRSRW-QtewYLVHRVDLHNKLKSEAtsTTRAGvPVQLHLACKVTDIDLHNASVTL------- 152
Cdd:PRK07538    73 YFNRHGQRIWSEPRGLAAGYDWpQ---YSIHRGELQMLLLDAV--RERLG-PDAVRTGHRVVGFEQDADVTVVflgdrag 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  153 EDGRTFNGDLLLGADGLHSFTRKRMVGEiQPYAVGKSCMRWlvsKETLLADPrtdrvsIETPGAFVEWSAPDRRLVAYPC 232
Cdd:PRK07538   147 GDLVSVRGDVLIGADGIHSAVRAQLYPD-EGPPRWNGVMMW---RGVTEAPP------FLTGRSMVMAGHLDGKLVVYPI 216

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  233 GDDK------IMNMCAFAPSSEFQDPentTVDEYNTSGNMSLMLRAFKNF------CPAVQAAMEnsgdslKIWD--MYD 298
Cdd:PRK07538   217 SEPVdadgrqLINWVAEVRVDDAGAP---RREDWNRPGDLEDFLPHFADWrfdwldVPALIRAAE------AIYEypMVD 287

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  299 MKTLPKWCEGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVAVLLplgtSKQEIPER-LRLYEKCRKQRNETVLMYTRMNG 377
Cdd:PRK07538   288 RDPLPRWTRGRVTLLGDAAHPMYPVGSNGASQAILDARALADAL----AAHGDPEAaLAAYEAERRPATAQIVLANRLNG 363


                   ..
gi 2092989885  378 RD 379
Cdd:PRK07538   364 PE 365
PRK07236 PRK07236
hypothetical protein; Provisional
 6-378 2.91e-22

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 100.38  E-value: 2.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    6 EQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVET-GAAMHMAPNATALLEWMDVRPSEVGGTLLRQMRRFDA 84
Cdd:PRK07236     3 HMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSPTELDGrGAGIVLQPELLRALAEAGVALPADIGVPSRERIYLDR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   85 NGNLLHTkefgpEDRSRWQTEWYLVHRVdLHNKLKSEatsttragvpvQLHLACKVTDI--DLHNASVTLEDGRTFNGDL 162
Cdd:PRK07236    83 DGRVVQR-----RPMPQTQTSWNVLYRA-LRAAFPAE-----------RYHLGETLVGFeqDGDRVTARFADGRRETADL 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  163 LLGADGLHSFTRKRMVGEIQP-YAvGKSCMRWLVSKETLladPRTDRVSIEtpGAFVEWSAPDRRLVAYPC-GDD----- 235
Cdd:PRK07236   146 LVGADGGRSTVRAQLLPDVRPtYA-GYVAWRGLVDEAAL---PPEARAALR--DRFTFQLGPGSHILGYPVpGEDgstep 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  236 --KIMNMCAFAPSSEFQDPENTTVDEYNTSGNMSL---MLR----------AFKNFCPAVQAAMENSGDSL--KIWDMyd 298
Cdd:PRK07236   220 gkRRYNWVWYRNAPAGEELDELLTDRDGTRRPFSVppgALRddvlaelrddAAELLAPVFAELVEATAQPFvqAIFDL-- 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  299 mkTLPKWCEGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVAvlLPLGTSKQEIPERLRLYEKCRKQRNETVLMYTRMNGR 378
Cdd:PRK07236   298 --EVPRMAFGRVALLGDAAFVARPHTAAGVAKAAADAVALA--EALAAAAGDIDAALAAWEAERLAVGAAIVARGRRLGA 373
PRK07588 PRK07588
FAD-binding domain;
10-339 1.62e-19

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 92.11  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVLER-SRFavETGAAM-HMAPNATALLEWMDVRPSEVG-GTLLRQMRRFDANG 86
Cdd:PRK07588     1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERaPEL--RTGGYMvDFWGVGYEVAKRMGITDQLREaGYQIEHVRSVDPTG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   87 NLlhTKEFGPEDRSRWQTEWYL-VHRVDLhnklkSEATSTTRAGvPVQLHLACKVTDIDLHNASV--TLEDG--RTFngD 161
Cdd:PRK07588    79 RR--KADLNVDSFRRMVGDDFTsLPRGDL-----AAAIYTAIDG-QVETIFDDSIATIDEHRDGVrvTFERGtpRDF--D 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  162 LLLGADGLHSFTRKRMVG--EIQPYAVGKSCMRWLVSKetllADPRTDRVsietpgaFVEWSAPDRRLVAYPCGDDKIMN 239
Cdd:PRK07588   149 LVIGADGLHSHVRRLVFGpeRDFEHYLGCKVAACVVDG----YRPRDERT-------YVLYNEVGRQVARVALRGDRTLF 217

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  240 McaFAPSSEFQDPENTTVDEyntsgnMSLMLRAFKNF---CPAVQAAMENSgDSLkIWDMYDMKTLPKWCEGSTAIIGDA 316
Cdd:PRK07588   218 L--FIFRAEHDNPPLTPAEE------KQLLRDQFGDVgweTPDILAALDDV-EDL-YFDVVSQIRMDRWSRGRVALVGDA 287

                          330       340
                   ....*....|....*....|...
gi 2092989885  317 AHPFQPYMGQGGAMAIEDAVSVA 339
Cdd:PRK07588   288 AACPSLLGGEGSGLAITEAYVLA 310
PLN02927 PLN02927
antheraxanthin epoxidase/zeaxanthin epoxidase
 2-375 1.20e-17

antheraxanthin epoxidase/zeaxanthin epoxidase


Pssm-ID: 178515 [Multi-domain]  Cd Length: 668  Bit Score: 88.23  E-value: 1.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    2 AVDIEQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVEtGAAMHMAP-----NATALLEWMDVRPSEvggtll 76
Cdd:PLN02927    74 AVTEKKKKSRVLVAGGGIGGLVFALAAKKKGFDVLVFEKDLSAIR-GEGKYRGPiqiqsNALAALEAIDIDVAE------ 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   77 RQMRRFDANGNLLHTKEFGPEDrsrwqtEWYLvhRVDLHNKLKSEATSTTR--AGVPVQLHLACKVTDIDLHNAS----- 149
Cdd:PLN02927   147 QVMEAGCITGDRINGLVDGISG------SWYV--KFDTFTPAASRGLPVTRviSRMTLQQILARAVGEDVIRNESnvvdf 218

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  150 --------VTLEDGRTFNGDLLLGADGLHSFTRKRMVGEIQPYAVGKSCMRWLVskETLLADprtdrvsIETPGAFVeWS 221
Cdd:PLN02927   219 edsgdkvtVVLENGQRYEGDLLVGADGIWSKVRNNLFGRSEATYSGYTCYTGIA--DFIPAD-------IESVGYRV-FL 288

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  222 APDRRLVAYPCGDDKiMNMCAF--APSSEFQDPenttvdeyntSGNMSLMLRAFKNFCPAVQAAMENSGDSLKIW-DMYD 298
Cdd:PLN02927   289 GHKQYFVSSDVGGGK-MQWYAFheEPAGGADAP----------NGMKKRLFEIFDGWCDNVLDLLHATEEDAILRrDIYD 357

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  299 MKTLPKWCEGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVAVLLPLG-------TSKQEIPERLRLYEKCRKQRNETVLM 371
Cdd:PLN02927   358 RSPGFTWGKGRVTLLGDSIHAMQPNMGQGGCMAIEDSFQLALELDEAwkqsvetNTPVDVVSSLKRYEESRRLRVAIIHA 437


                   ....
gi 2092989885  372 YTRM 375
Cdd:PLN02927   438 MARM 441
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
17-187 3.42e-17

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 83.09  E-value: 3.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   17 AGIAGLTAALALRKQGHEVTVLERSRFA---VETGAAMhmaPNATALLEWMDVRPSevggtLLRQMRRFDANGNLLHTKE 93
Cdd:COG0644      1 AGPAGSAAARRLARAGLSVLLLEKGSFPgdkICGGGLL---PRALEELEPLGLDEP-----LERPVRGARFYSPGGKSVE 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   94 FGPEdrsrwQTEWYLVHRVDLHNKLKSEAtstTRAGvpVQLHLACKVTDIDLHN--ASVTLEDGRTFNGDLLLGADGLHS 171
Cdd:COG0644     73 LPPG-----RGGGYVVDRARFDRWLAEQA---EEAG--AEVRTGTRVTDVLRDDgrVVVRTGDGEEIRADYVVDADGARS 142

                          170       180
                   ....*....|....*....|.
gi 2092989885  172 FTRKRM-----VGEIQPYAVG 187
Cdd:COG0644    143 LLARKLglkrrSDEPQDYALA 163
PRK07045 PRK07045
putative monooxygenase; Reviewed
 9-372 1.11e-14

