|
Name |
Accession |
Description |
Interval |
E-value |
| beta-trefoil_ABD_OTOG-like |
cd23398 |
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The ... |
1098-1241 |
4.56e-47 |
|
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The OTOG family includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOG or OTOGL gene may cause hearing loss. Members of this family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467808 Cd Length: 143 Bit Score: 165.96 E-value: 4.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1098 SGEGPYRLVMVN-GQTLMADYDT-QSVSLITKDTSGDVKVSFMVTPSLFVDPLygrKLISLESALHRNFFIVQNADGTLG 1175
Cdd:cd23398 1 LGEGPYKLSSYNyPGYLLGANDDsGVVSLIPTENSPSGGVSFMVTPGLNGDKA---NLVSFESAERPNYFLCVQANGTLK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148228559 1176 LRKWQPSASFRIQATFILREGRWINGYSTLESYSSRGQYLSFnnTNKVLVMTRVKSTN--MLAMNFKL 1241
Cdd:cd23398 78 LVKWENSALFRNAASFFLRQGTWIPGYVAFESTSKPGYFIRH--SNSSLKLQKYDHTEefRRSSSFKL 143
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
383-531 |
2.26e-26 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 107.07 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 383 CSVTGYQMVRTFDGSLYQSPGTCNYILVKT----SDFTISLSNKACSDqNPDAVCIDTVDIYVPNIaSIKVLQDGSVLSA 458
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDcseePDFSFSVTNKNCNG-GASGVCLKSVTVIVGDL-EITLQKGGTVLVN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 459 GQKVDLPFFLHESItVRRSSSTFLDVVTSM-FSLQYDIEGN-RLYVIIETSYKDQTSGLCGTYNDNRFDDFRSSS 531
Cdd:pfam00094 79 GQKVSLPYKSDGGE-VEILGSGFVVVDLSPgVGLQVDGDGRgQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
378-531 |
2.87e-24 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 101.32 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 378 NCPGVCSVTGYQMVRTFDGSLYQSPGTCNYILVKTS----DFTISLSNKACSdqnPDAVCIDTVDIYVPNIASIKVLQDG 453
Cdd:smart00216 7 ECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssepTFSVLLKNVPCG---GGATCLKSVKVELNGDEIELKDDNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 454 SVLSAGQKVDLPFFLHESITVRRSSSTFLDVVTS--MFSLQYDIEgNRLYVIIETSYKDQTSGLCGTYNDNRFDDFRSSS 531
Cdd:smart00216 84 KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSlgLIQVTFDGL-TLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1014-1088 |
9.59e-16 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 73.91 E-value: 9.59e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148228559 1014 KHYTEKRCSLLFSPD--FAECHTIVPVQPYYTACVEETEACreGESCLCFCTALSAYARACCRKGINV-DWRNPDTCP 1088
Cdd:smart00832 1 KYYACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1020-1087 |
4.06e-14 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 68.95 E-value: 4.06e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1020 RCSLLF-SPDFAECHTIVPVQPYYTACVEETeaCREGESCLCFCTALSAYARACCRKGINV-DWRNPDTC 1087
Cdd:pfam08742 1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDM--CSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-362 |
6.63e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 113 ETNNKFKPNQSNRNDNDDSSKEHK----DSNKGKGQKINNVLSKDSSE-----ENASKEKWSHEKNDKMKTNERKGKDHN 183
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEakkdEEEKKKIAHLKKEEEKKAEEirkekEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 184 DSSKESKEKNhekrqNNKNGWLKDSSEENDSASKE---KKDHDKNNKVRTNQNKGNDHDHSSKESKENSHEKGEKSKKRw 260
Cdd:PTZ00121 1805 DNFANIIEGG-----KEGNLVINDSKEMEDSAIKEvadSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKE- 1878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 261 qngSAEEKDDSSKEKKDHEKND--KVKPKHN-KGNGHDDSSKESKENSHEKREKNKNRwqkgsaEEKDDGSkeKKDKTLE 337
Cdd:PTZ00121 1879 ---DDEEEIEEADEIEKIDKDDieREIPNNNmAGKNNDIIDDKLDKDEYIKRDAEETR------EEIIKIS--KKDMCIN 1947
|
250 260 270
....*....|....*....|....*....|
gi 148228559 338 EMDTNACIFNKESIADG-----ETKDLSCS 362
Cdd:PTZ00121 1948 DFSSKFCDYMKDNISSGncsdeERKELCCS 1977
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
742-801 |
3.67e-10 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 57.40 E-value: 3.67e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 742 CPDDEVFSDClmgsGKSCEPSCQNMAViDQVCPLECEAGCICKYGKLRSNDGTCVPLQEC 801
Cdd:pfam01826 1 CPANEVYSEC----GSACPPTCANLSP-PDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
|
|
| DMP1 |
pfam07263 |
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ... |
86-323 |
2.10e-09 |
|
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.
Pssm-ID: 462128 [Multi-domain] Cd Length: 519 Bit Score: 62.64 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 86 IESSESKGNVRAKRAASGGHKknPSAYETNNKFkpNQSNRNDNDDSSKEHKDSNKgkgqkINNVLSkDSSEENASKE--- 162
Cdd:pfam07263 236 VKSKESKGDSEQASTQDSGDS--QSVEYPSRKF--FRKSRISEEDDRGELDDSNT-----MEEVKS-DSTESTSSKEagl 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 163 KWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNnkngwLKDSSEENDSASKEKKDHDK--NNKVRTNQNKGNDHD- 239
Cdd:pfam07263 306 SQSREDSKSESQEDSEESQSQEDSQNSQDPSSESSQE-----ADLPSQESSSESQEEVVSESrgDNPDNTSSSEEDQEDs 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 240 ------------HSSKESKE-----NSHEKGEKSKKRWQngSAEEKDDSSKE-----KKDHEKNDKVKPKHNKGNGHDDS 297
Cdd:pfam07263 381 dsseedslstfsSSESESREeqadsESNESLRSSEESPE--SSEDENSSSQEglqshSASTESQSEESQSEQDSQSEEDD 458
|
250 260
....*....|....*....|....*.
gi 148228559 298 SKESKENSHEKREKNkNRWQKGSAEE 323
Cdd:pfam07263 459 ESDSQDSSRSKEDSN-STESTSSSEE 483
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
742-801 |
2.45e-09 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 55.02 E-value: 2.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 742 CPDDEVFSDClmgsGKSCEPSCQNMAvIDQVCPLECEAGCICKYGKLRSNDGTCVPLQEC 801
Cdd:cd19941 1 CPPNEVYSEC----GSACPPTCANPN-APPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
831-975 |
5.23e-09 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 57.41 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 831 TCTNNACNVVCNAYAGGQFILFDNIWKTFkTGECQIILVesQDGQV-PKFRVVMQNTKTEnlGGALATKKIFIRFGGAYV 909
Cdd:smart00216 2 CCTQEECSPTCSVSGDPHYTTFDGVAYTF-PGNCYYVLA--QDCSSePTFSVLLKNVPCG--GGATCLKSVKVELNGDEI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 910 ELSDADPVLVQDLG--------STTQVRLYRSGFYIVA-HFLEGLAVYYDQHLDVIIQLQPHLQGKVQGMCGDAD 975
Cdd:smart00216 77 ELKDDNGKVTVNGQqvslpyktSDGSIQIRSSGGYLVViTSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFD 151
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
53-307 |
2.56e-07 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 56.46 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 53 TDCARDANCIFKKVATPEQNTDAIVYDDDDPNIIESSESKGNVRAKRAA-SGGHKKNPSAYETNNKFKPNQSNRNDNDDS 131
Cdd:NF033609 646 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 132 SKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKNGwlKDSSEE 211
Cdd:NF033609 726 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD--SDSDSD 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 212 NDSASKEKKDHDknnkvrTNQNKGNDHDHSSKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHE--KNDKVKPKHN 289
Cdd:NF033609 804 SDSDSDSDSDSD------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSEsgSNNNVVPPNS 877
|
250
....*....|....*...
gi 148228559 290 KGNGHDDSSKESKENSHE 307
Cdd:NF033609 878 PKNGTNASNKNEAKDSKE 895
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-358 |
4.68e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 116 NKFKPNQSNRNDNDDssKEHKDSNKgKGQKINNV---LSKDSSEENASKEKWShEKNDKMKTNERKGKDHNDSSKESKEK 192
Cdd:TIGR04523 221 SELKKQNNQLKDNIE--KKQQEINE-KTTEISNTqtqLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKELEKQLNQLKSE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 193 ----NHEKRQNnkngWLKDSSEENDsaSKEKKDHDKNNKVRTNQ---NKGNDHDHSSKESKENShekgekskkrwqngsa 265
Cdd:TIGR04523 297 isdlNNQKEQD----WNKELKSELK--NQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNS---------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 266 eEKDDSSKEKKDHEKNDKVKpKHNKGNghdDSSKESKEN-SHEKRE-KNKNRWQKGSAEEKD------DGSKEKKDKTLE 337
Cdd:TIGR04523 355 -ESENSEKQRELEEKQNEIE-KLKKEN---QSYKQEIKNlESQINDlESKIQNQEKLNQQKDeqikklQQEKELLEKEIE 429
|
250 260
....*....|....*....|..
