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Conserved domains on  [gi|1914657906|ref|XP_036358728|]
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uncharacterized protein LOC118763360 isoform X42 [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 6.60e-12

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: 64.61  E-value: 6.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107

                           90
                   ....*....|....*....
gi 1914657906  506 GGATGGSQGAGGATGGSQA 524
Cdd:pfam16210  108 SGGRGSSSGGVKSSGGSSS 126
ChtBD2 smart00494
Chitin-binding domain type 2;
1619-1664 2.42e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 45.90  E-value: 2.42e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1619 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1664
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 7.78e-06

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.36  E-value: 7.78e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1334-1381 1.86e-05

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.59  E-value: 1.86e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1334 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1381
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1252-1297 2.60e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.60e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1252 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1297
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.95e-04

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.95e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657906   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 3.87e-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: 39.70  E-value: 3.87e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657906  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 ...
 1026-1068 3.09e-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: 3.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657906 1026 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1068
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 3.99e-03

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


:

Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 3.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657906  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
ChtBD2 smart00494
Chitin-binding domain type 2;
1437-1481 9.37e-03

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 35.88  E-value: 9.37e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657906  1437 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1481
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
 
Name Accession Description Interval E-value
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
429-524 6.60e-12

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 64.61  E-value: 6.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107

                           90
                   ....*....|....*....
gi 1914657906  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 3.39e-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: 67.72  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657906  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
III PHA00370
attachment protein
 397-511 1.94e-10

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 63.78  E-value: 1.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657906  470 GGSQGvGGATGGSQGTGGVTGGSqgTGGATGGSQGTGGATGG 511
Cdd:PHA00370   106 GGGSG-GGDTGGSGGGGSDGGGS--EGGSTGKSLTKEGVGAG 144
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 428-529 7.67e-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: 7.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657906  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 7.89e-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: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657906  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 1.28e-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: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGA--GGATGGSQGVGGATGGSQGTG------GVTGGSQG--TGG 497
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADsvSQGTSWSEGTGTSQGQSVGTSeswstsQSETDSVGdsTGT 498

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1914657906  498 ATGGSQGTGGATGGSQGAGGATG--GSQATGSS 528
Cdd:NF033849   499 SESVSQGDGRSTGRSESQGTSLGtsGGRTSGAG 531
ChtBD2 smart00494
Chitin-binding domain type 2;
1619-1664 2.42e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 45.90  E-value: 2.42e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1619 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1664
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 7.78e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.36  E-value: 7.78e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906   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 ...
 432-528 1.28e-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: 50.39  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  432 GNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGAT----GGSQGTGG 507
Cdd:NF033849   276 TTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSshsdGTSQSTSI 353

                           90       100
                   ....*....|....*....|.
gi 1914657906  508 ATGGSQGAGGATGGSQATGSS 528
Cdd:NF033849   354 SHSESSSESTGTSVGHSTSSS 374
ChtBD2 smart00494
Chitin-binding domain type 2;
1334-1381 1.86e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.59  E-value: 1.86e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1334 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1381
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1622-1664 3.91e-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: 3.91e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657906 1622 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1664
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 4.55e-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: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTggATGGSQGAGGAT 519
Cdd:NF033849   240 GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGT--SESQSHGTTEGT 317

                           90
                   ....*....|
gi 1914657906  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 1.22e-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: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGgaTGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESES--TGQSSSVGTSE 307
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 433-528 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: 46.54  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  433 NGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGG----SQGTGGATGGS--QGTG 506
Cdd:NF033849   440 SGHSDSSSHSTSSGQADSVSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGDSTGTsesvSQGDGRSTGRSesQGTS 519

