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Conserved domains on  [gi|2124264618|gb|KAH6563704|]
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hypothetical protein BASA62_008357 [Batrachochytrium salamandrivorans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pantoate_ligase pfam02569
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ...
 62-347 3.82e-148

Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.


:

Pssm-ID: 460595 [Multi-domain]  Cd Length: 277  Bit Score: 433.00  E-value: 3.82e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:pfam02569   2 IIRTIAELRAWLRAWRRAGKTIGLVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDLDAYPRTLEADLALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGISldvseqvgTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQC 221
Cdd:pfam02569  82 EAAGVDLVFAPSVEEMYPEGFS--------TTVDVPGLSEVLEGASRPGHFRGVATVVTKLFNIVQPDRAYFGEKDYQQL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 222 SVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGvRSRSKLVSVAEKWIARN 301
Cdd:pfam02569 154 AVIRRMVRDLNLPVEIVGCPTVREADGLALSSRNVYLSPEERAAAPVLYRALQAAAEAIRAE-RDAAALLAAARERLAAA 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2124264618 302 SKVQLEYISLAEPMRLTEVDTvSDSKGAILSGAIRVGNTRIIDNVV 347
Cdd:pfam02569 233 GFARVDYVEIVDADTLEEPLE-DIAGPAVLLVAARLGKTRLIDNII 277
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 504-601 2.28e-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: 187.02  E-value: 2.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 504 GVVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLNPEDAKTAARRRKYKQNKRQNFTEGWVEFLDKSEAKRAAAALNNTIMG 583
Cdd:cd12263     1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRVAESLNNTPIG 80

                          90
                  ....*....|....*...
gi 2124264618 584 GKKRSRFHDDIWNIRYLP 601
Cdd:cd12263    81 GKKRSRFRDDLWNIKYLP 98
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 1.07e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 794

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  795 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 825
 
Name Accession Description Interval E-value
Pantoate_ligase pfam02569
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ...
 62-347 3.82e-148

Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.


Pssm-ID: 460595 [Multi-domain]  Cd Length: 277  Bit Score: 433.00  E-value: 3.82e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:pfam02569   2 IIRTIAELRAWLRAWRRAGKTIGLVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDLDAYPRTLEADLALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGISldvseqvgTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQC 221
Cdd:pfam02569  82 EAAGVDLVFAPSVEEMYPEGFS--------TTVDVPGLSEVLEGASRPGHFRGVATVVTKLFNIVQPDRAYFGEKDYQQL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 222 SVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGvRSRSKLVSVAEKWIARN 301
Cdd:pfam02569 154 AVIRRMVRDLNLPVEIVGCPTVREADGLALSSRNVYLSPEERAAAPVLYRALQAAAEAIRAE-RDAAALLAAARERLAAA 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2124264618 302 SKVQLEYISLAEPMRLTEVDTvSDSKGAILSGAIRVGNTRIIDNVV 347
Cdd:pfam02569 233 GFARVDYVEIVDADTLEEPLE-DIAGPAVLLVAARLGKTRLIDNII 277
PanC COG0414
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ...
 62-349 1.09e-145

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


Pssm-ID: 440183 [Multi-domain]  Cd Length: 280  Bit Score: 426.76  E-value: 1.09e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:COG0414     3 IIRTIAELRAALAAWRAAGKRIGLVPTMGALHEGHLSLVRRARAEADVVVVSIFVNPLQFGPNEDLDRYPRTLEADLALL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGISldvseqvgTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQC 221
Cdd:COG0414    83 EAAGVDLVFAPSVEEMYPEGFS--------TRVDVGGLSEVLEGASRPGHFDGVATVVTKLFNIVQPDVAYFGEKDYQQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 222 SVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIARN 301
Cdd:COG0414   155 AVIRRMVRDLNLPVEIVGVPTVREADGLALSSRNVYLSPEERAAAPALYRALQAAAEAIAAGERDAAALLAAARAALAAA 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2124264618 302 SKVQLEYISLAEPMRLTEVDTvsDSKGAILSGAIRVGNTRIIDNVVLG 349
Cdd:COG0414   235 PFVRLDYVEIVDAETLEPVEE--IDGPALLLVAARLGKTRLIDNIVLN 280
PanC cd00560
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate ...
 60-346 3.12e-133

Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate synthase, catalyzes the formation of pantothenate from pantoate and alanine. PanC belongs to a large superfamily of nucleotidyltransferases that includes , ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.