gi 148228559 338 EM-DTNacIFNKESIADGETKD 358
Cdd:TIGR04523 430 RLkETI--IKNNSEIKDLTNQD 449
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
841-975 |
2.03e-06 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 49.68 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 841 CNAYAGGQFILFDNIWKTFkTGECQIILVESQDGQvPKFRVVMQNTKTENLGGALATKKIFIRFGGAYVELSDADPVLVQ 920
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTF-PGTCTYVLAKDCSEE-PDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVN 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148228559 921 DLGSTT-------QVRLYRSGFYIVAHFLE-GLAVYYDQHLDVIIQLQPHLQGKVQGMCGDAD 975
Cdd:pfam00094 79 GQKVSLpyksdggEVEILGSGFVVVDLSPGvGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYN 141
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
64-342 |
5.76e-06 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 52.05 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 64 KKVATPEQNTDAIVYDDDDPNIIESSESKGNVRAKRA--ASGGHKKNPSAYETNNKFKPNQSN-RNDNDDSSKEHKDSNK 140
Cdd:COG5192 416 KAIAEETSREDELSFDDSDVSTSDENEDVDFTGKKGAinNEDESDNEEVAFDSDSQFDESEGNlRWKEGLASKLAYSQSG 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 141 GKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGKDHNDSSKESKEKNhEKRQNNKNGWLKDSSEEndsaSKEKK 220
Cdd:COG5192 496 KRGRNIQKIFYDESLSPEECIEEYKGESAKSSESDLVVQDEPEDFFDVSKVAN-ESISSNHEKLMESEFEE----LKKKW 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 221 DHDKNNKVRTnqnkgndhdhsSKESKENSHEKGEKSKKRWQNGSAEEKDD--SSKEKKDHEKNDKVKPKHNKGNGHDDSS 298
Cdd:COG5192 571 SSLAQLKSRF-----------QKDATLDSIEGEEELIQDDEKGNFEDLEDeeNSSDNEMEESRGSSVTAENEESADEVDY 639
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 148228559 299 KESKENSHEKREKNKNRW---QKGSAEEKD-DGSKEKKDKTLEEMDTN 342
Cdd:COG5192 640 ETEREENARKKEELRGNFeleERGDPEKKDvDWYTEEKRKIEEQLKIN 687
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1258-1309 |
1.95e-03 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 38.45 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148228559 1258 YRSCGPACIPTCQDP-LGEKCTLTLkVEGCFpiCAPGMVFDEvTHRCVNKDDC 1309
Cdd:cd19941 7 YSECGSACPPTCANPnAPPPCTKQC-VEGCF--CPEGYVRNS-GGKCVPPSQC 55
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| beta-trefoil_ABD_OTOG-like |
cd23398 |
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The ... |
1098-1241 |
4.56e-47 |
|
Arabinose-binding domain (ABD), beta-trefoil fold, found in the otogelin (OTOG) family; The OTOG family includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOG or OTOGL gene may cause hearing loss. Members of this family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467808 Cd Length: 143 Bit Score: 165.96 E-value: 4.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1098 SGEGPYRLVMVN-GQTLMADYDT-QSVSLITKDTSGDVKVSFMVTPSLFVDPLygrKLISLESALHRNFFIVQNADGTLG 1175
Cdd:cd23398 1 LGEGPYKLSSYNyPGYLLGANDDsGVVSLIPTENSPSGGVSFMVTPGLNGDKA---NLVSFESAERPNYFLCVQANGTLK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148228559 1176 LRKWQPSASFRIQATFILREGRWINGYSTLESYSSRGQYLSFnnTNKVLVMTRVKSTN--MLAMNFKL 1241
Cdd:cd23398 78 LVKWENSALFRNAASFFLRQGTWIPGYVAFESTSKPGYFIRH--SNSSLKLQKYDHTEefRRSSSFKL 143
|
|
| beta-trefoil_ABD_OTOGL |
cd23401 |
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and ... |
1093-1253 |
2.44e-28 |
|
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin-like protein (OTOGL) and similar proteins; OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in the OTOGL gene may cause hearing loss. OTOGL contains an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467811 Cd Length: 154 Bit Score: 112.64 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1093 YYNRDSGEGPYRLVMV--NGQTLMADYDTQSV-SLITKDTSGDVKVSFMVTPSLFVDPLYGRKLISLESALHRNFFIVQN 1169
Cdd:cd23401 1 YYNQGLGEGPYTLSSYgqSDCVLGANLTSGEVfPLPKISAQGSTFFHFMITPGLFKDKASSLPVVSLESAERPNYFLCVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1170 ADGTLGLRKWQPSASFRIQATFILREGRWINGYSTLESYSSRGQYLSFNntnkvlvmtrvkSTNMLAMNFKLTEETFGLP 1249
Cdd:cd23401 81 DNRTLRLEQWQPSSEFRRRATFFHHQGLWIPGYSSFELHSKKGFFITLT------------HSGAKASKYDDSEEFKTSS 148
|
....
gi 148228559 1250 SFSI 1253
Cdd:cd23401 149 SFSI 152
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
383-531 |
2.26e-26 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 107.07 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 383 CSVTGYQMVRTFDGSLYQSPGTCNYILVKT----SDFTISLSNKACSDqNPDAVCIDTVDIYVPNIaSIKVLQDGSVLSA 458
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTFPGTCTYVLAKDcseePDFSFSVTNKNCNG-GASGVCLKSVTVIVGDL-EITLQKGGTVLVN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 459 GQKVDLPFFLHESItVRRSSSTFLDVVTSM-FSLQYDIEGN-RLYVIIETSYKDQTSGLCGTYNDNRFDDFRSSS 531
Cdd:pfam00094 79 GQKVSLPYKSDGGE-VEILGSGFVVVDLSPgVGLQVDGDGRgQLFVTLSPSYQGKTCGLCGNYNGNQEDDFMTPD 152
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
378-531 |
2.87e-24 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 101.32 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 378 NCPGVCSVTGYQMVRTFDGSLYQSPGTCNYILVKTS----DFTISLSNKACSdqnPDAVCIDTVDIYVPNIASIKVLQDG 453
Cdd:smart00216 7 ECSPTCSVSGDPHYTTFDGVAYTFPGNCYYVLAQDCssepTFSVLLKNVPCG---GGATCLKSVKVELNGDEIELKDDNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 454 SVLSAGQKVDLPFFLHESITVRRSSSTFLDVVTS--MFSLQYDIEgNRLYVIIETSYKDQTSGLCGTYNDNRFDDFRSSS 531
Cdd:smart00216 84 KVTVNGQQVSLPYKTSDGSIQIRSSGGYLVVITSlgLIQVTFDGL-TLLSVQLPSKYRGKTCGLCGNFDGEPEDDFRTPD 162
|
|
| beta-trefoil_ABD_OTOG |
cd23400 |
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar ... |
1093-1217 |
9.81e-23 |
|
Arabinose-binding domain (ABD), beta-trefoil fold, found in otogelin (OTOG) and similar proteins; OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of the otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. Mutations in the OTOG gene may cause hearing loss. OTOG contains an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD of the related protein, alpha-L-arabinofuranosidase, binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467810 Cd Length: 152 Bit Score: 96.76 E-value: 9.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1093 YYNRDSGEGPYRLV-MVNGQTLMADYDTQS-VSLITKDTSGDVK-VSFMVTPSLFVDPLYGRKLISLESALHRNFFIVQN 1169
Cdd:cd23400 1 YFNKALGKGPYKLVtYLAGGALLAANKTGGlVFPVRGEDSVDEDlISFMLTPGLYKPKAHDSSLVSFEAADRPNYFLHVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 148228559 1170 ADGTLGLRKWQPSASFRIQATFILREGRWINGYSTLESYSSRGQYLSF 1217
Cdd:cd23400 81 ANGSLRLAKWEDSEEFQDRATFVLHRDTWIPGYDALESFAKPGFFLHF 128
|
|
| C8 |
smart00832 |
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have ... |
1014-1088 |
9.59e-16 |
|
This domain contains 8 conserved cysteine residues; Not all of the conserved cysteines have been included in the alignment model. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin.
