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Conserved domains on  [gi|1080062222|ref|XP_018573145|]
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host cell factor 2 isoform X1 [Anoplophora glabripennis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
14-334 7.06e-23

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.85  E-value: 7.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   14 PTGPQPRPRHGHRAVAIKDLMVVFGGGNEG-IVDELHVYNTATNQWfvpvTKGDVPPGCAAYGF--VVEGTRLLVFGGMV 90
Cdd:COG3055      5 SLPDLPTPRSEAAAALLDGKVYVAGGLSGGsASNSFEVYDPATNTW----SELAPLPGPPRHHAaaVAQDGKLYVFGGFT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   91 EY---GKYSNELYELQASKWEWKKLkprppkaNPAPCPRLGHSFTLVNARVYLFGGlandsadpkSNVPRYLNDLYTLDI 167
Cdd:COG3055     81 GAnpsSTPLNDVYVYDPATNTWTKL-------APMPTPRGGATALLLDGKIYVVGG---------WDDGGNVAWVEVYDP 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  168 RSNpiQWdipSTNGPSPPPRESHTGVAYVDknkGKsfLVIYGGMSGcrlgdlwflETETMTWSKPqvsGTTPLPRSLHTS 247
Cdd:COG3055    145 ATG--TW---TQLAPLPTPRDHLAAAVLPD---GK--ILVIGGRNG---------SGFSNTWTTL---APLPTARAGHAA 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  248 TLIGHRMFVFGGwvpvvadevktatnEKEWkcTSTMACLNLETMNWDELkidashkaeNTLPCARAGHCAVGISTRLYIW 327
Cdd:COG3055    203 AVLGGKILVFGG--------------ESGF--SDEVEAYDPATNTWTAL---------GELPTPRHGHAAVLTDGKVYVI 257


                   ....*....
gi 1080062222  328 SG--RDGYR 334
Cdd:COG3055    258 GGetKPGVR 266
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1058-1158 1.95e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1058 PGAPSAIKI-AKSADGAHLSWEPPSANQGEILEYSVYLavrgkeKANPPGQLAFVRVYSGPSNQCVVSNaslaaahLDTS 1136
Cdd:cd00063      1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGPITGYVVEY------REKGSGDWKEVEVTPGSETSYTLTG-------LKPG 67

                           90       100
                   ....*....|....*....|..
gi 1080062222 1137 TKaaIIFRIAAKNDKGYGPATQ 1158
Cdd:cd00063     68 TE--YEFRVRAVNGGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1022-1052 2.51e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.72  E-value: 2.51e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1080062222 1022 NLEPGTAYKFRVAAINSVGRGEWSEVSAFKT 1052
Cdd:cd00063     63 GLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
SP1-4_N super family cl41773
N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins ...
 414-692 7.50e-06

N-terminal domain of transcription factor Specificity Proteins (SP) 1-4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. SPs belong to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP1-4.


The actual alignment was detected with superfamily member cd22540:

Pssm-ID: 425404 [Multi-domain]  Cd Length: 511  Bit Score: 49.92  E-value: 7.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  414 TSPKQAQSVLGSPSTPTQGAKTTVIPNQIIAPKVVAPIIKAPPVRVQGTTGTIIRQATPQV-AGKQLVVKQGGNLIQKAg 492
Cdd:cd22540    206 TLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIqAGNNLLIVQSPGTGQPA- 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  493 GVQQQVVTLVKTSTGM-TLATLPKSGNLVQSKATGTVIPQQAKNTIVKIVPSSPANKVLTTlktiPSNMIQMnkttgKLV 571
Cdd:cd22540    285 VLQQVQVLQPKQEQQVvQIPQQALRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKT----PSGEVQT-----VLL 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  572 LSKGTGQIPTLSNQQVLVVSSNAglkNIQTFTNAQAVNVSTVKT-----------TTINAQPVAAASSIaglQGVKIAGk 640
Cdd:cd22540    356 QEAPAATATPSSSTSTVQQQVTA---NNGTGTSKPNYNVRKERTlpkiapaggiiSLNAAQLAAAAQAI---QTINING- 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1080062222  641 pitismpMQVVGSPKTVTlskNTKqvmiGGKQVTVQMATSSNKTLTLVQPNQ 692
Cdd:cd22540    429 -------VQVQGVPVTIT---NAG----GQQQLTVQTVSSNNLTISGLSPTQ 466
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
14-334 7.06e-23

