|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_interalpha_trypsin_inhibitor |
cd01461 |
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
280-464 |
5.44e-64 |
|
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.
Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 214.39 E-value: 5.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 280 LEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNIWKAeGSIQATVQNIHSAKNYVSRMEADGW 359
Cdd:cd01461 1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSP-SSVSATAENVAAAIEYVNRLQALGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 360 TDINAALLAAASVLNHSNqepgkgrgvGQIPLIMFLTDGEptagETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLR 439
Cdd:cd01461 80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146
|
170 180
....*....|....*....|....*
gi 2208424302 440 RLSLENQGEARRIYEDADAALQLEG 464
Cdd:cd01461 147 RLAREGRGIARRIYETDDIESQLLR 171
|
|
| ITI_HC_C |
pfam06668 |
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ... |
1087-1268 |
3.28e-54 |
|
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.
Pssm-ID: 429061 Cd Length: 189 Bit Score: 187.41 E-value: 3.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1087 KAGLHVSGQLLGAPSRPSHKDQTRTYFHIITITSdKPRAYNITISRSSISV-QGESTLSLSWNQRALVKKPHLELHVASA 1165
Cdd:pfam06668 1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVV-KPLGVKIEVTPEKITLkDGEKRLVLSWSDTASVKQPGLTVSVVKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1166 ALLTVRLGPHLNFFILRHQYRHPSTLQLPHLGFYVANGSGLSPSARGLMGQFQY-TDIRLVTGPSGS------YLQKHHG 1238
Cdd:pfam06668 80 SNVTVTIGDGISFVVLLHRVWKPHPYQVDHLGFYIVNSKGLSPSVHGLLGQFLHePEVEVTDVRPGSdpekpdATMKVKG 159
|
170 180 190
....*....|....*....|....*....|
gi 2208424302 1239 LDVPVVLGKRLLKESPRLLPRWTSCWIVKR 1268
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
|
|
| VIT |
smart00609 |
Vault protein Inter-alpha-Trypsin domain; |
40-150 |
3.02e-46 |
|
Vault protein Inter-alpha-Trypsin domain;
Pssm-ID: 197803 [Multi-domain] Cd Length: 130 Bit Score: 162.14 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:smart00609 20 LKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAGL 99
|
90 100 110
....*....|....*....|....*....|.
gi 2208424302 120 VGIRDRESENFRISTMLAAGTKATFALAYEE 150
Cdd:smart00609 100 VRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
|
|
| marine_srt_targ |
TIGR03788 |
marine proteobacterial sortase target protein; Members of this protein family are restricted ... |
51-630 |
2.74e-38 |
|
marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).
Pssm-ID: 274782 [Multi-domain] Cd Length: 596 Bit Score: 152.54 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 51 ANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAHVgirDRESENF 130
Cdd:TIGR03788 14 ARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV---EQQRPNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 131 RISTM--LAAGTKATFALAYEELLQRHQG----RYQLVVGLR--PGQLVrklNVEITVSERT-GIAYVHIP-PLRTSQVC 200
Cdd:TIGR03788 91 FTNKVanIGPGETVVVTIEYQQPVSYSSGtfslRLPLTVTPRyiPGSTV---NTVTDVNNSGwAIPTTQVPdADKISAPR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 201 TnnqTSEGDLPPSTR------IQRGETCVHITfSPT------LRDQSAFSSS----GIMADFTihYDVSMEDIIGDV--- 261
Cdd:TIGR03788 168 V---LDPDDDAPSSQasinvdLNAGLPLDSIT-SPShpiqieQQGQSGYTISlaqgQVIADRD--FVLTWRPAQGEApsa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 262 ----QVYGGYfiHY--------FAPRGLQPLEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN 329
Cdd:TIGR03788 242 alfrEQIGGE--RYglamvmppTEAAVAQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 330 -IWKaeGSIQATVQNIHSAKNYVSRMEADGWTDInaALLAAASVLNHSNQEPGKGRGVgqipliMFLTDGEpTAGEttpS 408
Cdd:TIGR03788 320 lLFP--VPVPATAHNLARARQFVAGLQADGGTEM--AGALSAALRDDGPESSGALRQV------VFLTDGA-VGNE---D 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 409 VILSNIRQALAHRvSLFSLAFGDDADFSLLRRLSLENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDYLGGWVGA 488
Cdd:TIGR03788 386 ALFQLIRTKLGDS-RLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGNAAD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 489 SSRAHFPNYFHGSELVVAGKVQPGEQELGIhlAARGPNGHLLVAHHSEEASNSSQkafgcpgkpalnvthfIHRLWAYVT 568
Cdd:TIGR03788 465 VYPSPIPDLYRGEPLQIAIKLQQAAGELQL--TGRTGSQPWSQQLDLDSAAPGKG----------------IDKLWARRK 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2208424302 569 IGELLKARFQAKDTTtrrllAAKA--LNLSLEYNFVTPLTSLVVVHLEKTNEEAMTQPSTTAKT 630
Cdd:TIGR03788 527 IDSLEDSLRYGANEE-----KVKDqvTALALNHHLVSPFTSFVAVEETPIRPAAESLNSEASPN 585
|
|
| VIT |
pfam08487 |
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ... |
40-148 |
2.04e-32 |
|
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilisation and tumor metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.