Pssm-ID: 214843 Cd Length: 76 Bit Score: 73.91 E-value: 9.59e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148228559 1014 KHYTEKRCSLLFSPD--FAECHTIVPVQPYYTACVEETEACreGESCLCFCTALSAYARACCRKGINV-DWRNPDTCP 1088
Cdd:smart00832 1 KYYACSQCGILLSPRgpFAACHSVVDPEPFFENCVYDTCAC--GGDCECLCDALAAYAAACAEAGVCIsPWRTPTFCP 76
|
|
| beta-trefoil_ABD_ABFB-like |
cd23265 |
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ... |
1099-1233 |
6.60e-15 |
|
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467807 Cd Length: 135 Bit Score: 73.47 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1099 GEGPYRLVMVNGQTLMADYDTQSVSLITKDTSGDVKVSFMVTPslfvdPLYGRKLISLESALHRNFFIVQNaDGTLGLRK 1178
Cdd:cd23265 2 GGTPVRLRSASDPGYYIRHDGGSGSVTSDDDDSAEDAFFRVVP-----GLAGEGTVSFESVDKPGYYLRHR-GGELRLEK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 1179 WQPSASFRIQATFILREGRWINGYSTLESYSSRGQYLSfnNTNKVLVMTRVKSTN 1233
Cdd:cd23265 76 NDGSAAFREDATFRPRPGLADPGGVSFESVNYPGYYLR--HRNNRLVLGKVDSTA 128
|
|
| C8 |
pfam08742 |
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 ... |
1020-1087 |
4.06e-14 |
|
C8 domain; This domain contains 8 conserved cysteine residues, but this family only contains 7 of them to overlaps with other domains. It is found in disease-related proteins including von Willebrand factor, Alpha tectorin, Zonadhesin and Mucin. It is often found on proteins containing pfam00094 and pfam01826.
Pssm-ID: 462584 Cd Length: 68 Bit Score: 68.95 E-value: 4.06e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1020 RCSLLF-SPDFAECHTIVPVQPYYTACVEETeaCREGESCLCFCTALSAYARACCRKGINV-DWRNPDTC 1087
Cdd:pfam08742 1 KCGLLSdSGPFAPCHSVVDPEPYFEACVYDM--CSCGGDDECLCAALAAYARACQAAGVCIgDWRTPTFC 68
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-362 |
6.63e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 113 ETNNKFKPNQSNRNDNDDSSKEHK----DSNKGKGQKINNVLSKDSSE-----ENASKEKWSHEKNDKMKTNERKGKDHN 183
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEakkdEEEKKKIAHLKKEEEKKAEEirkekEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 184 DSSKESKEKNhekrqNNKNGWLKDSSEENDSASKE---KKDHDKNNKVRTNQNKGNDHDHSSKESKENSHEKGEKSKKRw 260
Cdd:PTZ00121 1805 DNFANIIEGG-----KEGNLVINDSKEMEDSAIKEvadSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKE- 1878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 261 qngSAEEKDDSSKEKKDHEKND--KVKPKHN-KGNGHDDSSKESKENSHEKREKNKNRwqkgsaEEKDDGSkeKKDKTLE 337
Cdd:PTZ00121 1879 ---DDEEEIEEADEIEKIDKDDieREIPNNNmAGKNNDIIDDKLDKDEYIKRDAEETR------EEIIKIS--KKDMCIN 1947
|
250 260 270
....*....|....*....|....*....|
gi 148228559 338 EMDTNACIFNKESIADG-----ETKDLSCS 362
Cdd:PTZ00121 1948 DFSSKFCDYMKDNISSGncsdeERKELCCS 1977
|
|
| TIL |
pfam01826 |
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well ... |
742-801 |
3.67e-10 |
|
Trypsin Inhibitor like cysteine rich domain; This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.
Pssm-ID: 460351 Cd Length: 55 Bit Score: 57.40 E-value: 3.67e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 742 CPDDEVFSDClmgsGKSCEPSCQNMAViDQVCPLECEAGCICKYGKLRSNDGTCVPLQEC 801
Cdd:pfam01826 1 CPANEVYSEC----GSACPPTCANLSP-PDVCPEPCVEGCVCPPGFVRNSGGKCVPPSDC 55
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
129-332 |
1.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 129 DDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKNGW--LK 206
Cdd:PTZ00121 1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 207 DSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHSSKESKENSHE--KGEKSKKRwqngsAEEK---DDSSKEKKDHEKN 281
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKK-----AEEAkkaDEAKKKAEEAKKA 1459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148228559 282 DKVKPKHNKGNGHDDSSKESKENSHEKREKNKNRWQKGSAEEKDDGSKEKK 332
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
97-357 |
1.51e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 97 AKRAASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGK---GQKINNVLSKDSSEENASKEKWSHEKNDKMK 173
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeAKKKADAAKKKAEEKKKADEAKKKAEEDKKK 1406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 174 TNE-RKGKDHNDSSKESKEKNHEKRQNNKngwLKDSSEENDSASKEKKDHDKNNKVRtNQNKGNDHDHSSKESKENSHE- 251
Cdd:PTZ00121 1407 ADElKKAAAAKKKADEAKKKAEEKKKADE---AKKKAEEAKKADEAKKKAEEAKKAE-EAKKKAEEAKKADEAKKKAEEa 1482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 252 -KGEKSKKRWQNG--SAEEKDDSSKEKKdheKNDKVKPKHNKGNGHDDSSKESKENSHE--KREKNKNRWQKGSAEE--K 324
Cdd:PTZ00121 1483 kKADEAKKKAEEAkkKADEAKKAAEAKK---KADEAKKAEEAKKADEAKKAEEAKKADEakKAEEKKKADELKKAEElkK 1559
|
250 260 270
....*....|....*....|....*....|...
gi 148228559 325 DDGSKEKKDKTLEEMDTNACIFNKESIADGETK 357
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
90-332 |
1.56e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 90 ESKGNVRAKRAASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKinnvlskdsseenaSKEKwshEKN 169
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA--------------AEEK---AEA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 170 DKMKTNERKGKdhndsSKESKEKNHEKRQNNKngwLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHSSKESKENS 249
Cdd:PTZ00121 1369 AEKKKEEAKKK-----ADAAKKKAEEKKKADE---AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 250 HE--KGEKSKKRwqngsAEEKDDSSKEKKDHE---KNDKVKPKHNKGNGHDDSSKESKENSHEKREKNKNRWQKGSAEEK 324
Cdd:PTZ00121 1441 EEakKADEAKKK-----AEEAKKAEEAKKKAEeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
....*...
gi 148228559 325 DDGSKEKK 332
Cdd:PTZ00121 1516 KKAEEAKK 1523
|
|
| DMP1 |
pfam07263 |
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix ... |
86-323 |
2.10e-09 |
|
Dentin matrix protein 1 (DMP1); This family consists of several mammalian dentin matrix protein 1 (DMP1) sequences. The dentin matrix acidic phosphoprotein 1 (DMP1) gene has been mapped to human chromosome 4q21. DMP1 is a bone and teeth specific protein initially identified from mineralized dentin. DMP1 is primarily localized in the nuclear compartment of undifferentiated osteoblasts. In the nucleus, DMP1 acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the early phase of osteoblast maturation, Ca(2+) surges into the nucleus from the cytoplasm, triggering the phosphorylation of DMP1 by a nuclear isoform of casein kinase II. This phosphorylated DMP1 is then exported out into the extracellular matrix, where it regulates nucleation of hydroxyapatite. DMP1 is a unique molecule that initiates osteoblast differentiation by transcription in the nucleus and orchestrates mineralized matrix formation extracellularly, at later stages of osteoblast maturation. The DMP1 gene has been found to be ectopically expressed in lung cancer although the reason for this is unknown.
Pssm-ID: 462128 [Multi-domain] Cd Length: 519 Bit Score: 62.64 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 86 IESSESKGNVRAKRAASGGHKknPSAYETNNKFkpNQSNRNDNDDSSKEHKDSNKgkgqkINNVLSkDSSEENASKE--- 162
Cdd:pfam07263 236 VKSKESKGDSEQASTQDSGDS--QSVEYPSRKF--FRKSRISEEDDRGELDDSNT-----MEEVKS-DSTESTSSKEagl 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 163 KWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNnkngwLKDSSEENDSASKEKKDHDK--NNKVRTNQNKGNDHD- 239
Cdd:pfam07263 306 SQSREDSKSESQEDSEESQSQEDSQNSQDPSSESSQE-----ADLPSQESSSESQEEVVSESrgDNPDNTSSSEEDQEDs 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 240 ------------HSSKESKE-----NSHEKGEKSKKRWQngSAEEKDDSSKE-----KKDHEKNDKVKPKHNKGNGHDDS 297
Cdd:pfam07263 381 dsseedslstfsSSESESREeqadsESNESLRSSEESPE--SSEDENSSSQEglqshSASTESQSEESQSEQDSQSEEDD 458
|
250 260
....*....|....*....|....*.
gi 148228559 298 SKESKENSHEKREKNkNRWQKGSAEE 323
Cdd:pfam07263 459 ESDSQDSSRSKEDSN-STESTSSSEE 483
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
742-801 |
2.45e-09 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 55.02 E-value: 2.45e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 742 CPDDEVFSDClmgsGKSCEPSCQNMAvIDQVCPLECEAGCICKYGKLRSNDGTCVPLQEC 801
Cdd:cd19941 1 CPPNEVYSEC----GSACPPTCANPN-APPPCTKQCVEGCFCPEGYVRNSGGKCVPPSQC 55
|
|
| VWD |
smart00216 |
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D ... |
831-975 |
5.23e-09 |
|
von Willebrand factor (vWF) type D domain; Von Willebrand factor contains several type D domains: D1 and D2 are present within the N-terminal propeptide whereas the remaining D domains are required for multimerisation.