                           90       100
                   ....*....|....*....|..
gi 1914657906  507 GATGGSQGAGgaTGGSQATGSS 528
Cdd:NF033849   520 LGTSGGRTSG--AGGSMGLGPS 539
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 111-151 2.25e-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: 2.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657906  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
ChtBD2 smart00494
Chitin-binding domain type 2;
1252-1297 2.60e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.60e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1252 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1297
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1342-1386 2.66e-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: 2.66e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657906 1342 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1386
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.95e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.95e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657906   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 3.87e-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: 39.70  E-value: 3.87e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657906  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.97e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 39.73  E-value: 3.97e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657906   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 ...
 1251-1297 9.01e-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: 9.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657906 1251 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1297
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 9.37e-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: 9.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657906  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 ...
 1026-1068 3.09e-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: 3.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657906 1026 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1068
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 3.99e-03

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


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 3.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657906  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 431-529 4.05e-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: 39.04  E-value: 4.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906   431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGS----QGAGGAT---GGSQGVGGATG--GSQGTGGVTGGSQGTGGATGG 501
Cdd:smart01104    8 GASGSKTPAWGSRTPGTAAGGAPTARGGSGSRtpawGGAGSRTpawGGAGPTGSRTPawGGASAWGNKSSEGSASSWAAG 87

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1914657906   502 SQGTGGA-TGGSQG-----AGGATGGSQATGSSQ 529
Cdd:smart01104   88 PGGAYGApTPGYGGtpsayGPATPGGGAMAGSAS 121
ChtBD2 smart00494
Chitin-binding domain type 2;
1024-1064 5.61e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.65  E-value: 5.61e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657906  1024 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1064
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1437-1481 9.37e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 35.88  E-value: 9.37e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657906  1437 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1481
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
 
Name Accession Description Interval E-value
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
429-524 6.60e-12

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 64.61  E-value: 6.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGAtGGSQGVGGATGGSQGTGGVTGGSQG---TGGATGGSQGT 505
Cdd:pfam16210   29 GGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGG-GGSGSGGGSSGGHRGGSGGGGGSSGgrsGGGSSGGSFGS 107

                           90
                   ....*....|....*....
gi 1914657906  506 GGATGGSQGAGGATGGSQA 524
Cdd:pfam16210  108 SGGRGSSSGGVKSSGGSSS 126
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
450-528 9.53e-12

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 64.22  E-value: 9.53e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657906  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGGGSYGSGGGGGSGSGGGSSGGHRGGSGGGGGSSGGRSGGGSS 101
Keratin_2_tail pfam16210
Keratin type II cytoskeletal 1 tail;
440-528 3.13e-11

Keratin type II cytoskeletal 1 tail;


Pssm-ID: 406591 [Multi-domain]  Cd Length: 135  Bit Score: 62.68  E-value: 3.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGatgGSQGTGGvTGGSQGTGGATGGSQGTGGATGGSQGAGGAT 519
Cdd:pfam16210   23 GSSRGGGGGGGGSYGSGGGSYGSGGGGGSGSGSYGSGG---GSYGSGG-GGGSGSGGGSSGGHRGGSGGGGGSSGGRSGG 98


                   ....*....
gi 1914657906  520 GGSQATGSS 528
Cdd:pfam16210   99 GSSGGSFGS 107
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 418-531 3.39e-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: 67.72  E-value: 3.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  418 RGINAKPeNQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    182 QGAVAQP-GYGTVRGNNQNSGCTNPPPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSG 260

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1914657906  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQGT 531
Cdd:cd21118    261 NSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSS 294
III PHA00370
attachment protein
 397-511 1.94e-10

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 63.78  E-value: 1.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  397 LNTVWDGESTK-------CIYDelasaLRGINAKPENQTGegGNGRETAIGGSQGTGGaTGGNQGTGGATGGSQGaGGAT 469
Cdd:PHA00370    35 FNNVWKGDEGGryanyegCEYE-----ATGVTVCQNDGTV--CNGSWKPTGSADKDGD-GGGTGEGGSDTGGDTG-GGNT 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1914657906  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 ...
 429-528 2.52e-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: 2.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  429 GEGGNGRETAIG-GSQGT------GGATGGNQGTGGAT---GGSQGAGGATGGSQGVG---------------GATGGSQ 483
Cdd:cd21118    167 GQGGNGGPLNYGtNSQGAvaqpgyGTVRGNNQNSGCTNpppSGSHESFSNSGGSSSSGssgsqgshgsngqgsSGSSGGQ 246

