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Conserved domains on  [gi|2047900123|gb|KAG6573999|]
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Protein decapping 5, partial [Cucurbita argyrosperma subsp. sororia]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cytochrome_b_N super family cl23723
Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit ...
634-856 1.17e-100

Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit mitochondrial respiratory enzyme. Cytochrome b spans the mitochondrial membrane with 8 transmembrane helices (A-H) in eukaryotes. In plants and cyanobacteria, cytochrome b6 is analogous to eukaryote cytochrome b, containing two chains: helices A-D are encoded by the petB gene and helices E-H are encoded by the petD gene in these organisms. Cytochrome b/b6 contains two bound hemes and two ubiquinol/ubiquinone binding sites. The C-terminal portion of cytochrome b is described in a separate CD.


The actual alignment was detected with superfamily member PLN02351:

Pssm-ID: 474033  Cd Length: 242  Bit Score: 313.00  E-value: 1.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 634 MAAALP-SLAPLLIFARILGLLVAVLIFVWALAFSSSFGHLPPAPDDRIFDVLHPLFMVIGFILLSGEAILVHSWLPGSR 712
Cdd:PLN02351    1 MATVDSsSLLPLLLFARLSGLVVAVLVLYWALFFKSSFLPQSTSQEDLVYAVLHPLLMVIGFILISGEAILVHRWLPGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 713 NLRKSVHLILQGLALTSGFFGIWTKFHWDRGFLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHV 792
Cdd:PLN02351   81 KTKKSVHLWLQGLALASGVFGIWTKFHGQDGIVANFYSLHSWMGLICVSLFGAQWLTGFMSFWHRGEMRTTRTTVLPWHV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047900123 793 FLGLYSYALAVTVAETGLLEKLTLLQTKRNVPRKGPEAMVVNSLGLALALLGGTVVLTAISPKY 856
Cdd:PLN02351  161 FLGLYTYGLAVATAETGLLEKLTFLQTKRNVSKHGSESMVVNGLGLGLALLSGIVILAAVLPKY 224
LSm14_N cd01736
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of ...
16-87 1.83e-38

Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles.


:

Pssm-ID: 212483  Cd Length: 74  Bit Score: 137.33  E-value: 1.83e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123  16 YVGSLISLTSKSEIRYEGVLYNINTEESSIGLRNVRSFGTEGRKKDgPQVPPSDQVFEYILFRGSDIKDLQV 87
Cdd:cd01736     4 YIGSKISLISKSDIRYEGILYTIDTEDSTIALKNVRSFGTEGRPTG-RPIPPSDEVYDYIVFRGSDIKDLTV 74
FDF super family cl09757
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
449-552 3.38e-20

FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.


The actual alignment was detected with superfamily member pfam09532:

Pssm-ID: 430668  Cd Length: 104  Bit Score: 86.35  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 449 EKFTEDFDFMAMNEKFNKDEVWGHLGKNTKspkyNDGDEKFSDEDDDYEEDDGESSKLGIKSVYNKDDFFDTLSSNTTNN 528
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDK----LDEEKRLVNENNATRVATNEQPNEEVKGVYKKDDFFDNISSEANDR 76
                          90       100
                  ....*....|....*....|....*..
gi 2047900123 529 EAQNGRRTRYF---EQIKLDTETFGEF 552
Cdd:pfam09532  77 GIQSGPSPSGRdwrEERSLNTETFGVD 103
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
85-412 1.30e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.54  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  85 LQVKSSPPVQTTSlinNDPAIIQSHYPRPVSIPSSLPPPVSGPLPDINSQAMPMGIPGSNFQSGLPLY-----------Q 153
Cdd:pfam03154 174 LQAQSGAASPPSP---PPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQ 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 154 PGGNVGSWGASPSQPPPNPSAGGLGLPMYWQGYYG----------HPNGLPHMHQQSLLRPPPGLSLPSSLQQPLQYPNL 223
Cdd:pfam03154 251 PMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvppQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPS 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 224 NAYLPTGAP---NPLevssslfsanPTAP-SLSSTAMPPVTVSSTLPSVLSVPQTSEMSSSSMVNktINSALPQAPISTN 299
Cdd:pfam03154 331 QSQLQSQQPpreQPL----------PPAPlSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQ--MNSNLPPPPALKP 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 300 LTSLS---------------PLTASLDVSPVVPPTTNKTTTVSGPALSYQTVSQSTSsiiGTSNSVLTSAPAPALVTPdq 364
Cdd:pfam03154 399 LSSLSthhppsahppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQ---VPSQSPFPQHPFVPGGPP-- 473
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2047900123 365 llhtTVVSSSLPSQTVQKDVEVIQASSSLAAEQTVPVPADTQPPLLPL 412
Cdd:pfam03154 474 ----PITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPV 517
 
Name Accession Description Interval E-value
PLN02351 PLN02351
cytochromes b561 family protein
634-856 1.17e-100

cytochromes b561 family protein


Pssm-ID: 215201  Cd Length: 242  Bit Score: 313.00  E-value: 1.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 634 MAAALP-SLAPLLIFARILGLLVAVLIFVWALAFSSSFGHLPPAPDDRIFDVLHPLFMVIGFILLSGEAILVHSWLPGSR 712
Cdd:PLN02351    1 MATVDSsSLLPLLLFARLSGLVVAVLVLYWALFFKSSFLPQSTSQEDLVYAVLHPLLMVIGFILISGEAILVHRWLPGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 713 NLRKSVHLILQGLALTSGFFGIWTKFHWDRGFLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHV 792
Cdd:PLN02351   81 KTKKSVHLWLQGLALASGVFGIWTKFHGQDGIVANFYSLHSWMGLICVSLFGAQWLTGFMSFWHRGEMRTTRTTVLPWHV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047900123 793 FLGLYSYALAVTVAETGLLEKLTLLQTKRNVPRKGPEAMVVNSLGLALALLGGTVVLTAISPKY 856
Cdd:PLN02351  161 FLGLYTYGLAVATAETGLLEKLTFLQTKRNVSKHGSESMVVNGLGLGLALLSGIVILAAVLPKY 224
Cyt_b561_ACYB-1_like cd08766
Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1; Cytochrome b(561), as ...
679-818 4.23e-60

Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1; Cytochrome b(561), as found in plants, similar to the Arabidopsis thaliana ACYB-1 gene product, a cytochrome b561 isoform localized to the tonoplast. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), and might be capable of trans-membrane electron transport from intracellular ascorbate to extracellular ferric chelates. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176496  Cd Length: 144  Bit Score: 200.61  E-value: 4.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 679 DRIFDVlHPLFMVIGFILLSGEAILVHSWLPGSRNLRKSVHLILQGLALTSGFFGIWT--KFHWDRGfLANFHSVHSWLG 756
Cdd:cd08766     5 GLIFNV-HPVLMVIGFIFLAGEAILAYKTVPGSREVQKAVHLTLHLVALVLGIVGIYAafKFHNEVG-IPNLYSLHSWLG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123 757 LSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGLLEKLTLLQ 818
Cdd:cd08766    83 IGTISLFGLQWLFGFVTFWFPGASRNTRAALLPWHVFLGLAIYYLAIATAETGLLEKLTFLQ 144
Cytochrom_B561 pfam03188
Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ...
685-815 1.41e-41

Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport protein. It is an integral membrane protein, that binds two heme groups non-covalently. This is a eukaryotic family. Members of the 'prokaryotic cytochrome b561' family can be found in Pfam: PF01292.


Pssm-ID: 427188  Cd Length: 137  Bit Score: 148.52  E-value: 1.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 685 LHPLFMVIGFILLSGEAILVHSWLPG---SRNLRKSVHLILQGLALTSGFFGIWTKFHW-DRGFLANFHSVHSWLGLSVF 760
Cdd:pfam03188   1 WHPVLMVIGFIFLMGEAILVYRVNSTrrlSKKTKKLLHWILQALALILAVIGLVAVFKFhNLSGIPHFYSLHSWLGLLTV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2047900123 761 TLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGLLEKLT 815
Cdd:pfam03188  81 ILYALQWVGGFVTFLFPGLSKRIRPLLLPLHVFFGLVIFVLAIVTALLGLLEKLI 135
LSm14_N cd01736
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of ...
16-87 1.83e-38

Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles.


Pssm-ID: 212483  Cd Length: 74  Bit Score: 137.33  E-value: 1.83e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123  16 YVGSLISLTSKSEIRYEGVLYNINTEESSIGLRNVRSFGTEGRKKDgPQVPPSDQVFEYILFRGSDIKDLQV 87
Cdd:cd01736     4 YIGSKISLISKSDIRYEGILYTIDTEDSTIALKNVRSFGTEGRPTG-RPIPPSDEVYDYIVFRGSDIKDLTV 74
LSM14 pfam12701
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from ...
16-87 3.19e-38

Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain. In addition both EDC3 and Scd6p are found fused to the FDF domain.


Pssm-ID: 463675  Cd Length: 75  Bit Score: 136.48  E-value: 3.19e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123  16 YVGSLISLTSKSEIRYEGVLYNINTEESSIGLRNVRSFGTEGRkKDGPQVPPSDQVFEYILFRGSDIKDLQV 87
Cdd:pfam12701   2 FIGSRISLISKSDIRYEGILHSIDTEDSTITLKNVRSFGTEGR-GPGPQEPPSDEVYEYIVFRGSDIKDLKI 72
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
685-810 3.29e-35

Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.


Pssm-ID: 214769  Cd Length: 129  Bit Score: 130.04  E-value: 3.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  685 LHPLFMVIGFILLSGEAILVHSWL--PGSRNLRKSVHLILQGLALTSGFFGIWTKF-HWDRGFLANFHSVHSWLGLSVFT 761
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARPLtrFLSKPTWFLLHVVLQILALVLGVIGLLAIFiSHNESGIANFYSLHSWLGLAAFV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2047900123  762 LFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGL 810
Cdd:smart00665  81 LAGLQWLSGFLRPLPPGLPSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
449-552 3.38e-20

FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.


Pssm-ID: 430668  Cd Length: 104  Bit Score: 86.35  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 449 EKFTEDFDFMAMNEKFNKDEVWGHLGKNTKspkyNDGDEKFSDEDDDYEEDDGESSKLGIKSVYNKDDFFDTLSSNTTNN 528
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDK----LDEEKRLVNENNATRVATNEQPNEEVKGVYKKDDFFDNISSEANDR 76
                          90       100
                  ....*....|....*....|....*..
gi 2047900123 529 EAQNGRRTRYF---EQIKLDTETFGEF 552
Cdd:pfam09532  77 GIQSGPSPSGRdwrEERSLNTETFGVD 103
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
85-412 1.30e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.54  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  85 LQVKSSPPVQTTSlinNDPAIIQSHYPRPVSIPSSLPPPVSGPLPDINSQAMPMGIPGSNFQSGLPLY-----------Q 153
Cdd:pfam03154 174 LQAQSGAASPPSP---PPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQ 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 154 PGGNVGSWGASPSQPPPNPSAGGLGLPMYWQGYYG----------HPNGLPHMHQQSLLRPPPGLSLPSSLQQPLQYPNL 223
Cdd:pfam03154 251 PMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvppQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPS 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 224 NAYLPTGAP---NPLevssslfsanPTAP-SLSSTAMPPVTVSSTLPSVLSVPQTSEMSSSSMVNktINSALPQAPISTN 299
Cdd:pfam03154 331 QSQLQSQQPpreQPL----------PPAPlSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQ--MNSNLPPPPALKP 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 300 LTSLS---------------PLTASLDVSPVVPPTTNKTTTVSGPALSYQTVSQSTSsiiGTSNSVLTSAPAPALVTPdq 364
Cdd:pfam03154 399 LSSLSthhppsahppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQ---VPSQSPFPQHPFVPGGPP-- 473
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2047900123 365 llhtTVVSSSLPSQTVQKDVEVIQASSSLAAEQTVPVPADTQPPLLPL 412
Cdd:pfam03154 474 ----PITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPV 517
PRK10118 PRK10118
flagellar hook length control protein FliK;
212-425 4.30e-05