Pssm-ID: 214566 [Multi-domain] Cd Length: 163 Bit Score: 57.41 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 831 TCTNNACNVVCNAYAGGQFILFDNIWKTFkTGECQIILVesQDGQV-PKFRVVMQNTKTEnlGGALATKKIFIRFGGAYV 909
Cdd:smart00216 2 CCTQEECSPTCSVSGDPHYTTFDGVAYTF-PGNCYYVLA--QDCSSePTFSVLLKNVPCG--GGATCLKSVKVELNGDEI 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 910 ELSDADPVLVQDLG--------STTQVRLYRSGFYIVA-HFLEGLAVYYDQHLDVIIQLQPHLQGKVQGMCGDAD 975
Cdd:smart00216 77 ELKDDNGKVTVNGQqvslpyktSDGSIQIRSSGGYLVViTSLGLIQVTFDGLTLLSVQLPSKYRGKTCGLCGNFD 151
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-332 |
6.05e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 87 ESSESKGNVRAKRAASGGHKKNPSAyetnnKFKPNQSNRNDNDDSSKEHKDSNKGK-GQKINNVLSKDSSEENASKEKWS 165
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAA-----KKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEKKKEEAKKKADAAK 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 166 HEKNDKMKTNERKGKDHNDSSK--ESKEKNHEKRQNNKngwLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDhdhssK 243
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADE---AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE-----A 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 244 ESKENSHEKGEKSKKrwqngsAEEKDDSSKEKKdheKNDKVKPKHNKGNGHDDSSKEsKENSHEKREKNKNRWQKGSAEE 323
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKK------ADEAKKKAEEAK---KADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKKADE 1526
|
....*....
gi 148228559 324 KDDGSKEKK 332
Cdd:PTZ00121 1527 AKKAEEAKK 1535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
106-359 |
3.14e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 106 KKNPSAYETNNKFKPNQSNRNDNDDSSKEHK--DSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKgKDHN 183
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEE 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 184 DSSKESKEKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHSSKESKENSHEKGEKSKKRWQNG 263
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 264 SAEEKDDSSKEKKDHEKNdKVKPKHNKGNGHDDSsKESKENSHEKREKNKNRWQKGSAEEKDDGSKEKKDKTLEE-MDTN 342
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDK-KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEE 1788
|
250
....*....|....*..
gi 148228559 343 ACIFNKEsiADGETKDL 359
Cdd:PTZ00121 1789 DEKRRME--VDKKIKDI 1803
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
125-332 |
3.39e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 125 RNDNDDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGK-------DHNDSSKESKEKNHEKR 197
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKadeakkaEEKKKADEAKKKAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 198 QNNKngwLKDSSEEN----DSASKEKKDHDKNNKV-RTNQNKGNDHDHSSKESKENSHEKGEKSKKRWQ--NGSAEEKDD 270
Cdd:PTZ00121 1316 KADE---AKKKAEEAkkkaDAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKK 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 271 SSKEKKDHEKNDKVKPKHNKGNGHDDSSKESKENSHEKR---EKNKNRWQKGSAEEKDDGSKEKK 332
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKKAEEAKKADEAKKKAEEAK 1457
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
97-351 |
6.05e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 97 AKRAASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNE 176
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 177 RKGKDHNDSSK--ESKEKNHEKR-----------QNNKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKgNDHDHSSK 243
Cdd:PTZ00121 1666 EAKKAEEDKKKaeEAKKAEEDEKkaaealkkeaeEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAK-KEAEEDKK 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 244 ESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHEKNDKVKPKHNKGNGHDD-SSKESKENSHEKREKNK--NRWQKGS 320
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkKIKDIFDNFANIIEGGKegNLVINDS 1824
|
250 260 270
....*....|....*....|....*....|....*
gi 148228559 321 AEEKDDGSKE---KKDKTLEEMDT-NACIFNKESI 351
Cdd:PTZ00121 1825 KEMEDSAIKEvadSKNMQLEEADAfEKHKFNKNNE 1859
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
123-305 |
1.03e-07 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 57.49 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 123 SNRNDNDDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKwshEKNDKMKTNERKGKDHNDSSKESKEKNHeKRQNNKN 202
Cdd:PRK08581 31 QKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQ---DNNDKKFSTIDSSTSDSNNIIDFIYKNL-PQTNINQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 203 GWLKDSSEENDSAS-------KEKKDHDKNNKVRTNQNKGNDHDHSSKES-----KENSHEKGEKSKKRWQNGSAEEKDD 270
Cdd:PRK08581 107 LLTKNKYDDNYSLTtliqnlfNLNSDISDYEQPRNSEKSTNDSNKNSDSSikndtDTQSSKQDKADNQKAPSSNNTKPST 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 148228559 271 SSKEKKDHEKNDKVKPKH----NKGNGHDDSSKESKENS 305
Cdd:PRK08581 187 SNKQPNSPKPTQPNQSNSqpasDDTANQKSSSKDNQSMS 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
152-337 |
1.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 152 KDSSEENASKEKWSHEKND--KMKTNERKGKDHNDSSKESKEKNH-EKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKV 228
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 229 RTNQNKGNDHDHSSKE--SKENSHEKGEKSKKRwqngsAEEK---DDSSKEKKDHEKNDKVKPKHNKGNGHDDSSKESKE 303
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADElkKAAAAKKKADEAKKK-----AEEKkkaDEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
170 180 190
....*....|....*....|....*....|....
gi 148228559 304 NSHEKREKNKNRwQKGSAEEKDDGSKEKKDKTLE 337
Cdd:PTZ00121 1469 AKKADEAKKKAE-EAKKADEAKKKAEEAKKKADE 1501
|
|
| MSCRAMM_ClfA |
NF033609 |
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ... |
53-307 |
2.56e-07 |
|
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.
Pssm-ID: 468110 [Multi-domain] Cd Length: 934 Bit Score: 56.46 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 53 TDCARDANCIFKKVATPEQNTDAIVYDDDDPNIIESSESKGNVRAKRAA-SGGHKKNPSAYETNNKFKPNQSNRNDNDDS 131
Cdd:NF033609 646 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSdSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 132 SKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKNGwlKDSSEE 211
Cdd:NF033609 726 SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD--SDSDSD 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 212 NDSASKEKKDHDknnkvrTNQNKGNDHDHSSKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHE--KNDKVKPKHN 289
Cdd:NF033609 804 SDSDSDSDSDSD------SDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSEsgSNNNVVPPNS 877
|
250
....*....|....*...
gi 148228559 290 KGNGHDDSSKESKENSHE 307
Cdd:NF033609 878 PKNGTNASNKNEAKDSKE 895
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-352 |
3.14e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 87 ESSESKGNVRAKRAASGghKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEK--- 163
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEA--KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEari 1594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 164 ----WSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQnnKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHD 239
Cdd:PTZ00121 1595 eevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 240 hSSKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHEKNDKVKPKHNKgnghddssKESKENSHEKRE-KNKNRWQK 318
Cdd:PTZ00121 1673 -DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELK--------KAEEENKIKAEEaKKEAEEDK 1743
|
250 260 270
....*....|....*....|....*....|....*.
gi 148228559 319 GSAEE--KDDGSKEKKDKTLEEMDTNACIFNKESIA 352
Cdd:PTZ00121 1744 KKAEEakKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-358 |
4.68e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 116 NKFKPNQSNRNDNDDssKEHKDSNKgKGQKINNV---LSKDSSEENASKEKWShEKNDKMKTNERKGKDHNDSSKESKEK 192
Cdd:TIGR04523 221 SELKKQNNQLKDNIE--KKQQEINE-KTTEISNTqtqLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKELEKQLNQLKSE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 193 ----NHEKRQNnkngWLKDSSEENDsaSKEKKDHDKNNKVRTNQ---NKGNDHDHSSKESKENShekgekskkrwqngsa 265
Cdd:TIGR04523 297 isdlNNQKEQD----WNKELKSELK--NQEKKLEEIQNQISQNNkiiSQLNEQISQLKKELTNS---------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 266 eEKDDSSKEKKDHEKNDKVKpKHNKGNghdDSSKESKEN-SHEKRE-KNKNRWQKGSAEEKD------DGSKEKKDKTLE 337
Cdd:TIGR04523 355 -ESENSEKQRELEEKQNEIE-KLKKEN---QSYKQEIKNlESQINDlESKIQNQEKLNQQKDeqikklQQEKELLEKEIE 429
|
250 260
....*....|....*....|..
