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Conserved domains on  [gi|1914657894|ref|XP_036358722|]
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uncharacterized protein LOC118763360 isoform X36 [Octopus sinensis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Keratin_2_tail super family cl23814
Keratin type II cytoskeletal 1 tail;
429-524 3.67e-11

Keratin type II cytoskeletal 1 tail;


The actual alignment was detected with superfamily member pfam16210:

Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 62.68  E-value: 3.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107

                           90
                   ....*....|....*....
gi 1914657894  506 GGATGGSQGAGGATGGSQA 524
Cdd:pfam16210  108 SGGRGSSSGGVKSSGGSSS 126
ChtBD2 smart00494
Chitin-binding domain type 2;
1690-1735 2.20e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.20e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1690 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1735
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 7.42e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.74  E-value: 7.42e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1405-1452 1.69e-05

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.59  E-value: 1.69e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1405 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1452
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1323-1368 2.45e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.45e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1323 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1368
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.81e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.81e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657894   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 3.54e-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: 3.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657894  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 ...
 1097-1139 2.97e-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: 2.97e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657894 1097 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1139
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 3.73e-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: 37.01  E-value: 3.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657894  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
1508-1552 8.93e-03

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 35.88  E-value: 8.93e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657894  1508 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1552
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
 
Name Accession Description Interval E-value
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
429-524 3.67e-11

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 62.68  E-value: 3.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107

                           90
                   ....*....|....*....
gi 1914657894  506 GGATGGSQGAGGATGGSQA 524
Cdd:pfam16210  108 SGGRGSSSGGVKSSGGSSS 126
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 418-531 5.82e-11

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: 66.95  E-value: 5.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657894  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
III PHA00370
attachment protein
 397-511 3.91e-10

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 63.01  E-value: 3.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657894  470 GGSQGvGGATGGSQGTGGVTGGSqgTGGATGGSQGTGGATGG 511
Cdd:PHA00370   106 GGGSG-GGDTGGSGGGGSDGGGS--EGGSTGKSLTKEGVGAG 144
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 428-529 8.04e-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: 8.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657894  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 8.27e-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: 8.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657894  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 428-528 1.34e-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: 53.47  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGA--GGATGGSQGVGGATGGSQGTG------GVTGGSQG--TGG 497
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADsvSQGTSWSEGTGTSQGQSVGTSeswstsQSETDSVGdsTGT 498

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1914657894  498 ATGGSQGTGGATGGSQGAGGATG--GSQATGSS 528
Cdd:NF033849   499 SESVSQGDGRSTGRSESQGTSLGtsGGRTSGAG 531
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 442-529 2.01e-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: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  442 SQGTGGATGGNQGTGGATGGSQGAGGATGGSQGV--GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:NF033849   272 SQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTseSQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQST 351

                           90
                   ....*....|
gi 1914657894  520 GGSQATGSSQ 529
Cdd:NF033849   352 SISHSESSSE 361
ChtBD2 smart00494
Chitin-binding domain type 2;
1690-1735 2.20e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.20e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1690 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1735
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 7.42e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.74  E-value: 7.42e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1405-1452 1.69e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.59  E-value: 1.69e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1405 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1452
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1693-1735 3.66e-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: 3.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657894 1693 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1735
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 ...
 440-529 4.76e-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: 48.46  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTggATGGSQGAGGAT 519
Cdd:NF033849   240 GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGT--SESQSHGTTEGT 317

                           90
                   ....*....|
gi 1914657894  520 GGSQATGSSQ 529
Cdd:NF033849   318 STTDSSSHSQ 327
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 450-529 1.28e-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: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  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 2.15e-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: 2.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657894  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
ChtBD2 smart00494
Chitin-binding domain type 2;
1323-1368 2.45e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.45e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1323 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1368
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1413-1457 2.49e-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: 2.49e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657894 1413 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1457
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.81e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.81e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657894   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 3.54e-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: 3.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657894  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.71e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 39.73  E-value: 3.71e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657894   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 ...
 1322-1368 8.34e-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: 8.34e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657894 1322 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1368
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 9.12e-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: 9.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657894  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 ...
 1097-1139 2.97e-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: 2.97e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657894 1097 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1139
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 3.73e-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: 37.01  E-value: 3.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657894  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
1095-1135 5.35e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.65  E-value: 5.35e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657894  1095 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1135
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1508-1552 8.93e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 35.88  E-value: 8.93e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657894  1508 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1552
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 431-529 9.30e-03

