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Conserved domains on  [gi|1914657826|ref|XP_036358685|]
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uncharacterized protein LOC118763360 isoform X2 [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 2.88e-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: 65.02  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657826  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
COG4625 super family cl34793
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 419-884 5.86e-07

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: 54.78  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG4625     30 GGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGG 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  499 TGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGKGGVTGGSQGTG 578
Cdd:COG4625    110 GGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  579 GATGGTGGTQGSQIIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTGGG 658
Cdd:COG4625    190 GGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGG 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  659 ASGNQGTGGGTGGNQETGGVTGGIQGSREGTGGSQGTGEVAGGNQGTTEVAGGGQGTGGGTSGSGGIGGVTGGSKNTGGA 738
Cdd:COG4625    270 GGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGG 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  739 TGGKQVTGGATSGNQGTGGTGVNQGTGGGTGSSQGTGGDASGNQGTGGGTGGNQATGGGTSGNQGTEDGTGSSQGTGGVA 818
Cdd:COG4625    350 AGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGA 429

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657826  819 GGKQGTGSGTGSNQGTGGVANGNQAKGGGKDGKQGSGGETGGDQGAGGGTGSNQGTGGVangnQVS 884
Cdd:COG4625    430 GGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTT----TVN 491
ChtBD2 smart00494
Chitin-binding domain type 2;
1859-1904 1.74e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.67  E-value: 1.74e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1859 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1904
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 5.60e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 45.13  E-value: 5.60e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1574-1621 1.37e-05

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.97  E-value: 1.37e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1574 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1621
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1492-1537 2.00e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.89  E-value: 2.00e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1492 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1537
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.39e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.39e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657826   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 3.19e-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: 3.19e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657826  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 ...
 1266-1308 2.78e-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: 37.78  E-value: 2.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657826 1266 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1308
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 3.52e-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: 3.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657826  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
1677-1721 7.57e-03

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 7.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657826  1677 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1721
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 2.88e-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: 65.02  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657826  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
450-528 8.81e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 58.83  E-value: 8.81e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657826  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGGGGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS 101
III PHA00370
attachment protein
 397-511 2.39e-09

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 60.70  E-value: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657826  470 GGSQGvGGATGGSQGTGGVTGGSqgTGGATGGSQGTGGATGG 511
Cdd:PHA00370   106 GGGSG-GGDTGGSGGGGSDGGGS--EGGSTGKSLTKEGVGAG 144
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 428-529 8.91e-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: 8.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657826  500 GGSQGTGGATG-------GSQGAGGATGGSQATGSSQ 529
Cdd:COG3846    355 AGKAAFAQAAGfadsyraGSRAAWAATGGAAARGAGL 391
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 419-884 5.86e-07

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 54.78  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG4625     30 GGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGG 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  499 TGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGKGGVTGGSQGTG 578
Cdd:COG4625    110 GGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  579 GATGGTGGTQGSQIIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTGGG 658
Cdd:COG4625    190 GGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGG 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  659 ASGNQGTGGGTGGNQETGGVTGGIQGSREGTGGSQGTGEVAGGNQGTTEVAGGGQGTGGGTSGSGGIGGVTGGSKNTGGA 738
Cdd:COG4625    270 GGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGG 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  739 TGGKQVTGGATSGNQGTGGTGVNQGTGGGTGSSQGTGGDASGNQGTGGGTGGNQATGGGTSGNQGTEDGTGSSQGTGGVA 818
Cdd:COG4625    350 AGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGA 429

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657826  819 GGKQGTGSGTGSNQGTGGVANGNQAKGGGKDGKQGSGGETGGDQGAGGGTGSNQGTGGVangnQVS 884
Cdd:COG4625    430 GGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTT----TVN 491
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 425-529 1.08e-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: 53.86  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657826  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
ChtBD2 smart00494
Chitin-binding domain type 2;
1859-1904 1.74e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.67  E-value: 1.74e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1859 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1904
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 2.57e-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: 52.70  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  442 SQGTGGATGGNQGTGGATGGSQGAGGATGGSQGV--GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:NF033849   272 SQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTseSQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQST 351