gi 148228559 338 EM-DTNacIFNKESIADGETKD 358
Cdd:TIGR04523 430 RLkETI--IKNNSEIKDLTNQD 449
|
|
| PTZ00112 |
PTZ00112 |
origin recognition complex 1 protein; Provisional |
92-325 |
8.96e-07 |
|
origin recognition complex 1 protein; Provisional
Pssm-ID: 240274 [Multi-domain] Cd Length: 1164 Bit Score: 54.61 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 92 KGNVRAKRA---ASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKeHKDSNKGKGQKINNVLSKDSSEENasKEKWSHEK 168
Cdd:PTZ00112 113 KANKKEKHNldsSSSSSISSSLTNISFFSSPTSIYSCLSNSLSSK-HSPKVIKENQSTHVNISSDNSPRN--KEISNKQL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 169 NDKMKTNERKGKDHNDSSKeskeKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKgNDHDHSSKESKEN 248
Cdd:PTZ00112 190 KKQTNVTHTTCYDKMRRSP----RNTSTIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEKSK-VQNSHFDVRILRS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 249 SHEKGEKSKKRWQNGS-------------AEEKDDSSKEKKDHEKNDKVKPKHNKGNGHDDSSKESKENSHEKREKNKNR 315
Cdd:PTZ00112 265 YTKENKKDEKNVVSGIrssvllkrksqclRKDSYVYSNHQKKAKTGDPKNIIHRNNGSSNSNNDDTSSSNHLGSNRISNR 344
|
250
....*....|....
gi 148228559 316 W----QKGSAEEKD 325
Cdd:PTZ00112 345 NpsspYKKQTTTKH 358
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
86-339 |
1.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 86 IESSESKGNVRAKRAASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNVLSKDSSE----ENASK 161
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKK 1438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 162 EKWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHS 241
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 242 SKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHEkndkVKPKHNKGNGHDDSSKESKENSHEKREKNKNRWQKGSA 321
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
250
....*....|....*...
gi 148228559 322 EEKDDGSKEKKDKTLEEM 339
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEA 1612
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
113-338 |
1.92e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 113 ETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNVLSKDSSEENaSKEKWSHEKNDKMKTNERK--GKDHNDSSKESK 190
Cdd:pfam02463 237 ERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK-LQEEELKLLAKEEEELKSEllKLERRKVDDEEK 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 191 EKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKN-----NKV-----RTNQNKGNDHDHSSKESKENSHEKGEKSKKRW 260
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKreaeeEEEeelekLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 261 QNGSAEEKDDSSKEKKDHE--KNDKVKPKHNKGNGHDDSSKESKENSHEKREKNKNRWQKGSAEEKDDGSKEKKDKTLEE 338
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELArqLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
|
| VWD |
pfam00094 |
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is ... |
841-975 |
2.03e-06 |
|
von Willebrand factor type D domain; Swiss:P17554 contains a vwd domain. Its function is unrelated but the similarity is very strong by several methods.
Pssm-ID: 459671 [Multi-domain] Cd Length: 154 Bit Score: 49.68 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 841 CNAYAGGQFILFDNIWKTFkTGECQIILVESQDGQvPKFRVVMQNTKTENLGGALATKKIFIRFGGAYVELSDADPVLVQ 920
Cdd:pfam00094 1 CSVSGDPHYVTFDGVKYTF-PGTCTYVLAKDCSEE-PDFSFSVTNKNCNGGASGVCLKSVTVIVGDLEITLQKGGTVLVN 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148228559 921 DLGSTT-------QVRLYRSGFYIVAHFLE-GLAVYYDQHLDVIIQLQPHLQGKVQGMCGDAD 975
Cdd:pfam00094 79 GQKVSLpyksdggEVEILGSGFVVVDLSPGvGLQVDGDGRGQLFVTLSPSYQGKTCGLCGNYN 141
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-338 |
2.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 87 ESSESKGNVRAKRAASGGHKKNPSAYETNNKFKPNQSNRNdNDDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSH 166
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 167 EKNDKMKTNERKGKDHNDSSKESKE-----KNHEKRQNN---KNGWLKDSSEENDSASKEKKDHDKNNKVRTNQnkgndh 238
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKadeakKAEEKKKADelkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------ 1584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 239 dhSSKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHE---KNDKVKPKHNKGNGHDDSSKESKENSHEKREKNKNR 315
Cdd:PTZ00121 1585 --EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
|
250 260
....*....|....*....|...
gi 148228559 316 WQKGSAEEKDDGSKEKKDKTLEE 338
Cdd:PTZ00121 1663 AAEEAKKAEEDKKKAEEAKKAEE 1685
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
78-267 |
3.54e-06 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 52.48 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 78 YDDDDPNIIESSESKGNVrakraASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEH------KDSNKGKGQKINNVLS 151
Cdd:PRK08581 84 STSDSNNIIDFIYKNLPQ-----TNINQLLTKNKYDDNYSLTTLIQNLFNLNSDISDYeqprnsEKSTNDSNKNSDSSIK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 152 KDSSEENASKEKWSHEK-----NDKMKTNERKGKDHNDSSKESkeKNHEKRQNNKNGwLKDSSEENDSAS---------K 217
Cdd:PRK08581 159 NDTDTQSSKQDKADNQKapssnNTKPSTSNKQPNSPKPTQPNQ--SNSQPASDDTAN-QKSSSKDNQSMSdsaldsildQ 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148228559 218 EKKDHDKNNKVRTNQNKgNDHDHSSKESKENSHEKGEKSKKRWQNGSAEE 267
Cdd:PRK08581 236 YSEDAKKTQKDYASQSK-KDKTETSNTKNPQLPTQDELKHKSKPAQSFEN 284
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
64-342 |
5.76e-06 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 52.05 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 64 KKVATPEQNTDAIVYDDDDPNIIESSESKGNVRAKRA--ASGGHKKNPSAYETNNKFKPNQSN-RNDNDDSSKEHKDSNK 140
Cdd:COG5192 416 KAIAEETSREDELSFDDSDVSTSDENEDVDFTGKKGAinNEDESDNEEVAFDSDSQFDESEGNlRWKEGLASKLAYSQSG 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 141 GKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGKDHNDSSKESKEKNhEKRQNNKNGWLKDSSEEndsaSKEKK 220
Cdd:COG5192 496 KRGRNIQKIFYDESLSPEECIEEYKGESAKSSESDLVVQDEPEDFFDVSKVAN-ESISSNHEKLMESEFEE----LKKKW 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 221 DHDKNNKVRTnqnkgndhdhsSKESKENSHEKGEKSKKRWQNGSAEEKDD--SSKEKKDHEKNDKVKPKHNKGNGHDDSS 298
Cdd:COG5192 571 SSLAQLKSRF-----------QKDATLDSIEGEEELIQDDEKGNFEDLEDeeNSSDNEMEESRGSSVTAENEESADEVDY 639
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 148228559 299 KESKENSHEKREKNKNRW---QKGSAEEKD-DGSKEKKDKTLEEMDTN 342
Cdd:COG5192 640 ETEREENARKKEELRGNFeleERGDPEKKDvDWYTEEKRKIEEQLKIN 687
|
|
| Fibrinogen_BP |
pfam08017 |
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family ... |
89-342 |
8.95e-06 |
|
Fibrinogen binding protein; Proteins in this family bind to fibrinogen. Members of this family includes the fibrinogen receptor, FbsA, which mediates platelet aggregation.