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 37.89  E-value: 9.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894   431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGS----QGAGGAT---GGSQGVGGATG--GSQGTGGVTGGSQGTGGATGG 501
Cdd:smart01104    8 GASGSKTPAWGSRTPGTAAGGAPTARGGSGSRtpawGGAGSRTpawGGAGPTGSRTPawGGASAWGNKSSEGSASSWAAG 87

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1914657894   502 SQGTGGA-TGGSQG-----AGGATGGSQATGSSQ 529
Cdd:smart01104   88 PGGAYGApTPGYGGtpsayGPATPGGGAMAGSAS 121
 
Name Accession Description Interval E-value
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
429-524 3.67e-11

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 62.68  E-value: 3.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107

                           90
                   ....*....|....*....
gi 1914657894  506 GGATGGSQGAGGATGGSQA 524
Cdd:pfam16210  108 SGGRGSSSGGVKSSGGSSS 126
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
450-528 4.20e-11

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 62.30  E-value: 4.20e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657894  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGGGGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS 101
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 418-531 5.82e-11

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: 66.95  E-value: 5.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657894  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
440-528 1.63e-10

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 60.76  E-value: 1.63e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGatgGSQGTGGvTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGG---GSYGSGG-GGGSGSGGGSSGGHRGGSGGGGGSSGGRSGG 98


                   ....*....
gi 1914657894  520 GGSQATGSS 528
Cdd:pfam16210   99 GSSGGSFGS 107
III PHA00370
attachment protein
 397-511 3.91e-10

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 63.01  E-value: 3.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657894  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 1.55e-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: 62.71  E-value: 1.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  401 WDGESTKCIYDELASALRGINAKPENQTGE---GGNGRETAIGGSQGTGGATGG-NQGT-----------GGATGGSQ-- 463
Cdd:cd21118    121 WQGSGGHGAYGSQGGPGVQGHGIPGGTGGPwasGGNYGTNSLGGSVGQGGNGGPlNYGTnsqgavaqpgyGTVRGNNQns 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657894  464 ------GAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:cd21118    201 gctnppPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSSG 271
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 428-529 8.04e-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: 8.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657894  500 GGSQGTGGATG-------GSQGAGGATGGSQATGSSQ 529
Cdd:COG3846    355 AGKAAFAQAAGfadsyraGSRAAWAATGGAAARGAGL 391
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 440-526 1.69e-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: 1.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGnqgTGGATGGSQGAGGATGGsqGVGGATGGSQGTGGVTGGSQGTGGATG----GSQGTGgaTGGSQGA 515
Cdd:COG3846    265 GGPQLGAGAAAG---TGAAAGGAAVAAGAAAA--AAAGGAAAAGGAAAARGGASAAGGAKAayslGSAGSG--SGAAGVA 337

                           90
                   ....*....|.
gi 1914657894  516 GGATGGSQATG 526
Cdd:COG3846    338 AGMGGVGRAGG 348
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-528 3.97e-07

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 54.53  E-value: 3.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQ-GTGGATGgnqgTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA-TGGSQGTGGATGGSQGAGG 517
Cdd:PRK13875   265 GAPQlGAGAAVG----TGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGAsSAYSAGAAGGSGAAGVAAG 340

                           90
                   ....*....|.
gi 1914657894  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 8.27e-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: 8.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657894  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 428-528 1.34e-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: 53.47  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGA--GGATGGSQGVGGATGGSQGTG------GVTGGSQG--TGG 497
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADsvSQGTSWSEGTGTSQGQSVGTSeswstsQSETDSVGdsTGT 498

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1914657894  498 ATGGSQGTGGATGGSQGAGGATG--GSQATGSS 528
Cdd:NF033849   499 SESVSQGDGRSTGRSESQGTSLGtsGGRTSGAG 531
III PHA00370
attachment protein
 461-528 1.66e-06

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 51.84  E-value: 1.66e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657894  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 ...
 442-529 2.01e-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: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  442 SQGTGGATGGNQGTGGATGGSQGAGGATGGSQGV--GGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:NF033849   272 SQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGTseSQSHGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSSHSDGTSQST 351