Pssm-ID: 430025 [Multi-domain] Cd Length: 111 Bit Score: 121.86 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:pfam08487 4 VSVEATITGRIARTTVTQTFVNPSSEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKTAGL 83
|
90 100 110
....*....|....*....|....*....|
gi 2208424302 120 VgiRDRESENFRIST-MLAAGTKATFALAY 148
Cdd:pfam08487 84 L--EQDDPDVFTTSVgNIPPGEKVTVELTY 111
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
283-458 |
7.12e-22 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 94.06 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQAS---DSFNIITFSDTVNIWKAEGSIqatvQNIHSAKNYVSRME--AD 357
Cdd:smart00327 1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdgDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSykLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 358 GWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGettPSVILSNIRQALAHRVSLFSLAFGDDADFSL 437
Cdd:smart00327 77 GGTNLGAALQYALENLFSKSA--GSRRGAPKV--VILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVGNDVDEEE 149
|
170 180
....*....|....*....|.
gi 2208424302 438 LRRLSLENQGEARRIYEDADA 458
Cdd:smart00327 150 LKKLASAPGGVYVFLPELLDL 170
|
|
| VWA |
pfam00092 |
von Willebrand factor type A domain; |
283-468 |
6.56e-16 |
|
von Willebrand factor type A domain;
Pssm-ID: 425461 [Multi-domain] Cd Length: 174 Bit Score: 76.93 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQA---SDSFNIITFSDTVNIWkaegsIQ-ATVQNIHSAKNYVSRME--A 356
Cdd:pfam00092 1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIgpdGTRVGLVQYSSDVRTE-----FPlNDYSSKEELLSAVDNLRylG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 357 DGWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGEttpsvILSNIRQALAHRVSLFSLAFGdDADFS 436
Cdd:pfam00092 76 GGTTNTGKALKYALENLFSSAA--GARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVG-NADDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 2208424302 437 LLRRLSLENqgEARRIYEDADAAlQLEGLYAE 468
Cdd:pfam00092 146 ELRKIASEP--GEGHVFTVSDFE-ALEDLQDQ 174
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
655-996 |
1.80e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 655 KVFSKSRPTKPTSTIIAPTMKvtsskelgALGWWSNSLTTSVQPKPQ------IPGQDSSTLALPTLKMKPLAHVPSNSN 728
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRR--------AARPTVGSLTSLADPPPPpptpepAPHALVSATPLPPGPAAARQASPALPA 2737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 729 DPLPRKPSTSTHQNPGITSLVNSGTYILPLNPVSPSQPKGGTMKHFNSFSPFKLPASSDAHPTPDTPS-----YLQPVSQ 803
Cdd:PHA03247 2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaaVLAPAAA 2817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 804 EPISQS-SQSVPQPkyisTFQIPKHPlhlsskdlaPKTSPNLPHSKP--GNVLPKSP---KIPSSHEPSVSSHQTSP--S 875
Cdd:PHA03247 2818 LPPAASpAGPLPPP----TSAQPTAP---------PPPPGPPPPSLPlgGSVAPGGDvrrRPPSRSPAAKPAAPARPpvR 2884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 876 LLLSKSRTPTTYSTQIPLPARPRPLVPQSlntfsntlssstspsstvatsiPGEPLPSPFTPTLTSLLPTARRWHQQDPL 955
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQA----------------------PPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2208424302 956 LGPKS-TSTLPEAITLHLLPEKLHLLSESVEESKFVESLNPP 996
Cdd:PHA03247 2943 LAPTTdPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
283-481 |
4.19e-06 |
|
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];
Pssm-ID: 225187 [Multi-domain] Cd Length: 399 Bit Score: 50.72 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNiWKAEGSIQATVQNIHSAKNYVSRmeADGWTDI 362
Cdd:COG2304 39 NLTLAIDTSGSMTGALLELAKSAAIELVNGLNPGDLLSIVTFAGSAD-VLIPPTGATNKESITAAIDQSLQ--AGGATAV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 363 naALLAAASVLNHSnqepgKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLRRLS 442