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.85  E-value: 7.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   14 PTGPQPRPRHGHRAVAIKDLMVVFGGGNEG-IVDELHVYNTATNQWfvpvTKGDVPPGCAAYGF--VVEGTRLLVFGGMV 90
Cdd:COG3055      5 SLPDLPTPRSEAAAALLDGKVYVAGGLSGGsASNSFEVYDPATNTW----SELAPLPGPPRHHAaaVAQDGKLYVFGGFT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   91 EY---GKYSNELYELQASKWEWKKLkprppkaNPAPCPRLGHSFTLVNARVYLFGGlandsadpkSNVPRYLNDLYTLDI 167
Cdd:COG3055     81 GAnpsSTPLNDVYVYDPATNTWTKL-------APMPTPRGGATALLLDGKIYVVGG---------WDDGGNVAWVEVYDP 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  168 RSNpiQWdipSTNGPSPPPRESHTGVAYVDknkGKsfLVIYGGMSGcrlgdlwflETETMTWSKPqvsGTTPLPRSLHTS 247
Cdd:COG3055    145 ATG--TW---TQLAPLPTPRDHLAAAVLPD---GK--ILVIGGRNG---------SGFSNTWTTL---APLPTARAGHAA 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  248 TLIGHRMFVFGGwvpvvadevktatnEKEWkcTSTMACLNLETMNWDELkidashkaeNTLPCARAGHCAVGISTRLYIW 327
Cdd:COG3055    203 AVLGGKILVFGG--------------ESGF--SDEVEAYDPATNTWTAL---------GELPTPRHGHAAVLTDGKVYVI 257


                   ....*....
gi 1080062222  328 SG--RDGYR 334
Cdd:COG3055    258 GGetKPGVR 266
PLN02193 PLN02193
nitrile-specifier protein
 7-296 2.16e-20

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 95.79  E-value: 2.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222    7 QW-KLVANPTGPQPRPRHGHRAVAIKdlMVVFGGG---NEGIVDELHVYNTATNQWFVPVTKGDVPP-GCAAYGFVVEGT 81
Cdd:PLN02193   152 KWiKVEQKGEGPGLRCSHGIAQVGNK--IYSFGGEftpNQPIDKHLYVFDLETRTWSISPATGDVPHlSCLGVRMVSIGS 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   82 RLLVFGGMVEYGKYsNELYELQASKWEWKKLKPrppkANPAPCPRLGHSFTLVNARVYLFGGLandSADPKsnvpryLND 161
Cdd:PLN02193   230 TLYVFGGRDASRQY-NGFYSFDTTTNEWKLLTP----VEEGPTPRSFHSMAADEENVYVFGGV---SATAR------LKT 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  162 LYTLDIRSNpiQWDIPSTNGPSPPPReshtGVAYVDKNKGKSFlVIYGgMSGCRLGDLWFLETETMTWSKPQVSGTTPLP 241
Cdd:PLN02193   296 LDSYNIVDK--KWFHCSTPGDSFSIR----GGAGLEVVQGKVW-VVYG-FNGCEVDDVHYYDPVQDKWTQVETFGVRPSE 367

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1080062222  242 RSLHTSTLIGHRMFVFGGWVPvvadeVKTATNEKEWKCTSTMACLNLETMNWDEL 296
Cdd:PLN02193   368 RSVFASAAVGKHIVIFGGEIA-----MDPLAHVGPGQLTDGTFALDTETLQWERL 417
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1058-1158 1.95e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1058 PGAPSAIKI-AKSADGAHLSWEPPSANQGEILEYSVYLavrgkeKANPPGQLAFVRVYSGPSNQCVVSNaslaaahLDTS 1136
Cdd:cd00063      1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGPITGYVVEY------REKGSGDWKEVEVTPGSETSYTLTG-------LKPG 67

                           90       100
                   ....*....|....*....|..
gi 1080062222 1137 TKaaIIFRIAAKNDKGYGPATQ 1158
Cdd:cd00063     68 TE--YEFRVRAVNGGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1022-1052 2.51e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.72  E-value: 2.51e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1080062222 1022 NLEPGTAYKFRVAAINSVGRGEWSEVSAFKT 1052
Cdd:cd00063     63 GLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 414-692 7.50e-06