                           90
                   ....*....|
gi 1914657894  520 GGSQATGSSQ 529
Cdd:NF033849   352 SISHSESSSE 361
ChtBD2 smart00494
Chitin-binding domain type 2;
1690-1735 2.20e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 46.28  E-value: 2.20e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1690 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1735
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 418-547 3.26e-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: 51.92  E-value: 3.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  418 RGINAKPENQTGEGGNGretaIGGSQGtgGATGGNQGTGGATGGSQGAGG-----ATGGSQGVGGATGG-SQGTGGVTGG 491
Cdd:cd21118    112 HGVDAVHNSWQGSGGHG----AYGSQG--GPGVQGHGIPGGTGGPWASGGnygtnSLGGSVGQGGNGGPlNYGTNSQGAV 185

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  492 SQGTGGATGGSQGTGGAT----GGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGG 547
Cdd:cd21118    186 AQPGYGTVRGNNQNSGCTnpppSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGG 245
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 7.42e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.74  E-value: 7.42e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 451-527 1.30e-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: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  451 GNQGTGGA----TGGSQ-GAGGATGGSQGVGGATGGsqGTGGVTGGsqgtGGATGGSQGTGGATGGSQGAGGATG----G 521
Cdd:COG3846    252 GIFGPGIAaglvSGGPQlGAGAAAGTGAAAGGAAVA--AGAAAAAA----AGGAAAAGGAAAARGGASAAGGAKAayslG 325


                   ....*.
gi 1914657894  522 SQATGS 527
Cdd:COG3846    326 SAGSGS 331
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 413-528 1.67e-05

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


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 49.77  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  413 LASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGS 492
Cdd:COG5295    465 VGAATTAASAAATAAAATSSAAIAGATATGAGAAAGGAGAGAAGGAGSAAAGGAANAAAASGATATAGSAGGGAAAAAGG 544

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1914657894  493 QGTGGATGGSQ---GTGGATGGSQGAGGAtgGSQATGSS 528
Cdd:COG5295    545 GSTTAATGTNSvavGNNTATGANSVALGA--GSVASGAN 581
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 440-527 1.68e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 49.46  E-value: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGNQ--GTGGATGGSQGAGGAT-GGSQGVGGAT-GGSQGTGGVT-GGSQGTGGATGGSQGTGGA--TGGS 512
Cdd:PTZ00473   312 HDSRGPYNANYGGQfnSRSGRTGSSESIRGFTyDSSTTYGGSSyGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGS 391

                           90
                   ....*....|....*
gi 1914657894  513 QGAGGATGGSQATGS 527
Cdd:PTZ00473   392 STFDGSSRGSSDSFG 406
ChtBD2 smart00494
Chitin-binding domain type 2;
1405-1452 1.69e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.59  E-value: 1.69e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1405 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1452
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 429-525 2.58e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 48.69  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGAT--GGSQGAGGATGGSQGVGGAT-GGSQGTGGVTGGSQGTGGA--TGGSQ 503
Cdd:PTZ00473   313 DSRGPYNANYGGQFNSRSGRTGSSESIRGFTydSSTTYGGSSYGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGSS 392

                           90       100
                   ....*....|....*....|...
gi 1914657894  504 GTGGATGGS-QGAGGATGGSQAT 525
Cdd:PTZ00473   393 TFDGSSRGSsDSFGVSYFGPQQT 415
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
 431-528 3.49e-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: 48.51  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  431 GGNGRETAIGGSQGTGGATGGNQG-TGGATGGSQGAGGA-----TGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG 504
Cdd:pfam15967    8 GGPGSTATAGGGFSFGAAAASNPGsTGGFSFGTLGAAPAatattTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTG 87

                           90       100
                   ....*....|....*....|....*..
gi 1914657894  505 -TGGATGGSQGA--GGATGGSQATGSS 528
Cdd:pfam15967   88 lTLGTPAATTAAstGFSLGFNKPAASA 114
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1693-1735 3.66e-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: 3.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657894 1693 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1735
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 ...
 440-529 4.76e-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: 48.46  E-value: 4.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTggATGGSQGAGGAT 519
Cdd:NF033849   240 GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGT--SESQSHGTTEGT 317

                           90
                   ....*....|
gi 1914657894  520 GGSQATGSSQ 529
Cdd:NF033849   318 STTDSSSHSQ 327
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 428-529 4.99e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.98  E-value: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGAT-------GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATG 500
Cdd:PRK13875   290 AGAGLAAGGGAAAAGGAAAAARGGAAAAGGASsaysagaAGGSGAAGVAAGLGGVARAGASAAASPLRRAASRAAESMKS 369