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1914657906  484 GTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:cd21118    247 GNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGS 291
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 401-527 1.27e-09

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


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 62.71  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  401 WDGESTKCIYDELASALRGINAKPENQTGE---GGNGRETAIGGSQGTGGATGG-NQGT-----------GGATGGSQ-- 463
Cdd:cd21118    121 WQGSGGHGAYGSQGGPGVQGHGIPGGTGGPwasGGNYGTNSLGGSVGQGGNGGPlNYGTnsqgavaqpgyGTVRGNNQns 200

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  464 ------GAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGGSQATGS 527
Cdd:cd21118    201 gctnppPSGSHESFSNSGGSSSSGSSGSQGSHGSNGQGSSGSSGGQGNGGNNGSSSSNSGNSGGSNGGSS 270
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 428-529 7.67e-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: 7.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  428 TGEGGNGRETAIGGsqGTGGATGGNQGTGGAT---GGSQGAGGATG----GSQGVG-GATGGSQGTGGVTGGSQGTGGAT 499
Cdd:COG3846    277 TGAAAGGAAVAAGA--AAAAAAGGAAAAGGAAaarGGASAAGGAKAayslGSAGSGsGAAGVAAGMGGVGRAGGSAAASP 354

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1914657906  500 GGSQGTGGATG-------GSQGAGGATGGSQATGSSQ 529
Cdd:COG3846    355 AGKAAFAQAAGfadsyraGSRAAWAATGGAAARGAGL 391
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 440-526 1.62e-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: 1.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGnqgTGGATGGSQGAGGATGGsqGVGGATGGSQGTGGVTGGSQGTGGATG----GSQGTGgaTGGSQGA 515
Cdd:COG3846    265 GGPQLGAGAAAG---TGAAAGGAAVAAGAAAA--AAAGGAAAAGGAAAARGGASAAGGAKAayslGSAGSG--SGAAGVA 337

                           90
                   ....*....|.
gi 1914657906  516 GGATGGSQATG 526
Cdd:COG3846    338 AGMGGVGRAGG 348
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-528 3.79e-07

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 54.53  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQ-GTGGATGgnqgTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGA-TGGSQGTGGATGGSQGAGG 517
Cdd:PRK13875   265 GAPQlGAGAAVG----TGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGAsSAYSAGAAGGSGAAGVAAG 340

                           90
                   ....*....|.
gi 1914657906  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 7.89e-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: 7.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  425 ENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGAT----GGSQGTG---GVTGGSQGTGG 497
Cdd:NF033849   349 QSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTseglGASQGGSegwGSGDSVQSVSQ 428

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1914657906  498 ATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:NF033849   429 SYGSSSSTGTSSGHSDSSSHSTSSGQADSVSQ 460
III PHA00370
attachment protein
 461-528 1.01e-06

attachment protein


Pssm-ID: 164795 [Multi-domain]  Cd Length: 297  Bit Score: 52.61  E-value: 1.01e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657906  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 ...
 428-528 1.28e-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: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGA--GGATGGSQGVGGATGGSQGTG------GVTGGSQG--TGG 497
Cdd:NF033849   419 SGDSVQSVSQSYGSSSSTGTSSGHSDSSSHSTSSGQADsvSQGTSWSEGTGTSQGQSVGTSeswstsQSETDSVGdsTGT 498

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1914657906  498 ATGGSQGTGGATGGSQGAGGATG--GSQATGSS 528
Cdd:NF033849   499 SESVSQGDGRSTGRSESQGTSLGtsGGRTSGAG 531
ChtBD2 smart00494
Chitin-binding domain type 2;
1619-1664 2.42e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 45.90  E-value: 2.42e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1619 IPCQ--PNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1664
Cdd:smart00494    1 NECPgrGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
103-150 7.78e-06