Pssm-ID: 311808 [Multi-domain] Cd Length: 393 Bit Score: 50.63 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 89 SESKGNVRAKRAASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGkgqkinNVLSKDSSE-ENASK----EK 163
Cdd:pfam08017 56 NRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQGNVLERRQRDAENRSQG------NVLERRQRDaENKSQgnvlER 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 164 WSHEKNDKMKTN--ERKGKdhnDSSKESKEKNHEKRQnnkngwlKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHS 241
Cdd:pfam08017 130 RQRDAENRSQGNvlERRQR---DAENRSQGNVLERRQ-------RDAENRSQGNVLERRQRDAENKSQGNVLERRQRDAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 242 SKeSKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDH----EKNDKVKPKHNKGN----GHDDSSKESKENSHEKREKNK 313
Cdd:pfam08017 200 NR-SQGNVLERRQRDAENRSQGNVLERRQRDAENRSQgnvlERRQRDAENKSQGNvlerRQRDAENRSQGNVLERRQRDA 278
|
250 260
....*....|....*....|....*....
gi 148228559 314 NRWQKGSAEEKDDGSKEKKDKTLEEMDTN 342
Cdd:pfam08017 279 ENRSQGNVLERRQRDAENKSQVGQLIGKN 307
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
71-358 |
9.01e-06 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 51.28 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 71 QNTDAIVYDDDDPNIIESSESKgnvrAKRAASGGHKKNPSAYETNNKF-KPNQSNRNDNDDSS---KEHKDSNKGKGQKI 146
Cdd:COG5192 387 SNSDAIDTVDRESSEIDNVGRK----TRRQPTGKAIAEETSREDELSFdDSDVSTSDENEDVDftgKKGAINNEDESDNE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 147 NNVLSKDSS-EENASKEKWSHEKNDKMKTNERK------GKDHNDSSKESKEKNHEKRqnnknGWLKDSSEENDSASKEK 219
Cdd:COG5192 463 EVAFDSDSQfDESEGNLRWKEGLASKLAYSQSGkrgrniQKIFYDESLSPEECIEEYK-----GESAKSSESDLVVQDEP 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 220 KDHDKNNKVrtnqnkgNDHDHSSKESKENSHEKgEKSKKRWQNGSA-EEKDDSSKEKKDHEKNDKVKPKHNKGNGHDDSS 298
Cdd:COG5192 538 EDFFDVSKV-------ANESISSNHEKLMESEF-EELKKKWSSLAQlKSRFQKDATLDSIEGEEELIQDDEKGNFEDLED 609
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148228559 299 KESkENSHEKREKNKNRWQKGSAEEKDDGS----KEKKDKTLEEMDTNaciFNKESIADGETKD 358
Cdd:COG5192 610 EEN-SSDNEMEESRGSSVTAENEESADEVDyeteREENARKKEELRGN---FELEERGDPEKKD 669
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
70-347 |
9.08e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 70 EQNTDAIVYDDDdPNIIESSESkgNVRAKRaasgGHKKNpsAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNV 149
Cdd:TIGR01612 1156 EDVADKAISNDD-PEEIEKKIE--NIVTKI----DKKKN--IYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKL 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 150 LSKDSSEEnasKEKWSHekndKMKTNERKGKDHNDSSKESKEknhekrQNNKNGWLKDSSEE----NDSASKEKkdhdkn 225
Cdd:TIGR01612 1227 FLEKIDEE---KKKSEH----MIKAMEAYIEDLDEIKEKSPE------IENEMGIEMDIKAEmetfNISHDDDK------ 1287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 226 nkvrtnqnkgnDHDHSSKESKENSHEKGEKSKKRWQNGSaeEKDDSSKEKKDHEKNDKVKPKHN---------------- 289
Cdd:TIGR01612 1288 -----------DHHIISKKHDENISDIREKSLKIIEDFS--EESDINDIKKELQKNLLDAQKHNsdinlylneianiyni 1354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148228559 290 -KGNGHDDSSKESKENSHEKREKNKNRWQKGSAEE------KDDGS----KEKKDKTLEEMDTNACIFN 347
Cdd:TIGR01612 1355 lKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEklikkiKDDINleecKSKIESTLDDKDIDECIKK 1423
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-332 |
1.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 136 KDSNKGKGQKINNVLSKDSSEE-NASKEKWSHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKNGWLKDSSEENDS 214
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEaKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 215 ASKEKKDHDKNNKVRTNQNKGNDHDHSSKESKENSHE--KGEKSKKRWQNGS--AEEKDDSSKEKKdheKNDKVKPKHNK 290
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKkkADELKKAAAAKK---KADEAKKKAEE 1429
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148228559 291 GNGHDDSSKESKENSHEKREKNKNRwQKGSAEEKDDGSKEKK 332
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAK 1470
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
180-360 |
1.14e-05 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 50.56 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 180 KDHNDSSKESKEKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHSSKESKENSHEKGEKSKKR 259
Cdd:PRK08581 33 DSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTNINQLLTKNK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 260 WQNG-----SAEEKDDSSKEKKDHEKNDKVKPKHNKGNGHDDSS--KESKENSHE-------KREKNKNRWQKGSAEEKD 325
Cdd:PRK08581 113 YDDNyslttLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSikNDTDTQSSKqdkadnqKAPSSNNTKPSTSNKQPN 192
|
170 180 190
....*....|....*....|....*....|....*...
gi 148228559 326 DG---SKEKKDKTLEEMDTNAcifNKESIADGETKDLS 360
Cdd:PRK08581 193 SPkptQPNQSNSQPASDDTAN---QKSSSKDNQSMSDS 227
|
|
| PTZ00112 |
PTZ00112 |
origin recognition complex 1 protein; Provisional |
85-344 |
1.63e-05 |
|
origin recognition complex 1 protein; Provisional
Pssm-ID: 240274 [Multi-domain] Cd Length: 1164 Bit Score: 50.37 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 85 IIESSESKGNVRAKRAASGGH-----KKNPSAYETNNKFKPNQSNrNDNDDSSKEHKDSNKgkgqkinNVLSKDSSEENA 159
Cdd:PTZ00112 150 LSNSLSSKHSPKVIKENQSTHvnissDNSPRNKEISNKQLKKQTN-VTHTTCYDKMRRSPR-------NTSTIKNNTNDK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 160 SKEKWSHEKNDK---------MKTNERKGKDHND----------SSKESKEKNHEKRQNNKNGWLKDSSE--ENDS---- 214
Cdd:PTZ00112 222 NKEKNKEKDKNIkkdrdgdkqTKRNSEKSKVQNShfdvrilrsyTKENKKDEKNVVSGIRSSVLLKRKSQclRKDSyvys 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 215 --ASKEKKDHDKNNKVRTNQNKGNDHDHSSkeskENSHEKGEKSKKRwQNGSAEEKDDSSKEKKDHEKNDKVKPKHNKGN 292
Cdd:PTZ00112 302 nhQKKAKTGDPKNIIHRNNGSSNSNNDDTS----SSNHLGSNRISNR-NPSSPYKKQTTTKHTNNTKNNKYNKTKTTQKF 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148228559 293 GH--DDSSKESKENSHEKREKNKNRWQKGSAEEKDDGSKEK-----KDKTLEEMDTNAC 344
Cdd:PTZ00112 377 NHplRHHATINKRSSMLPMSEQKGRGASEKSEYIKEFTMEEvakltKDTTIKLVEENSC 435
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
133-354 |
1.76e-05 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 50.47 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 133 KEHKDSNKGKGQKINNVLSkdsSEENASKEKWSHEKNDKMKTNERKG----KDHNDSSKESKEKNHEKRqnnkngwLKDS 208
Cdd:COG5644 4 PQGKHQRKGKKQLENKILH---SYEEESAGFDSEELEDNDEQGYSFGvnseDDEEIDSDEAFDEEDEKR-------FADW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 209 SEENDSASKEKKDHDK-NNKVRTNQNKGNDHDHSSKESKENSHEKGEKSK-----KRWqngsaeekDDSSKEKKDHEKND 282
Cdd:COG5644 74 SFNASKSGKSNKDHKNlNNTKEISLNDSDDSVNSDKLENEGSVSSIDENElvdldTLL--------DNDQPEKNESGNND 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 283 KVKPKHNK----GNGHDDSSKESKENSHEKREKNKNRWQKGSAEEKDD-----GSK---EKKDKTLEEMDTNACI----- 345
Cdd:COG5644 146 HATDKENLlesdASSSNDSESEESDSESEIESSDSDHDDENSDSKLDNlrnyiVSLkkdEADAESVLSSDDNDSIeeiky 225
|
250
....*....|...
