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Conserved domains on  [gi|1914657860|ref|XP_036358703|]
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uncharacterized protein LOC118763360 isoform X19 [Octopus sinensis]

Protein Classification

chitin binding peritrophin-A domain-containing protein; glycoside hydrolase family 18 protein( domain architecture ID 10649518)

chitin binding peritrophin-A domain-containing protein similar to Blomia tropicalis major allergen Blo t 12 and Caenorhabditis elegans chondroitin proteoglycan 1| glycoside hydrolase family 18 protein similar to chitinase, which catalyzes the random endo-hydrolysis of the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
418-531 1.01e-10

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21118:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 495  Bit Score: 66.56  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657860  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
ChtBD2 smart00494
Chitin-binding domain type 2;
1809-1854 2.04e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.04e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1809 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1854
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 6.83e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.74  E-value: 6.83e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1524-1571 1.61e-05

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.97  E-value: 1.61e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1524 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1571
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1442-1487 2.28e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.28e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1442 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1487
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.78e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.78e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657860   258 DTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
194-237 3.50e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.09  E-value: 3.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657860  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1216-1258 2.99e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 2.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657860 1216 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1258
Cdd:pfam01607    8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
382-416 3.75e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657860  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
COG4625 super family cl34793
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
419-761 7.24e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


The actual alignment was detected with superfamily member COG4625:

Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 41.30  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG4625     80 GGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGG 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  499 TGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGI--AGGSQGTGGEGGASGSQGKGGVTGGSQG 576
Cdd:COG4625    160 AGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGggGGAGGGGGGGGGGGGGGGGGGGGGGGGG 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  577 TGGATGGTGGTQGSQIIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTG 656
Cdd:COG4625    240 GGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  657 GGASGNQGTGGGTGGNQETGGVTGGIQGSREGTGGSQGTGEVAGGSQGTSGGTGGNQGTTEVAGGGQGTGGGTSGSGGIG 736
Cdd:COG4625    320 GGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGG 399
                          330       340
                   ....*....|....*....|....*
gi 1914657860  737 GVTGGSKNTGGATGGKQVTGGATSG 761
Cdd:COG4625    400 GGGGGAGGTGGGGAGGGGGAAGGGG 424
ChtBD2 smart00494
Chitin-binding domain type 2;
1627-1671 8.47e-03

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 8.47e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657860  1627 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1671
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
 
Name Accession Description Interval E-value
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
418-531 1.01e-10

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 66.56  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657860  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
450-528 1.28e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 61.14  E-value: 1.28e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657860  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGGGGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS 101
III PHA00370
attachment protein
397-511 7.46e-10

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 62.24  E-value: 7.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657860  470 GGSQGvGGATGGSQGTGGVTGGSqgTGGATGGSQGTGGATGG 511
Cdd:PHA00370   106 GGGSG-GGDTGGSGGGGSDGGGS--EGGSTGKSLTKEGVGAG 144
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
428-529 8.65e-08

Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443056 [Multi-domain]  Cd Length: 443  Bit Score: 56.87  E-value: 8.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657860  500 GGSQGTGGATG-------GSQGAGGATGGSQATGSSQ 529
Cdd:COG3846    355 AGKAAFAQAAGfadsyraGSRAAWAATGGAAARGAGL 391
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
425-529 8.90e-07

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 54.24  E-value: 8.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657860  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
ChtBD2 smart00494
Chitin-binding domain type 2;
1809-1854 2.04e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.04e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1809 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1854
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
442-529 2.16e-06

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 53.09  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  442 SQGTGGATGGNQGTGGATGGSQGAGGATGGSQGV--GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:NF033849   272 SQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTseSQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQST 351
                           90
                   ....*....|
gi 1914657860  520 GGSQATGSSQ 529
Cdd:NF033849   352 SISHSESSSE 361
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
428-531 5.15e-06

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 51.93  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG--T 505
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADS--VSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGdsT 496
                           90       100
                   ....*....|....*....|....*.
gi 1914657860  506 GGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:NF033849   497 GTSESVSQGDGRSTGRSESQGTSLGT 522
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 6.83e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.74  E-value: 6.83e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1524-1571 1.61e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.97  E-value: 1.61e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1524 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1571
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
432-529 3.27e-05