Pssm-ID: 185673 [Multi-domain]  Cd Length: 277  Bit Score: 394.59  E-value: 3.12e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  60 PLVIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIA 139
Cdd:cd00560     1 MRIITTIAELRAWLRNWRAQGKTIGFVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPLQFGPNEDLDRYPRTLEADLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 140 MLAAEGVDVVFAPSVAEMYPSGISldvseqvGTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQ 219
Cdd:cd00560    81 LLEEAGVDLLFAPSVEEMYPEGLF-------STFVDVGPLSEVLEGASRPGHFRGVATVVAKLFNLVQPDRAYFGEKDAQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 220 QCSVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKwIA 299
Cdd:cd00560   154 QLAVIRRMVRDLNLPVEIVGCPTVREEDGLALSSRNVYLSAEERKEALALYRALKAAAEAIAAGERDAEDIIAAARD-VL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2124264618 300 RNSKVQLEYISLAEPMRLTEVDTvsDSKGAILSGAIRVGNTRIIDNV 346
Cdd:cd00560   233 EAAGFRVDYLEIVDPETLEPVEE--IDKPAVILVAARVGKTRLIDNI 277
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
62-350 6.35e-102

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 322.22  E-value: 6.35e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWyrEGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:PRK13477    3 ILRTVAGLRAWLRQQ--RSETIGFVPTMGALHQGHLSLIRRARQENDVVLVSIFVNPLQFGPNEDLERYPRTLEADRELC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGisldvsEQVGTFVHV-QGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQ 220
Cdd:PRK13477   81 ESAGVDAIFAPSPEELYPGG------AKSITQVQPpSELTSHLCGASRPGHFDGVATVVTRLLNLVQPKRAYFGEKDWQQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 221 CSVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIAR 300
Cdd:PRK13477  155 LAIIRRLVADLNLPVTIVGCPTVREADGLALSSRNQYLSAEERQQAAALYRALQAAKKAFQAGKRINLNLLAAVQEELLS 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2124264618 301 NSKVQLEYISLAEPMRLTEVDTVSDSkgAILSGAIRVGNTRIIDNVVLGH 350
Cdd:PRK13477  235 EPGLEVEYLELVDPQTLQPLEQIENI--GLLAIAVRCGSTRLIDNVFLMK 282
panC TIGR00018
pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme ...
 61-348 6.13e-97

pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme of pantothenate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272857 [Multi-domain]  Cd Length: 282  Bit Score: 301.30  E-value: 6.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  61 LVIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAM 140
Cdd:TIGR00018   2 RIIETIPLLRQYIRQLRMEGKTVGFVPTMGNLHDGHMSLIDRAVAENDVVVVSIFVNPMQFGPNEDLEAYPRTLEEDCAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 141 LAAEGVDVVFAPSVAEMYPSGIsldvsEQVGTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQ 220
Cdd:TIGR00018  82 LEKLGVDVVFAPSVHEMYPNGT-----EQHTTVDVPLGLSEVLEGASRPGHFRGVATIVTKLFNLVQPDVAYFGEKDAQQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 221 CSVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIAR 300
Cdd:TIGR00018 157 LAVIRKLVADLFLDIEIVPVPIVREEDGLALSSRNVYLTAEQRKIAPGLYRALQAIAQAIQAGERDLDAVITIAGDILDT 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2124264618 301 NSkVQLEYISLAEPMRLTEVDTVSdSKGAILSGAIRVGNTRIIDNVVL 348
Cdd:TIGR00018 237 KS-FRIDYVQLRDADTLEPVSETE-PTSAVILVAAYVGDARLIDNIVV 282
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 504-601 2.28e-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: 187.02  E-value: 2.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 504 GVVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLNPEDAKTAARRRKYKQNKRQNFTEGWVEFLDKSEAKRAAAALNNTIMG 583
Cdd:cd12263     1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRVAESLNNTPIG 80