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 46.78  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 212 SSLQQPLQYPNLNAYLPTGAPNPLEVSSSLFSANPTAPSLSSTAMPPVTVSSTLPSVLSVPQTSemSSSSMVNKTINSAL 291
Cdd:PRK10118   53 ADLQAAGGKLSKGLLTTKGEPLVSDKLADLLAQQANLLIPVDETLPVITDEQSLSSPLTPALKT--SALAALSKNAQKDE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 292 PQAPIS-TNLTSLSPLTASLDVSPVVPPTTNKTTTVSG---PALSYQTVSQSTSSIIGTSNS-----VLTSAPAPAlVTP 362
Cdd:PRK10118  131 KADDLSdEDLASLSALFAMLPGQDNTTPVADAPSTVLPaekPTLLTKDMPSAPQDETHTLSSdehekGLTSAQLTT-AQP 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047900123 363 DQLLHTTVVSSSLPSQTVQKDVEVIQASSSL-AAEQTVPVPADTQPplLPlPTSSRVVQKPNGS 425
Cdd:PRK10118  210 DDAPGTPAQPLTPLAAEAQAKAEVISTPSPVtAAASPTITPHQTQP--LP-TAAAPVLSAPLGS 270
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
635-803 7.24e-03

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 39.61  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 635 AAALPSLAPLLIFARILGLLVAVLIFVWALAFSSSFGHLppAPDDRIFDVLHPLFMVIGF-------ILLSGEAILVHSW 707
Cdd:COG1807   117 AALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRAL--ERRRLRWLLLAGLALGLGFltkgpvaLLLPGLALLLYLL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 708 LPGSRNLRKSVHLILqGLALTSGFFGIW---TKFHWDRGFLANFHSVHSWLGLSVFTLFG---AQWMMGFLSF------W 775
Cdd:COG1807   195 LTRRWRRLRRLRLLL-GLLLALLLALPWyiaNDWATGPAFLEYFFGYENLVPLLFFSLSAtklPRYLLPLLPAlallaaA 273
                         170       180
                  ....*....|....*....|....*...
gi 2047900123 776 HWREVRATRERVLPWHVFLGLYSYALAV 803
Cdd:COG1807   274 GLARLRRRRRALLLLALVLLLALLIALL 301
 
Name Accession Description Interval E-value
PLN02351 PLN02351
cytochromes b561 family protein
634-856 1.17e-100

cytochromes b561 family protein


Pssm-ID: 215201  Cd Length: 242  Bit Score: 313.00  E-value: 1.17e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 634 MAAALP-SLAPLLIFARILGLLVAVLIFVWALAFSSSFGHLPPAPDDRIFDVLHPLFMVIGFILLSGEAILVHSWLPGSR 712
Cdd:PLN02351    1 MATVDSsSLLPLLLFARLSGLVVAVLVLYWALFFKSSFLPQSTSQEDLVYAVLHPLLMVIGFILISGEAILVHRWLPGSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 713 NLRKSVHLILQGLALTSGFFGIWTKFHWDRGFLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHV 792
Cdd:PLN02351   81 KTKKSVHLWLQGLALASGVFGIWTKFHGQDGIVANFYSLHSWMGLICVSLFGAQWLTGFMSFWHRGEMRTTRTTVLPWHV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047900123 793 FLGLYSYALAVTVAETGLLEKLTLLQTKRNVPRKGPEAMVVNSLGLALALLGGTVVLTAISPKY 856
Cdd:PLN02351  161 FLGLYTYGLAVATAETGLLEKLTFLQTKRNVSKHGSESMVVNGLGLGLALLSGIVILAAVLPKY 224
Cyt_b561_ACYB-1_like cd08766
Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1; Cytochrome b(561), as ...
679-818 4.23e-60

Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1; Cytochrome b(561), as found in plants, similar to the Arabidopsis thaliana ACYB-1 gene product, a cytochrome b561 isoform localized to the tonoplast. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), and might be capable of trans-membrane electron transport from intracellular ascorbate to extracellular ferric chelates. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176496  Cd Length: 144  Bit Score: 200.61  E-value: 4.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 679 DRIFDVlHPLFMVIGFILLSGEAILVHSWLPGSRNLRKSVHLILQGLALTSGFFGIWT--KFHWDRGfLANFHSVHSWLG 756
Cdd:cd08766     5 GLIFNV-HPVLMVIGFIFLAGEAILAYKTVPGSREVQKAVHLTLHLVALVLGIVGIYAafKFHNEVG-IPNLYSLHSWLG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123 757 LSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGLLEKLTLLQ 818
Cdd:cd08766    83 IGTISLFGLQWLFGFVTFWFPGASRNTRAALLPWHVFLGLAIYYLAIATAETGLLEKLTFLQ 144
PLN02680 PLN02680
carbon-monoxide oxygenase
636-854 8.22e-56