                           90
                   ....*....|
gi 1914657826  520 GGSQATGSSQ 529
Cdd:NF033849   352 SISHSESSSE 361
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 5.60e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 45.13  E-value: 5.60e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
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 ...
 428-531 6.07e-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: 51.54  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG--T 505
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADS--VSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGdsT 496

                           90       100
                   ....*....|....*....|....*.
gi 1914657826  506 GGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:NF033849   497 GTSESVSQGDGRSTGRSESQGTSLGT 522
ChtBD2 smart00494
Chitin-binding domain type 2;
1574-1621 1.37e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.97  E-value: 1.37e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1574 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1621
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1862-1904 3.29e-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: 43.17  E-value: 3.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657826 1862 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1904
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 1.07e-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: 47.31  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  437 TAIGGSQGTGGATggNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAG 516
Cdd:NF033849   233 ANLGQSAGTGYGE--SVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS 310

                           90
                   ....*....|...
gi 1914657826  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 1.62e-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: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQ 309
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 111-151 1.99e-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: 1.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657826  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
ChtBD2 smart00494
Chitin-binding domain type 2;
1492-1537 2.00e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.89  E-value: 2.00e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1492 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1537
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1582-1626 2.33e-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: 2.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657826 1582 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1626
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.39e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.39e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657826   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 3.19e-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: 3.19e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657826  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.21e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 3.21e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657826   193 PCEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:smart00494    2 ECPGrgDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1491-1537 7.81e-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: 39.32  E-value: 7.81e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657826 1491 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1537
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 8.53e-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: 8.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657826  256 LQDTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICD 45
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 428-533 8.84e-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: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEG-GNGRETAIGGSQGTGgaTGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGatggSQGTG 506
Cdd:NF033849   291 TSESeSTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQSTSISHSESS----SESTG 364

                           90       100
                   ....*....|....*....|....*..
gi 1914657826  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 ...
 1266-1308 2.78e-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: 37.78  E-value: 2.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657826 1266 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1308
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 3.52e-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: 3.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657826  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
1264-1304 4.67e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 37.04  E-value: 4.67e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657826  1264 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1304
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1677-1721 7.57e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 7.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657826  1677 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1721
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 2.88e-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: 65.02  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657826  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
450-528 8.81e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 58.83  E-value: 8.81e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657826  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGGGGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS 101
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
429-528 1.31e-09

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 58.06  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSqgtGGA 508
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS---GGS 104

                           90       100
                   ....*....|....*....|
gi 1914657826  509 TGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210  105 FGSSGGRGSSSGGVKSSGGS 124
III PHA00370
attachment protein
 397-511 2.39e-09

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 60.70  E-value: 2.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657826  470 GGSQGvGGATGGSQGTGGVTGGSqgTGGATGGSQGTGGATGG 511
Cdd:PHA00370   106 GGGSG-GGDTGGSGGGGSDGGGS--EGGSTGKSLTKEGVGAG 144
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
440-528 5.36e-09

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 56.52  E-value: 5.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGatgGSQGTGGvTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGG---GSYGSGG-GGGSGSGGGSSGGHRGGSGGGGGSSGGRSGG 98


                   ....*....
gi 1914657826  520 GGSQATGSS 528
Cdd:pfam16210   99 GSSGGSFGS 107
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 429-528 1.13e-08

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: 60.01  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  429 GEGGNGRETAIG-GSQGT------GGATGGNQGTGGATGGSQGAGGatGGSQGVGGATGGSQGTGGVTGGSQGTGGATGG 501
Cdd:cd21118    167 GQGGNGGPLNYGtNSQGAvaqpgyGTVRGNNQNSGCTNPPPSGSHE--SFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSG 244

                           90       100
                   ....*....|....*....|....*..
gi 1914657826  502 SQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:cd21118    245 GQGNGGNNGSSSSNSGNSGGSNGGSSG 271
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 428-529 8.91e-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: 8.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657826  500 GGSQGTGGATG-------GSQGAGGATGGSQATGSSQ 529
Cdd:COG3846    355 AGKAAFAQAAGfadsyraGSRAAWAATGGAAARGAGL 391
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 440-526 1.88e-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: 1.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  440 GGSQGTGGATGGnqgTGGATGGSQGAGGATGGsqGVGGATGGSQGTGGVTGGSQGTGGATG----GSQGTGgaTGGSQGA 515
Cdd:COG3846    265 GGPQLGAGAAAG---TGAAAGGAAVAAGAAAA--AAAGGAAAAGGAAAARGGASAAGGAKAayslGSAGSG--SGAAGVA 337