                          90
                  ....*....|....*...
gi 2124264618 584 GKKRSRFHDDIWNIRYLP 601
Cdd:cd12263    81 GKKRSRFRDDLWNIKYLP 98
RRM smart00360
RNA recognition motif;
505-586 9.00e-06

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.12  E-value: 9.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  505 VVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLNPEdaKTAARRRKYkqnkrqnfteGWVEFLDKSEAKRAAAALNNTIMGG 584
Cdd:smart00360   1 TLFVGNLPPDTTEEELRELFSKFGKVESVRLVRD--KETGKSKGF----------AFVEFESEEDAEKALEALNGKELDG 68


                   ..
gi 2124264618  585 KK 586
Cdd:smart00360  69 RP 70
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 1.07e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 794

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  795 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 825
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 2.67e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  725 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 804

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2124264618 448 HGDGSSSVEDDNETDA---SQSDEKTEGALTAD 477
Cdd:NF033609  805 DSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSD 837
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 3.57e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.13  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  651 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 730

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  731 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 761
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 4.50e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.74  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  755 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 834

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 448 HGDGSSSVEDDNETDaSQSDEKTEGALTAD 477
Cdd:NF033609  835 DSDSDSDSDSDSDSD-SDSDSDSESDSNSD 863
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 506-586 5.80e-04

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


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 38.75  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 506 VYLSRIPPFMKPTKVRSLLTRYGKLGRIYLnpedaktaaRRRKYKQNKRQNFtegwVEFLDKSEAKRAAAALNNTIMGGK 585
Cdd:pfam00076   1 LFVGNLPPDTTEEDLKDLFSKFGPIKSIRL---------VRDETGRSKGFAF----VEFEDEEDAEKAIEALNGKELGGR 67


                  .
gi 2124264618 586 K 586
Cdd:pfam00076  68 E 68
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 6.94e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  663 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 448 HGDGSSSVEDDNETDaSQSDEKTEGALTAD 477
Cdd:NF033609  743 DSDSDSDSDSDSDSD-SDSDSDSDSDSDSD 771
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 7.89e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  679 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 758

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 448 HGDGSSSVEDDNETDaSQSDEKTEGALTAD 477
Cdd:NF033609  759 DSDSDSDSDSDSDSD-SDSDSDSDSDSDSD 787
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 8.37e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  709 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 788

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  789 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 819
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 1.88e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  745 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 824

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  825 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 855
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 369-477 2.90e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 369 DDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLSH 448
Cdd:NF033609  568 DSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSD 647

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 449 GDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  648 SDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 677
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 368-477 8.05e-03

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 39.52  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAA-------EDALSEGSEDDRSGSDIDDKDDKESL 440
Cdd:pfam07263 136 DEDSADTTQSREDSASQGEDSAQDTTSESRDLDNEDEVSSRPESGDStqdseseEHWVGGGSEGDSSHGDGSEFDDEGMQ 215

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124264618 441 TDDPDLSHGDGSSSVEDDNETDASQSDEKTEGALTAD 477
Cdd:pfam07263 216 SDDPDSIRSERGNSRMSSASVKSKESKGDSEQASTQD 252
 
Name Accession Description Interval E-value
Pantoate_ligase pfam02569
Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, ...
 62-347 3.82e-148

Pantoate-beta-alanine ligase; Pantoate-beta-alanine ligase, also know as pantothenate synthase, (EC:6.3.2.1) catalyzes the formation of pantothenate from pantoate and alanine.