carbon-monoxide oxygenase


Pssm-ID: 215365  Cd Length: 232  Bit Score: 192.32  E-value: 8.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 636 AALPSLA-PLLIFARILGLLVAVLIFVWALAFSSSFGhLPPAPDDRIFDVlHPLFMVIGFILLSGEAILVHSWLPGSRNL 714
Cdd:PLN02680    1 MAVPVIRfPIFMLVRLLGVIVAALVLTWTVHYRGGLA-LSSDNKDLIFNV-HPVLMVIGLVLLNGEAMLAYKTVPGTKNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 715 RKSVHLILQGLALTSGFFGIWT--KFHWDRGfLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHV 792
Cdd:PLN02680   79 KKLVHLTLQFLAFCLSLIGVWAalKFHNEKG-IDNFYSLHSWLGLACLFLFSLQWAAGFVTFWYPGGSRNSRASLLPWHV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123 793 FLGLYSYALAVTVAETGLLEKLTLLQTKRNVPRKGPEAMVVNSLGLALALLGGTVVLTAISP 854
Cdd:PLN02680  158 FFGIYIYALAVATATTGILEKATFLQSNKVISRYSTEAMLVNSLGILIVVLGGFVILAIVTP 219
Cytochrom_B561 pfam03188
Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ...
685-815 1.41e-41

Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport protein. It is an integral membrane protein, that binds two heme groups non-covalently. This is a eukaryotic family. Members of the 'prokaryotic cytochrome b561' family can be found in Pfam: PF01292.


Pssm-ID: 427188  Cd Length: 137  Bit Score: 148.52  E-value: 1.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 685 LHPLFMVIGFILLSGEAILVHSWLPG---SRNLRKSVHLILQGLALTSGFFGIWTKFHW-DRGFLANFHSVHSWLGLSVF 760
Cdd:pfam03188   1 WHPVLMVIGFIFLMGEAILVYRVNSTrrlSKKTKKLLHWILQALALILAVIGLVAVFKFhNLSGIPHFYSLHSWLGLLTV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2047900123 761 TLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGLLEKLT 815
Cdd:pfam03188  81 ILYALQWVGGFVTFLFPGLSKRIRPLLLPLHVFFGLVIFVLAIVTALLGLLEKLI 135
LSm14_N cd01736
Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of ...
16-87 1.83e-38

Like-Sm protein 14, N-terminal domain; LSm14 (also known as RAP55) belongs to a family of Sm-like proteins that associate with RNA to form the core domain of the ribonucleoprotein particles involved in a variety of RNA processing events including pre-mRNA splicing, telomere replication, and mRNA degradation. Members of this family share a highly conserved Sm fold, containing an N-terminal helix followed by a strongly bent five-stranded antiparallel beta-sheet, that associates with other Sm proteins to form hexameric and heptameric ring structures. In addition to the N-terminal Sm-like domain, LSm14 has an uncharacterized C-terminal domain containing a conserved DFDF box. In Xenopus laevis, LSm14 is an oocyte-specific constituent of ribonucleoprotein particles.


Pssm-ID: 212483  Cd Length: 74  Bit Score: 137.33  E-value: 1.83e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123  16 YVGSLISLTSKSEIRYEGVLYNINTEESSIGLRNVRSFGTEGRKKDgPQVPPSDQVFEYILFRGSDIKDLQV 87
Cdd:cd01736     4 YIGSKISLISKSDIRYEGILYTIDTEDSTIALKNVRSFGTEGRPTG-RPIPPSDEVYDYIVFRGSDIKDLTV 74
PLN02810 PLN02810
carbon-monoxide oxygenase
643-853 2.50e-38

carbon-monoxide oxygenase


Pssm-ID: 178406  Cd Length: 231  Bit Score: 142.65  E-value: 2.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 643 PLLIFARILGLLVAVLIFVWALAFSSSFGhLPPAPDDRIFDvLHPLFMVIGFILLSGEAILVHSWLPGSRNLRKSVHLIL 722
Cdd:PLN02810    9 PLTFVAHALAVIGAIMVLVWSIYYRGGLA-WEATNKNLIFN-LHPVLMLIGLIIIGGEAIMSYKSLPLKKEVKKLIHLVL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 723 QGLALTSGFFGIWTKF--HWDRGfLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYA 800
Cdd:PLN02810   87 HAIALILGIFGICAAFknHNESG-IANLYSLHSWLGIGIISLYGIQWIYGFIVFFFPGGSTNLRSGSLPWHVLFGLFVYI 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2047900123 801 LAVTVAETGLLEKLTLLQTKrNVPRKGPEAMVVNSLGLALALLGGTVVLTAIS 853
Cdd:PLN02810  166 LAVGNAALGFLEKLTFLESG-GLDKYGSEALLVNFTAIITILYGAFVVLTALA 217
LSM14 pfam12701
Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from ...
16-87 3.19e-38

Scd6-like Sm domain; The Scd6-like Sm domain is found in Scd6p from S. cerevisiae, Rap55 from the newt Pleurodeles walt, and its orthologs from fungi, animals, plants and apicomplexans. The domain is also found in Dcp3p and the human EDC3/FLJ21128 protein where it is fused to the the Rossmanoid YjeF-N domain. In addition both EDC3 and Scd6p are found fused to the FDF domain.


Pssm-ID: 463675  Cd Length: 75  Bit Score: 136.48  E-value: 3.19e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047900123  16 YVGSLISLTSKSEIRYEGVLYNINTEESSIGLRNVRSFGTEGRkKDGPQVPPSDQVFEYILFRGSDIKDLQV 87
Cdd:pfam12701   2 FIGSRISLISKSDIRYEGILHSIDTEDSTITLKNVRSFGTEGR-GPGPQEPPSDEVYEYIVFRGSDIKDLKI 72
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
685-810 3.29e-35

Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.