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 49.23  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  432 GNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:NF033849   276 TTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQSTSI 353
                           90       100
                   ....*....|....*....|....
gi 1914657860  512 SQG------AGGATGGSQATGSSQ 529
Cdd:NF033849   354 SHSesssesTGTSVGHSTSSSVSS 377
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1812-1854 3.61e-05

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 42.79  E-value: 3.61e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657860 1812 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1854
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
437-529 9.09e-05

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 47.69  E-value: 9.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  437 TAIGGSQGTGGATggNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAG 516
Cdd:NF033849   233 ANLGQSAGTGYGE--SVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS 310
                           90
                   ....*....|...
gi 1914657860  517 GATGGSQATGSSQ 529
Cdd:NF033849   311 HGTTEGTSTTDSS 323
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
450-529 1.38e-04

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 46.92  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGgaTGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESES--TGQSSSVGTSE 307
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
111-151 2.08e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.86  E-value: 2.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657860  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
ChtBD2 smart00494
Chitin-binding domain type 2;
1442-1487 2.28e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.28e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1442 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1487
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1532-1576 2.48e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.47  E-value: 2.48e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657860 1532 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1576
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.78e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.78e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657860   258 DTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
194-237 3.50e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.09  E-value: 3.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657860  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.52e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 3.52e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657860   193 PCEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:smart00494    2 ECPGrgDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
428-533 8.03e-04

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 44.61  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEG-GNGRETAIGGSQGTGgaTGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGatggSQGTG 506
Cdd:NF033849   291 TSESeSTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQSTSISHSESS----SESTG 364
                           90       100
                   ....*....|....*....|....*..
gi 1914657860  507 GATGGSQGAGGATGGSQATGSSQGTGG 533
Cdd:NF033849   365 TSVGHSTSSSVSSSESSSRSSSSGVSG 391
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1441-1487 8.39e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 38.93  E-value: 8.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657860 1441 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1487
Cdd:pfam01607    1 CAGKEDG-YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
256-297 9.08e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 38.93  E-value: 9.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657860  256 LQDTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICD 45
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1216-1258 2.99e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 2.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657860 1216 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1258
Cdd:pfam01607    8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
382-416 3.75e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657860  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
1214-1254 5.22e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.65  E-value: 5.22e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657860  1214 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1254
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
419-761 7.24e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 41.30  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG4625     80 GGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGG 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  499 TGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGI--AGGSQGTGGEGGASGSQGKGGVTGGSQG 576
Cdd:COG4625    160 AGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGggGGAGGGGGGGGGGGGGGGGGGGGGGGGG 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  577 TGGATGGTGGTQGSQIIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTG 656
Cdd:COG4625    240 GGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  657 GGASGNQGTGGGTGGNQETGGVTGGIQGSREGTGGSQGTGEVAGGSQGTSGGTGGNQGTTEVAGGGQGTGGGTSGSGGIG 736
Cdd:COG4625    320 GGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGG 399
                          330       340
                   ....*....|....*....|....*
gi 1914657860  737 GVTGGSKNTGGATGGKQVTGGATSG 761
Cdd:COG4625    400 GGGGGAGGTGGGGAGGGGGAAGGGG 424
ChtBD2 smart00494
Chitin-binding domain type 2;
1627-1671 8.47e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 8.47e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657860  1627 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1671
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
 
Name Accession Description Interval E-value
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
418-531 1.01e-10

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 66.56  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657860  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
450-528 1.28e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 61.14  E-value: 1.28e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657860  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGGGGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS 101
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
429-524 1.33e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 61.14  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107
                           90
                   ....*....|....*....
gi 1914657860  506 GGATGGSQGAGGATGGSQA 524
Cdd:pfam16210  108 SGGRGSSSGGVKSSGGSSS 126
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
440-528 5.71e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 59.22  E-value: 5.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGatgGSQGTGGvTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGG---GSYGSGG-GGGSGSGGGSSGGHRGGSGGGGGSSGGRSGG 98

                   ....*....
gi 1914657860  520 GGSQATGSS 528
Cdd:pfam16210   99 GSSGGSFGS 107
III PHA00370
attachment protein
397-511 7.46e-10