gi 148228559 346 ----FNKESIADG 354
Cdd:COG5644 226 dpheTNKESGSSE 238
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
33-362 |
1.79e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.44 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 33 KDGDTIKYDCQICECTNGRITDCARDANCI------FKKVATPEQNTDAIVYD--DDDPNIIESSESKGNV-------RA 97
Cdd:TIGR01612 1250 EDLDEIKEKSPEIENEMGIEMDIKAEMETFnishddDKDHHIISKKHDENISDirEKSLKIIEDFSEESDIndikkelQK 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 98 KRAASGGHKKNPSAY--ETNNKFKPNQSNRNDND-DSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKT 174
Cdd:TIGR01612 1330 NLLDAQKHNSDINLYlnEIANIYNILKLNKIKKIiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIE 1409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 175 NERKGKDHNDSSKESKE-KNH-EKRQNNKNGWLKDSSEENDSASKEKKD----HDKNNKVRTNQ--NKGNDHDHSSKESK 246
Cdd:TIGR01612 1410 STLDDKDIDECIKKIKElKNHiLSEESNIDTYFKNADENNENVLLLFKNiemaDNKSQHILKIKkdNATNDHDFNINELK 1489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 247 ENshekgekskkrwqngsaeeKDDSSKEKKDHEKNDKVKPKH---------------NK------GNGHDDSSKESKENS 305
Cdd:TIGR01612 1490 EH-------------------IDKSKGCKDEADKNAKAIEKNkelfeqykkdvtellNKysalaiKNKFAKTKKDSEIII 1550
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148228559 306 HEKRE-KNKNRWQKGSAEEKDDGSKEKKDKTLEEMDTN-----ACIFNKESIADGETKDLSCS 362
Cdd:TIGR01612 1551 KEIKDaHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNdksnkAAIDIQLSLENFENKFLKIS 1613
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
151-285 |
3.30e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 46.61 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 151 SKDSSEENASKEKWSHEKNdkMKTNERKGKdhNDSSKESKEKNHEKRQNNKNGwLKDSSEENDSASKEKKDHDKNNKvrt 230
Cdd:pfam11600 3 SQKSVQSQEEKEKQRLEKD--KERLRRQLK--LEAEKEEKERLKEEAKAEKER-AKEEARRKKEEEKELKEKERREK--- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148228559 231 nqnkgNDHDHSSKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHEKNDKVK 285
Cdd:pfam11600 75 -----KEKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIK 124
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
113-314 |
5.44e-05 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 48.63 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 113 ETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNVLSKDSSEENASKEKWSHEKNDKMKTNERKGKDHND-------- 184
Cdd:PRK08581 45 KSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTNINQLLTKNKYDDNyslttliq 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 185 --SSKESKEKNHEKRQNNKNGwLKDSSEENDSASKEKKDHDKNNKVRTNQNKGNdHDHSSKESKENSHEKGEKSKKRWQN 262
Cdd:PRK08581 125 nlFNLNSDISDYEQPRNSEKS-TNDSNKNSDSSIKNDTDTQSSKQDKADNQKAP-SSNNTKPSTSNKQPNSPKPTQPNQS 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148228559 263 GSAEEKDDSSKEKKDHEKNDKVKPK----------HNKGNGHDDSSKeSKENSHEKREKNKN 314
Cdd:PRK08581 203 NSQPASDDTANQKSSSKDNQSMSDSaldsildqysEDAKKTQKDYAS-QSKKDKTETSNTKN 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
152-337 |
6.04e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 152 KDSSEENASKEKwshEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKngwLKDSSE----ENDSASKEKKDHDKNNK 227
Cdd:PTZ00121 1236 KKDAEEAKKAEE---ERNNEEIRKFEEARMAHFARRQAAIKAEEARKADE---LKKAEEkkkaDEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 228 VRTNQNKGNDhdhsSKESKENSHEKGEKSKKRwqngsAEE--KDDSSKEKKDHEKNDKVKPKHNKGNGHDDSSKESKENS 305
Cdd:PTZ00121 1310 KAEEAKKADE----AKKKAEEAKKKADAAKKK-----AEEakKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380
|
170 180 190
....*....|....*....|....*....|..
gi 148228559 306 HEKREKNKnrwQKGSAEEKDDGSKEKKDKTLE 337
Cdd:PTZ00121 1381 DAAKKKAE---EKKKADEAKKKAEEDKKKADE 1409
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
206-338 |
6.54e-05 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 45.83 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 206 KDSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDhssKESKENSHEKGEKSKKRWQNgSAEEKDDSSKEKKDHEKNDKvK 285
Cdd:pfam11600 1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAE---KEEKERLKEEAKAEKERAKE-EARRKKEEEKELKEKERREK-K 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 148228559 286 PKhnkgnghDDSSKESKENSHEKREKNKNRWQKGSAEEKDDGSKEKKDKTLEE 338
Cdd:pfam11600 76 EK-------DEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEK 121
|
|
| beta-trefoil_ABD_ABFB |
cd23399 |
Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF ... |
1136-1219 |
1.70e-04 |
|
Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF B) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. The family also includes Hungateiclostridium thermocellum anti-sigma-I factor RsgI5. It negatively regulates SigI5 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI5 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI5. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.
Pssm-ID: 467809 Cd Length: 138 Bit Score: 43.74 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 1136 SFMVTPSLfvdplYGRKLISLESALHRNFFIvQNADGTLGLRKWQPSASFRIQATFILREGRWINGYSTLESYSSRGQYL 1215
Cdd:cd23399 41 TFKVVPGL-----ADSGCVSFESVNYPGYYL-RHYNFRLRLDKNDGSALFKEDATFCPRPGLADGGGVSFRSYNYPGRYI 114
|
....
gi 148228559 1216 SFNN 1219
Cdd:cd23399 115 RHRN 118
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
153-357 |
2.12e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 153 DSSEENASKEKWSHEKNDKMKTNERKgkdhnDSSKESKEKNHEKRQNnkngwlkdsSEENDSASKEkkdhdknnkvrtNQ 232
Cdd:pfam02029 1 IEDEEEAARERRRRAREERRRQKEEE-----EPSGQVTESVEPNEHN---------SYEEDSELKP------------SG 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 233 NKGNDHDHSSKESKENSHEKGEKSKKRWQNGsAEEKDDSSKEKKD----HEKNDKVKPKHNKGNGHDDSSKESKENSHEK 308
Cdd:pfam02029 55 QGGLDEEEAFLDRTAKREERRQKRLQEALER-QKEFDPTIADEKEsvaeRKENNEEEENSSWEKEEKRDSRLGRYKEEET 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148228559 309 ----REKNKNRWQKGSAEEKDDGsKEKKDKTLEEMDTNACIFNKESIADGETK 357
Cdd:pfam02029 134 eireKEYQENKWSTEVRQAEEEG-EEEEDKSEEAEEVPTENFAKEEVKDEKIK 185
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
148-337 |
2.34e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 148 NVLSKDSSEENASKEKWSHEKND-KMKTNERKGKDHNDSSKESKEKNhekrQNNKNGWLKdsSEENDSASKEKKDHDKNN 226
Cdd:TIGR04523 26 NIANKQDTEEKQLEKKLKTIKNElKNKEKELKNLDKNLNKDEEKINN----SNNKIKILE--QQIKDLNDKLKKNKDKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 227 KVRTNQNKGNDHDHSSKESKENSHEKGEKSKKRWQNGSAEEKDDSSKEKKDHEKNDKVKPKHNKGNghddSSKESKEN-- 304
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK----KQKEELENel 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148228559 305 ---SHEKREKNKN----RWQKGSAEEK--DDGSKEKKDKTLE 337
Cdd:TIGR04523 176 nllEKEKLNIQKNidkiKNKLLKLELLlsNLKKKIQKNKSLE 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
87-337 |
2.61e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 87 ESSESKGNVRAKRAASGGHKKNPSAYETNNKFKPNQSNRNDNDDSSKEHKdsnKGKGQKINNVLSKDSSEE--NASKEKW 164
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEAKKADEakKAEEKKK 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 165 SHE--KNDKMKTNERKGKDHnDSSKESKEKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKVRtnqnKGNDHDHSS 242
Cdd:PTZ00121 1548 ADElkKAEELKKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK----KAEEAKIKA 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 243 KESKENSHEKgeKSKKRWQNGSAEEKDDSSKEKKDHEKNdKVKPKHNKGNGHDDSSKESKENSHEKREKNKNRWQKGSAE 322
Cdd:PTZ00121 1623 EELKKAEEEK--KKVEQLKKKEAEEKKKAEELKKAEEEN-KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
250
....*....|....*
gi 148228559 323 EKDDGSKEKKDKTLE 337
Cdd:PTZ00121 1700 EAKKAEELKKKEAEE 1714
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
167-332 |
5.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 167 EKNDKMKTNERKGKDHNDSSKESKEKNHEK-RQNNKNGWLKDSSEENDSASKEKKDHDKNNKV----RTNQNKGNDHDHS 241
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEiRKFEEARMAHFARRQAAIKAEEARKADELKKAeekkKADEAKKAEEKKK 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 242 SKESKENSHE--KGEKSKKRWQngSAEEKDDSSKEK-KDHEKNDKVKPKHNKGNGHD-DSSKESKENSHEKREKNKNRWQ 317
Cdd:PTZ00121 1304 ADEAKKKAEEakKADEAKKKAE--EAKKKADAAKKKaEEAKKAAEAAKAEAEAAADEaEAAEEKAEAAEKKKEEAKKKAD 1381
|
170
....*....|....*..