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 44.36  E-value: 7.78e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906   103 ECQPcVTGGFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIF 150
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
TrbL COG3846
Type IV secretory pathway, TrbL components [Intracellular trafficking, secretion, and ...
 451-527 1.24e-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: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  451 GNQGTGGA----TGGSQ-GAGGATGGSQGVGGATGGsqGTGGVTGGsqgtGGATGGSQGTGGATGGSQGAGGATG----G 521
Cdd:COG3846    252 GIFGPGIAaglvSGGPQlGAGAAAGTGAAAGGAAVA--AGAAAAAA----AGGAAAAGGAAAARGGASAAGGAKAayslG 325


                   ....*.
gi 1914657906  522 SQATGS 527
Cdd:COG3846    326 SAGSGS 331
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 432-528 1.28e-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: 50.39  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  432 GNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGgaTGGSQGVGGATGGSQGTGGVTGGSQGTGGAT----GGSQGTGG 507
Cdd:NF033849   276 TTGHGSTRGWSHTQSTSESESTGQSSSVGTSESQS--HGTTEGTSTTDSSSHSQSSSYNVSSGTGVSSshsdGTSQSTSI 353

                           90       100
                   ....*....|....*....|.
gi 1914657906  508 ATGGSQGAGGATGGSQATGSS 528
Cdd:NF033849   354 SHSESSSESTGTSVGHSTSSS 374
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 440-527 1.59e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 49.46  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGNQ--GTGGATGGSQGAGGAT-GGSQGVGGAT-GGSQGTGGVT-GGSQGTGGATGGSQGTGGA--TGGS 512
Cdd:PTZ00473   312 HDSRGPYNANYGGQfnSRSGRTGSSESIRGFTyDSSTTYGGSSyGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGS 391

                           90
                   ....*....|....*
gi 1914657906  513 QGAGGATGGSQATGS 527
Cdd:PTZ00473   392 STFDGSSRGSSDSFG 406
ChtBD2 smart00494
Chitin-binding domain type 2;
1334-1381 1.86e-05

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 43.59  E-value: 1.86e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1334 DCEPcQQGGYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVY 1381
Cdd:smart00494    2 ECPG-RGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
Nucleoporin_FG2 pfam15967
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ...
 431-528 2.21e-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: 49.28  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  431 GGNGRETAIGGSQGTGGATGGNQG-TGGATGGSQGAGGA-----TGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQG 504
Cdd:pfam15967    8 GGPGSTATAGGGFSFGAAAASNPGsTGGFSFGTLGAAPAatattTTATLGLGGGLFGQKPATGFTFGTPASSTAATGPTG 87

                           90       100
                   ....*....|....*....|....*..
gi 1914657906  505 -TGGATGGSQGA--GGATGGSQATGSS 528
Cdd:pfam15967   88 lTLGTPAATTAAstGFSLGFNKPAASA 114
PTZ00473 PTZ00473
Plasmodium Vir superfamily; Provisional
 429-525 2.49e-05

Plasmodium Vir superfamily; Provisional


Pssm-ID: 240430 [Multi-domain]  Cd Length: 420  Bit Score: 48.69  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGAT--GGSQGAGGATGGSQGVGGAT-GGSQGTGGVTGGSQGTGGA--TGGSQ 503
Cdd:PTZ00473   313 DSRGPYNANYGGQFNSRSGRTGSSESIRGFTydSSTTYGGSSYGTSQTDSTSTyGSRSTFDSSTGGGSQSGGGstYGGSS 392

                           90       100
                   ....*....|....*....|...
gi 1914657906  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 ...
 1622-1664 3.91e-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: 3.91e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657906 1622 QPNSYYPKFKSISQFYQCSHGLLFLMQCPDKTVWNEASIKCVY 1664
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 425-528 4.22e-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: 48.07  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  425 ENQTGEGGNGRETAIGgsQGTGGATGGNQGTGG-ATGGSQGagGATGGSQGVGGATGGSQGTGGV-----TGGSQGTGGA 498
Cdd:cd21118     96 GNAGNEIGRQAEDIIR--HGVDAVHNSWQGSGGhGAYGSQG--GPGVQGHGIPGGTGGPWASGGNygtnsLGGSVGQGGN 171