                           90
                   ....*....|.
gi 1914657826  516 GGATGGSQATG 526
Cdd:COG3846    338 AGMGGVGRAGG 348
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-528 4.40e-07

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 54.53  E-value: 4.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  440 GGSQ-GTGGATGgnqgTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA-TGGSQGTGGATGGSQGAGG 517
Cdd:PRK13875   265 GAPQlGAGAAVG----TGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGAsSAYSAGAAGGSGAAGVAAG 340

                           90
                   ....*....|.
gi 1914657826  518 ATGGSQATGSS 528
Cdd:PRK13875   341 LGGVARAGASA 351
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 419-884 5.86e-07

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 54.78  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  419 GINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA 498
Cdd:COG4625     30 GGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGG 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  499 TGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGKGGVTGGSQGTG 578
Cdd:COG4625    110 GGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  579 GATGGTGGTQGSQIIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTGGG 658
Cdd:COG4625    190 GGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGG 269

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  659 ASGNQGTGGGTGGNQETGGVTGGIQGSREGTGGSQGTGEVAGGNQGTTEVAGGGQGTGGGTSGSGGIGGVTGGSKNTGGA 738
Cdd:COG4625    270 GGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGG 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  739 TGGKQVTGGATSGNQGTGGTGVNQGTGGGTGSSQGTGGDASGNQGTGGGTGGNQATGGGTSGNQGTEDGTGSSQGTGGVA 818
Cdd:COG4625    350 AGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGA 429

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657826  819 GGKQGTGSGTGSNQGTGGVANGNQAKGGGKDGKQGSGGETGGDQGAGGGTGSNQGTGGVangnQVS 884
Cdd:COG4625    430 GGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTYTGTT----TVN 491
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 425-529 1.08e-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: 53.86  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657826  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
ChtBD2 smart00494
Chitin-binding domain type 2;
1859-1904 1.74e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.67  E-value: 1.74e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1859 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1904
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 414-527 2.41e-06

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 52.86  E-value: 2.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  414 ASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQ 493
Cdd:COG4625     51 GGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAG 130

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657826  494 GTGGATGGSQGTGGATGGSQGAGGATGGSQATGS 527
Cdd:COG4625    131 GGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGG 164
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 442-529 2.57e-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: 52.70  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  442 SQGTGGATGGNQGTGGATGGSQGAGGATGGSQGV--GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:NF033849   272 SQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTseSQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQST 351

                           90
                   ....*....|
gi 1914657826  520 GGSQATGSSQ 529
Cdd:NF033849   352 SISHSESSSE 361
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 5.60e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 45.13  E-value: 5.60e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
III PHA00370
attachment protein
 461-528 5.80e-06

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 50.30  E-value: 5.80e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657826  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 6.07e-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: 51.54  E-value: 6.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG--T 505
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADS--VSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGdsT 496

                           90       100
                   ....*....|....*....|....*.
gi 1914657826  506 GGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:NF033849   497 GTSESVSQGDGRSTGRSESQGTSLGT 522
ChtBD2 smart00494
Chitin-binding domain type 2;
1574-1621 1.37e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.97  E-value: 1.37e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1574 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1621
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 451-527 1.44e-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: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  451 GNQGTGGA----TGGSQ-GAGGATGGSQGVGGATGGsqGTGGVTGGsqgtGGATGGSQGTGGATGGSQGAGGATG----G 521
Cdd:COG3846    252 GIFGPGIAaglvSGGPQlGAGAAAGTGAAAGGAAVA--AGAAAAAA----AGGAAAAGGAAAARGGASAAGGAKAayslG 325


                   ....*.
gi 1914657826  522 SQATGS 527
Cdd:COG3846    326 SAGSGS 331
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 440-527 1.89e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 49.46  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  440 GGSQGTGGATGGNQ--GTGGATGGSQGAGGAT-GGSQGVGGAT-GGSQGTGGVT-GGSQGTGGATGGSQGTGGA--TGGS 512
Cdd:PTZ00473   312 HDSRGPYNANYGGQfnSRSGRTGSSESIRGFTyDSSTTYGGSSyGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGS 391