Pssm-ID: 460595 [Multi-domain]  Cd Length: 277  Bit Score: 433.00  E-value: 3.82e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:pfam02569   2 IIRTIAELRAWLRAWRRAGKTIGLVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPTQFGPNEDLDAYPRTLEADLALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGISldvseqvgTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQC 221
Cdd:pfam02569  82 EAAGVDLVFAPSVEEMYPEGFS--------TTVDVPGLSEVLEGASRPGHFRGVATVVTKLFNIVQPDRAYFGEKDYQQL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 222 SVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGvRSRSKLVSVAEKWIARN 301
Cdd:pfam02569 154 AVIRRMVRDLNLPVEIVGCPTVREADGLALSSRNVYLSPEERAAAPVLYRALQAAAEAIRAE-RDAAALLAAARERLAAA 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2124264618 302 SKVQLEYISLAEPMRLTEVDTvSDSKGAILSGAIRVGNTRIIDNVV 347
Cdd:pfam02569 233 GFARVDYVEIVDADTLEEPLE-DIAGPAVLLVAARLGKTRLIDNII 277
PanC COG0414
Panthothenate synthetase [Coenzyme transport and metabolism]; Panthothenate synthetase is part ...
 62-349 1.09e-145

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


Pssm-ID: 440183 [Multi-domain]  Cd Length: 280  Bit Score: 426.76  E-value: 1.09e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:COG0414     3 IIRTIAELRAALAAWRAAGKRIGLVPTMGALHEGHLSLVRRARAEADVVVVSIFVNPLQFGPNEDLDRYPRTLEADLALL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGISldvseqvgTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQC 221
Cdd:COG0414    83 EAAGVDLVFAPSVEEMYPEGFS--------TRVDVGGLSEVLEGASRPGHFDGVATVVTKLFNIVQPDVAYFGEKDYQQL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 222 SVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIARN 301
Cdd:COG0414   155 AVIRRMVRDLNLPVEIVGVPTVREADGLALSSRNVYLSPEERAAAPALYRALQAAAEAIAAGERDAAALLAAARAALAAA 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2124264618 302 SKVQLEYISLAEPMRLTEVDTvsDSKGAILSGAIRVGNTRIIDNVVLG 349
Cdd:COG0414   235 PFVRLDYVEIVDAETLEPVEE--IDGPALLLVAARLGKTRLIDNIVLN 280
PanC cd00560
Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate ...
 60-346 3.12e-133

Pantoate-beta-alanine ligase; PanC Pantoate-beta-alanine ligase, also known as pantothenate synthase, catalyzes the formation of pantothenate from pantoate and alanine. PanC belongs to a large superfamily of nucleotidyltransferases that includes , ATP sulfurylase (ATPS), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.


Pssm-ID: 185673 [Multi-domain]  Cd Length: 277  Bit Score: 394.59  E-value: 3.12e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  60 PLVIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIA 139
Cdd:cd00560     1 MRIITTIAELRAWLRNWRAQGKTIGFVPTMGALHEGHLSLVRRARAENDVVVVSIFVNPLQFGPNEDLDRYPRTLEADLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 140 MLAAEGVDVVFAPSVAEMYPSGISldvseqvGTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQ 219
Cdd:cd00560    81 LLEEAGVDLLFAPSVEEMYPEGLF-------STFVDVGPLSEVLEGASRPGHFRGVATVVAKLFNLVQPDRAYFGEKDAQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 220 QCSVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKwIA 299
Cdd:cd00560   154 QLAVIRRMVRDLNLPVEIVGCPTVREEDGLALSSRNVYLSAEERKEALALYRALKAAAEAIAAGERDAEDIIAAARD-VL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2124264618 300 RNSKVQLEYISLAEPMRLTEVDTvsDSKGAILSGAIRVGNTRIIDNV 346
Cdd:cd00560   233 EAAGFRVDYLEIVDPETLEPVEE--IDKPAVILVAARVGKTRLIDNI 277
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
62-350 6.35e-102