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 49.92  E-value: 7.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  414 TSPKQAQSVLGSPSTPTQGAKTTVIPNQIIAPKVVAPIIKAPPVRVQGTTGTIIRQATPQV-AGKQLVVKQGGNLIQKAg 492
Cdd:cd22540    206 TLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIqAGNNLLIVQSPGTGQPA- 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  493 GVQQQVVTLVKTSTGM-TLATLPKSGNLVQSKATGTVIPQQAKNTIVKIVPSSPANKVLTTlktiPSNMIQMnkttgKLV 571
Cdd:cd22540    285 VLQQVQVLQPKQEQQVvQIPQQALRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKT----PSGEVQT-----VLL 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  572 LSKGTGQIPTLSNQQVLVVSSNAglkNIQTFTNAQAVNVSTVKT-----------TTINAQPVAAASSIaglQGVKIAGk 640
Cdd:cd22540    356 QEAPAATATPSSSTSTVQQQVTA---NNGTGTSKPNYNVRKERTlpkiapaggiiSLNAAQLAAAAQAI---QTINING- 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1080062222  641 pitismpMQVVGSPKTVTlskNTKqvmiGGKQVTVQMATSSNKTLTLVQPNQ 692
Cdd:cd22540    429 -------VQVQGVPVTIT---NAG----GQQQLTVQTVSSNNLTISGLSPTQ 466
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1022-1109 9.17e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 46.53  E-value: 9.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1022 NLEPGTAYKFRVAAINSVG-RGEWSEVSAFKTCLPGfPGAPSAIKI-AKSADGAHLSWEPPSANQgeILEYSVYlavRGK 1099
Cdd:COG3401    291 GLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP-PAAPSGLTAtAVGSSSITLSWTASSDAD--VTGYNVY---RST 364

                           90
                   ....*....|
gi 1080062222 1100 EKANPPGQLA 1109
Cdd:COG3401    365 SGGGTYTKIA 374
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 21-58 1.24e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 40.67  E-value: 1.24e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1080062222   21 PRHGHRAVAIKDLMVVFGGGNEG-IVDELHVYNTATNQW 58
Cdd:pfam01344    1 RRSGAGVVVVGGKIYVIGGFDGNqSLNSVEVYDPETNTW 39
fn3 pfam00041
Fibronectin type III domain;
1059-1157 2.33e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1059 GAPSAIKI-AKSADGAHLSWEPPSANQGEILEYSVYLAVRGKEKANPPGQLafvrvySGPSNQCVVSNaslaaahLDTST 1137
Cdd:pfam00041    1 SAPSNLTVtDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV------PGTTTSVTLTG-------LKPGT 67

                           90       100
                   ....*....|....*....|
gi 1080062222 1138 KaaIIFRIAAKNDKGYGPAT 1157
Cdd:pfam00041   68 E--YEVRVQAVNGGGEGPPS 85
fn3 pfam00041
Fibronectin type III domain;
1022-1045 6.02e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 6.02e-04
                           10        20
                   ....*....|....*....|....
gi 1080062222 1022 NLEPGTAYKFRVAAINSVGRGEWS 1045
Cdd:pfam00041   62 GLKPGTEYEVRVQAVNGGGEGPPS 85
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1022-1042 7.45e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.82  E-value: 7.45e-03
                            10        20
                    ....*....|....*....|.
gi 1080062222  1022 NLEPGTAYKFRVAAINSVGRG 1042
Cdd:smart00060   63 GLKPGTEYEFRVRAVNGAGEG 83
 
Name Accession Description Interval E-value
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
14-334 7.06e-23