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 62.24  E-value: 7.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657860  470 GGSQGvGGATGGSQGTGGVTGGSqgTGGATGGSQGTGGATGG 511
Cdd:PHA00370   106 GGGSG-GGDTGGSGGGGSDGGGS--EGGSTGKSLTKEGVGAG 144
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
401-528 3.27e-09

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 61.55  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  401 WDGESTKCIYDELASALRGINAKPENQTGE---GGNGRETAIGGSQGTGGATGG-NQGT-----------GGATGGSQ-- 463
Cdd:cd21118    121 WQGSGGHGAYGSQGGPGVQGHGIPGGTGGPwasGGNYGTNSLGGSVGQGGNGGPlNYGTnsqgavaqpgyGTVRGNNQns 200
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657860  464 ------GAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:cd21118    201 gctnppPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSG 271
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
428-529 8.65e-08

Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443056 [Multi-domain]  Cd Length: 443  Bit Score: 56.87  E-value: 8.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657860  500 GGSQGTGGATG-------GSQGAGGATGGSQATGSSQ 529
Cdd:COG3846    355 AGKAAFAQAAGfadsyraGSRAAWAATGGAAARGAGL 391
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
440-526 1.82e-07

Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443056 [Multi-domain]  Cd Length: 443  Bit Score: 55.71  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  440 GGSQGTGGATGGnqgTGGATGGSQGAGGATGGsqGVGGATGGSQGTGGVTGGSQGTGGATG----GSQGTGgaTGGSQGA 515
Cdd:COG3846    265 GGPQLGAGAAAG---TGAAAGGAAVAAGAAAA--AAAGGAAAAGGAAAARGGASAAGGAKAayslGSAGSG--SGAAGVA 337
                           90
                   ....*....|.
gi 1914657860  516 GGATGGSQATG 526
Cdd:COG3846    338 AGMGGVGRAGG 348
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
440-528 4.27e-07

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 54.53  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  440 GGSQ-GTGGATGgnqgTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA-TGGSQGTGGATGGSQGAGG 517
Cdd:PRK13875   265 GAPQlGAGAAVG----TGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGAsSAYSAGAAGGSGAAGVAAG 340
                           90
                   ....*....|.
gi 1914657860  518 ATGGSQATGSS 528
Cdd:PRK13875   341 LGGVARAGASA 351
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
425-529 8.90e-07

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 54.24  E-value: 8.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657860  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
ChtBD2 smart00494
Chitin-binding domain type 2;
1809-1854 2.04e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.04e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1809 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1854
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
442-529 2.16e-06

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 53.09  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  442 SQGTGGATGGNQGTGGATGGSQGAGGATGGSQGV--GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:NF033849   272 SQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTseSQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQST 351
                           90
                   ....*....|
gi 1914657860  520 GGSQATGSSQ 529
Cdd:NF033849   352 SISHSESSSE 361
III PHA00370
attachment protein
461-528 2.69e-06

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 51.46  E-value: 2.69e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657860  461 GSQGAGGATGGSQGVGGATGGSQGTGGVTGGSqgTGGATGGSQGtggatGGSQGaGGATGGSQATGSS 528
Cdd:PHA00370    78 GSADKDGDGGGTGEGGSDTGGDTGGGNTGGGS--GGGDTGGSGG-----GGSDG-GGSEGGSTGKSLT 137
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
428-531 5.15e-06

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 51.93  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG--T 505
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADS--VSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGdsT 496
                           90       100
                   ....*....|....*....|....*.
gi 1914657860  506 GGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:NF033849   497 GTSESVSQGDGRSTGRSESQGTSLGT 522
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
418-547 6.28e-06

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 51.15  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  418 RGINAKPENQTGEGGNGretaIGGSQGtgGATGGNQGTGGATGGSQGAGG-----ATGGSQGVGGATGG-SQGTGGVTGG 491
Cdd:cd21118    112 HGVDAVHNSWQGSGGHG----AYGSQG--GPGVQGHGIPGGTGGPWASGGnygtnSLGGSVGQGGNGGPlNYGTNSQGAV 185
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  492 SQGTGGATGGSQGTGGAT----GGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGG 547
Cdd:cd21118    186 AQPGYGTVRGNNQNSGCTnpppSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGG 245
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
426-528 6.72e-06