                           90
                   ....*....|....*
gi 1914657826  513 QGAGGATGGSQATGS 527
Cdd:PTZ00473   392 STFDGSSRGSSDSFG 406
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 429-525 2.95e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 48.69  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGAT--GGSQGAGGATGGSQGVGGAT-GGSQGTGGVTGGSQGTGGA--TGGSQ 503
Cdd:PTZ00473   313 DSRGPYNANYGGQFNSRSGRTGSSESIRGFTydSSTTYGGSSYGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGSS 392

                           90       100
                   ....*....|....*....|...
gi 1914657826  504 GTGGATGGS-QGAGGATGGSQAT 525
Cdd:PTZ00473   393 TFDGSSRGSsDSFGVSYFGPQQT 415
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1862-1904 3.29e-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: 43.17  E-value: 3.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657826 1862 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1904
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 428-529 5.51e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.98  E-value: 5.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGAT-------GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATG 500
Cdd:PRK13875   290 AGAGLAAGGGAAAAGGAAAAARGGAAAAGGASsaysagaAGGSGAAGVAAGLGGVARAGASAAASPLRRAASRAAESMKS 369

                           90       100
                   ....*....|....*....|....*....
gi 1914657826  501 GSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:PRK13875   370 SFRAGARSTGGGAGGAAAAAAAGAAAAGP 398
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 437-528 5.65e-05

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


Pssm-ID: 442691 [Multi-domain]  Cd Length: 846  Bit Score: 48.40  E-value: 5.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  437 TAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAG 516
Cdd:COG3468      4 GGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGG 83

                           90
                   ....*....|..
gi 1914657826  517 GATGGSQATGSS 528
Cdd:COG3468     84 TGGNSTGGGGGN 95
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-528 5.86e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.60  E-value: 5.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTG----GSQGTGGATGGSQGTGG-ATGGSQG 514
Cdd:PRK13875   272 GAAVGTGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGASSaysaGAAGGSGAAGVAAGLGGvARAGASA 351

                           90
                   ....*....|....*....
gi 1914657826  515 AG-----GATGGSQATGSS 528
Cdd:PRK13875   352 AAsplrrAASRAAESMKSS 370
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
 431-528 9.45e-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: 47.35  E-value: 9.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  431 GGNGRETAIGGSQGTGGATGGNQG-TGGATGGSQGAGGA-----TGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG 504
Cdd:pfam15967    8 GGPGSTATAGGGFSFGAAAASNPGsTGGFSFGTLGAAPAatattTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTG 87

                           90       100
                   ....*....|....*....|....*..
gi 1914657826  505 -TGGATGGSQGA--GGATGGSQATGSS 528
Cdd:pfam15967   88 lTLGTPAATTAAstGFSLGFNKPAASA 114
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 437-529 1.07e-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: 47.31  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  437 TAIGGSQGTGGATggNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAG 516
Cdd:NF033849   233 ANLGQSAGTGYGE--SVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS 310

                           90
                   ....*....|...
gi 1914657826  517 GATGGSQATGSSQ 529
Cdd:NF033849   311 HGTTEGTSTTDSS 323
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-526 1.41e-04

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 46.44  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  440 GGSQGTGGATGGNQ-GTGGATGGSQGAGG-ATGGSQGVGGATGGsqgtgGVTGGSQGTGGATGGSQGTGGA-TGGSQGAG 516
Cdd:PRK13875   255 GPGIANGLVSGAPQlGAGAAVGTGLAAGGaAVAAAAGAGLAAGG-----GAAAAGGAAAAARGGAAAAGGAsSAYSAGAA 329

                           90
                   ....*....|
gi 1914657826  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 1.62e-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: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQ 309
PTZ00146 PTZ00146
fibrillarin; Provisional
 470-521 1.84e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.49  E-value: 1.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657826  470 GGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGG 521
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 111-151 1.99e-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: 1.99e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657826  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
ChtBD2 smart00494
Chitin-binding domain type 2;
1492-1537 2.00e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.89  E-value: 2.00e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657826  1492 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1537
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1582-1626 2.33e-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: 2.33e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657826 1582 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1626
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.39e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.39e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657826   258 DTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 413-528 2.67e-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: 2.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  413 LASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGS 492
Cdd:COG5295    465 VGAATTAASAAATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGG 544