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657906  499 TG------GSQGTGGATG-------------------GSQGAGGATGGSQATGSS 528
Cdd:cd21118    172 GGplnygtNSQGAVAQPGygtvrgnnqnsgctnpppsGSHESFSNSGGSSSSGSS 226
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 440-529 4.55e-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: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTggATGGSQGAGGAT 519
Cdd:NF033849   240 GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESESTGQSSSVGT--SESQSHGTTEGT 317

                           90
                   ....*....|
gi 1914657906  520 GGSQATGSSQ 529
Cdd:NF033849   318 STTDSSSHSQ 327
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 428-529 4.77e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.98  E-value: 4.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGAT-------GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATG 500
Cdd:PRK13875   290 AGAGLAAGGGAAAAGGAAAAARGGAAAAGGASsaysagaAGGSGAAGVAAGLGGVARAGASAAASPLRRAASRAAESMKS 369

                           90       100
                   ....*....|....*....|....*....
gi 1914657906  501 GSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:PRK13875   370 SFRAGARSTGGGAGGAAAAAAAGAAAAGP 398
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-528 5.06e-05

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 47.60  E-value: 5.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTG----GSQGTGGATGGSQGTGG-ATGGSQG 514
Cdd:PRK13875   272 GAAVGTGLAAGGAAVAAAAGAGLAAGGGAAAAGGAAAAARGGAAAAGGASSaysaGAAGGSGAAGVAAGLGGvARAGASA 351

                           90
                   ....*....|....*....
gi 1914657906  515 AG-----GATGGSQATGSS 528
Cdd:PRK13875   352 AAsplrrAASRAAESMKSS 370
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 426-528 5.50e-05

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


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 48.23  E-value: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  426 NQTGEGGNGRETAIGGSQGTGGATGGNQGTGG-----ATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATG 500
Cdd:COG5295    133 GSTAAAGGAAASTGGSSAAGGSNTATATGSSTanaatAAAGATSTSASGSSSGASGAAAASAATGASAGGTASAAASASS 212

                           90       100
                   ....*....|....*....|....*...
gi 1914657906  501 GSQGTGGATGGSQGAGGATGGSQATGSS 528
Cdd:COG5295    213 SATGTSASVGVNAGAATGSAASAGGSAS 240
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
 452-529 1.08e-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: 42.60  E-value: 1.08e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914657906  452 NQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQgTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQ 529
Cdd:pfam13634    7 TSTSGGLFGNTSTTAASGGGLFGAASTATATTSGGGLFGNSS-SNAPSGGLFGATNTTTQTATGGGLFGNNAATTTST 83
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 440-526 1.22e-04

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 46.44  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  440 GGSQGTGGATGGNQ-GTGGATGGSQGAGG-ATGGSQGVGGATGGsqgtgGVTGGSQGTGGATGGSQGTGGA-TGGSQGAG 516
Cdd:PRK13875   255 GPGIANGLVSGAPQlGAGAAVGTGLAAGGaAVAAAAGAGLAAGG-----GAAAAGGAAAAARGGAAAAGGAsSAYSAGAA 329

                           90
                   ....*....|
gi 1914657906  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 1.22e-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: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  450 GGNQGTGGatGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGgaTGGSQATGSSQ 529
Cdd:NF033849   232 AANLGQSA--GTGYGESVGHSTSQGQSHSVGTSESHSVGTSQSQSHTTGHGSTRGWSHTQSTSESES--TGQSSSVGTSE 307
PTZ00146 PTZ00146
fibrillarin; Provisional
 470-521 1.24e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.88  E-value: 1.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657906  470 GGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQGAGGATGG 521
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
ser_rich_anae_1 NF033849
serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 ...
 433-528 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: 46.54  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  433 NGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGG----SQGTGGATGGS--QGTG 506
Cdd:NF033849   440 SGHSDSSSHSTSSGQADSVSQGTSWSEGTGTSQGQSVGTSESWSTSQSETDSVGDSTGTsesvSQGDGRSTGRSesQGTS 519