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.85  E-value: 7.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   14 PTGPQPRPRHGHRAVAIKDLMVVFGGGNEG-IVDELHVYNTATNQWfvpvTKGDVPPGCAAYGF--VVEGTRLLVFGGMV 90
Cdd:COG3055      5 SLPDLPTPRSEAAAALLDGKVYVAGGLSGGsASNSFEVYDPATNTW----SELAPLPGPPRHHAaaVAQDGKLYVFGGFT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   91 EY---GKYSNELYELQASKWEWKKLkprppkaNPAPCPRLGHSFTLVNARVYLFGGlandsadpkSNVPRYLNDLYTLDI 167
Cdd:COG3055     81 GAnpsSTPLNDVYVYDPATNTWTKL-------APMPTPRGGATALLLDGKIYVVGG---------WDDGGNVAWVEVYDP 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  168 RSNpiQWdipSTNGPSPPPRESHTGVAYVDknkGKsfLVIYGGMSGcrlgdlwflETETMTWSKPqvsGTTPLPRSLHTS 247
Cdd:COG3055    145 ATG--TW---TQLAPLPTPRDHLAAAVLPD---GK--ILVIGGRNG---------SGFSNTWTTL---APLPTARAGHAA 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  248 TLIGHRMFVFGGwvpvvadevktatnEKEWkcTSTMACLNLETMNWDELkidashkaeNTLPCARAGHCAVGISTRLYIW 327
Cdd:COG3055    203 AVLGGKILVFGG--------------ESGF--SDEVEAYDPATNTWTAL---------GELPTPRHGHAAVLTDGKVYVI 257


                   ....*....
gi 1080062222  328 SG--RDGYR 334
Cdd:COG3055    258 GGetKPGVR 266
PLN02193 PLN02193
nitrile-specifier protein
 7-296 2.16e-20

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 95.79  E-value: 2.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222    7 QW-KLVANPTGPQPRPRHGHRAVAIKdlMVVFGGG---NEGIVDELHVYNTATNQWFVPVTKGDVPP-GCAAYGFVVEGT 81
Cdd:PLN02193   152 KWiKVEQKGEGPGLRCSHGIAQVGNK--IYSFGGEftpNQPIDKHLYVFDLETRTWSISPATGDVPHlSCLGVRMVSIGS 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   82 RLLVFGGMVEYGKYsNELYELQASKWEWKKLKPrppkANPAPCPRLGHSFTLVNARVYLFGGLandSADPKsnvpryLND 161
Cdd:PLN02193   230 TLYVFGGRDASRQY-NGFYSFDTTTNEWKLLTP----VEEGPTPRSFHSMAADEENVYVFGGV---SATAR------LKT 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  162 LYTLDIRSNpiQWDIPSTNGPSPPPReshtGVAYVDKNKGKSFlVIYGgMSGCRLGDLWFLETETMTWSKPQVSGTTPLP 241
Cdd:PLN02193   296 LDSYNIVDK--KWFHCSTPGDSFSIR----GGAGLEVVQGKVW-VVYG-FNGCEVDDVHYYDPVQDKWTQVETFGVRPSE 367

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1080062222  242 RSLHTSTLIGHRMFVFGGWVPvvadeVKTATNEKEWKCTSTMACLNLETMNWDEL 296
Cdd:PLN02193   368 RSVFASAAVGKHIVIFGGEIA-----MDPLAHVGPGQLTDGTFALDTETLQWERL 417
PLN02153 PLN02153
epithiospecifier protein
 7-296 1.64e-16

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 82.34  E-value: 1.64e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222    7 QWKLVANPTGPQPRPRHGHRAVAIKDLMVVFGGG---NEGIVDELHVYNTATNQWFVPVTKGDVPP-GCAAYGFVVEGTR 82
Cdd:PLN02153     8 GWIKVEQKGGKGPGPRCSHGIAVVGDKLYSFGGElkpNEHIDKDLYVFDFNTHTWSIAPANGDVPRiSCLGVRMVAVGTK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   83 LLVFGGMVEYGKYSNeLYELQASKWEWKKLKPRPPKANPAPcpRLGHSFTLVNARVYLFGGLandSADPKSNVPRYLNDL 162
Cdd:PLN02153    88 LYIFGGRDEKREFSD-FYSYDTVKNEWTFLTKLDEEGGPEA--RTFHSMASDENHVYVFGGV---SKGGLMKTPERFRTI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  163 YTLDIRSNpiQWdipsTNGPSPPPRESHTGVAYVDKNKGKSFLV-------IYGGMSGCRLGDLWFLETETMTWSKPQVS 235
Cdd:PLN02153   162 EAYNIADG--KW----VQLPDPGENFEKRGGAGFAVVQGKIWVVygfatsiLPGGKSDYESNAVQFFDPASGKWTEVETT 235

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1080062222  236 GTTPLPRSLHTSTLIGHRMFVFGGWV-PVVADEVKTATNEKEWkctstmACLNLETMNWDEL 296
Cdd:PLN02153   236 GAKPSARSVFAHAVVGKYIIIFGGEVwPDLKGHLGPGTLSNEG------YALDTETLVWEKL 291
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
3-103 6.45e-07