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657826  493 QGTGGATGGSQGTGGATGGSQGAGGATG-GSQATGSS 528
Cdd:COG5295    545 GSTTAATGTNSVAVGNNTATGANSVALGaGSVASGAN 581
PTZ00146 PTZ00146
fibrillarin; Provisional
 460-511 3.13e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 3.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657826  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 194-237 3.19e-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: 3.19e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657826  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.21e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 3.21e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657826   193 PCEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:smart00494    2 ECPGrgDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PTZ00146 PTZ00146
fibrillarin; Provisional
 450-501 4.00e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 4.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657826  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGG 501
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 440-495 5.27e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.34  E-value: 5.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657826  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvtGGSQGT 495
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGG--GGPGKV 57
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 425-528 5.70e-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: 44.61  E-value: 5.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  425 ENQTGEGGNGRETAIGgsQGTGGATGGNQGTGG-ATGGSQGagGATGGSQGVGGATGGSQGTGGV-----TGGSQGTGGA 498
Cdd:cd21118     96 GNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGhGAYGSQG--GPGVQGHGIPGGTGGPWASGGNygtnsLGGSVGQGGN 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657826  499 TG------GSQGTGGATG-------------------GSQGAGGATGGSQATGSS 528
Cdd:cd21118    172 GGplnygtNSQGAVAQPGygtvrgnnqnsgctnpppsGSHESFSNSGGSSSSGSS 226
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1491-1537 7.81e-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: 39.32  E-value: 7.81e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657826 1491 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1537
Cdd:pfam01607    1 CAGKEDG-YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 426-528 8.30e-04

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


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 44.76  E-value: 8.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  426 NQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGT 505
Cdd:COG3210    413 TIAGNGGSANAGGFTTTGGVLGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGT 492

                           90       100
                   ....*....|....*....|...
gi 1914657826  506 GGATGGSQGAGGATGGSQATGSS 528
Cdd:COG3210    493 VTTNATISNNAGGDANGIATGLT 515
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 256-297 8.53e-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: 8.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657826  256 LQDTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICD 45
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 428-533 8.84e-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: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  428 TGEG-GNGRETAIGGSQGTGgaTGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGatggSQGTG 506
Cdd:NF033849   291 TSESeSTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQSTSISHSESS----SESTG 364

                           90       100
                   ....*....|....*....|....*..
gi 1914657826  507 GATGGSQGAGGATGGSQATGSSQGTGG 533
Cdd:NF033849   365 TSVGHSTSSSVSSSESSSRSSSSGVSG 391
AidA COG3468
Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...
 454-529 9.54e-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: 44.17  E-value: 9.54e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657826  454 GTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:COG3468      1 TASGGGGGATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGL 76
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 411-502 9.57e-04

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 42.33  E-value: 9.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  411 DELASALRGINAKPENQTGEGGNGretaiggsqgtggatGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTG 490
Cdd:PRK07772   104 DEIGPSLRYATAKVTRASRGGGGG---------------GGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPADDPW 168

                           90
                   ....*....|..
gi 1914657826  491 GSQGTGGATGGS 502
Cdd:PRK07772   169 SSAPASGGFGGG 180
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 432-928 9.62e-04

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 44.38  E-value: 9.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  432 GNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:COG4625      1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  512 SQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGkggvtggsqGTGGATGGTGGTQGSQ 591
Cdd:COG4625     81 GGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGG---------GAGGGGGGGGGGGAGG 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  592 IIGGGAGGSQATGGGTGGVESTGTGTGGSQGTGGEGGVSGSQGTGGVAGGSQGTGGGAGGGQVTGGGASGNQGTGGGTGG 671
Cdd:COG4625    152 GGGGGAGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGG 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  672 NQETGGVTGGIQGSREGTGGSQGTGEVAGGNQGTTEVAGGGQGTGGGTSGSGGIGGVTGGSKNTGGATGGKQVTGGATSG 751
Cdd:COG4625    232 GGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGG 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  752 NQGTGGTGVNQGTGGGTGSSQGTGGDASGNQGTGGGTGGNQATGGGTSGNQGTEDGTGSSQGTGGVAGGKQGTGSGTGSN 831
Cdd:COG4625    312 GGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGG 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  832 QGTGGVANGNQAKGGGKDGKQGSGGETGGDQGAGGGTGSNQGTGGVANGNQVSGGGAGGNQGTIGGIGGNQGTGGGTGSI 911
Cdd:COG4625    392 GGGGAGGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGS 471