Pssm-ID: 214769  Cd Length: 129  Bit Score: 130.04  E-value: 3.29e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  685 LHPLFMVIGFILLSGEAILVHSWL--PGSRNLRKSVHLILQGLALTSGFFGIWTKF-HWDRGFLANFHSVHSWLGLSVFT 761
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARPLtrFLSKPTWFLLHVVLQILALVLGVIGLLAIFiSHNESGIANFYSLHSWLGLAAFV 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2047900123  762 LFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGL 810
Cdd:smart00665  81 LAGLQWLSGFLRPLPPGLPSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
Cyt_b561 cd08554
Eukaryotic cytochrome b(561); Cytochrome b(561) is a family of endosomal or secretory ...
685-810 5.43e-30

Eukaryotic cytochrome b(561); Cytochrome b(561) is a family of endosomal or secretory vesicle-specific electron transport proteins. They are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments. This is an exclusively eukaryotic family. Members of the prokaryotic cytochrome b561 family are not deemed homologous.


Pssm-ID: 176489  Cd Length: 131  Bit Score: 115.46  E-value: 5.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 685 LHPLFMVIGFILLSGEAILV-HSWLPGSRNLRKSVHLILQGLALTSGFFGIWTKF-HWDRGFLANFHSVHSWLGLSVFTL 762
Cdd:cd08554     4 WHPLLMVIGFVFLMGEALLVyRVFRLLTKRALKLLHAILHLLAFVLGLVGLLAVFlFHNAGGIANLYSLHSWLGLATVLL 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2047900123 763 FGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGL 810
Cdd:cd08554    84 FLLQFLSGFVLFLLPLLRLSYRSSLLPFHRFFGLAIFVLAIATILLGI 131
Cyt_b561_CG1275_like cd08764
Non-vertebrate eumetazoan cytochrome b(561); Cytochrome b(561), as found in non-vertebrate ...
657-856 2.29e-27

Non-vertebrate eumetazoan cytochrome b(561); Cytochrome b(561), as found in non-vertebrate eumetazoans, similar to the Drosophila melanogaster CG1275 gene product. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176494  Cd Length: 214  Bit Score: 110.50  E-value: 2.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 657 VLIFVWALAFSSSFGHLPPapdDRIFDvLHPLFMVIGFILLSGEAILVHSWLPGSRNLR-KSVHLILQGLALTSGFFGIW 735
Cdd:cd08764     2 VLVGIWLGKFRGGFSWTGP---GLQFN-WHPLLMVLGLIFLYGNSILVYRVFRNTRKKRlKLLHAVLHLLAFILAVIGLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 736 TKF---HWDRGFLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSYALAVTVAETGLLE 812
Cdd:cd08764    78 AVFdshNLAKPPIPNMYSLHSWLGLTAVILFSLQWVGGFVSFLFPGLPETLRAAYLPLHVFFGLFIFVLAVATALLGITE 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2047900123 813 KltLLQTKRNVPRKGPEAMVVNSLGLALALLGGTVVLTAISPKY 856
Cdd:cd08764   158 K--AFFSLNKYSNLPAEGVLGNFIGIVLVIFGGLVVYLVTEPDY 199
FDF pfam09532
FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an ...
449-552 3.38e-20

FDF domain; The FDF domain, so called because of the conserved FDF at its N termini, is an entirely alpha-helical domain with multiple exposed hydrophilic loops. It is found at the C terminus of Scd6p-like SM domains. It is also found with other divergent Sm domains and in proteins such as Dcp3p and FLJ21128, where it is found N terminal to the YjeF-N domain, a novel Rossmann fold domain.


Pssm-ID: 430668  Cd Length: 104  Bit Score: 86.35  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 449 EKFTEDFDFMAMNEKFNKDEVWGHLGKNTKspkyNDGDEKFSDEDDDYEEDDGESSKLGIKSVYNKDDFFDTLSSNTTNN 528
Cdd:pfam09532   1 IKFDEDFDFESNNAKFNKQEVFAELRKNDK----LDEEKRLVNENNATRVATNEQPNEEVKGVYKKDDFFDNISSEANDR 76
                          90       100
                  ....*....|....*....|....*..
gi 2047900123 529 EAQNGRRTRYF---EQIKLDTETFGEF 552
Cdd:pfam09532  77 GIQSGPSPSGRdwrEERSLNTETFGVD 103
Cyt_b561_CYB561 cd08763
Vertebrate cytochrome b(561), CYB561 gene product; Cytochrome b(561), as found in vertebrates, ...
686-814 6.00e-16

Vertebrate cytochrome b(561), CYB561 gene product; Cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176493  Cd Length: 143  Bit Score: 75.62  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 686 HPLFMVIGFILLSGEAILVHSWLPG-SRNLRKSVHLILQGLALTSGFFGIWT--KFHWDRGFlANFHSVHSWLGLSVFTL 762
Cdd:cd08763    10 HPLCMVLGLVFLCGEALLVYRVFRNeTKRSTKILHGLLHIMALVISLVGLVAvfDYHQANGY-PDMYSLHSWCGILTFVL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2047900123 763 FGAQWMMGFlSFWHWREVRAT-RERVLPWHVFLGLYSYALAVTVAETGLLEKL 814
Cdd:cd08763    89 YFLQWLIGF-SFFLFPGASFTlRSQYKPLHEFFGRALFLSSVGTSLLGLTEKL 140
Cyt_b561_CYB561D2_like cd08761
Eukaryotic cytochrome b(561), including the CYB561D2 gene product; Cytochrome b(561), as found ...
663-812 2.71e-15