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 322.22  E-value: 6.35e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWyrEGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:PRK13477    3 ILRTVAGLRAWLRQQ--RSETIGFVPTMGALHQGHLSLIRRARQENDVVLVSIFVNPLQFGPNEDLERYPRTLEADRELC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGisldvsEQVGTFVHV-QGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQ 220
Cdd:PRK13477   81 ESAGVDAIFAPSPEELYPGG------AKSITQVQPpSELTSHLCGASRPGHFDGVATVVTRLLNLVQPKRAYFGEKDWQQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 221 CSVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIAR 300
Cdd:PRK13477  155 LAIIRRLVADLNLPVTIVGCPTVREADGLALSSRNQYLSAEERQQAAALYRALQAAKKAFQAGKRINLNLLAAVQEELLS 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2124264618 301 NSKVQLEYISLAEPMRLTEVDTVSDSkgAILSGAIRVGNTRIIDNVVLGH 350
Cdd:PRK13477  235 EPGLEVEYLELVDPQTLQPLEQIENI--GLLAIAVRCGSTRLIDNVFLMK 282
PLN02660 PLN02660
pantoate--beta-alanine ligase
 62-348 1.66e-98

pantoate--beta-alanine ligase


Pssm-ID: 178266 [Multi-domain]  Cd Length: 284  Bit Score: 305.43  E-value: 1.66e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  62 VIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAML 141
Cdd:PLN02660    2 VIRDKAAMRAWSRAQRAQGKRIALVPTMGYLHEGHLSLVRAARARADVVVVSIYVNPGQFAPGEDLDTYPRDFDGDLRKL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 142 AAEGVDVVFAPSVAEMYPSGISLDVSEQVgTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQC 221
Cdd:PLN02660   82 AALGVDAVFNPHDLYVYVSCLEEGGAGHE-TWVRVERLEKGLCGKSRPVFFRGVATIVTKLFNIVEPDVAVFGKKDYQQW 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 222 SVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIArN 301
Cdd:PLN02660  161 RVIRRMVRDLDFDIEVVGSPIVREADGLAMSSRNVRLSAEEREKALSISRSLARAEELVEEGETDADELKEQVRQAIA-E 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2124264618 302 SKVQLEYISLAEPMRLTEVDTVSDskGAILSGAIRVGNTRIIDNVVL 348
Cdd:PLN02660  240 AGGEVDYVEIVDQETLQPVEEIKS--PVVIAVAAWFGSVRLIDNIEL 284
panC TIGR00018
pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme ...
 61-348 6.13e-97

pantoate--beta-alanine ligase; This family is pantoate--beta-alanine ligase, the last enzyme of pantothenate biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]