                          490
                   ....*....|....*..
gi 1914657826  912 QGTGGIASGSQSTGGGT 928
Cdd:COG4625    472 GAGTLTLTGNNTYTGTT 488
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
 452-529 1.13e-03

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: 39.91  E-value: 1.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657826  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 ...
 1266-1308 2.78e-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: 37.78  E-value: 2.78e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657826 1266 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1308
Cdd:pfam01607    8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
 422-528 3.08e-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: 42.35  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  422 AKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG-TGGVTGGSQG--TGGA 498
Cdd:pfam15967   25 AAASNPGSTGGFSFGTLGAAPAATATTTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTGlTLGTPAATTAasTGFS 104

                           90       100       110
                   ....*....|....*....|....*....|
gi 1914657826  499 TGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam15967  105 LGFNKPAASATPFSLPASSTSGGGLSLGSV 134
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 460-520 3.29e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 40.79  E-value: 3.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657826  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQgtGGATGGSQGAGGATG 520
Cdd:PRK07772   124 GGGGGGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPADDP--WSSAPASGGFGGGDD 182
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 382-416 3.52e-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: 3.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657826  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
 427-522 3.99e-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: 41.11  E-value: 3.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  427 QTGEGGNGRETAIGGSQGtGGATGGNQGTGGATGGSQ------------------GAGGATGGSQGVGGATGGSQGTGGV 488
Cdd:pfam12810   55 GKGEYNNSTNMNPGGFNG-GGNYKGSSGDGSGGGGGAtdirfdenslksriivagGGGGSGEGDDGSGGYGGGLTGGGGG 133

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1914657826  489 TGGSQGTGGATGGSQGTGG-ATGGSQGAGGATGGS 522
Cdd:pfam12810  134 SGCYEGSYGATQTSGGIGGyGINGSFGQGGNGRNS 168
ChtBD2 smart00494
Chitin-binding domain type 2;
1264-1304 4.67e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 37.04  E-value: 4.67e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657826  1264 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1304
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 450-510 4.82e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 40.02  E-value: 4.82e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657826  450 GGNQGTGGATGGsqGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATG 510
Cdd:PRK07772   124 GGGGGGGGGFGG--GGGGSGGGGGGGGGGGAPGGGGAQASAPADDPWSSAPASGGFGGGDD 182
PTZ00146 PTZ00146
fibrillarin; Provisional
 431-484 5.90e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 5.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914657826  431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG 484
Cdd:PTZ00146     2 MGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 454-508 6.33e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 6.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657826  454 GTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGA 508
Cdd:PTZ00146     1 GMGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 446-498 6.55e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 6.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657826  446 GGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvTGGSQGTGGA 498
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGG-RGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 429-481 6.97e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.49  E-value: 6.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657826  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGG 481
Cdd:PTZ00146     3 GGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
 431-512 7.32e-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: 40.34  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657826  431 GGNGRETAIGGSQGtGGATGGNQGTGGA---TGGSQGAGG----ATGGSQGVGGATGGSQGTGGVTGGSqGTGGATGGSQ 503
Cdd:pfam12810  111 GGSGEGDDGSGGYG-GGLTGGGGGSGCYegsYGATQTSGGiggyGINGSFGQGGNGRNSGGGGGGGGGG-GYYGGFGGGS 188


                   ....*....
gi 1914657826  504 GTGGATGGS 512
Cdd:pfam12810  189 YGGGGGGGS 197
ChtBD2 smart00494
Chitin-binding domain type 2;
1677-1721 7.57e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.27  E-value: 7.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657826  1677 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1721
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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