Eukaryotic cytochrome b(561), including the CYB561D2 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human CYB561D2 gene product. CYB561D2 is a candidate tumor suppressor. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176491  Cd Length: 183  Bit Score: 75.02  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 663 ALAFSSSFGHLPPaPDDRIFdVLHPLFMVIGFILLSGEAILV----HSWLPGSRNLRKSVHLILQGLALTSGFFGIWTKF 738
Cdd:cd08761     3 AVVFAAFLLYIAR-PGTSLF-SWHPLLMSLGFLLLMTEALLLlqptSSLTKLARKTKVRLHWILQLLALLCILAGLVAIY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047900123 739 --HWDRGfLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPW--HVFLGLYSYALAVTVAETGLLE 812
Cdd:cd08761    81 ynKERNG-KPHFTSWHGILGLVTVILIVLQALGGLALLYPPGLRRGESKAKKLKkyHRLSGYVAYLLGLATLVLGLET 157
Cyt_b561_CYBASC3 cd08762
Vertebrate cytochrome b(561), CYBASC3 gene product; Cytochrome b ascorbate-dependent 3, as ...
646-814 7.80e-13

Vertebrate cytochrome b(561), CYBASC3 gene product; Cytochrome b ascorbate-dependent 3, as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176492  Cd Length: 179  Bit Score: 67.59  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 646 IFARILGLLVAVLIFVWALAFSSSFghlppAPDDRIFDV-LHPLFMVIGFILLSGEAILVH----SWLpGSRNLRKSVHL 720
Cdd:cd08762     2 LLLGILGIACVVLVVHWNQMWRGGF-----AWDGSSKNFnWHPVLMVTGMVVLYGNAALVYriplTWG-GPKLPWKLLHA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 721 ILQGLALTSGFFGIWTKFHW-DRGFLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERVLPWHVFLGLYSY 799
Cdd:cd08762    76 GLLLLAFILTVIGLCAVFNFhNVHHTANLYSLHSWVGICTVALFTCQWVMGFTSFLLPWAPMWLRALVKPIHVFFGAMIL 155
                         170
                  ....*....|....*
gi 2047900123 800 ALAVTVAETGLLEKL 814
Cdd:cd08762   156 VLSIASCISGINEKL 170
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
686-814 7.96e-13

Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate reductase 3, a cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. This protein is expressed at the brush border of duodenal enterocytes and may play a role in the uptake of dietary Fe(3+), facilitating its transport into the mucosal cells. It may also be involved in the recycling of extracellular ascorbate in erythrocyte membranes, and act as a ferrireductase in epithelial cells of the respiratory system. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176495  Cd Length: 153  Bit Score: 66.84  E-value: 7.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 686 HPLFMVIGFILLSGEAILVHSwLPG----SRNLRKSVHLILQGLALTSGFFGIWTKFHW-DRGFLANFHSVHSWLGLSVF 760
Cdd:cd08765    15 HPVLMVIGFIFIQGIAIIVYR-LPWtwkcSKLLMKLIHAGLHILAFILAIISVVAVFVFhNAKNIPNMYSLHSWVGLAAV 93
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2047900123 761 TLFGAQWMMGFLSF---WHWREVRATrerVLPWHVFLGLYSYALAVTVAETGLLEKL 814
Cdd:cd08765    94 ILYPLQLVLGISVYllpVAPVRLRAA---LMPLHVYSGLFIFGTVIATALMGITEKL 147
SM-ATX pfam14438
Ataxin 2 SM domain; This SM domain is found in Ataxin-2.
16-88 2.72e-12

Ataxin 2 SM domain; This SM domain is found in Ataxin-2.


Pssm-ID: 464173  Cd Length: 78  Bit Score: 62.96  E-value: 2.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047900123  16 YVGSLISLTSKSEIRYEGVLYNINTE-ESSIGLRNVRSFGTEGRKKDgpqVPPSDQVFEYILFRGSDIKDLQVK 88
Cdd:pfam14438   8 LVGLVVEVTTKNGEVYEGIFSTASLEkDFGVVLKMARRIKKSNGSGL---NPVRGEIVDTMIFPAKDIVDIEAK 78
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
658-810 4.98e-09

Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176490  Cd Length: 191  Bit Score: 56.97  E-value: 4.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 658 LIFVWALAFSSSFGHLPPAPDDRIFD----VLHPLFMVIGF-ILLSGEAILVHSWLPGSRnLRKSVHLILQGLALTSGFF 732
Cdd:cd08760     7 LDLASGTSSSGGSPFLLPNGSSVGSSdtliKAHGVLMAIAWgILMPIGALLARYFLLGDP-VWFYLHAGLQLLAVLLAIA 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047900123 733 GIWTKFHWDRGFLANFHSVHSWLGLSVFTLFGAQWMMGFLSFWHWREVRATRERvlpWHVFLGLYSYALAVTVAETGL 810
Cdd:cd08760    86 GFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNW---AHRWLGRAALILAIVNIFLGL 160
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
85-412 1.30e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 55.54  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  85 LQVKSSPPVQTTSlinNDPAIIQSHYPRPVSIPSSLPPPVSGPLPDINSQAMPMGIPGSNFQSGLPLY-----------Q 153
Cdd:pfam03154 174 LQAQSGAASPPSP---PPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHpqrlpsphpplQ 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 154 PGGNVGSWGASPSQPPPNPSAGGLGLPMYWQGYYG----------HPNGLPHMHQQSLLRPPPGLSLPSSLQQPLQYPNL 223
Cdd:pfam03154 251 PMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvppQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPS 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 224 NAYLPTGAP---NPLevssslfsanPTAP-SLSSTAMPPVTVSSTLPSVLSVPQTSEMSSSSMVNktINSALPQAPISTN 299
Cdd:pfam03154 331 QSQLQSQQPpreQPL----------PPAPlSMPHIKPPPTTPIPQLPNPQSHKHPPHLSGPSPFQ--MNSNLPPPPALKP 398
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 300 LTSLS---------------PLTASLDVSPVVPPTTNKTTTVSGPALSYQTVSQSTSsiiGTSNSVLTSAPAPALVTPdq 364
Cdd:pfam03154 399 LSSLSthhppsahppplqlmPQSQQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQ---VPSQSPFPQHPFVPGGPP-- 473
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2047900123 365 llhtTVVSSSLPSQTVQKDVEVIQASSSLAAEQTVPVPADTQPPLLPL 412
Cdd:pfam03154 474 ----PITPPSGPPTSTSSAMPGIQPPSSASVSSSGPVPAAVSCPLPPV 517
PRK10118 PRK10118
flagellar hook length control protein FliK;
212-425 4.30e-05