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 77.25  E-value: 1.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    9 PLKVTIIGAGIAGLTAALALRKQGHEVTVLERsrfavetgAAMHMAPNATALLEWMDVRPSEVGGTL----LRQMRRFDA 84
Cdd:PRK07045     5 PVDVLINGSGIAGVALAHLLGARGHSVTVVER--------AARNRAQNGADLLKPSGIGVVRAMGLLddvfAAGGLRRDA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   85 NgNLLHTKE-FGPEDRSRWQTEWYLVH------RVDLHNKLKSEATsttragvpVQLHLACKVT----DIDLHNASVTLE 153
Cdd:PRK07045    77 M-RLYHDKElIASLDYRSASALGYFILipceqlRRLLLAKLDGLPN--------VRLRFETSIErierDADGTVTSVTLS 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  154 DGRTFNGDLLLGADGLHSFTRK---RMVGEIQPYAvgkSCMrwLVSKETLLADPRT-DRVSIETPGAFVEWsapdrrlva 229
Cdd:PRK07045   148 DGERVAPTVLVGADGARSMIRDdvlRMPAERVPYA---TPM--AFGTIALTDSVREcNRLYVDSNQGLAYF--------- 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  230 YPCGDDKIMNMCAFaPSSEFQDpenttvdeYNTSGNMSLMLRAFKNFC---PAVQAAMENSGDSLKIWDMYDMkTLPKWC 306
Cdd:PRK07045   214 YPIGDQATRLVVSF-PADEMQG--------YLADTTRTKLLARLNEFVgdeSADAMAAIGAGTAFPLIPLGRM-NLDRYH 283

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2092989885  307 EGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVAVLLPLGTSKQ-EIPERLRLYEKCRKQRNETVLMY 372
Cdd:PRK07045   284 KRNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGQiALADALERFERIRRPVNEAVISY 350
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 11-101 8.13e-12

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 68.71  E-value: 8.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSR-------------FAVETGAamH-MAPNATALLEWMD--------VRP 68
Cdd:COG1232      3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrvgglirtvevdgFRIDRGP--HsFLTRDPEVLELLRelglgdelVWP 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2092989885   69 SEVGGTLLRQMRRFD---ANGNLLHTKEFGPEDRSR 101
Cdd:COG1232     81 NTRKSYIYYGGKLHPlpqGPLALLRSPLLSLAGKLR 116
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 857-937 2.65e-11

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: 59.99  E-value: 2.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtpedpvaqkqrVRNGGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:cd00590      1 LFVGNLPPDTTEEDLRELFSKFGEVVSVRI-----------VRDRDGKSKGF--AFVEFESPEDAEKALEALNGTELGGR 67


                   .
gi 2092989885  937 K 937
Cdd:cd00590     68 P 68
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
7-65 4.80e-11

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 66.10  E-value: 4.80e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092989885    7 QRPLKVTIIGAGIAGLTAALALRKQGHEVTVLE-RSR--------------FAVETGaAMHMAPNATALLEWMD 65
Cdd:COG1231      5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRDRvggrvwtlrfgddgLYAELG-AMRIPPSHTNLLALAR 77
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
8-42 2.10e-10

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 63.36  E-value: 2.10e-10
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2092989885    8 RPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSR 42
Cdd:COG3380      2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSR 36
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
12-371 3.92e-10

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 63.05  E-value: 3.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMH-----MAPNATALLEWMDV-------RPSEVggtllRQM 79
Cdd:PRK07608     8 VVVVGGGLVGASLALALAQSGLRVALLAPRAPPRPADDAWDsrvyaISPSSQAFLERLGVwqaldaaRLAPV-----YDM 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   80 RRF-DANGNLlhtkEFgpedrSRWQT---------EWYLVHRVdLHNKLKSEATSTTRAGVPVQLhlackvtDIDLHNAS 149
Cdd:PRK07608    83 RVFgDAHARL----HF-----SAYQAgvpqlawivESSLIERA-LWAALRFQPNLTWFPARAQGL-------EVDPDAAT 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  150 VTLEDGRTFNGDLLLGADGLHSFTRKR--MVGEIQPYavgkscmrwlvsKET-LLADPRTDRVSIETpgAFvEWSAPDRR 226
Cdd:PRK07608   146 LTLADGQVLRADLVVGADGAHSWVRSQagIKAERRPY------------RQTgVVANFKAERPHRGT--AY-QWFRDDGI 210

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  227 LVAYPCGDDKiMNMCAFAPSSEFQDpenttvdeyntsgnmsLMLRAFKNFCPAVQAAMENS-----------GDSLKiwd 295
Cdd:PRK07608   211 LALLPLPDGH-VSMVWSARTAHADE----------------LLALSPEALAARVERASGGRlgrlecvtpaaGFPLR--- 270

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2092989885  296 mydMKTLPKWCEGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVA-VLLPLGTSKQEIPER-LRLYEkcRKQRNETVLM 371
Cdd:PRK07608   271 ---LQRVDRLVAPRVALVGDAAHLIHPLAGQGMNLGLRDVAALAdVLAGREPFRDLGDLRlLRRYE--RARREDILAL 343
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
12-175 4.93e-10

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 62.61  E-value: 4.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERsRFAVE---TGAAMHmapNATALLE----WMDVRPSevgGTLLRQMRRFDA 84
Cdd:PRK07494    10 IAVIGGGPAGLAAAIALARAGASVALVAP-EPPYAdlrTTALLG---PSIRFLErlglWARLAPH---AAPLQSMRIVDA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   85 NGNLLHTKE--FGPEDRSRWQTEWYLVHRVdLHNKLKSEATST---TRAGVPVqlhlacKVTDIDLHNASVTLEDGRTFN 159
Cdd:PRK07494    83 TGRLIRAPEvrFRAAEIGEDAFGYNIPNWL-LNRALEARVAELpniTRFGDEA------ESVRPREDEVTVTLADGTTLS 155

                          170
                   ....*....|....*.
gi 2092989885  160 GDLLLGADGLHSFTRK 175
Cdd:PRK07494   156 ARLVVGADGRNSPVRE 171
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 12-376 5.88e-10

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 62.48  E-value: 5.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLErsrfavetgaamHMAPNATALLEWMDVRPSEVGGTLLRQMRRFDANGNL--- 88
Cdd:PRK08849     6 IAVVGGGMVGAATALGFAKQGRSVAVIE------------GGEPKAFEPSQPMDIRVSAISQTSVDLLESLGAWSSIvam 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   89 -------LHTKEFgPEDRSRWQTEWYLVHRVD--LHNKLKSEATSTTRAGVPvQLHLAC--KVTDIDLHNA--SVTLEDG 155
Cdd:PRK08849    74 rvcpykrLETWEH-PECRTRFHSDELNLDQLGyiVENRLIQLGLWQQFAQYP-NLTLMCpeKLADLEFSAEgnRVTLESG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  156 RTFNGDLLLGADGLHSFTRKRMVGEIQPYAVGKSCMrwLVSKETLLAD------------PRTDRVSIETPGAFVEWSAP 223
Cdd:PRK08849   152 AEIEAKWVIGADGANSQVRQLAGIGITAWDYRQHCM--LINVETEQPQqditwqqftpsgPRSFLPLCGNQGSLVWYDSP 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  224 DRrlvaypcgddkIMNMCAFAPSSEFQDPENTTVDEyntsgnmslmLRAFKnfcpavqaaMENSGdSLKIWDMYDMKTLP 303
Cdd:PRK08849   230 KR-----------IKQLSAMNPEQLRSEILRHFPAE----------LGEIK---------VLQHG-SFPLTRRHAQQYVK 278

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092989885  304 KWCegstAIIGDAAHPFQPYMGQGGAMAIEDavsVAVLLPLGTSKQEIPER-LRLYEKCRKQRNetVLMYTRMN 376
Cdd:PRK08849   279 NNC----VLLGDAAHTINPLAGQGVNLGFKD---VDVLLAETEKQGVLNDAsFARYERRRRPDN--LLMQTGMD 343
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
12-339 1.09e-09

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 62.23  E-value: 1.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVE-------------TGAAMHMAPNATAllewmDVRPSevggtllRQ 78
Cdd:PRK06183    13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDlpravgiddealrVLQAIGLADEVLP-----HTTPN-------HG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   79 MRRFDANGNLLHTKEFGPEDRSRW-QTEWYLVHRVD--LHNKLKSEATSTTRAGvpvqlhlaCKVTDIDLHNASVTLE-- 153
Cdd:PRK06183    81 MRFLDAKGRCLAEIARPSTGEFGWpRRNAFHQPLLEavLRAGLARFPHVRVRFG--------HEVTALTQDDDGVTVTlt 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  154 --DG--RTFNGDLLLGADGLHSFTRKR----MVGEIQPYavgkscmRWLVsketllADPRTDRVSIETPGAFVeWSAPDR 225
Cdd:PRK06183   153 daDGqrETVRARYVVGCDGANSFVRRTlgvpFEDLTFPE-------RWLV------VDVLIANDPLGGPHTYQ-YCDPAR 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  226 RLVAYPCGDDKImnmcafapSSEFQDPENTTVDEYNTSGNMSLMLRAFKnfcPAV-------------QAAMENSgdslk 292
Cdd:PRK06183   219 PYTSVRLPHGRR--------RWEFMLLPGETEEQLASPENVWRLLAPWG---PTPddaelirhavytfHARVADR----- 282