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 52.47  E-value: 6.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222    3 GKALQWKLVANPtgpqPRPRHGHRAVAIKDLMVVFGGGNeGIVDELHVYNTATNQWfvpVTKGDVPPGCAAYGFVVEGTR 82
Cdd:COG3055    182 GFSNTWTTLAPL----PTARAGHAAAVLGGKILVFGGES-GFSDEVEAYDPATNTW---TALGELPTPRHGHAAVLTDGK 253

                           90       100
                   ....*....|....*....|.
gi 1080062222   83 LLVFGGMVEYGKYSNELYELQ 103
Cdd:COG3055    254 VYVIGGETKPGVRTPLVTSAE 274
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1058-1158 1.95e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 1.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1058 PGAPSAIKI-AKSADGAHLSWEPPSANQGEILEYSVYLavrgkeKANPPGQLAFVRVYSGPSNQCVVSNaslaaahLDTS 1136
Cdd:cd00063      1 PSPPTNLRVtDVTSTSVTLSWTPPEDDGGPITGYVVEY------REKGSGDWKEVEVTPGSETSYTLTG-------LKPG 67

                           90       100
                   ....*....|....*....|..
gi 1080062222 1137 TKaaIIFRIAAKNDKGYGPATQ 1158
Cdd:cd00063     68 TE--YEFRVRAVNGGGESPPSE 87
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1022-1052 2.51e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 46.72  E-value: 2.51e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1080062222 1022 NLEPGTAYKFRVAAINSVGRGEWSEVSAFKT 1052
Cdd:cd00063     63 GLKPGTEYEFRVRAVNGGGESPPSESVTVTT 93
SP2_N cd22540
N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins ...
 414-692 7.50e-06

N-terminal domain of transcription factor Specificity Protein (SP) 2; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. SP2 contains the least conserved DNA-binding domain within the SP subfamily of proteins, and its DNA sequence specificity differs from the other SP proteins. It localizes primarily within subnuclear foci associated with the nuclear matrix, and can activate, or in some cases, repress expression from different promoters. The transcription factor SP2 serves as a paradigm for indirect genomic binding. It does not require its DNA-binding domain for genomic DNA binding and occupies target promoters independently of whether they contain a cognate DNA-binding motif. SP2 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP2.


Pssm-ID: 411776 [Multi-domain]  Cd Length: 511  Bit Score: 49.92  E-value: 7.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  414 TSPKQAQSVLGSPSTPTQGAKTTVIPNQIIAPKVVAPIIKAPPVRVQGTTGTIIRQATPQV-AGKQLVVKQGGNLIQKAg 492
Cdd:cd22540    206 TLPVNNLVGTQDGATQLQLAAAPSKPSKKIRKKSAQAAQPAVTVAEQVETVLIETTADNIIqAGNNLLIVQSPGTGQPA- 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  493 GVQQQVVTLVKTSTGM-TLATLPKSGNLVQSKATGTVIPQQAKNTIVKIVPSSPANKVLTTlktiPSNMIQMnkttgKLV 571
Cdd:cd22540    285 VLQQVQVLQPKQEQQVvQIPQQALRVVQAASATLPTVPQKPLQNIQIQNSEPTPTQVYIKT----PSGEVQT-----VLL 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  572 LSKGTGQIPTLSNQQVLVVSSNAglkNIQTFTNAQAVNVSTVKT-----------TTINAQPVAAASSIaglQGVKIAGk 640
Cdd:cd22540    356 QEAPAATATPSSSTSTVQQQVTA---NNGTGTSKPNYNVRKERTlpkiapaggiiSLNAAQLAAAAQAI---QTINING- 428

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1080062222  641 pitismpMQVVGSPKTVTlskNTKqvmiGGKQVTVQMATSSNKTLTLVQPNQ 692
Cdd:cd22540    429 -------VQVQGVPVTIT---NAG----GQQQLTVQTVSSNNLTISGLSPTQ 466
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1022-1109 9.17e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 46.53  E-value: 9.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1022 NLEPGTAYKFRVAAINSVG-RGEWSEVSAFKTCLPGfPGAPSAIKI-AKSADGAHLSWEPPSANQgeILEYSVYlavRGK 1099
Cdd:COG3401    291 GLTNGTTYYYRVTAVDAAGnESAPSNVVSVTTDLTP-PAAPSGLTAtAVGSSSITLSWTASSDAD--VTGYNVY---RST 364