flagellar hook length control protein FliK;


Pssm-ID: 236652 [Multi-domain]  Cd Length: 408  Bit Score: 46.78  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 212 SSLQQPLQYPNLNAYLPTGAPNPLEVSSSLFSANPTAPSLSSTAMPPVTVSSTLPSVLSVPQTSemSSSSMVNKTINSAL 291
Cdd:PRK10118   53 ADLQAAGGKLSKGLLTTKGEPLVSDKLADLLAQQANLLIPVDETLPVITDEQSLSSPLTPALKT--SALAALSKNAQKDE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 292 PQAPIS-TNLTSLSPLTASLDVSPVVPPTTNKTTTVSG---PALSYQTVSQSTSSIIGTSNS-----VLTSAPAPAlVTP 362
Cdd:PRK10118  131 KADDLSdEDLASLSALFAMLPGQDNTTPVADAPSTVLPaekPTLLTKDMPSAPQDETHTLSSdehekGLTSAQLTT-AQP 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2047900123 363 DQLLHTTVVSSSLPSQTVQKDVEVIQASSSL-AAEQTVPVPADTQPplLPlPTSSRVVQKPNGS 425
Cdd:PRK10118  210 DDAPGTPAQPLTPLAAEAQAKAEVISTPSPVtAAASPTITPHQTQP--LP-TAAAPVLSAPLGS 270
PHA03247 PHA03247
large tegument protein UL36; Provisional
102-415 5.29e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  102 DPAIIQSHYPRPVSIPSSLPPPVSGPLPD---INSQAMPMGIPGsnfQSGLPlYQPGGNVGSWGASPSQPPPNPSAGGL- 177
Cdd:PHA03247  2550 DPPPPLPPAAPPAAPDRSVPPPRPAPRPSepaVTSRARRPDAPP---QSARP-RAPVDDRGDPRGPAPPSPLPPDTHAPd 2625
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  178 -----GLPMYWQGYYGHPNGLPHMHQQSLLRPPPGLSLPSSLQQPLQYPNLNAylPTGAPNPLevssslfSANPTAPSLS 252
Cdd:PHA03247  2626 ppppsPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASS--PPQRPRRR-------AARPTVGSLT 2696
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  253 STAMPPVTVSSTLPSVLSVPQTSEMSSSSMVNKTINSALPQAPIsTNLTSLSPLTASLDVSPVVPPTTNKTTTVSGPALS 332
Cdd:PHA03247  2697 SLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPA-PPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP 2775
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123  333 YQTVSQSTSSIIGTSNSV-LTSAPAPalvtPDQLLHTTVVSSSLPSQTVQkdveviQASSSLAAEQTVPVPADTQPPLLP 411
Cdd:PHA03247  2776 AAGPPRRLTRPAVASLSEsRESLPSP----WDPADPPAAVLAPAAALPPA------ASPAGPLPPPTSAQPTAPPPPPGP 2845

                   ....
gi 2047900123  412 LPTS 415
Cdd:PHA03247  2846 PPPS 2849
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
241-429 8.20e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 46.45  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 241 LFSANP----TAPSLSSTAMPPVTVSSTLPSVLSVPqtSEMSSSSMVNKTINSALPQAPISTNLTS-LSPLTASLD---- 311
Cdd:pfam05109 420 IFSKAPesttTSPTLNTTGFAAPNTTTGLPSSTHVP--TNLTAPASTGPTVSTADVTSPTPAGTTSgASPVTPSPSprdn 497
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 312 ------------VSPVVPPTTNKTTTVsgPALSYQTVSQSTSSIIGTSNSVLTSAPAPALVTPDQLLHTTVVSSSLPSqt 379
Cdd:pfam05109 498 gteskapdmtspTSAVTTPTPNATSPT--PAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPT-- 573
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2047900123 380 vqkdveviQASSSLAAEQTVPVPADTQPPLLPLPTSSRVVQKPNGSTSQT 429
Cdd:pfam05109 574 --------LGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSST 615
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
259-396 4.16e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 43.92  E-value: 4.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 259 VTVSSTLPSVLSVPQTSEMSSSsmvNKTINSALPQAPISTNLTSLSPLTASLDVSPVVPPTTNKTTTVSGPALSYQTVSQ 338
Cdd:PRK06347   37 IATSITVPGIEVIVSADETAPA---DEASKSAEANTTKEAPATATPENTTEPTVEPKQTETKEQTKTPEEKQPAAKQVEK 113
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 339 STSSIIGTSNS-VLTSAPAPALVtpdQLLHTTVVSSSlpsQTVQKDVEVIQASSS-LAAE 396
Cdd:PRK06347  114 APAEPATVSNPdNATSSSTPATY---NLLQKSALRSG---ATVQSFIQTIQASSSqIAAE 167
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
206-429 7.98e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 43.02  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 206 PGLSLPSSLQQPLqyPNLNAYLPTgapnplEVSSSLFSANPTAPSLSSTAMPPVTVSSTLPSVlSVPQTSEMSSSSMVNK 285
Cdd:pfam17823 118 AASSSPSSAAQSL--PAAIAALPS------EAFSAPRAAACRANASAAPRAAIAAASAPHAAS-PAPRTAASSTTAASST 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 286 TINSA-------------LPQAPISTNLT-----SLSPLTASLDVSPVVPPTTNKTTTVSGPAlSYQTVSQSTSSIIGTS 347
Cdd:pfam17823 189 TAASSapttaassapatlTPARGISTAATatghpAAGTALAAVGNSSPAAGTVTAAVGTVTPA-ALATLAAAAGTVASAA 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 348 NSVLTSAPAPALVTPDQLLHT-TVVSSSLPSQTVQKDVEVIQASSSLAAEQTVPVPADTQPPLLPLPTSSRVVQKPNGST 426
Cdd:pfam17823 268 GTINMGDPHARRLSPAKHMPSdTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAV 347