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2092989885  293 iwdmydmktlpkWCEGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVA 339
Cdd:PRK06183   283 ------------WRSGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLA 317
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 11-103 1.26e-09

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 61.79  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSR-------------FAVETGAAMHMAPNAT----ALLEWMD----VRPS 69
Cdd:COG1233      5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDtpggrartferpgFRFDVGPSVLTMPGVLerlfRELGLEDylelVPLD 84

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2092989885   70 EVGGTLLRQMRRFDANGNLLHTKE----FGPEDRSRWQ 103
Cdd:COG1233     85 PAYRVPFPDGRALDLPRDLERTAAelerLFPGDAEAYR 122
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 8-44 1.55e-09

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 61.41  E-value: 1.55e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2092989885    8 RPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFA 44
Cdd:COG3349      2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRL 38
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
11-47 1.97e-09

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 60.69  E-value: 1.97e-09
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVET 47
Cdd:COG0665      4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGA 40
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 12-388 5.39e-09

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 59.40  E-value: 5.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSrfavetgaamhmAPNATaLLEWMDVRPSEVGGTLLRQMRRFDANGNLLhT 91
Cdd:PRK08850     7 VAIIGGGMVGLALAAALKESDLRIAVIEGQ------------LPEEA-LNELPDVRVSALSRSSEHILRNLGAWQGIE-A 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   92 KEFGPEDRSR-WQTewylvhrvDLHNKLKSEATSTTRAGVP-------VQLHLACKVTDID---LH-------------N 147
Cdd:PRK08850    73 RRAAPYIAMEvWEQ--------DSFARIEFDAESMAQPDLGhivenrvIQLALLEQVQKQDnvtLLmparcqsiavgesE 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  148 ASVTLEDGRTFNGDLLLGADGLHSFTRKRMVGEIQPYAVGKScmrwlvskeTLLADPRT----DRVS--IETPG---AFV 218
Cdd:PRK08850   145 AWLTLDNGQALTAKLVVGADGANSWLRRQMDIPLTHWDYGHS---------ALVANVRTvdphNSVArqIFTPQgplAFL 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  219 EWSAPdrrlvaypcgddkimNMCAFAPSSEFQDPENTTV---DEYNTSgnmslMLRAFKNFCPAVQAAMENSGDSLKiwd 295
Cdd:PRK08850   216 PMSEP---------------NMSSIVWSTEPLRAEALLAmsdEQFNKA-----LTAEFDNRLGLCEVVGERQAFPLK--- 272

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  296 mydMKTLPKWCEGSTAIIGDAAHPFQPYMGQGGAMAIEDAVSVA-VLLPLGTSKQEIPER--LRLYEKCRKQrnETVLMY 372
Cdd:PRK08850   273 ---MRYARDFVRERVALVGDAAHTIHPLAGQGVNLGLLDAASLAqEILALWQQGRDIGLKrnLRGYERWRKA--EAAKMI 347

                          410
                   ....*....|....*....
gi 2092989885  373 TRMNG-RD--EGDDSVKRM 388
Cdd:PRK08850   348 AAMQGfRDlfSGSNPAKKL 366
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 11-373 1.74e-08

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 57.72  E-value: 1.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDV--------RPSEVGGTLLRQMRRF 82
Cdd:pfam01494    3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPRAHGLNQRTMELLRQAGLedrilaegVPHEGMGLAFYNTRRR 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   83 dangnLLHTKEFGPEDrsrwqteWYLVHRVDLHNKLKSEATSTtragvPVQLHLACKVTDIDLHNASVT-----LEDG-- 155
Cdd:pfam01494   83 -----ADLDFLTSPPR-------VTVYPQTELEPILVEHAEAR-----GAQVRFGTEVLSLEQDGDGVTavvrdRRDGee 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  156 RTFNGDLLLGADGLHSFTRKRmVGeIQPYAVGKSCMRWL--VSKETLLADPRTDRVSIETPGAfvewsAPDRRLVAYPCG 233
Cdd:pfam01494  146 YTVRAKYLVGCDGGRSPVRKT-LG-IEFEGFEGVPFGSLdvLFDAPDLSDPVERAFVHYLIYA-----PHSRGFMVGPWR 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  234 DDKIMNMCAFAPSSEFQD--PENTTVDEYNTsgnmsLMLRAFknfcpaVQAAMENSGDSLKIWDMYDMkTLPKWCEGSTA 311
Cdd:pfam01494  219 SAGRERYYVQVPWDEEVEerPEEFTDEELKQ-----RLRSIV------GIDLALVEILWKSIWGVASR-VATRYRKGRVF 286

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2092989885  312 IIGDAAHPFQPYMGQGGAMAIEDAVSVAVLLPLGTSKQEIPERLRLYEKCRKQRNETVLMYT 373
Cdd:pfam01494  287 LAGDAAHIHPPTGGQGLNTAIQDAFNLAWKLAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
RRM_Nop15p cd12552
RNA recognition motif in yeast ribosome biogenesis protein 15 (Nop15p) and similar proteins; ...
 856-937 2.35e-08

RNA recognition motif in yeast ribosome biogenesis protein 15 (Nop15p) and similar proteins; This subgroup corresponds to the RRM of Nop15p, also termed nucleolar protein 15, which is encoded by YNL110C from Saccharomyces cerevisiae, and localizes to the nucleoplasm and nucleolus. Nop15p has been identified as a component of a pre-60S particle. It interacts with RNA components of the early pre-60S particles. Furthermore, Nop15p binds directly to a pre-rRNA transcript in vitro and is required for pre-rRNA processing. It functions as a ribosome synthesis factor required for the 5' to 3' exonuclease digestion that generates the 5' end of the major, short form of the 5.8S rRNA as well as for processing of 27SB to 7S pre-rRNA. Nop15p also play a specific role in cell cycle progression. Nop15p contains an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409968 [Multi-domain]  Cd Length: 77  Bit Score: 52.18  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  856 VIYISRIPPFMKPATLKHYLSPYGEIGRVfltpedpvaQKQRVRNGGNKKKSftdGWVEFIDKKDAKAAAETLNGNIIGG 935
Cdd:cd12552      1 IIYVSHLPHGFHEKELKKYFAQFGDLKNV---------RLARSKKTGNSKHY---GFLEFVNPEDAMIAQKSMNNYLLMG 68


                   ..
gi 2092989885  936 KK 937
Cdd:cd12552     69 KL 70
PRK05868 PRK05868
FAD-binding protein;
11-339 2.37e-08

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 57.30  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDV-RPSEVGGTLLRQMRRFDANGNLL 89
Cdd:PRK05868     3 TVVVSGASVAGTAAAYWLGRHGYSVTMVERHPGLRPGGQAIDVRGPALDVLERMGLlAAAQEHKTRIRGASFVDRDGNEL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   90 H-----TKEFGPEDRSRWQtewylVHRVDLHNKLKSEATSTTragvpvQLHLACKVTDIDLHNAS--VTLEDGRTFNGDL 162
Cdd:PRK05868    83 FrdtesTPTGGPVNSPDIE-----LLRDDLVELLYGATQPSV------EYLFDDSISTLQDDGDSvrVTFERAAAREFDL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  163 LLGADGLHSFTRKRMVGEIQPYavgkscMRWLVSKETLLADPRtdrvsietpgaFVE------WSAPDRRLVAYPCGDDK 236
Cdd:PRK05868   152 VIGADGLHSNVRRLVFGPEEQF------VKRLGTHAAIFTVPN-----------FLEldywqtWHYGDSTMAGVYSARNN 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  237 IMNMCAFApsseFQDPEnTTVDEYNTSGNMSLMLRAFKN---FCPAVQAAMENSGDSLkiWDMYDMKTLPKWCEGSTAII 313
Cdd:PRK05868   215 TEARAALA----FMDTE-LRIDYRDTEAQFAELQRRMAEdgwVRAQLLHYMRSAPDFY--FDEMSQILMDRWSRGRVALV 287

                          330       340
                   ....*....|....*....|....*.
gi 2092989885  314 GDAAHPFQPYMGQGGAMAIEDAVSVA 339
Cdd:PRK05868   288 GDAGYCCSPLSGQGTSVALLGAYILA 313
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
14-65 2.44e-08

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 51.38  E-value: 2.44e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2092989885   14 IIGAGIAGLTAALALRKQGHEVTVLERSR-------------FAVETGAAMHMAPNATALLEWMD 65
Cdd:pfam13450    1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDrlggnaysyrvpgYVFDYGAHIFHGSDEPNVRDLLD 65
PRK07364 PRK07364
FAD-dependent hydroxylase;
12-373 4.90e-08