                           90
                   ....*....|
gi 1080062222 1100 EKANPPGQLA 1109
Cdd:COG3401    365 SGGGTYTKIA 374
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 21-58 1.24e-04

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 40.67  E-value: 1.24e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1080062222   21 PRHGHRAVAIKDLMVVFGGGNEG-IVDELHVYNTATNQW 58
Cdd:pfam01344    1 RRSGAGVVVVGGKIYVIGGFDGNqSLNSVEVYDPETNTW 39
PRK14131 PRK14131
N-acetylneuraminate epimerase;
7-88 1.87e-04

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 45.39  E-value: 1.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222    7 QWKLVANPTGPqprPRHGHRAVAIKDLMVVFGG----GNEG---IVDELHVYNTATNQWFVPVTKGdvPPGCA-AYGFVV 78
Cdd:PRK14131    63 GWTKIAAFPGG---PREQAVAAFIDGKLYVFGGigktNSEGspqVFDDVYKYDPKTNSWQKLDTRS--PVGLAgHVAVSL 137

                           90
                   ....*....|
gi 1080062222   79 EGTRLLVFGG 88
Cdd:PRK14131   138 HNGKAYITGG 147
Kelch_3 pfam13415
Galactose oxidase, central domain;
135-195 2.16e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.97  E-value: 2.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1080062222  135 NARVYLFGGLANDSADpksnvprYLNDLYTLDIRSNpiQWDipsTNGPSPPPRESHTGVAY 195
Cdd:pfam13415    1 GDKLYIFGGLGFDGQT-------RLNDLYVYDLDTN--TWT---QIGDLPPPRSGHSATYI 49
fn3 pfam00041
Fibronectin type III domain;
1059-1157 2.33e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.25  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1059 GAPSAIKI-AKSADGAHLSWEPPSANQGEILEYSVYLAVRGKEKANPPGQLafvrvySGPSNQCVVSNaslaaahLDTST 1137
Cdd:pfam00041    1 SAPSNLTVtDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITV------PGTTTSVTLTG-------LKPGT 67

                           90       100
                   ....*....|....*....|
gi 1080062222 1138 KaaIIFRIAAKNDKGYGPAT 1157
Cdd:pfam00041   68 E--YEVRVQAVNGGGEGPPS 85
Kelch_3 pfam13415
Galactose oxidase, central domain;
202-250 5.74e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 38.81  E-value: 5.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1080062222  202 KSFLVIYGG---MSGCRLGDLWFLETETMTWSKPqvsGTTPLPRSLHTSTLI 250
Cdd:pfam13415    1 GDKLYIFGGlgfDGQTRLNDLYVYDLDTNTWTQI---GDLPPPRSGHSATYI 49
fn3 pfam00041
Fibronectin type III domain;
1022-1045 6.02e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 39.71  E-value: 6.02e-04
                           10        20
                   ....*....|....*....|....
gi 1080062222 1022 NLEPGTAYKFRVAAINSVGRGEWS 1045
Cdd:pfam00041   62 GLKPGTEYEVRVQAVNGGGEGPPS 85
Kelch_4 pfam13418
Galactose oxidase, central domain;
21-58 1.17e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 37.98  E-value: 1.17e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1080062222   21 PRHGHRAVAIKDLMV-VFGG--GNEGIVDELHVYNTATNQW 58
Cdd:pfam13418    1 PRAYHTSTSIPDDTIyLFGGegEDGTLLSDLWVFDLSTNEW 41
Kelch_3 pfam13415
Galactose oxidase, central domain;
82-134 1.51e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 37.65  E-value: 1.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1080062222   82 RLLVFGGMVEYG-KYSNELYELQASKWEWKKLKPRPPkanpapcPRLGHSFTLV 134
Cdd:pfam13415    3 KLYIFGGLGFDGqTRLNDLYVYDLDTNTWTQIGDLPP-------PRSGHSATYI 49
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 19-56 1.91e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 37.16  E-value: 1.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1080062222   19 PRPRHGHRAVAIKDLMVVFGG---GNEGIVDELHVYNTATN 56
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGytgGEGQPSDDVYVLSLPTF 41
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 309-336 2.42e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 36.77  E-value: 2.42e-03
                           10        20
                   ....*....|....*....|....*...
gi 1080062222  309 PCARAGHCAVGISTRLYIWSGRDGYRKA 336
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYTGGEGQ 28
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 123-170 3.07e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 36.39  E-value: 3.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1080062222  123 PCPRLGHSFTLVNARVYLFGGLAndsadpkSNVPRYLNDLYTLDIRSN 170
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYT-------GGEGQPSDDVYVLSLPTF 41
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1021-1111 3.85e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 41.53  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222 1021 INLEPGTAYKFRVAAINSVGRGEWS-EVSAFKTCLPgfPGAPSAIK-IAKSADGAHLSWEPPSANqgEILEYSVYlavRG 1098
Cdd:COG3401    197 GDIEPGTTYYYRVAATDTGGESAPSnEVSVTTPTTP--PSAPTGLTaTADTPGSVTLSWDPVTES--DATGYRVY---RS 269