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 51.10  E-value: 6.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  426 NQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG--TGGVTGGSQGTGGATGGSQ 503
Cdd:COG3468      3 SGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGgaGGGGGGAGSGGGLAGAGSG 82
                           90       100
                   ....*....|....*....|....*
gi 1914657860  504 GTGGATGGSQGAGGATGGSQATGSS 528
Cdd:COG3468     83 GTGGNSTGGGGGNSGTGGTGGGGGG 107
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 6.83e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.74  E-value: 6.83e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
451-527 1.40e-05

Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443056 [Multi-domain]  Cd Length: 443  Bit Score: 49.94  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  451 GNQGTGGA----TGGSQ-GAGGATGGSQGVGGATGGsqGTGGVTGGsqgtGGATGGSQGTGGATGGSQGAGGATG----G 521
Cdd:COG3846    252 GIFGPGIAaglvSGGPQlGAGAAAGTGAAAGGAAVA--AGAAAAAA----AGGAAAAGGAAAARGGASAAGGAKAayslG 325

                   ....*.
gi 1914657860  522 SQATGS 527
Cdd:COG3846    326 SAGSGS 331
ChtBD2 smart00494
Chitin-binding domain type 2;
1524-1571 1.61e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.97  E-value: 1.61e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1524 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1571
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
440-527 1.82e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 49.46  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  440 GGSQGTGGATGGNQ--GTGGATGGSQGAGGAT-GGSQGVGGAT-GGSQGTGGVT-GGSQGTGGATGGSQGTGGA--TGGS 512
Cdd:PTZ00473   312 HDSRGPYNANYGGQfnSRSGRTGSSESIRGFTyDSSTTYGGSSyGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGS 391
                           90
                   ....*....|....*
gi 1914657860  513 QGAGGATGGSQATGS 527
Cdd:PTZ00473   392 STFDGSSRGSSDSFG 406
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
429-525 2.77e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 48.69  E-value: 2.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGAT--GGSQGAGGATGGSQGVGGAT-GGSQGTGGVTGGSQGTGGA--TGGSQ 503
Cdd:PTZ00473   313 DSRGPYNANYGGQFNSRSGRTGSSESIRGFTydSSTTYGGSSYGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGSS 392
                           90       100
                   ....*....|....*....|...
gi 1914657860  504 GTGGATGGS-QGAGGATGGSQAT 525
Cdd:PTZ00473   393 TFDGSSRGSsDSFGVSYFGPQQT 415
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
432-529 3.27e-05

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 49.23  E-value: 3.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  432 GNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:NF033849   276 TTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQSTSI 353
                           90       100
                   ....*....|....*....|....
gi 1914657860  512 SQG------AGGATGGSQATGSSQ 529
Cdd:NF033849   354 SHSesssesTGTSVGHSTSSSVSS 377
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1812-1854 3.61e-05

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 42.79  E-value: 3.61e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657860 1812 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1854
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
431-528 4.76e-05

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 48.12  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  431 GGNGRETAIGGSQGTGGATGGNQG-TGGATGGSQGAGGA-----TGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG 504
Cdd:pfam15967    8 GGPGSTATAGGGFSFGAAAASNPGsTGGFSFGTLGAAPAatattTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTG 87
                           90       100
                   ....*....|....*....|....*..
gi 1914657860  505 -TGGATGGSQGA--GGATGGSQATGSS 528
Cdd:pfam15967   88 lTLGTPAATTAAstGFSLGFNKPAASA 114
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
428-529 5.36e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.98  E-value: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGAT-------GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATG 500
Cdd:PRK13875   290 AGAGLAAGGGAAAAGGAAAAARGGAAAAGGASsaysagaAGGSGAAGVAAGLGGVARAGASAAASPLRRAASRAAESMKS 369
                           90       100
                   ....*....|....*....|....*....
gi 1914657860  501 GSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:PRK13875   370 SFRAGARSTGGGAGGAAAAAAAGAAAAGP 398
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
440-528 5.69e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.60  E-value: 5.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTG----GSQGTGGATGGSQGTGG-ATGGSQG 514
Cdd:PRK13875   272 GAAVGTGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGASSaysaGAAGGSGAAGVAAGLGGvARAGASA 351
                           90
                   ....*....|....*....
gi 1914657860  515 AG-----GATGGSQATGSS 528
Cdd:PRK13875   352 AAsplrrAASRAAESMKSS 370
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
444-551 7.91e-05