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 56.57  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLER--SRFAVETGAAMHMAPNATALLE----WMDVRPSEvggTLLRQMRRFDAn 85
Cdd:PRK07364    21 VAIVGGGIVGLTLAAALKDSGLRIALIEAqpAEAAAAKGQAYALSLLSARIFEgigvWEKILPQI---GKFRQIRLSDA- 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   86 gNLLHTKEFGPEDrsrWQTEwYL----VHRVdLHNKLKSEATSTTRagvpVQLHLACKVTDIDLHNASVTLE---DG--R 156
Cdd:PRK07364    97 -DYPGVVKFQPTD---LGTE-ALgyvgEHQV-LLEALQEFLQSCPN----ITWLCPAEVVSVEYQQDAATVTleiEGkqQ 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  157 TFNGDLLLGADGLHSFTRKRMVGEIQPYAVGKSCMRWLVSKETlladPRTDrVSIET------------PG--AFVEWSA 222
Cdd:PRK07364   167 TLQSKLVVAADGARSPIRQAAGIKTKGWKYWQSCVTATVKHEA----PHND-IAYERfwpsgpfailplPGnrCQIVWTA 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  223 PDRRLVAypcgddkimnMCAFAPSSEFQDPENTTVDEYntsGNMSLMLRAFknfcpAVQAAMENSgdslkiwDMYDMKTL 302
Cdd:PRK07364   242 PHAQAKA----------LLALPEAEFLAELQQRYGDQL---GKLELLGDRF-----LFPVQLMQS-------DRYVQHRL 296

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2092989885  303 pkwcegstAIIGDAAHPFQPYMGQGGAMAIEDAVSVA-VLLPLGTSKQEIPER--LRLYEKCRKQRNETVLMYT 373
Cdd:PRK07364   297 --------ALVGDAAHCCHPVGGQGLNLGIRDAAALAqVLQTAHQRGEDIGSLavLKRYERWRKRENWLILGFT 362
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 11-44 5.13e-08

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 56.25  E-value: 5.13e-08
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRFA 44
Cdd:pfam01266    1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDP 34
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
10-373 5.47e-08

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 56.41  E-value: 5.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVLE-----RSRFAVETGAAMHMAPNATALLE----WMDVRPSEVggTLLRQMR 80
Cdd:PRK08773     7 RDAVIVGGGVVGAACALALADAGLSVALVEgreppRWQADQPDLRVYAFAADNAALLDrlgvWPAVRAARA--QPYRRMR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   81 RFDA-NGNLLHtkeFGPEDRSRWQTEWYLVHRVdLHNKLKSeatSTTRAGvpVQLHLACKVTDIDLHNASV--TLEDGRT 157
Cdd:PRK08773    85 VWDAgGGGELG---FDADTLGREQLGWIVENDL-LVDRLWA---ALHAAG--VQLHCPARVVALEQDADRVrlRLDDGRR 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  158 FNGDLLLGADGLHSFTRKRMVGEIQPYAVGKSCMRWLVSKETLLADPRTDRVSIETPGAFVEWsAPDRRLVAYPCGDDKI 237
Cdd:PRK08773   156 LEAALAIAADGAASTLRELAGLPVSRHDYAQRGVVAFVDTEHPHQATAWQRFLPTGPLALLPF-ADGRSSIVWTLPDAEA 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  238 MNMCAfapssefqdpenttVDEYNTSGNMSlmlRAFKNFCPAVQAAMENSGDSLKiwdmydMKTLPKWCEGSTAIIGDAA 317
Cdd:PRK08773   235 ERVLA--------------LDEAAFSRELT---QAFAARLGEVRVASPRTAFPLR------RQLVQQYVSGRVLTLGDAA 291

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2092989885  318 HPFQPYMGQGGAMAIEDAVSVAVLLPLGTSKQ---EIPERLRLYEKCRKQRNeTVLMYT 373
Cdd:PRK08773   292 HVVHPLAGQGVNLGLRDVAALQQLVRQAHARRadwAAPHRLQRWARTRRSDN-TVAAYG 349
RRM smart00360
RNA recognition motif;
856-937 6.23e-08

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 50.67  E-value: 6.23e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   856 VIYISRIPPFMKPATLKHYLSPYGEIGRVfltpedpvaqkqRVRNGGNKKKSFTDGWVEFIDKKDAKAAAETLNGNIIGG 935
Cdd:smart00360    1 TLFVGNLPPDTTEEELRELFSKFGKVESV------------RLVRDKETGKSKGFAFVEFESEEDAEKALEALNGKELDG 68


                    ..
gi 2092989885   936 KK 937
Cdd:smart00360   69 RP 70
PRK07233 PRK07233
hypothetical protein; Provisional
 11-41 9.44e-08

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 55.66  E-value: 9.44e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:PRK07233     1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEAD 31
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 857-937 2.41e-07

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: 48.77  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtpedpvaqkqrVRNGGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:pfam00076    1 LFVGNLPPDTTEEDLKDLFSKFGPIKSIRL-----------VRDETGRSKGF--AFVEFEDEEDAEKAIEALNGKELGGR 67


                   .
gi 2092989885  937 K 937
Cdd:pfam00076   68 E 68
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 11-50 4.22e-07

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 53.49  E-value: 4.22e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRF-AVETGAA 50
Cdd:PRK12409     3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRHRYaAMETSFA 43
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 11-40 4.58e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 53.64  E-value: 4.58e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:PRK11749   142 KVAVIGAGPAGLTAAHRLARKGYDVTIFEA 171
PRK09126 PRK09126
FAD-dependent hydroxylase;
12-179 4.83e-07

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 53.41  E-value: 4.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAM--------HMapnATALLE----WMDVRPSEVGgtLLRQM 79
Cdd:PRK09126     6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPLAALADPAFdgreialtHA---SREILQrlgaWDRIPEDEIS--PLRDA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   80 RRFdaNGNLLHTKEFGPEDRSRWQTEW----YLVHRVdLHNKLKSEATSTTRAGVPVQlhlacKVTDIDLHnASVTLEDG 155
Cdd:PRK09126    81 KVL--NGRSPFALTFDARGRGADALGYlvpnHLIRRA-AYEAVSQQDGIELLTGTRVT-----AVRTDDDG-AQVTLANG 151

                          170       180
                   ....*....|....*....|....
gi 2092989885  156 RTFNGDLLLGADGLHSFTRkRMVG 179
Cdd:PRK09126   152 RRLTARLLVAADSRFSATR-RQLG 174
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 11-40 5.22e-07

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 53.22  E-value: 5.22e-07
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:COG0493    123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEA 152
PRK00711 PRK00711
D-amino acid dehydrogenase;
11-50 6.72e-07

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 52.88  E-value: 6.72e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER-SRFAVETGAA 50
Cdd:PRK00711     2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRqPGPALETSFA 42
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
8-70 1.81e-06

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 51.66  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    8 RPLKVTIIGAGIAGLTAALALRKQgHEVTVLERS-----------------RFAVETGaam---hmaPNATALLEWMDV- 66
Cdd:COG2907      2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANdrlgghthtvdvdldgrTVPVDTGfivfnertyPNLTALFAELGVp 80


                   ....*
gi 2092989885   67 -RPSE 70
Cdd:COG2907     81 tQPSD 85
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 10-42 1.91e-06

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 51.40  E-value: 1.91e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVLERSR 42
Cdd:COG2072      7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKAD 39
RRM_NIFK_like cd12307
RNA recognition motif in nucleolar protein interacting with the FHA domain of pKI-67 (NIFK) ...
 856-937 2.10e-06

RNA recognition motif in nucleolar protein interacting with the FHA domain of pKI-67 (NIFK) and similar proteins; This subgroup corresponds to the RRM of NIFK and Nop15p. NIFK, also termed MKI67 FHA domain-interacting nucleolar phosphoprotein, or nucleolar phosphoprotein Nopp34, is a putative RNA-binding protein interacting with the forkhead associated (FHA) domain of pKi-67 antigen in a mitosis-specific and phosphorylation-dependent manner. It is nucleolar in interphase but associates with condensed mitotic chromosomes. This family also includes Saccharomyces cerevisiae YNL110C gene encoding ribosome biogenesis protein 15 (Nop15p), also termed nucleolar protein 15. Both, NIFK and Nop15p, contain an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain).