                           90
                   ....*....|...
gi 1080062222 1099 KEKANPPGQLAFV 1111
Cdd:COG3401    270 NSGDGPFTKVATV 282
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 68-107 4.00e-03

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 36.00  E-value: 4.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1080062222   68 PPGCAAYGFVVEGTRLLVFGGMV-EYGKYSNELYELQASKW 107
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYTgGEGQPSDDVYVLSLPTF 41
SP4_N cd22536
N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins ...
 596-715 5.26e-03

N-terminal domain of transcription factor Specificity Protein (SP) 4; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. Human SP4 is a risk gene of multiple psychiatric disorders including schizophrenia, bipolar disorder, and major depression. SP4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. SP1-4 have similar N-terminal transactivation domains characterized by glutamine-rich regions, which, in most cases, have adjacent serine/threonine-rich regions. This model represents the N-terminal domain of SP4.


Pssm-ID: 411773 [Multi-domain]  Cd Length: 623  Bit Score: 41.06  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  596 LKNIQTFTNAQAVNVSTVKTTTINaqPVAAASS---IAGLQGVKIAGKPITI------SMP--------------MQVVG 652
Cdd:cd22536    448 VQNIQSLSNLQVQNAGLPQQLTLT--PVSSSAGgttIAQIAPVAVAGTPITLnaaqlaSVPnlqtvnvanlgaagVQVQG 525

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222  653 SPKTVTLSKNTKQVMIGGK-------QVTVQMATSSNKTLTLVQPNQTGGvgkiVRLPMSSAASNNSEQP 715
Cdd:cd22536    526 VPVTITSVAGQQQGQDGVKvqqatiaPVTVAVGNIANATIGAVSPDQITQ----VQLQQAQQASDQEVQP 591
PRK14131 PRK14131
N-acetylneuraminate epimerase;
46-146 7.09e-03

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 40.00  E-value: 7.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080062222   46 DELHVYNTATNQWFVpvtKGDVP-PGCAAYGFVVEGTRLLVFGGMVEYGKYSNE--LYELQASKWEWKKLKPRPPKANPA 122
Cdd:PRK14131   189 KEVLSYDPSTNQWKN---AGESPfLGTAGSAVVIKGNKLWLINGEIKPGLRTDAvkQGKFTGNNLKWQKLPDLPPAPGGS 265

                           90       100
                   ....*....|....*....|....
gi 1080062222  123 PCPRLGHSFTLVNARVYLFGGLAN 146
Cdd:PRK14131   266 SQEGVAGAFAGYSNGVLLVAGGAN 289
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1022-1042 7.45e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.82  E-value: 7.45e-03
                            10        20
                    ....*....|....*....|.
gi 1080062222  1022 NLEPGTAYKFRVAAINSVGRG 1042
Cdd:smart00060   63 GLKPGTEYEFRVRAVNGAGEG 83
Kelch_4 pfam13418
Galactose oxidase, central domain;
73-117 8.24e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 35.67  E-value: 8.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1080062222   73 AYGFVVEGTRLLVFGGMVEYGKYSNELYELQASKWEWKKLKPRPP 117
Cdd:pfam13418    5 HTSTSIPDDTIYLFGGEGEDGTLLSDLWVFDLSTNEWTRLGSLPS 49
 
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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