Pssm-ID: 272857 [Multi-domain]  Cd Length: 282  Bit Score: 301.30  E-value: 6.13e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  61 LVIRTISQYRTLRQTWYREGASVGFVPTMGALHSGHTELAREARLICDKVVASVFVNPAQFAPTEDLAKYPRTEENDIAM 140
Cdd:TIGR00018   2 RIIETIPLLRQYIRQLRMEGKTVGFVPTMGNLHDGHMSLIDRAVAENDVVVVSIFVNPMQFGPNEDLEAYPRTLEEDCAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 141 LAAEGVDVVFAPSVAEMYPSGIsldvsEQVGTFVHVQGKSHQMEGSIRPHFFRGVSTVVSKLFNIIQPTHAFFGQKDVQQ 220
Cdd:TIGR00018  82 LEKLGVDVVFAPSVHEMYPNGT-----EQHTTVDVPLGLSEVLEGASRPGHFRGVATIVTKLFNLVQPDVAYFGEKDAQQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 221 CSVIRSMVRDLFFPVQIMVVPTVREADGLAKSSRNRFLSPEERALAPLLYQALLAVSKEFDSGVRSRSKLVSVAEKWIAR 300
Cdd:TIGR00018 157 LAVIRKLVADLFLDIEIVPVPIVREEDGLALSSRNVYLTAEQRKIAPGLYRALQAIAQAIQAGERDLDAVITIAGDILDT 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2124264618 301 NSkVQLEYISLAEPMRLTEVDTVSdSKGAILSGAIRVGNTRIIDNVVL 348
Cdd:TIGR00018 237 KS-FRIDYVQLRDADTLEPVSETE-PTSAVILVAAYVGDARLIDNIVV 282
RRM_ABT1_like cd12263
RNA recognition motif (RRM) found in activator of basal transcription 1 (ABT1) and similar ...
 504-601 2.28e-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: 187.02  E-value: 2.28e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 504 GVVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLNPEDAKTAARRRKYKQNKRQNFTEGWVEFLDKSEAKRAAAALNNTIMG 583
Cdd:cd12263     1 GIVYLSRIPPGMNPAKLRQLLSQYGEVGRIYLQPEDPSKRKKRKKKGGNKKKKFTEGWVEFEDKKVAKRVAESLNNTPIG 80

                          90
                  ....*....|....*...
gi 2124264618 584 GKKRSRFHDDIWNIRYLP 601
Cdd:cd12263    81 GKKRSRFRDDLWNIKYLP 98
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 506-586 1.15e-07

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


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 49.20  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 506 VYLSRIPPFMKPTKVRSLLTRYGKLGRIYLnpedaktaarrRKYKQNKRQNFteGWVEFLDKSEAKRAAAALNNTIMGGK 585
Cdd:cd00590     1 LFVGNLPPDTTEEDLRELFSKFGEVVSVRI-----------VRDRDGKSKGF--AFVEFESPEDAEKALEALNGTELGGR 67


                  .
gi 2124264618 586 K 586
Cdd:cd00590    68 P 68
RRM smart00360
RNA recognition motif;
505-586 9.00e-06

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.12  E-value: 9.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  505 VVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLNPEdaKTAARRRKYkqnkrqnfteGWVEFLDKSEAKRAAAALNNTIMGG 584
Cdd:smart00360   1 TLFVGNLPPDTTEEELRELFSKFGKVESVRLVRD--KETGKSKGF----------AFVEFESEEDAEKALEALNGKELDG 68


                   ..
gi 2124264618  585 KK 586
Cdd:smart00360  69 RP 70
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 1.07e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  715 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 794

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  795 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 825
RRM_NIFK_like cd12307
RNA recognition motif in nucleolar protein interacting with the FHA domain of pKI-67 (NIFK) ...
 505-586 1.37e-04

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: 40.63  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 505 VVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLnpedaktaARRRKYKQNKRQNFtegwVEFLDKSEAKRAAAALNNTIMGG 584
Cdd:cd12307     1 VVYIGHLPHGFYEPELRKYFSQFGTVTRLRL--------SRSKKTGKSKGYAF----VEFEDPEVAKIVAETMNNYLLFE 68


                  ..
gi 2124264618 585 KK 586
Cdd:cd12307    69 RL 70
cytidylyltransferase_like cd02039
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ...
 83-255 1.84e-04

Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.