Pssm-ID: 409748 [Multi-domain]  Cd Length: 74  Bit Score: 46.41  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  856 VIYISRIPPFMKPATLKHYLSPYGEIGRVFLTpedpvaqkqRVRNGGNKKKSftdGWVEFIDKKDAKAAAETLNGNIIGG 935
Cdd:cd12307      1 VVYIGHLPHGFYEPELRKYFSQFGTVTRLRLS---------RSKKTGKSKGY---AFVEFEDPEVAKIVAETMNNYLLFE 68


                   ..
gi 2092989885  936 KK 937
Cdd:cd12307     69 RL 70
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
1-41 2.25e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 51.78  E-value: 2.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2092989885    1 MAV-------DIEQRPLKVT----IIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:COG1148    121 MAVakakllePLEPIKVPVNkralVIGGGIAGMTAALELAEQGYEVYLVEKE 172
PRK07208 PRK07208
hypothetical protein; Provisional
 11-42 3.45e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 51.04  E-value: 3.45e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSR 42
Cdd:PRK07208     6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADP 37
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 11-40 1.30e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.10  E-value: 1.30e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:PRK12771   139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEA 168
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 8-41 1.51e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 45.96  E-value: 1.51e-05
                            10        20        30
                    ....*....|....*....|....*....|....
gi 2092989885     8 RPLKVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:smart01002   19 PPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVR 52
RRM_PPIE cd12347
RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This ...
 857-936 1.78e-05

RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This subfamily corresponds to the RRM of Cyp33, also termed peptidyl-prolyl cis-trans isomerase E (PPIase E), or cyclophilin E, or rotamase E. Cyp33 is a nuclear RNA-binding cyclophilin with an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal PPIase domain. Cyp33 possesses RNA-binding activity and preferentially binds to polyribonucleotide polyA and polyU, but hardly to polyG and polyC. It binds specifically to mRNA, which can stimulate its PPIase activity. Moreover, Cyp33 interacts with the third plant homeodomain (PHD3) zinc finger cassette of the mixed lineage leukemia (MLL) proto-oncoprotein and a poly-A RNA sequence through its RRM domain. It further mediates downregulation of the expression of MLL target genes HOXC8, HOXA9, CDKN1B, and C-MYC, in a proline isomerase-dependent manner. Cyp33 also possesses a PPIase activity that catalyzes cis-trans isomerization of the peptide bond preceding a proline, which has been implicated in the stimulation of folding and conformational changes in folded and unfolded proteins. The PPIase activity can be inhibited by the immunosuppressive drug cyclosporin A.


Pssm-ID: 409783 [Multi-domain]  Cd Length: 75  Bit Score: 43.75  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtPEDPVAQKQRvrnggnkkkSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:cd12347      1 LYVGGLAEEVDEKVLHAAFIPFGDIVDIQI-PLDYETEKHR---------GF--AFVEFEEAEDAAAAIDNMNESELFGR 68
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 11-39 2.34e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 48.57  E-value: 2.34e-05
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLE 39
Cdd:PRK12814   195 KVAIIGAGPAGLTAAYYLLRKGHDVTIFD 223
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 11-41 2.79e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 47.85  E-value: 2.79e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:PRK12810   145 KVAVVGSGPAGLAAADQLARAGHKVTVFERA 175
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
 774-853 3.77e-05

Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.


Pssm-ID: 462530  Cd Length: 239  Bit Score: 46.52  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  774 DFDDEDEEAldktsaiVKKPAPVAPKGRFelDDEDADDFVPEDDEDDNDTLEPATTSTKEKTVKPLTQKQLLKaQKAAKK 853
Cdd:pfam08597    3 DWDDEDFEP-------SSPAPPPARRDKW--DDEDEDEDVKDSWDAEEEEEEEKEKAAKAAAAKAKKKKKSKK-QKIAEK 72
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
11-166 4.17e-05

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 47.05  E-value: 4.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQ---GHEVTVLERSRFavetgaaMHMAPN----ATALLEWMDVRPSevggtLLRQMRRFD 83
Cdd:COG1252      3 RIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPY-------HLFQPLlpevAAGTLSPDDIAIP-----LRELLRRAG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   84 angnllhtkefgpedrsrwqtewylvhrvdlhnklkseatsttragvpVQLHLAcKVTDIDLHNASVTLEDGRTFNGDLL 163
Cdd:COG1252     71 ------------------------------------------------VRFIQG-EVTGIDPEARTVTLADGRTLSYDYL 101


                   ....*.
gi 2092989885  164 ---LGA 166
Cdd:COG1252    102 viaTGS 107
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
11-41 4.30e-05

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 47.06  E-value: 4.30e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:COG1251    144 RVVVIGGGLIGLEAAAALRKRGLEVTVVERA 174
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 12-41 4.51e-05

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 47.14  E-value: 4.51e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:COG1053      6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKV 35
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
11-164 5.07e-05

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 47.06  E-value: 5.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGH--EVTVLersrfavetGAAMHMAPNATALlewmdvrPSEVGGTLlrqmrrfdangnl 88
Cdd:COG1251      3 RIVIIGAGMAGVRAAEELRKLDPdgEITVI---------GAEPHPPYNRPPL-------SKVLAGET------------- 53

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2092989885   89 lhtkefGPEDRSRWQTEWYLVHRVDlhnklkseatsttragvpvqLHLACKVTDIDLHNASVTLEDGRTFNGDLLL 164
Cdd:COG1251     54 ------DEEDLLLRPADFYEENGID--------------------LRLGTRVTAIDRAARTVTLADGETLPYDKLV 103
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 6-164 5.09e-05

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 46.73  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    6 EQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERsrfavetgaamhmapnATALLEWMDvrpSEVGGTLLRQMRRfdaN 85
Cdd:COG0446    121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVER----------------APRLLGVLD---PEMAALLEEELRE---H 178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   86 GnllhtkefgpedrsrwqtewylvhrvdlhnklkseatsttragvpVQLHLACKVTDIDLHN-ASVTLEDGRTFNGDLLL 164
Cdd:COG0446    179 G---------------------------------------------VELRLGETVVAIDGDDkVAVTLTDGEEIPADLVV 213
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 11-41 5.51e-05

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 46.77  E-value: 5.51e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQG--HEVTVLERS 41
Cdd:PRK11883     2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEAS 34
PLN02976 PLN02976
amine oxidase
 11-42 5.74e-05

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 47.55  E-value: 5.74e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLE-RSR 42
Cdd:PLN02976   695 KIIVVGAGPAGLTAARHLQRQGFSVTVLEaRSR 727
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
11-43 6.69e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 46.27  E-value: 6.69e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERSRF 43
Cdd:COG0492      2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP 34
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 6-40 6.89e-05

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 46.52  E-value: 6.89e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2092989885    6 EQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:PRK12770    15 PPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDK 49
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 12-40 6.99e-05

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 46.51  E-value: 6.99e-05
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:pfam00890    2 VLVIGGGLAGLAAALAAAEAGLKVAVVEK 30
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 11-40 7.02e-05

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 46.16  E-value: 7.02e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:pfam07992    2 DVVVIGGGPAGLAAALTLAQLGGKVTLIED 31
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
12-38 9.20e-05

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 46.00  E-value: 9.20e-05
                           10        20
                   ....*....|....*....|....*..
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVL 38
Cdd:PRK05329     5 VLVIGGGLAGLTAALAAAEAGKRVALV 31
PLN02487 PLN02487
zeta-carotene desaturase
 10-43 1.04e-04

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 46.33  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVLERSRF 43
Cdd:PLN02487    76 LKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPF 109
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 802-987 1.67e-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: 45.57  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  802 FElDDEDADDFVpeddeddnDTLEPATTSTKEKTVKPLTQKQLLKAQKAAKKTGViYISRIPPFMKPATLKHYLSPYGEI 881
Cdd:TIGR01628  136 FE-KEESAKAAI--------QKVNGMLLNDKEVYVGRFIKKHEREAAPLKKFTNL-YVKNLDPSVNEDKLRELFAKFGEI 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  882 grvfltpedpVAQKQRvRNGGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGKKgnfyhddmwnmkylTGFKwshLTE 961
Cdd:TIGR01628  206 ----------TSAAVM-KDGSGRSRGF--AFVNFEKHEDAAKAVEEMNGKKIGLAK--------------EGKK---LYV 255

                          170       180
                   ....*....|....*....|....*.
gi 2092989885  962 QIANENAERAARLRAEVARTRRENKS 987
Cdd:TIGR01628  256 GRAQKRAEREAELRRKFEELQQERKM 281
RRM3_I_PABPs cd12380
RNA recognition motif 3 (RRM3) found found in type I polyadenylate-binding proteins; This ...
 857-937 2.15e-04