                           90       100
                   ....*....|....*....|..
gi 1914657906  507 GATGGSQGAGgaTGGSQATGSS 528
Cdd:NF033849   520 LGTSGGRTSG--AGGSMGLGPS 539
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 426-527 2.10e-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: 45.76  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  426 NQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAG--------GatggsqGVGGATGGSQGTGGVTGGSQGTGG 497
Cdd:cd21118    249 GGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGgssssggsG------GSGGGNKPECNNPGNDVRMAGGGG 322

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1914657906  498 ATGGSQGTGG-ATGGSQGAGGATGGSQATGS 527
Cdd:cd21118    323 SQGSKESSGShGSNGGNGQAEAVGGLNTLNS 353
PTZ00146 PTZ00146
fibrillarin; Provisional
 460-511 2.11e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 45.11  E-value: 2.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657906  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 ...
 111-151 2.25e-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: 2.25e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1914657906  111 GFYSHPNDQGRYYQCVYGVLLPKYCQSGTIWYQHTRTCIFD 151
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 414-581 2.48e-04

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


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 45.92  E-value: 2.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  414 ASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQ 493
Cdd:COG4625      9 GGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGGGG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  494 GTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEGGASGSQGKGGVTGG 573
Cdd:COG4625     89 GTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGGGG 168


                   ....*...
gi 1914657906  574 SQGTGGAT 581
Cdd:COG4625    169 GGGGGGGG 176
ChtBD2 smart00494
Chitin-binding domain type 2;
1252-1297 2.60e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.60e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1914657906  1252 EACEKGS--YYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1297
Cdd:smart00494    1 NECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1342-1386 2.66e-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: 2.66e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1914657906 1342 GYYPIIGSLSEFFQCSHGQLVPMKCPARTIWNNKIIRCVYDRSQV 1386
Cdd:pfam01607    7 GYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVV 51
PTZ00146 PTZ00146
fibrillarin; Provisional
 450-501 2.71e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 2.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1914657906  450 GGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGG 501
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
ChtBD2 smart00494
Chitin-binding domain type 2;
258-297 2.95e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 40.12  E-value: 2.95e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1914657906   258 DTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCD 47
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 411-500 3.47e-04

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 43.48  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  411 DELASALRGINAKPENQTGEGGNGretaiggsqgtggatGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTG---- 486
Cdd:PRK07772   104 DEIGPSLRYATAKVTRASRGGGGG---------------GGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPAddpw 168

                           90
                   ....*....|....
gi 1914657906  487 GVTGGSQGTGGATG 500
Cdd:PRK07772   169 SSAPASGGFGGGDD 182
PTZ00146 PTZ00146
fibrillarin; Provisional
 440-495 3.50e-04

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 44.72  E-value: 3.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657906  440 GGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvtGGSQGT 495
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGG--GGPGKV 57
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 194-237 3.87e-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: 39.70  E-value: 3.87e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1914657906  194 CEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:pfam01607    1 CAGkeDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDY 46
ChtBD2 smart00494
Chitin-binding domain type 2;
193-237 3.97e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 39.73  E-value: 3.97e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657906   193 PCEN--DSYHSKTASLTHFYHCKNGWLYLMYCPSGTIWNSTLSACVY 237
Cdd:smart00494    2 ECPGrgDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
Hia COG5295
Autotransporter adhesin [Intracellular trafficking, secretion, and vesicular transport, ...
 414-559 4.95e-04

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


Pssm-ID: 444098 [Multi-domain]  Cd Length: 785  Bit Score: 45.15  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  414 ASALRGINAKPENQTGEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQ 493
Cdd:COG5295    190 AAASAATGASAGGTASAAASASSSATGTSASVGVNAGAATGSAASAGGSASAGAASGNATTASASSVSGSAVAAGTASTA 269