                           90       100
                   ....*....|....*....|....*....
gi 1914657894  501 GSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:PRK13875   370 SFRAGARSTGGGAGGAAAAAAAGAAAAGP 398
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-528 5.30e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.60  E-value: 5.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTG----GSQGTGGATGGSQGTGG-ATGGSQG 514
Cdd:PRK13875   272 GAAVGTGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGASSaysaGAAGGSGAAGVAAGLGGvARAGASA 351

                           90
                   ....*....|....*....
gi 1914657894  515 AG-----GATGGSQATGSS 528
Cdd:PRK13875   352 AAsplrrAASRAAESMKSS 370
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 444-525 5.57e-05

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 48.24  E-value: 5.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  444 GTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQ 523
Cdd:COG4625      1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGG 80


                   ..
gi 1914657894  524 AT 525
Cdd:COG4625     81 GG 82
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 425-528 7.71e-05

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: 47.30  E-value: 7.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  425 ENQTGEGGNGRETAIGgsQGTGGATGGNQGTGG-ATGGSQGagGATGGSQGVGGATGGSQGTGGV-----TGGSQGTGGA 498
Cdd:cd21118     96 GNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGhGAYGSQG--GPGVQGHGIPGGTGGPWASGGNygtnsLGGSVGQGGN 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657894  499 TG------GSQGTGGATG-------------------GSQGAGGATGGSQATGSS 528
Cdd:cd21118    172 GGplnygtNSQGAVAQPGygtvrgnnqnsgctnpppsGSHESFSNSGGSSSSGSS 226
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-526 1.27e-04

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 46.44  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  440 GGSQGTGGATGGNQ-GTGGATGGSQGAGG-ATGGSQGVGGATGGsqgtgGVTGGSQGTGGATGGSQGTGGA-TGGSQGAG 516
Cdd:PRK13875   255 GPGIANGLVSGAPQlGAGAAVGTGLAAGGaAVAAAAGAGLAAGG-----GAAAAGGAAAAARGGAAAAGGAsSAYSAGAA 329

                           90
                   ....*....|
gi 1914657894  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 1.28e-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: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGgaTGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESES--TGQSSSVGTSE 307
PTZ00146 PTZ00146
fibrillarin; Provisional
 470-521 1.30e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.88  E-value: 1.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657894  470 GGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGG 521
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 1.94e-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: 41.83  E-value: 1.94e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657894  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 ...
 111-151 2.15e-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: 2.15e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657894  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
PTZ00146 PTZ00146
fibrillarin; Provisional
 460-511 2.21e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.11  E-value: 2.21e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657894  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
ChtBD2 smart00494
Chitin-binding domain type 2;
1323-1368 2.45e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.50  E-value: 2.45e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657894  1323 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1368
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1413-1457 2.49e-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: 2.49e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657894 1413 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1457
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.81e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.81e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657894   258 DTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
PTZ00146 PTZ00146
fibrillarin; Provisional
 450-501 2.83e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 2.83e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657894  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGG 501
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 3.54e-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: 3.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657894  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
PTZ00146 PTZ00146
fibrillarin; Provisional
 440-495 3.66e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 3.66e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657894  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvtGGSQGT 495
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGG--GGPGKV 57
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.71e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 39.73  E-value: 3.71e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657894   193 PCEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:smart00494    2 ECPGrgDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 411-500 4.53e-04

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 43.10  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  411 DELASALRGINAKPENQTGEGGNGretaiggsqgtggatGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTG---- 486
Cdd:PRK07772   104 DEIGPSLRYATAKVTRASRGGGGG---------------GGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPAddpw 168

                           90
                   ....*....|....
gi 1914657894  487 GVTGGSQGTGGATG 500
Cdd:PRK07772   169 SSAPASGGFGGGDD 182
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1322-1368 8.34e-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: 8.34e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657894 1322 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1368
Cdd:pfam01607    1 CAGKEDG-YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 444-528 9.04e-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: 44.37  E-value: 9.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  444 GTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQ 523
Cdd:COG3210    816 GSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGT 895


                   ....*
gi 1914657894  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 ...
 256-297 9.12e-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: 9.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657894  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 1.09e-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: 42.65  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  427 QTGEGGNGRETAIGGSQGtGGATGGNQGTGGATGGSQ------------------GAGGATGGSQGVGGATGGSQGTGGV 488
Cdd:pfam12810   55 GKGEYNNSTNMNPGGFNG-GGNYKGSSGDGSGGGGGAtdirfdenslksriivagGGGGSGEGDDGSGGYGGGLTGGGGG 133