RNA recognition motif 3 (RRM3) found found in type I polyadenylate-binding proteins; This subfamily corresponds to the RRM3 of type I poly(A)-binding proteins (PABPs), highly conserved proteins that bind to the poly(A) tail present at the 3' ends of most eukaryotic mRNAs. They have been implicated in the regulation of poly(A) tail length during the polyadenylation reaction, translation initiation, mRNA stabilization by influencing the rate of deadenylation and inhibition of mRNA decapping. The family represents type I polyadenylate-binding proteins (PABPs), including polyadenylate-binding protein 1 (PABP-1 or PABPC1), polyadenylate-binding protein 3 (PABP-3 or PABPC3), polyadenylate-binding protein 4 (PABP-4 or APP-1 or iPABP), polyadenylate-binding protein 5 (PABP-5 or PABPC5), polyadenylate-binding protein 1-like (PABP-1-like or PABPC1L), polyadenylate-binding protein 1-like 2 (PABPC1L2 or RBM32), polyadenylate-binding protein 4-like (PABP-4-like or PABPC4L), yeast polyadenylate-binding protein, cytoplasmic and nuclear (PABP or ACBP-67), and similar proteins. PABP-1 is an ubiquitously expressed multifunctional protein that may play a role in 3' end formation of mRNA, translation initiation, mRNA stabilization, protection of poly(A) from nuclease activity, mRNA deadenylation, inhibition of mRNA decapping, and mRNP maturation. Although PABP-1 is thought to be a cytoplasmic protein, it is also found in the nucleus. PABP-1 may be involved in nucleocytoplasmic trafficking and utilization of mRNP particles. PABP-1 contains four copies of RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), a less well conserved linker region, and a proline-rich C-terminal conserved domain (CTD). PABP-3 is a testis-specific poly(A)-binding protein specifically expressed in round spermatids. It is mainly found in mammalian and may play an important role in the testis-specific regulation of mRNA homeostasis. PABP-3 shows significant sequence similarity to PABP-1. However, it binds to poly(A) with a lower affinity than PABP-1. PABP-1 possesses an A-rich sequence in its 5'-UTR and allows binding of PABP and blockage of translation of its own mRNA. In contrast, PABP-3 lacks the A-rich sequence in its 5'-UTR. PABP-4 is an inducible poly(A)-binding protein (iPABP) that is primarily localized to the cytoplasm. It shows significant sequence similarity to PABP-1 as well. The RNA binding properties of PABP-1 and PABP-4 appear to be identical. PABP-5 is encoded by PABPC5 gene within the X-specific subinterval, and expressed in fetal brain and in a range of adult tissues in mammalian, such as ovary and testis. It may play an important role in germ cell development. Moreover, unlike other PABPs, PABP-5 contains only four RRMs, but lacks both the linker region and the CTD. PABP-1-like and PABP-1-like 2 are the orthologs of PABP-1. PABP-4-like is the ortholog of PABP-5. Their cellular functions remain unclear. The family also includes the yeast PABP, a conserved poly(A) binding protein containing poly(A) tails that can be attached to the 3'-ends of mRNAs. The yeast PABP and its homologs may play important roles in the initiation of translation and in mRNA decay. Like vertebrate PABP-1, the yeast PABP contains four RRMs, a linker region, and a proline-rich CTD as well. The first two RRMs are mainly responsible for specific binding to poly(A). The proline-rich region may be involved in protein-protein interactions.


Pssm-ID: 409814 [Multi-domain]  Cd Length: 80  Bit Score: 41.01  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtpedpvaqkqrVRNGGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:cd12380      4 VYVKNFGEDVDDDELKELFEKYGKITSAKV-----------MKDDSGKSKGF--GFVNFENHEAAQKAVEELNGKELNGK 70


                   .
gi 2092989885  937 K 937
Cdd:cd12380     71 K 71
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 11-175 2.34e-04

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 44.79  E-value: 2.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER-SRFAVEtgaamhMAPNATALLEWMdVRpsevggtLLRQM---RRFDANG 86
Cdd:PRK08243     4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLERrSREYVE------GRIRAGVLEQGT-VD-------LLREAgvgERMDREG 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   87 NLLHTKEFGPEDRSrwqtewylvHRVDLHnKLKSEATST---------------TRAGVP-------VQLHlackvtDID 144
Cdd:PRK08243    70 LVHDGIELRFDGRR---------HRIDLT-ELTGGRAVTvygqtevtrdlmaarLAAGGPirfeasdVALH------DFD 133

                          170       180       190
                   ....*....|....*....|....*....|....
gi 2092989885  145 LHNASVTLE-DGRTF--NGDLLLGADGLHSFTRK 175
Cdd:PRK08243   134 SDRPYVTYEkDGEEHrlDCDFIAGCDGFHGVSRA 167
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 11-41 2.64e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 40.65  E-value: 2.64e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:pfam00070    1 RVVVVGGGYIGLELAGALARLGSKVTVVERR 31
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
14-40 2.85e-04

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 44.66  E-value: 2.85e-04
                           10        20
                   ....*....|....*....|....*..
gi 2092989885   14 IIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:COG2081      2 VIGAGAAGLMAAITAAERGARVLLLEK 28
RRM_SR140 cd12223
RNA recognition motif (RRM) found in U2-associated protein SR140 and similar proteins; This ...
 857-935 2.85e-04

RNA recognition motif (RRM) found in U2-associated protein SR140 and similar proteins; This subgroup corresponds to the RRM of SR140 (also termed U2 snRNP-associated SURP motif-containing protein orU2SURP, or 140 kDa Ser/Arg-rich domain protein) which is a putative splicing factor mainly found in higher eukaryotes. Although it is initially identified as one of the 17S U2 snRNP-associated proteins, the molecular and physiological function of SR140 remains unclear. SR140 contains an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), a SWAP/SURP domain that is found in a number of pre-mRNA splicing factors in the middle region, and a C-terminal arginine/serine-rich domain (RS domain).


Pssm-ID: 409670 [Multi-domain]  Cd Length: 84  Bit Score: 40.74  E-value: 2.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRV-FLTPEDPvAQKQRVRNGGnkkksftdgWVEFIDKKDAKAAAETLNGNIIGG 935
Cdd:cd12223      4 LYVGNLPPSVTEEVLLREFGRFGPLASVkIMWPRTE-EERRRNRNCG---------FVAFMSRADAERAMRELNGKDVMG 73
RRM1_RBM28_like cd12413
RNA recognition motif 1 (RRM1) found in RNA-binding protein 28 (RBM28) and similar proteins; ...
 857-937 2.86e-04

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: 40.27  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtpedpvaqkqrVRNGGNKK-KSFtdGWVEFIDKKDAKAAAETLNGNIIGG 935
Cdd:cd12413      2 LFVRNLPYDTTDEQLEELFSDVGPVKRCFV-----------VKDKGKDKcRGF--GYVTFALAEDAQRALEEVKGKKFGG 68


                   ..
gi 2092989885  936 KK 937
Cdd:cd12413     69 RK 70
RRM2_EAR1_like cd12527
RNA recognition motif 2 (RRM2) found in terminal EAR1-like proteins; This subgroup corresponds ...
 855-937 3.16e-04

RNA recognition motif 2 (RRM2) found in terminal EAR1-like proteins; This subgroup corresponds to the RRM2 of terminal EAR1-like proteins, including terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) found in land plants. They may play a role in the regulation of leaf initiation. The terminal EAR1-like proteins are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and TEL characteristic motifs that allow sequence and putative functional discrimination between the terminal EAR1-like proteins and Mei2-like proteins.


Pssm-ID: 409947 [Multi-domain]  Cd Length: 71  Bit Score: 40.21  E-value: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  855 GVIYISRIPPFMKPATLKHYLSPYGEIGRVfltPEDPVAQKQRvrnggnkkksftdgWVEFIDKKDAKAAAETLNGNIIG 934
Cdd:cd12527      2 GSLVILNLLPAVSSFTLREIFQVYGDVKDV---RETPLKPSQR--------------FVEFFDVRDAARALHEMNGKEIF 64


                   ...
gi 2092989885  935 GKK 937
Cdd:cd12527     65 GKR 67
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
12-38 3.17e-04

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 44.40  E-value: 3.17e-04
                           10        20
                   ....*....|....*....|....*..
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVL 38
Cdd:COG3075      5 VVVIGGGLAGLTAAIRAAEAGLRVAIV 31
PRK08401 PRK08401
L-aspartate oxidase; Provisional
 10-38 3.39e-04

L-aspartate oxidase; Provisional


Pssm-ID: 236259 [Multi-domain]  Cd Length: 466  Bit Score: 44.41  E-value: 3.39e-04
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   10 LKVTIIGAGIAGLTAALALRKQGHEVTVL 38
Cdd:PRK08401     2 MKVGIVGGGLAGLTAAISLAKKGFDVTII 30
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-41 3.70e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 43.85  E-value: 3.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2092989885    6 EQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:pfam07992  149 KLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEAL 184
RRM2_NsCP33_like cd21608
RNA recognition motif 2 (RRM2) found in Nicotiana sylvestris chloroplastic 33 kDa ...
 857-936 3.77e-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: 39.84  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLTpedpvaqkqRVRNGGnKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:cd21608      2 LYVGNLSWDTTEDDLRDLFSEFGEVESAKVI---------TDRETG-RSRGF--GFVTFSTAEAAEAAIDALNGKELDGR 69
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 12-38 4.72e-04

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 43.94  E-value: 4.72e-04
                           10        20
                   ....*....|....*....|....*..
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGhEVTVL 38
Cdd:COG0029      7 VLVIGSGIAGLSAALKLAERG-RVTLL 32
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
12-52 5.16e-04

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 43.60  E-value: 5.16e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2092989885   12 VTIIGAGIAGLTAALAL-RKQGHEVTVLERsrfavETGAAMH 52
Cdd:COG0579      7 VVIIGAGIVGLALARELsRYEDLKVLVLEK-----EDDVAQE 43
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 11-40 5.24e-04

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 44.07  E-value: 5.24e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:PRK01747   262 DAAIIGGGIAGAALALALARRGWQVTLYEA 291
PRK12831 PRK12831
putative oxidoreductase; Provisional
 5-39 5.28e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 43.85  E-value: 5.28e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2092989885    5 IEQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLE 39
Cdd:PRK12831   136 EEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFE 170
PRK06185 PRK06185
FAD-dependent oxidoreductase;
12-344 6.46e-04