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914657906  494 GTGGATGGSQGTGGATGGSQGAGGATGGSQATGSSQGTGGATGGSEGGSQIPGGIAGGSQGTGGEG 559
Cdd:COG5295    270 TTASTTAASGAAGTATAAAGGDAAAAGSASSTGAANATAGGGNAGSGGGGAAALGSAGGSSGVGTA 335
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 438-528 5.00e-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: 45.14  E-value: 5.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  438 AIGGSQGT---GGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGGSQG 514
Cdd:COG3210    813 NVTGSGGTitiNTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTAN 892

                           90
                   ....*....|....
gi 1914657906  515 AGGATGGSQATGSS 528
Cdd:COG3210    893 AGTLTNLGTTTNAA 906
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
 427-528 6.17e-04

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: 43.42  E-value: 6.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  427 QTGEGGNGRETAIGGSQGtGGATGGNQGTGGATGGSQ------------------GAGGATGGSQGVGGATGGSQGTGGV 488
Cdd:pfam12810   55 GKGEYNNSTNMNPGGFNG-GGNYKGSSGDGSGGGGGAtdirfdenslksriivagGGGGSGEGDDGSGGYGGGLTGGGGG 133

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1914657906  489 TGGSQGTGGATggsQGTGG----ATGGSQGAGGATGGSQATGSS 528
Cdd:pfam12810  134 SGCYEGSYGAT---QTSGGiggyGINGSFGQGGNGRNSGGGGGG 174
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1251-1297 9.01e-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: 9.01e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1914657906 1251 CEACEKGsYYPKAESIAEFYQCSHGILFLMQCPESTIWHGESLRCIY 1297
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 9.37e-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: 9.37e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1914657906  256 LQDTYYSKPGSVRQFYQCVHGWLFVRSCPTGTVWAGLLKECV 297
Cdd:pfam01607    4 KEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICD 45
Gly_rich pfam12810
Glycine rich protein; This family of proteins is greatly expanded in Trichomonas vaginalis. ...
 431-512 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  431 GGNGRETAIGGSQGtGGATGGNQGTGGA---TGGSQGAGG----ATGGSQGVGGATGGSQGTGGVTGGSqGTGGATGGSQ 503
Cdd:pfam12810  111 GGSGEGDDGSGGYG-GGLTGGGGGSGCYegsYGATQTSGGiggyGINGSFGQGGNGRNSGGGGGGGGGG-GYYGGFGGGS 188


                   ....*....
gi 1914657906  504 GTGGATGGS 512
Cdd:pfam12810  189 YGGGGGGGS 197
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 460-520 1.33e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 41.56  E-value: 1.33e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657906  460 GGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQgtGGATGGSQGAGGATG 520
Cdd:PRK07772   124 GGGGGGGGGFGGGGGGSGGGGGGGGGGGAPGGGGAQASAPADDP--WSSAPASGGFGGGDD 182
PRK07772 PRK07772
single-stranded DNA-binding protein; Provisional
 450-510 2.05e-03

single-stranded DNA-binding protein; Provisional


Pssm-ID: 236092 [Multi-domain]  Cd Length: 186  Bit Score: 41.17  E-value: 2.05e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914657906  450 GGNQGTGGATGGsqGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATG 510
Cdd:PRK07772   124 GGGGGGGGGFGG--GGGGSGGGGGGGGGGGAPGGGGAQASAPADDPWSSAPASGGFGGGDD 182
DUF4766 pfam15973
Domain of unknown function (DUF4766); This presumed domain is functionally uncharacterized. ...
 453-521 2.77e-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: 39.44  E-value: 2.77e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914657906  453 QGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGatGGSQGTGGATGGSQGAGGATGG 521
Cdd:pfam15973   18 EGQGYSNGGGGGGSGGYGGGYGSGHGHGGGQEVKIVKVIEQQAPI--GGHGGSGGGSGGGYSYGGGYAG 84
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 1026-1068 3.09e-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: 3.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1914657906 1026 YYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVYESNP 1068
Cdd:pfam01607    8 YYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNV 50
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 432-527 3.87e-03