Pssm-ID: 185678 [Multi-domain]  Cd Length: 143  Bit Score: 42.04  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618  83 VGFVPTMG-ALHSGHTELAREARLIC-DKVVASVFVNPAQFAPTEDLAKYPRTeendIAMLAA-----EGVDVVFAPSVA 155
Cdd:cd02039     1 VGIIIGRFePFHLGHLKLIKEALEEAlDEVIIIIVSNPPKKKRNKDPFSLHER----VEMLKEilkdrLKVVPVDFPEVK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 156 EMYPsgisldvseqvGTFVHvqgkshqmegsirphffrgvstvvsKLFNIIQPTHAFFGQKDVQQCSVIR-SMVRDLFFP 234
Cdd:cd02039    77 ILLA-----------VVFIL-------------------------KILLKVGPDKVVVGEDFAFGKNASYnKDLKELFLD 120

                         170       180
                  ....*....|....*....|.
gi 2124264618 235 VQIMVVPTVReaDGLAKSSRN 255
Cdd:cd02039   121 IEIVEVPRVR--DGKKISSTL 139
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 2.67e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  725 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 804

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2124264618 448 HGDGSSSVEDDNETDA---SQSDEKTEGALTAD 477
Cdd:NF033609  805 DSDSDSDSDSDSDSDSdsdSDSDSDSDSDSDSD 837
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 3.57e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.13  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  651 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 730

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  731 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 761
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 4.50e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 43.74  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  755 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 834

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 448 HGDGSSSVEDDNETDaSQSDEKTEGALTAD 477
Cdd:NF033609  835 DSDSDSDSDSDSDSD-SDSDSDSESDSNSD 863
RRM_ZCRB1 cd12393
RNA recognition motif (RRM) found in Zinc finger CCHC-type and RNA-binding motif-containing ...
 506-586 5.04e-04

RNA recognition motif (RRM) found in Zinc finger CCHC-type and RNA-binding motif-containing protein 1 (ZCRB1) and similar proteins; This subfamily corresponds to the RRM of ZCRB1, also termed MADP-1, or U11/U12 small nuclear ribonucleoprotein 31 kDa protein (U11/U12 snRNP 31 or U11/U12-31K), a novel multi-functional nuclear factor, which may be involved in morphine dependence, cold/heat stress, and hepatocarcinoma. It is located in the nucleoplasm, but outside the nucleolus. ZCRB1 is one of the components of U11/U12 snRNPs that bind to U12-type pre-mRNAs and form a di-snRNP complex, simultaneously recognizing the 5' splice site and branchpoint sequence. ZCRB1 is characterized by an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a CCHC-type Zinc finger motif. In addition, it contains core nucleocapsid motifs, and Lys- and Glu-rich domains.


Pssm-ID: 409827 [Multi-domain]  Cd Length: 76  Bit Score: 39.19  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 506 VYLSRIPPFMKPTKVRSLLTRYGKLGRIylnpedakTAARRRKYKQNKRQNFtegwVEFLDKSEAKRAAAALNNTIMGGK 585
Cdd:cd12393     4 VYVSNLPFSLTNNDLHQIFSKYGKVVKV--------TILKDKETRKSKGVAF----VLFLDRESAHNAVRAMNNKELFGR 71


                  .
gi 2124264618 586 K 586
Cdd:cd12393    72 T 72
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 506-586 5.80e-04

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


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 38.75  E-value: 5.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 506 VYLSRIPPFMKPTKVRSLLTRYGKLGRIYLnpedaktaaRRRKYKQNKRQNFtegwVEFLDKSEAKRAAAALNNTIMGGK 585
Cdd:pfam00076   1 LFVGNLPPDTTEEDLKDLFSKFGPIKSIRL---------VRDETGRSKGFAF----VEFEDEEDAEKAIEALNGKELGGR 67


                  .
gi 2124264618 586 K 586
Cdd:pfam00076  68 E 68
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 6.94e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  663 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 448 HGDGSSSVEDDNETDaSQSDEKTEGALTAD 477
Cdd:NF033609  743 DSDSDSDSDSDSDSD-SDSDSDSDSDSDSD 771
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 7.89e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  679 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 758

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 448 HGDGSSSVEDDNETDaSQSDEKTEGALTAD 477
Cdd:NF033609  759 DSDSDSDSDSDSDSD-SDSDSDSDSDSDSD 787
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 8.37e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 8.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  709 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 788