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 43.31  E-value: 6.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSR-----FAVETgaaMHmaPNATALLE---WMDvRPSEVGGTLLRQMRRFD 83
Cdd:PRK06185     9 CCIVGGGPAGMMLGLLLARAGVDVTVLEKHAdflrdFRGDT---VH--PSTLELMDelgLLE-RFLELPHQKVRTLRFEI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   84 ANGNLLHTkefgpeDRSRWQTEW---YLVHRVDLHNKLKSEATS----TTRAGVPVQ--LHLACKVTDIDLHNASVTLEd 154
Cdd:PRK06185    83 GGRTVTLA------DFSRLPTPYpyiAMMPQWDFLDFLAEEASAypnfTLRMGAEVTglIEEGGRVTGVRARTPDGPGE- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  155 grtFNGDLLLGADGLHSFTRKR--MVGEIQPYAVGKSCMRwlVSKETllADPRTDRVSIEtpgafvewsaPDRRLVAYPC 232
Cdd:PRK06185   156 ---IRADLVVGADGRHSRVRALagLEVREFGAPMDVLWFR--LPREP--DDPESLMGRFG----------PGQGLIMIDR 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  233 GDDKimnMCAFA-PSSEFQDPENTTVDeyntsgnmslmlrAFKNFCPAVQAAMENSGDSLKIWDmyDMKTL-------PK 304
Cdd:PRK06185   219 GDYW---QCGYViPKGGYAALRAAGLE-------------AFRERVAELAPELADRVAELKSWD--DVKLLdvrvdrlRR 280

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 2092989885  305 W------CegstaiIGDAAHPFQPYMGQGGAMAIEDAVSVAVLL--PL 344
Cdd:PRK06185   281 WhrpgllC------IGDAAHAMSPVGGVGINLAIQDAVAAANILaePL 322
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 12-177 6.98e-04

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 43.30  E-value: 6.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALA---LRKQGHEVTVLErsrfAVETGAAMH--------------------------MAPNATALLe 62
Cdd:PRK05732     6 VIIVGGGMAGATLALAlsrLSHGGLPVALIE----AFAPESDAHpgfdaraialaagtcqqlarlgvwqaLADCATPIT- 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   63 wmDVRPSE---VGGTLLRQMR-RFDANGNLLHTKEFGpedrsrwqtewylvHRvdLHNKLKSEatsttragVPVQLHLAC 138
Cdd:PRK05732    81 --HIHVSDrghAGFVRLDAEDyGVPALGYVVELHDVG--------------QR--LFALLDKA--------PGVTLHCPA 134

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2092989885  139 KVTDI--DLHNASVTLEDGRTFNGDLLLGADGLHSFTRKRM 177
Cdd:PRK05732   135 RVANVerTQGSVRVTLDDGETLTGRLLVAADGSHSALREAL 175
PLN02268 PLN02268
probable polyamine oxidase
 12-42 7.93e-04

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 43.14  E-value: 7.93e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLE-RSR 42
Cdd:PLN02268     3 VIVIGGGIAGIAAARALHDASFKVTLLEsRDR 34
DNA_pol_phi pfam04931
DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7. ...
 738-820 1.15e-03

DNA polymerase phi; This family includes the fifth essential DNA polymerase in yeast EC:2.7.7.7. Pol5p is localized exclusively to the nucleolus and binds near or at the enhancer region of rRNA-encoding DNA repeating units.


Pssm-ID: 461488  Cd Length: 765  Bit Score: 43.00  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  738 DEEEDAGYNSEEQEESRgarsikrrrVEQDSDNDSQDFDDEDEEALDKTSAIVKKPAPVAPKGRFELDDEDADDfvpEDD 817
Cdd:pfam04931  645 DDDEEEDDDDEDDEDSE---------EDDDEDDDDEDEEDDDDEDVDEIDELRAKLAEALGEHGDDADDDDSDS---DED 712


                   ...
gi 2092989885  818 EDD 820
Cdd:pfam04931  713 MDD 715
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 3-107 1.75e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 42.33  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885    3 VDIEQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFA------VETGAAMHMApNATALLEWM-DVRPSEVGGTL 75
Cdd:PRK07803     2 TEVERHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFGkahtvmAEGGCAAAMG-NVNPKDNWQvHFRDTMRGGKF 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2092989885   76 LRQMRRFDangnlLHTKEfGPeDRSrWQTEWY 107
Cdd:PRK07803    81 LNNWRMAE-----LHAKE-AP-DRV-WELETY 104
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 19-106 1.89e-03

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 42.09  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   19 IAGLTAALALRKQGHEVTVLERS----------RFA---VETGA-AMHMA-PNATALLEwmdvrpsEVGGTLLRQMRRFD 83
Cdd:pfam01593    1 LAGLAAARELLRAGHDVTVLEARdrvggrirtvRDDgflIELGAmWFHGAqPPLLALLK-------ELGLEDRLVLPDPA 73

                           90       100
                   ....*....|....*....|....
gi 2092989885   84 ANGNLLH-TKEFGPEDRSRWQTEW 106
Cdd:pfam01593   74 PFYTVLFaGGRRYPGDFRRVPAGW 97
PRK07190 PRK07190
FAD-binding protein;
12-175 2.04e-03

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 42.11  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVETGAAMHMAPNATALLEWMDV-----------RPSEV---GGTLLR 77
Cdd:PRK07190     8 VVIIGAGPVGLMCAYLGQLCGLNTVIVDKSDGPLEVGRADALNARTLQLLELVDLfdelyplgkpcNTSSVwanGKFISR 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885   78 QMRRFDANGNLLHtKEFGPEDRSrwqtewYLVHRVDlhNKLKSEATSTTRAGVpvqlhlackVTDIDLHNAS--VTLEDG 155
Cdd:PRK07190    88 QSSWWEELEGCLH-KHFLMLGQS------YVEKLLD--DKLKEAGAAVKRNTS---------VVNIELNQAGclTTLSNG 149

                          170       180
                   ....*....|....*....|
gi 2092989885  156 RTFNGDLLLGADGLHSFTRK 175
Cdd:PRK07190   150 ERIQSRYVIGADGSRSFVRN 169
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 12-42 2.04e-03

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 41.77  E-value: 2.04e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLERSR 42
Cdd:PLN02172    13 VAVIGAGAAGLVAARELRREGHTVVVFEREK 43
HI0933_like pfam03486
HI0933-like protein;
11-40 2.08e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 41.80  E-value: 2.08e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:pfam03486    2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEK 31
RRM2_MEI2_EAR1_like cd12276
RNA recognition motif 2 (RRM2) found in Mei2-like proteins and terminal EAR1-like proteins; ...
 854-937 2.08e-03

RNA recognition motif 2 (RRM2) found in Mei2-like proteins and terminal EAR1-like proteins; This subfamily corresponds to the RRM2 of Mei2-like proteins from plant and fungi, terminal EAR1-like proteins from plant, and other eukaryotic homologs. Mei2-like proteins represent an ancient eukaryotic RNA-binding proteins family whose corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. In the fission yeast Schizosaccharomyces pombe, the Mei2 protein is an essential component of the switch from mitotic to meiotic growth. S. pombe Mei2 stimulates meiosis in the nucleus upon binding a specific non-coding RNA. The terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) are mainly found in land plants. They may play a role in the regulation of leaf initiation. All members in this family are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In addition to the RRMs, the terminal EAR1-like proteins also contain TEL characteristic motifs that allow sequence and putative functional discrimination between them and Mei2-like proteins.


Pssm-ID: 409718 [Multi-domain]  Cd Length: 71  Bit Score: 37.62  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  854 TGVIYISRIPPFMKPATLKHYLSPYGEIGRVFLTPEDPvaqKQRVrnggnkkksftdgwVEFIDKKDAKAAAETLNGNII 933
Cdd:cd12276      1 QGTLLVFNLDAPVSNDELKSLFSKFGEIKEIRPTPDKP---SQKF--------------VEFYDVRDAEAALDGLNGREL 63


                   ....
gi 2092989885  934 GGKK 937
Cdd:cd12276     64 LGGK 67
RRM2_PUF60 cd12371
RNA recognition motif 2 (RRM2) found in (U)-binding-splicing factor PUF60 and similar proteins; ...
 857-936 2.08e-03

RNA recognition motif 2 (RRM2) found in (U)-binding-splicing factor PUF60 and similar proteins; This subfamily corresponds to the RRM2 of PUF60, also termed FUSE-binding protein-interacting repressor (FBP-interacting repressor or FIR), or Ro-binding protein 1 (RoBP1), or Siah-binding protein 1 (Siah-BP1). PUF60 is an essential splicing factor that functions as a poly-U RNA-binding protein required to reconstitute splicing in depleted nuclear extracts. Its function is enhanced through interaction with U2 auxiliary factor U2AF65. PUF60 also controls human c-myc gene expression by binding and inhibiting the transcription factor far upstream sequence element (FUSE)-binding-protein (FBP), an activator of c-myc promoters. PUF60 contains two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal U2AF (U2 auxiliary factor) homology motifs (UHM) that harbors another RRM and binds to tryptophan-containing linear peptide motifs (UHM ligand motifs, ULMs) in several nuclear proteins. Research indicates that PUF60 binds FUSE as a dimer, and only the first two RRM domains participate in the single-stranded DNA recognition.