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


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 42.06  E-value: 3.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906  432 GNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGATGG 511
Cdd:COG3210    800 ADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITV 879

                           90
                   ....*....|....*.
gi 1914657906  512 SQGAGGATGGSQATGS 527
Cdd:COG3210    880 GSGGVATSTGTANAGT 895
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 382-416 3.99e-03

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


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 37.01  E-value: 3.99e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1914657906  382 FYQCLSGWLFIMECPLNTVWDGESTKCIYDELASA 416
Cdd:pfam01607   18 YYVCSNGEAVEFTCPNGLVFDPTLGICDYPDNVVD 52
PTZ00146 PTZ00146
fibrillarin; Provisional
 431-484 4.00e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1914657906  431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQG 484
Cdd:PTZ00146     2 MGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 431-529 4.05e-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: 39.04  E-value: 4.05e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906   431 GGNGRETAIGGSQGTGGATGGNQGTGGATGGS----QGAGGAT---GGSQGVGGATG--GSQGTGGVTGGSQGTGGATGG 501
Cdd:smart01104    8 GASGSKTPAWGSRTPGTAAGGAPTARGGSGSRtpawGGAGSRTpawGGAGPTGSRTPawGGASAWGNKSSEGSASSWAAG 87

                            90       100       110
                    ....*....|....*....|....*....|....
gi 1914657906   502 SQGTGGA-TGGSQG-----AGGATGGSQATGSSQ 529
Cdd:smart01104   88 PGGAYGApTPGYGGtpsayGPATPGGGAMAGSAS 121
PTZ00146 PTZ00146
fibrillarin; Provisional
 454-508 4.10e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1914657906  454 GTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGVTGGSQGTGGATGGSQGTGGA 508
Cdd:PTZ00146     1 GMGGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 446-498 4.21e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 41.26  E-value: 4.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657906  446 GGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGGSQGTGGvTGGSQGTGGA 498
Cdd:PTZ00146     4 GGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGG-RGGGGGGGPG 55
PTZ00146 PTZ00146
fibrillarin; Provisional
 429-481 4.81e-03

fibrillarin; Provisional


Pssm-ID: 240291  Cd Length: 293  Bit Score: 40.87  E-value: 4.81e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1914657906  429 GEGGNGRETAIGGSQGTGGATGGNQGTGGATGGSQGAGGATGGSQGVGGATGG 481
Cdd:PTZ00146     3 GGGFGGGRGGGRGGGGGGGRGGGGRGGGRGGGRGRGRGGGGGGRGGGGGGGPG 55
ChtBD2 smart00494
Chitin-binding domain type 2;
1024-1064 5.61e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 36.65  E-value: 5.61e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1914657906  1024 YTYYSKLGSNKQFYHCNYGVLYVLECPTQTVWNRRLGSCVY 1064
Cdd:smart00494    8 DGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
ChtBD2 smart00494
Chitin-binding domain type 2;
1437-1481 9.37e-03

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 35.88  E-value: 9.37e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1914657906  1437 PCQKGS--YYPKYQSEAHFYQCSQGLLFLMNCPDNTIWHGKSIRCIY 1481
Cdd:smart00494    2 ECPGRGdgLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDW 48
CTD smart01104
Spt5 C-terminal nonapeptide repeat binding Spt4; The C-terminal domain of the transcription ...
 428-519 9.54e-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: 9.54e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914657906   428 TGEGGNGRETAIGGSQGTGGATGGNQGTGGATgGSQGAGGATGGSQGVGGATGGSQGTGGvTGGSQGTGGATGGSQGTGG 507
Cdd:smart01104   32 ARGGSGSRTPAWGGAGSRTPAWGGAGPTGSRT-PAWGGASAWGNKSSEGSASSWAAGPGG-AYGAPTPGYGGTPSAYGPA 109

                            90
                    ....*....|..
gi 1914657906   508 ATGGSQGAGGAT 519
Cdd:smart01104  110 TPGGGAMAGSAS 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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