                  ...
gi 2047900123 427 SQT 429
Cdd:pfam17823 348 VTT 350
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
246-418 2.20e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 41.48  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 246 PTAPSLSSTAMPPVTVSSTLPSVLSVPQTSEMSSSSMVNKTINSALPQAPISTNLTSLSPLTASLDVSPVVPPTTNKTTT 325
Cdd:pfam17823  66 APAPVTLTKGTSAAHLNSTEVTAEHTPHGTDLSEPATREGAADGAASRALAAAASSSPSSAAQSLPAAIAALPSEAFSAP 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 326 VSGPALSYQTVSQSTSSIIGTSNSVLTSAPAPALVTPDQLLHTTVVSSSLPSQTVQKDVEVIQAS-SSLAAEQTVPVPAD 404
Cdd:pfam17823 146 RAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARgISTAATATGHPAAG 225
                         170
                  ....*....|....
gi 2047900123 405 TQppLLPLPTSSRV 418
Cdd:pfam17823 226 TA--LAAVGNSSPA 237
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
204-416 4.91e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 40.67  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 204 PPPGLSLPSSlqqPLQYPNLNAYLPTGAPNPLEVSSSLFSANPTAPSLSSTAMPPVTVSSTLPSVLSVPqtseMSSSSMV 283
Cdd:pfam05109 551 PTPNATSPTP---AVTTPTPNATIPTLGKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGGTSSTP----VVTSPPK 623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 284 NKTINSALPQAPISTNLTSLSPLTASlDVSPVVPPTTNKTTTVSGPALS--YQTVSQSTSSIIGTSNS---VLTSAPAPA 358
Cdd:pfam05109 624 NATSAVTTGQHNITSSSTSSMSLRPS-SISETLSPSTSDNSTSHMPLLTsaHPTGGENITQVTPASTSthhVSTSSPAPR 702
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2047900123 359 LVTPDQllhttvVSSSLPSQTVQKDVEVIQASSSLAAEQTVPVPADTQPPLLPLPTSS 416
Cdd:pfam05109 703 PGTTSQ------ASGPGNSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTST 754
ArnT COG1807
PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA ...
635-803 7.24e-03

PMT family glycosyltransferase ArnT/Agl22, involved in glycosylation of proteins and lipid IVA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441412 [Multi-domain]  Cd Length: 309  Bit Score: 39.61  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 635 AAALPSLAPLLIFARILGLLVAVLIFVWALAFSSSFGHLppAPDDRIFDVLHPLFMVIGF-------ILLSGEAILVHSW 707
Cdd:COG1807   117 AALLLLTSPLLLLFGRLATPDALLLLFWTLALYALLRAL--ERRRLRWLLLAGLALGLGFltkgpvaLLLPGLALLLYLL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 708 LPGSRNLRKSVHLILqGLALTSGFFGIW---TKFHWDRGFLANFHSVHSWLGLSVFTLFG---AQWMMGFLSF------W 775
Cdd:COG1807   195 LTRRWRRLRRLRLLL-GLLLALLLALPWyiaNDWATGPAFLEYFFGYENLVPLLFFSLSAtklPRYLLPLLPAlallaaA 273
                         170       180
                  ....*....|....*....|....*...
gi 2047900123 776 HWREVRATRERVLPWHVFLGLYSYALAV 803
Cdd:COG1807   274 GLARLRRRRRALLLLALVLLLALLIALL 301
OafA COG1835
Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains ...
641-801 8.59e-03

Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441440  Cd Length: 309  Bit Score: 39.24  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 641 LAPLLIFA--RILGLLVAVLIFVWALAFSSSFGHLPPAPDDRIFDVLHPLF-MVIGFILlsgeAILVHSWLPGSRnlrks 717
Cdd:COG1835   110 LFPLLLLLlrRLRRRLLALLALLALASLLLLALLLTGDPSAAYFLTLTRLWeFLLGALL----ALLYRRLRRLRR----- 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047900123 718 vhlILQGLALTSGFFGIWtkfhwdrgflanFHSVHSWLGLSVFTLFGAqWMMGFLSFWHWREVRATRERVLpwhVFLGLY 797
Cdd:COG1835   181 ---LLALAGLALLLAALL------------LLDGAPFPGFGLLPLLAA-LLVLAAAAGSGLLSRLLSSRPL---VFLGDI 241

                  ....
gi 2047900123 798 SYAL 801
Cdd:COG1835   242 SYSL 245
 
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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