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657894  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 1.35e-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: 43.50  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  422 AKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG-TGGVTGGSQG--TGGA 498
Cdd:pfam15967   25 AAASNPGSTGGFSFGTLGAAPAATATTTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTGlTLGTPAATTAasTGFS 104

                           90       100       110
                   ....*....|....*....|....*....|
gi 1914657894  499 TGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam15967  105 LGFNKPAASATPFSLPASSTSGGGLSLGSV 134
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 460-520 1.73e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 41.56  E-value: 1.73e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657894  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQgtGGATGGSQGAGGATG 520
Cdd:PRK07772   124 GGGGGGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPADDP--WSSAPASGGFGGGDD 182
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
 431-512 2.12e-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: 41.88  E-value: 2.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  431 GGNGRETAIGGSQGtGGATGGNQGTGGA---TGGSQGAGG----ATGGSQGVGGATGGSQGTGGVTGGSqGTGGATGGSQ 503
Cdd:pfam12810  111 GGSGEGDDGSGGYG-GGLTGGGGGSGCYegsYGATQTSGGiggyGINGSFGQGGNGRNSGGGGGGGGGG-GYYGGFGGGS 188


                   ....*....
gi 1914657894  504 GTGGATGGS 512
Cdd:pfam12810  189 YGGGGGGGS 197
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 450-510 2.60e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 40.79  E-value: 2.60e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657894  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 ...
 1097-1139 2.97e-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: 2.97e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657894 1097 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1139
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 3.73e-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: 37.01  E-value: 3.73e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657894  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
PTZ00146 PTZ00146
fibrillarin; Provisional
 431-484 4.18e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914657894  431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG 484
Cdd:PTZ00146     2 MGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 454-508 4.29e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657894  454 GTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGA 508
Cdd:PTZ00146     1 GMGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 446-498 4.41e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657894  446 GGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvTGGSQGTGGA 498
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGG-RGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 429-481 5.03e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 5.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657894  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGG 481
Cdd:PTZ00146     3 GGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 426-581 5.19e-03

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 41.69  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894  426 NQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGT 505
Cdd:COG4625    208 GGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGS 287

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657894  506 GGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGKGGVTGGSQGTGGAT 581
Cdd:COG4625    288 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGT 363
ChtBD2 smart00494
Chitin-binding domain type 2;
1095-1135 5.35e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.65  E-value: 5.35e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657894  1095 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1135
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
DUF4766 pfam15973
Domain of unknown function (DUF4766); This presumed domain is functionally uncharacterized. ...
 453-521 5.52e-03

Domain of unknown function (DUF4766); This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is typically between 106 and 128 amino acids in length. There is a conserved KVI sequence motif.


Pssm-ID: 435045 [Multi-domain]  Cd Length: 114  Bit Score: 38.67  E-value: 5.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657894  453 QGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGatGGSQGTGGATGGSQGAGGATGG 521
Cdd:pfam15973   18 EGQGYSNGGGGGGSGGYGGGYGSGHGHGGGQEVKIVKVIEQQAPI--GGHGGSGGGSGGGYSYGGGYAG 84
ChtBD2 smart00494
Chitin-binding domain type 2;
1508-1552 8.93e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 35.88  E-value: 8.93e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657894  1508 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1552
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 431-529 9.30e-03

Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription elongation factor protein Spt5 is necessary for binding to Spt4 to form the functional complex that regulates early transcription elongation by RNA polymerase II. The complex may be involved in pre-mRNA processing through its association with mRNA capping enzymes. This CTD domain carries a regular nonapeptide repeat that can be present in up to 18 copies, as in S. pombe. The repeat has a characteristic TPA motif.


Pssm-ID: 215026 [Multi-domain]  Cd Length: 121  Bit Score: 37.89  E-value: 9.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657894   431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGS----QGAGGAT---GGSQGVGGATG--GSQGTGGVTGGSQGTGGATGG 501
Cdd:smart01104    8 GASGSKTPAWGSRTPGTAAGGAPTARGGSGSRtpawGGAGSRTpawGGAGPTGSRTPawGGASAWGNKSSEGSASSWAAG 87

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1914657894   502 SQGTGGA-TGGSQG-----AGGATGGSQATGSSQ 529
Cdd:smart01104   88 PGGAYGApTPGYGGtpsayGPATPGGGAMAGSAS 121
 
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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