Pssm-ID: 409806 [Multi-domain]  Cd Length: 77  Bit Score: 38.04  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLTPeDPVaqkqrvrngGNKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:cd12371      3 IYVASVHPDLSEDDIKSVFEAFGKIKSCSLAP-DPE---------TGKHKGY--GFIEYENPQSAQDAIASMNLFDLGGQ 70
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 5-46 2.09e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 41.59  E-value: 2.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2092989885    5 IEQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLERSRFAVE 46
Cdd:COG0569     91 IKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVE 132
RRM_FOX1_like cd12407
RNA recognition motif (RRM) found in vertebrate RNA binding protein fox-1 homologs and similar ...
 857-937 2.45e-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: 37.76  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRV---FltpedpvaqkqrvrnggNKKKSFTDGWVEFIDKKDAKAAAETLNGNII 933
Cdd:cd12407      3 LHVSNIPFRFRDPDLRQMFGQFGTILDVeiiF-----------------NERGSKGFGFVTFANSADADRAREKLNGTVV 65


                   ....
gi 2092989885  934 GGKK 937
Cdd:cd12407     66 EGRK 69
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
12-40 3.05e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 41.32  E-value: 3.05e-03
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:COG3573      8 VIVVGAGLAGLVAAAELADAGRRVLLLDQ 36
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 12-38 3.13e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 41.49  E-value: 3.13e-03
                           10        20
                   ....*....|....*....|....*..
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVL 38
Cdd:PRK07804    19 VVVVGSGVAGLTAALAARRAGRRVLVV 45
PRK13984 PRK13984
putative oxidoreductase; Provisional
 3-39 3.21e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 41.29  E-value: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2092989885    3 VDIEQRPLKVTIIGAGIAGLTAALALRKQGHEVTVLE 39
Cdd:PRK13984   277 DEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYE 313
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 11-39 4.07e-03

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 41.27  E-value: 4.07e-03
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLE 39
Cdd:PRK12778   433 KVAVIGSGPAGLSFAGDLAKRGYDVTVFE 461
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 8-41 4.31e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 39.79  E-value: 4.31e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2092989885    8 RPLKVTIIGAGIAGLTAALALRKQGHEVTVLERS 41
Cdd:pfam01262   27 APAKVLVIGGGVAGLNAAATAKGLGAIVTILDVR 60
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 11-37 4.59e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 40.83  E-value: 4.59e-03
                           10        20
                   ....*....|....*....|....*..
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTV 37
Cdd:COG0771      6 KVLVLGLGKSGLAAARLLAKLGAEVTV 32
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
12-40 4.64e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 40.63  E-value: 4.64e-03
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   12 VTIIGAGIAGLTAALALRKQGHEVTVLER 40
Cdd:PRK08274     7 VLVIGGGNAALCAALAAREAGASVLLLEA 35
COG5644 COG5644
U3 small nucleolar RNA-associated protein 14 [Function unknown];
736-841 5.06e-03

U3 small nucleolar RNA-associated protein 14 [Function unknown];


Pssm-ID: 227931 [Multi-domain]  Cd Length: 869  Bit Score: 40.84  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  736 LSDEEEDAGYNSEEQEESR------GARSIKRRRVEQDSDndsqdFDDEDEE-----ALDKTSAIVKKPAPVAPKGRFEL 804
Cdd:COG5644     22 HSYEEESAGFDSEELEDNDeqgysfGVNSEDDEEIDSDEA-----FDEEDEKrfadwSFNASKSGKSNKDHKNLNNTKEI 96

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2092989885  805 DDEDADDFVPEDDEDDndtlEPATTSTKEKTVKPLTQ 841
Cdd:COG5644     97 SLNDSDDSVNSDKLEN----EGSVSSIDENELVDLDT 129
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 11-50 5.10e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 40.25  E-value: 5.10e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVL----ERSRFAVETGAA 50
Cdd:cd08261    162 TVLVVGAGPIGLGVIQVAKARGARVIVVdiddERLEFARELGAD 205
Trp_halogenase pfam04820
Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form ...
 11-39 5.65e-03

Tryptophan halogenase; Tryptophan halogenase catalyzes the chlorination of tryptophan to form 7-chlorotryptophan. This is the first step in the biosynthesis of pyrrolnitrin, an antibiotic with broad-spectrum anti-fungal activity. Tryptophan halogenase is NADH-dependent.


Pssm-ID: 398475 [Multi-domain]  Cd Length: 457  Bit Score: 40.39  E-value: 5.65e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQ---GHEVTVLE 39
Cdd:pfam04820    1 KIVIVGGGTAGWMAAAALARAlkgGLDVTLVE 32
PRK08013 PRK08013
oxidoreductase; Provisional
 311-408 7.44e-03

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 40.03  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  311 AIIGDAAHPFQPYMGQGGAMAIEDAVS-VAVLLPLGTSKQEIPER--LRLYEKCRKQRneTVLMYTRMNG-RD--EGDDS 384
Cdd:PRK08013   285 ALVGDAAHTIHPLAGQGVNLGFMDAAElIAELRRLHRQGKDIGQHlyLRRYERSRKHS--AALMLAGMQGfRDlfAGNNP 362

                           90       100
                   ....*....|....*....|....
gi 2092989885  385 VKRMtdtltqpLELIWLAMADPYP 408
Cdd:PRK08013   363 AKKL-------LRDIGLKLADTLP 379
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 8-41 7.79e-03

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 39.99  E-value: 7.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2092989885    8 RPLKVTIIGAGIAGLTA---ALALrkqGHEVTVLERS 41
Cdd:COG0686    167 PPAKVVILGGGVVGTNAarmALGL---GADVTVLDIN 200
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 8-41 8.37e-03

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 39.70  E-value: 8.37e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2092989885    8 RPLKVTIIGAGIAGLTA---ALALrkqGHEVTVLERS 41
Cdd:cd05305    167 PPAKVVILGAGVVGENAarvALGL---GAEVTVLDIN 200
RRM1_SECp43_like cd12344
RNA recognition motif 1 (RRM1) found in tRNA selenocysteine-associated protein 1 (SECp43) and ...
 911-941 8.39e-03

RNA recognition motif 1 (RRM1) found in tRNA selenocysteine-associated protein 1 (SECp43) and similar proteins; This subfamily corresponds to the RRM1 in tRNA selenocysteine-associated protein 1 (SECp43), yeast negative growth regulatory protein NGR1 (RBP1), yeast protein NAM8, and similar proteins. SECp43 is an RNA-binding protein associated specifically with eukaryotic selenocysteine tRNA [tRNA(Sec)]. It may play an adaptor role in the mechanism of selenocysteine insertion. SECp43 is located primarily in the nucleus and contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal polar/acidic region. Yeast proteins, NGR1 and NAM8, show high sequence similarity with SECp43. NGR1 is a putative glucose-repressible protein that binds both RNA and single-stranded DNA (ssDNA). It may function in regulating cell growth in early log phase, possibly through its participation in RNA metabolism. NGR1 contains three RRMs, two of which are followed by a glutamine-rich stretch that may be involved in transcriptional activity. In addition, NGR1 has an asparagine-rich region near the C-terminus which also harbors a methionine-rich region. NAM8 is a putative RNA-binding protein that acts as a suppressor of mitochondrial splicing deficiencies when overexpressed in yeast. It may be a non-essential component of the mitochondrial splicing machinery. NAM8 also contains three RRMs.


Pssm-ID: 409780 [Multi-domain]  Cd Length: 82  Bit Score: 36.51  E-value: 8.39e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2092989885  911 GWVEFIDKKDAKAAAETLNGNIIGGKKGNFY 941
Cdd:cd12344     45 CFVEFATQEAAEQALEHLNGKPIPNTQQRFR 75
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 11-39 8.97e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 39.90  E-value: 8.97e-03
                           10        20
                   ....*....|....*....|....*....
gi 2092989885   11 KVTIIGAGIAGLTAALALRKQGHEVTVLE 39
Cdd:TIGR03026    2 KIAVIGLGYVGLPLAALLADLGHDVTGVD 30
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
857-937 9.38e-03

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


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 36.23  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2092989885  857 IYISRIPPFMKPATLKHYLSPYGEIGRVFLtPEDpvaqkqrvRNGGnKKKSFtdGWVEFIDKKDAKAAAETLNGNIIGGK 936
Cdd:COG0724      4 IYVGNLPYSVTEEDLRELFSEYGEVTSVKL-ITD--------RETG-RSRGF--GFVEMPDDEEAQAAIEALNGAELMGR 71


                   .
gi 2092989885  937 K 937
Cdd:COG0724     72 T 72
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 11-44 9.58e-03

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 39.45  E-value: 9.58e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2092989885   11 KVTIIGAG-IAGLTAALaLRKQGHEVTVLERSRFA 44
Cdd:COG1893      2 KIAILGAGaIGGLLGAR-LARAGHDVTLVARGAHA 35
 
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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