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 47.85  E-value: 7.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  444 GTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQ 523
Cdd:COG4625      1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80
                           90       100
                   ....*....|....*....|....*...
gi 1914657860  524 ATGSSQGTGGATGGSEGGSQIPGGIAGG 551
Cdd:COG4625     81 GGGGGGGGGTGGVGGGGGGGGGGGGGGG 108
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
437-529 9.09e-05

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 47.69  E-value: 9.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  437 TAIGGSQGTGGATggNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAG 516
Cdd:NF033849   233 ANLGQSAGTGYGE--SVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS 310
                           90
                   ....*....|...
gi 1914657860  517 GATGGSQATGSSQ 529
Cdd:NF033849   311 HGTTEGTSTTDSS 323
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
440-526 1.37e-04

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 46.44  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  440 GGSQGTGGATGGNQ-GTGGATGGSQGAGG-ATGGSQGVGGATGGsqgtgGVTGGSQGTGGATGGSQGTGGA-TGGSQGAG 516
Cdd:PRK13875   255 GPGIANGLVSGAPQlGAGAAVGTGLAAGGaAVAAAAGAGLAAGG-----GAAAAGGAAAAARGGAAAAGGAsSAYSAGAA 329
                           90
                   ....*....|
gi 1914657860  517 GATGGSQATG 526
Cdd:PRK13875   330 GGSGAAGVAA 339
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
450-529 1.38e-04

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 46.92  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGgaTGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESES--TGQSSSVGTSE 307
PTZ00146 PTZ00146
fibrillarin; Provisional
470-521 1.46e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.88  E-value: 1.46e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657860  470 GGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGG 521
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
425-528 1.55e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 46.53  E-value: 1.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  425 ENQTGEGGNGRETAIGgsQGTGGATGGNQGTGG-ATGGSQGagGATGGSQGVGGATGGSQGTGGV-----TGGSQGTGGA 498
Cdd:cd21118     96 GNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGhGAYGSQG--GPGVQGHGIPGGTGGPWASGGNygtnsLGGSVGQGGN 171
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657860  499 TG------GSQGTGGATG-------------------GSQGAGGATGGSQATGSS 528
Cdd:cd21118    172 GGplnygtNSQGAVAQPGygtvrgnnqnsgctnpppsGSHESFSNSGGSSSSGSS 226
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
399-528 1.71e-04

Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 46.69  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  399 TVWDGESTKCIYDELASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGA---TGGSQGV 475
Cdd:COG5295    271 TASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTASGASAaaaTNDGTAN 350
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657860  476 GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:COG5295    351 GAGTSAAADATSGGGAGGGGAAATSSSGGSATAAGNAAGAAGAGSAGSGGSST 403
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
111-151 2.08e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.86  E-value: 2.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657860  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
ChtBD2 smart00494
Chitin-binding domain type 2;
1442-1487 2.28e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.28e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657860  1442 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1487
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1532-1576 2.48e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.47  E-value: 2.48e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657860 1532 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1576
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
PTZ00146 PTZ00146
fibrillarin; Provisional
460-511 2.50e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.11  E-value: 2.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657860  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
437-533 2.61e-04

Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 45.92  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  437 TAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAG 516
Cdd:COG5295      3 SNAGAVAAGTALTTVASGASTTASGSSATVTSAAQSTGSAATSSGSSSAAGGSGSTSSLTAAAATAGAGSGGTSATAASS 82
                           90
                   ....*....|....*..
gi 1914657860  517 GATGGSQATGSSQGTGG 533
Cdd:COG5295     83 VASGGASAATAASTGTG 99
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.78e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.78e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657860   258 DTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
PTZ00146 PTZ00146
fibrillarin; Provisional
450-501 3.18e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 3.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657860  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGG 501
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
452-529 3.34e-04

Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in nucleoporin proteins. This family includes the yeast nucleoporins Nup116, Nup100, Nup49, Nup57 and Nup 145.