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  789 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 819
RRM_Nop15p cd12552
RNA recognition motif in yeast ribosome biogenesis protein 15 (Nop15p) and similar proteins; ...
 505-601 8.91e-04

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: 38.69  E-value: 8.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 505 VVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLnpEDAKTAARRRKYkqnkrqnfteGWVEFLDKSEAKRAAAALNNTIMGG 584
Cdd:cd12552     1 IIYVSHLPHGFHEKELKKYFAQFGDLKNVRL--ARSKKTGNSKHY----------GFLEFVNPEDAMIAQKSMNNYLLMG 68

                          90
                  ....*....|....*..
gi 2124264618 585 KKrsrfhddiWNIRYLP 601
Cdd:cd12552    69 KL--------LQVRVLP 77
nt_trans cd02156
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 85-147 1.41e-03

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


Pssm-ID: 173912 [Multi-domain]  Cd Length: 105  Bit Score: 38.67  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124264618  85 FVPTM-GALHSGHTELAREARLICDKVVASVFVNPAQFApTEDLAKYPRTEENDIAMLAAEGVD 147
Cdd:cd02156     3 RFPGEpGYLHIGHAKLICRAKGIADQCVVRIDDNPPVKV-WQDPHELEERKESIEEDISVCGED 65
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 368-477 1.88e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLS 447
Cdd:NF033609  745 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 824

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2124264618 448 HGDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  825 DSDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 855
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 369-477 2.90e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.05  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 369 DDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAAEDALSEGSEDDRSGSDIDDKDDKESLTDDPDLSH 448
Cdd:NF033609  568 DSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSASDSDSDSDSD 647

                          90       100       110
                  ....*....|....*....|....*....|
gi 2124264618 449 GDGSSSVEDDNETDA-SQSDEKTEGALTAD 477
Cdd:NF033609  648 SDSDSDSDSDSDSDSdSDSDSDSDSDSDSD 677
RRM4_RBM19 cd12569
RNA recognition motif 4 (RRM4) found in RNA-binding protein 19 (RBM19) and similar proteins; ...
 505-573 6.30e-03

RNA recognition motif 4 (RRM4) found in RNA-binding protein 19 (RBM19) and similar proteins; This subgroup corresponds to the RRM4 of RBM19, also termed RNA-binding domain-1 (RBD-1), which is a nucleolar protein conserved in eukaryotes. It is involved in ribosome biogenesis by processing rRNA. In addition, it is essential for preimplantation development. RBM19 has a unique domain organization containing 6 conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains).


Pssm-ID: 409984 [Multi-domain]  Cd Length: 72  Bit Score: 35.83  E-value: 6.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124264618 505 VVYLSRIPPFMKPTKVRSLLTRYGKLGRIYLnPEDAKTAArrrkykqnkrqnftegwVEFLDKSEAKRA 573
Cdd:cd12569     2 VILVKNLPAGTEVAELEELFSKFGSLGRVVL-PPAGVTAI-----------------VEFLEPTEAKRA 52
DMP1 pfam07263
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ...
 368-477 8.05e-03

Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.


Pssm-ID: 462128 [Multi-domain]  Cd Length: 519  Bit Score: 39.52  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124264618 368 DDDFADELASDSGSSMDERDQGKATTAAAAAVDVIPRVSNESDALAA-------EDALSEGSEDDRSGSDIDDKDDKESL 440
Cdd:pfam07263 136 DEDSADTTQSREDSASQGEDSAQDTTSESRDLDNEDEVSSRPESGDStqdseseEHWVGGGSEGDSSHGDGSEFDDEGMQ 215

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2124264618 441 TDDPDLSHGDGSSSVEDDNETDASQSDEKTEGALTAD 477
Cdd:pfam07263 216 SDDPDSIRSERGNSRMSSASVKSKESKGDSEQASTQD 252
 
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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