gi 148228559 318 --KGSAEEKDDGSKEKK 332
Cdd:PTZ00121 1382 aaKKKAEEKKKADEAKK 1398
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
165-291 |
5.81e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 165 SHEKNDKMKTNERKGKDHNDSSKESKEKNHEKRQNNKNGWLKDSSEENDSASKEKKDHD--------------KNNKV-- 228
Cdd:PTZ00265 653 SNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDalmknkngiyytmiNNQKVss 732
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148228559 229 RTNQNKGNDHDHSSKESKENSHEKGEKSKKrwQNGSAEEKDDSSKEKKDHEKNDKVKPKHNKG 291
Cdd:PTZ00265 733 KKSSNNDNDKDSDMKSSAYKDSERGYDPDE--MNGNSKHENESASNKKSCKMSDENASENNAG 793
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
162-357 |
6.79e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 162 EKWSHEKNDK-MKTNERKGKDHNDSSKESKEKNHEKRQNNKNGWLKDSSEENDSaskeKKDHDKNNKVRTNQNKGNDHDH 240
Cdd:pfam02463 236 EERIDLLQELlRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK----LLAKEEEELKSELLKLERRKVD 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 241 SSKESKENSHEKGEKSKKrwQNGSAEEKDDSSKEKKDHEKNDKVkpkhnkgnghDDSSKESKENSHEKREKNKNRWQKGS 320
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKE--LKKEKEEIEELEKELKELEIKREA----------EEEEEEELEKLQEKLEQLEEELLAKK 379
|
170 180 190
....*....|....*....|....*....|....*..
gi 148228559 321 AEEKDDGSKEKKDKTLEEmdtnACIFNKESIADGETK 357
Cdd:pfam02463 380 KLESERLSSAAKLKEEEL----ELKSEEEKEAQLLLE 412
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
187-352 |
6.91e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 187 KESKEKNHEKRQNNKNGWLKDSSEENDSASKEKKDHDKNNKVRTNQNKGND--HDHSSKESKE---------NSHEKGEK 255
Cdd:pfam05262 187 REDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADfaQDNADKQRDEvrqkqqeakNLPKPADT 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 256 SKKRWQNGSAEE-KDDSSKEKKDHEKNDKVKPKhNKGNGHDDSSKESKENshEKREKNKnrwqkgSAEEKDDGSKEKKD- 333
Cdd:pfam05262 267 SSPKEDKQVAENqKREIEKAQIEIKKNDEEALK-AKDHKAFDLKQESKAS--EKEAEDK------ELEAQKKREPVAEDl 337
|
170 180
....*....|....*....|
gi 148228559 334 -KTLEEMDTNACIFNKESIA 352
Cdd:pfam05262 338 qKTKPQVEAQPTSLNEDAID 357
|
|
| TIL |
cd19941 |
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich ... |
1258-1309 |
1.95e-03 |
|
trypsin inhibitor-like cysteine rich domain; TIL (trypsin inhibitor-like) cysteine rich domains are found in smapins (small serine proteinase inhibitor), or Ascaris trypsin inhibitor (ATI)-like proteins, whose members include anticoagulant proteins, elastase inhibitors, trypsin inhibitors, thrombin inhibitors, and chymotrypsin inhibitors. The TIL domain is also found in some large modular glycoproteins, including the von Willebrand factor (VWF), mucin-6, mucin-19, and SCO-spondin, among others. The TIL domain is characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. The cysteine residues that form the disulfide bonds are linked in the pattern: cysteines 1-7, 2-6, 3-5, 4-10 and 8-9. TILs can occur as a single domain or in multiple tandem arrangements. The disulfide bonds account for the unusual resistance to proteolysis and heat denaturation of these proteins. Smapins possess an unusual fold and, with the exception of the reactive site, shows no similarity to other serine protease inhibitors. The serine protease inhibitors comprise a large family of molecules involved in inflammatory responses, blood clotting, and complement activation.
Pssm-ID: 410995 Cd Length: 55 Bit Score: 38.45 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 148228559 1258 YRSCGPACIPTCQDP-LGEKCTLTLkVEGCFpiCAPGMVFDEvTHRCVNKDDC 1309
Cdd:cd19941 7 YSECGSACPPTCANPnAPPPCTKQC-VEGCF--CPEGYVRNS-GGKCVPPSQC 55
|
|
| Merozoite_SPAM |
pfam07133 |
Merozoite surface protein (SPAM); This family consists of several Plasmodium falciparum SPAM ... |
186-360 |
2.37e-03 |
|
Merozoite surface protein (SPAM); This family consists of several Plasmodium falciparum SPAM (secreted polymorphic antigen associated with merozoites) proteins. Variation among SPAM alleles is the result of deletions and amino acid substitutions in non-repetitive sequences within and flanking the alanine heptad-repeat domain. Heptad repeats in which the a and d position contain hydrophobic residues generate amphipathic alpha-helices which give rise to helical bundles or coiled-coil structures in proteins. SPAM is an example of a P. falciparum antigen in which a repetitive sequence has features characteriztic of a well-defined structural element.
Pssm-ID: 429310 [Multi-domain] Cd Length: 176 Bit Score: 41.12 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 186 SKESKEKNHEKRQNNKNGWLK-DSSEENDSASKEKKDHDKNNKVRTNQNKGNDHDHSSKESKENSHEKGEKSKKrwqngs 264
Cdd:pfam07133 13 SEEDKKKGCLLEHVKLTSWDKeDIAKENEDVEDEKEDEEEETEDEETEEKNEEETEEETEDEEDEEEVEEEEEK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 265 aEEKDDSSKEKKDHEKNDKVKPKHNKGNGHDDSSKESKENSHEKREKNKNrwqkgsaeekddgskEKKDKTLEE-MDTNA 343
Cdd:pfam07133 87 -EENEDKKKELEEEQINKNTDTSDLEKKGKNDSEKDEKAQNLISKNYKNN---------------DELKKTAETlVNTLI 150
|
170
....*....|....*..
gi 148228559 344 CIFNKESIADGETKDLS 360
Cdd:pfam07133 151 SLLNEKNELDSTLNDLV 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-255 |
2.49e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 119 KPNQSNRNDNDDSSKEHKDSNKGkgQKINNVLS-------KDSSEENASKEKWSHEKNDKMktnerkgkdhndSSKESKE 191
Cdd:PTZ00265 672 KDNKENNNKNNKDDNNNNNNNNN--NKINNAGSyiieqgtHDALMKNKNGIYYTMINNQKV------------SSKKSSN 737
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148228559 192 KNHEKRQNNKNGWLKDSSEENDSaskekkDHDKNNKVRTNQNKGNDHDHSSKESKENSHEKGEK 255
Cdd:PTZ00265 738 NDNDKDSDMKSSAYKDSERGYDP------DEMNGNSKHENESASNKKSCKMSDENASENNAGGK 795
|
|
| COG5024 |
COG5024 |
Cyclin [Cell division and chromosome partitioning]; |
183-343 |
4.73e-03 |
|
Cyclin [Cell division and chromosome partitioning];
Pssm-ID: 227357 [Multi-domain] Cd Length: 440 Bit Score: 42.07 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 183 NDSSKESKEKNHEKRQNNKNgwlkdsseeNDSASKEKKDHDKNNKVRTNQNKGNDHD--HSSKESKENSHEKGEKSKKRW 260
Cdd:COG5024 15 NVAVQSSKNKPNVKLILQQP---------EMNILETRSAIVDFLNQLSTVTRLSNGInfHSSKSTKLVVGTCLWLAKKTW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 261 QNGSAEEkDDSSKEKKDHEKNDKVKPKHNKGNGHDDSSKESKENSHEKREKNKNRWQKGSAEEK-DDGSKEKKDKTLEEM 339
Cdd:COG5024 86 GIISSGE-SNERARIPRLSECNLDSILFIQMTLNEDSYEPMIDYILKKDENSLSPYELDENQLAlDEKQAESKRESQSWQ 164
|
....
gi 148228559 340 DTNA 343
Cdd:COG5024 165 DLDA 168
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
72-347 |
7.62e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 41.74 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 72 NTDAIVyDDDDPNIIESSESKGNVRAKRAASGGHKKN--PSAYETNNKFKPNQSNRNDNDDSSKEHKDSNKGKGQKINNV 149
Cdd:PTZ00440 921 NTDNII-QKNEKLNLLNNLNKEKEKIEKQLSDTKINNlkMQIEKTLEYYDKSKENINGNDGTHLEKLDKEKDEWEHFKSE 999
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 150 LSKDSSEENASKEKwsheKNDKMKtnerkgKDHND----SSKESKEKNHEkrqnnkngwLKDSSEENDSASKEKKdhDKN 225
Cdd:PTZ00440 1000 IDKLNVNYNILNKK----IDDLIK------KQHDDiielIDKLIKEKGKE---------IEEKVDQYISLLEKMK--TKL 1058
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148228559 226 NKVRTNQNKGNDHDHSSKEskensHEKGEKSKKrwqngsaeeKDDSSKEKKDHEKNDKVKPKHnkgNGHDDSSKESKENS 305
Cdd:PTZ00440 1059 SSFHFNIDIKKYKNPKIKE-----EIKLLEEKV---------EALLKKIDENKNKLIEIKNKS---HEHVVNADKEKNKQ 1121
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148228559 306 HEKREKNKNrwqkgsAEEKDDGSKEKKDKTLEEMDTNACIFN 347
Cdd:PTZ00440 1122 TEHYNKKKK------SLEKIYKQMEKTLKELENMNLEDITLN 1157
|
|
| |