Pssm-ID: 463941 [Multi-domain]  Cd Length: 90  Bit Score: 41.45  E-value: 3.34e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657860  452 NQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQgTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:pfam13634    7 TSTSGGLFGNTSTTAASGGGLFGAASTATATTSGGGLFGNSS-SNAPSGGLFGATNTTTQTATGGGLFGNNAATTTST 83
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
194-237 3.50e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 40.09  E-value: 3.50e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657860  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.52e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 3.52e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657860   193 PCEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:smart00494    2 ECPGrgDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PTZ00146 PTZ00146
fibrillarin; Provisional
440-495 3.96e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 3.96e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657860  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvtGGSQGT 495
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGG--GGPGKV 57
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
454-529 4.59e-04

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 45.32  E-value: 4.59e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657860  454 GTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:COG3468      1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGL 76
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
411-502 6.18e-04

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 42.71  E-value: 6.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  411 DELASALRGINAKPENQTGEGGNGretaiggsqgtggatGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTG 490
Cdd:PRK07772   104 DEIGPSLRYATAKVTRASRGGGGG---------------GGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPADDPW 168
                           90
                   ....*....|..
gi 1914657860  491 GSQGTGGATGGS 502
Cdd:PRK07772   169 SSAPASGGFGGG 180
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
428-533 8.03e-04

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.


Pssm-ID: 468206 [Multi-domain]  Cd Length: 1122  Bit Score: 44.61  E-value: 8.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  428 TGEG-GNGRETAIGGSQGTGgaTGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGatggSQGTG 506
Cdd:NF033849   291 TSESeSTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQSTSISHSESS----SESTG 364
                           90       100
                   ....*....|....*....|....*..
gi 1914657860  507 GATGGSQGAGGATGGSQATGSSQGTGG 533
Cdd:NF033849   365 TSVGHSTSSSVSSSESSSRSSSSGVSG 391
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1441-1487 8.39e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 38.93  E-value: 8.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657860 1441 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1487
Cdd:pfam01607    1 CAGKEDG-YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
256-297 9.08e-04

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 38.93  E-value: 9.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657860  256 LQDTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICD 45
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
427-522 1.65e-03

Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. The proteins are composed of several glycine rich motifs interspersed through the sequence. Although many proteins have been annotated by similarity in the family these annotations given the biased composition of the sequences these are unlikely to be functionally relevant.


Pssm-ID: 403882 [Multi-domain]  Cd Length: 257  Bit Score: 42.26  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  427 QTGEGGNGRETAIGGSQGtGGATGGNQGTGGATGGSQ------------------GAGGATGGSQGVGGATGGSQGTGGV 488
Cdd:pfam12810   55 GKGEYNNSTNMNPGGFNG-GGNYKGSSGDGSGGGGGAtdirfdenslksriivagGGGGSGEGDDGSGGYGGGLTGGGGG 133
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657860  489 TGGSQGTGGAT---GGSQGTGGatGGSQGAGGATGGS 522
Cdd:pfam12810  134 SGCYEGSYGATqtsGGIGGYGI--NGSFGQGGNGRNS 168
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
422-528 1.91e-03

Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.


Pssm-ID: 435043 [Multi-domain]  Cd Length: 586  Bit Score: 43.12  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  422 AKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG-TGGVTGGSQG--TGGA 498
Cdd:pfam15967   25 AAASNPGSTGGFSFGTLGAAPAATATTTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTGlTLGTPAATTAasTGFS 104
                           90       100       110
                   ....*....|....*....|....*....|
gi 1914657860  499 TGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam15967  105 LGFNKPAASATPFSLPASSTSGGGLSLGSV 134
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
460-520 2.43e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 41.17  E-value: 2.43e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657860  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQgtGGATGGSQGAGGATG 520
Cdd:PRK07772   124 GGGGGGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPADDP--WSSAPASGGFGGGDD 182
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
444-528 2.83e-03

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 42.83  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  444 GTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQ 523
Cdd:COG3210    816 GSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGT 895

                   ....*
gi 1914657860  524 ATGSS 528
Cdd:COG3210    896 LTNLG 900
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
1216-1258 2.99e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 2.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657860 1216 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1258
Cdd:pfam01607    8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
431-512 3.16e-03

Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. The proteins are composed of several glycine rich motifs interspersed through the sequence. Although many proteins have been annotated by similarity in the family these annotations given the biased composition of the sequences these are unlikely to be functionally relevant.


Pssm-ID: 403882 [Multi-domain]  Cd Length: 257  Bit Score: 41.49  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  431 GGNGRETAIGGSQGtGGATGGNQGTGGA---TGGSQGAGG----ATGGSQGVGGATGGSQGTGGVTGGSqGTGGATGGSQ 503
Cdd:pfam12810  111 GGSGEGDDGSGGYG-GGLTGGGGGSGCYegsYGATQTSGGiggyGINGSFGQGGNGRNSGGGGGGGGGG-GYYGGFGGGS 188

                   ....*....
gi 1914657860  504 GTGGATGGS 512
Cdd:pfam12810  189 YGGGGGGGS 197
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
450-510 3.48e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 40.40  E-value: 3.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657860  450 GGNQGTGGATGGsqGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATG 510
Cdd:PRK07772   124 GGGGGGGGGFGG--GGGGSGGGGGGGGGGGAPGGGGAQASAPADDPWSSAPASGGFGGGDD 182
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
382-416 3.75e-03

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.39  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657860  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
PTZ00146 PTZ00146
fibrillarin; Provisional
431-484 4.60e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914657860  431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG 484
Cdd:PTZ00146     2 MGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
454-508 4.98e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657860  454 GTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGA 508
Cdd:PTZ00146     1 GMGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
446-498 4.98e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657860  446 GGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvTGGSQGTGGA 498
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGG-RGGGGGGGPG 55
ChtBD2 smart00494
Chitin-binding domain type 2;
1214-1254 5.22e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.65  E-value: 5.22e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657860  1214 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1254
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
419-525 5.43e-03

Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 41.68  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATggsqgVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG5295    253 ASSVSGSAVAAGTASTATTASTTAASGAAGTATAAAGGDAAAAGSASSTGA-----ANATAGGGNAGSGGGGAAALGSAG 327
                           90       100
                   ....*....|....*....|....*..
gi 1914657860  499 TGGSQGTGGATGGSQGAGGATGGSQAT 525
Cdd:COG5295    328 GSSGVGTASGASAAAATNDGTANGAGT 354
PTZ00146 PTZ00146
fibrillarin; Provisional
429-481 5.73e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 5.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657860  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGG 481
Cdd:PTZ00146     3 GGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
414-581 6.82e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 41.30  E-value: 6.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  414 ASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQ 493
Cdd:COG4625    196 GGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGS 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  494 GTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGKGGVTGG 573
Cdd:COG4625    276 GGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGA 355

                   ....*...
gi 1914657860  574 SQGTGGAT 581
Cdd:COG4625    356 GGGGGGGT 363
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
419-761 7.24e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 41.30  E-value: 7.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG4625     80 GGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGG 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  499 TGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGI--AGGSQGTGGEGGASGSQGKGGVTGGSQG 576
Cdd:COG4625    160 AGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGggGGAGGGGGGGGGGGGGGGGGGGGGGGGG 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  577 TGGATGGTGGTQGSQIIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTG 656
Cdd:COG4625    240 GGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 319
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657860  657 GGASGNQGTGGGTGGNQETGGVTGGIQGSREGTGGSQGTGEVAGGSQGTSGGTGGNQGTTEVAGGGQGTGGGTSGSGGIG 736
Cdd:COG4625    320 GGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGG 399
                          330       340
                   ....*....|....*....|....*
gi 1914657860  737 GVTGGSKNTGGATGGKQVTGGATSG 761
Cdd:COG4625    400 GGGGGAGGTGGGGAGGGGGAAGGGG 424
ChtBD2 smart00494
Chitin-binding domain type 2;
1627-1671 8.47e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 8.47e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657860  1627 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1671
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
 
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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