Cdd:COG2304 116 --EASLSLAVELAA-----KALPRGTLNRILLLTDGENNLGLVDPSRLSALAKLAAGKGIVLDTLGLGDDVNEDELTGIA 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 2208424302 443 LENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDY 481
Cdd:COG2304 189 AAANGNLAFIYLSSLSEAQFVIALEKSQTVLLVIGVTDA 227
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
690-905 |
1.78e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 427171 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 690 NSLTTSVQPKPQIPGQDS-STLALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPgiTSLVNSGTYILPLNPVSP-SQPK 767
Cdd:pfam03154 141 NRSTSPSIPSPQDNESDSdSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA--TAGPTPSAPSVPPQGSPAtSQPP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 768 GGTMKHFNSFSPFKLPASSDAHPTPDTPSYLQPVSQE--PISQSSQSVPQPKYISTFQIPKHPLHLSskdlapktSPNLP 845
Cdd:pfam03154 219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPppPSQVSPQPLPQPSLHGQMPPMPHSLQTG--------PSHMQ 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 846 HSKPGNVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARPRPLVPQSL 905
Cdd:pfam03154 291 HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
694-906 |
1.94e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 411408 [Multi-domain] Cd Length: 557 Bit Score: 42.45 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 694 TSVQPKPQIPGQDSST-LALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPGITSlvnsgtyilPLNPVSPSQPKGGTMK 772
Cdd:NF033839 297 PGMQPSPQPEKKEVKPePETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK---------PEVKPQPEKPKPEVKP 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 773 HFNSFSPfklpassDAHPTPDTPSYL---QPVSQEPISQSSQSVPQPKYISTFQIPKHPLHLSSKDLAPKTSPNLPHSKP 849
Cdd:NF033839 368 QPEKPKP-------EVKPQPETPKPEvkpQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKP 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2208424302 850 G-NVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARP-----RPLVPQSLN 906
Cdd:NF033839 441 EvKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPqaddkKPSTPNNLS 503
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| vWA_interalpha_trypsin_inhibitor |
cd01461 |
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
280-464 |
5.44e-64 |
|
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.
Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 214.39 E-value: 5.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 280 LEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNIWKAeGSIQATVQNIHSAKNYVSRMEADGW 359
Cdd:cd01461 1 LPKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSP-SSVSATAENVAAAIEYVNRLQALGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 360 TDINAALLAAASVLNHSNqepgkgrgvGQIPLIMFLTDGEptagETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLR 439
Cdd:cd01461 80 TNMNDALEAALELLNSSP---------GSVPQIILLTDGE----VTNESQILKNVREALSGRIRLFTFGIGSDVNTYLLE 146
|
170 180
....*....|....*....|....*
gi 2208424302 440 RLSLENQGEARRIYEDADAALQLEG 464
Cdd:cd01461 147 RLAREGRGIARRIYETDDIESQLLR 171
|
|
| ITI_HC_C |
pfam06668 |
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal ... |
1087-1268 |
3.28e-54 |
|
Inter-alpha-trypsin inhibitor heavy chain C-terminus; This family represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact in vitro and in vivo with hyaluronic acid, which promotes the stability of the extra-cellular matrix. All family members contain the pfam00092 domain.
Pssm-ID: 429061 Cd Length: 189 Bit Score: 187.41 E-value: 3.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1087 KAGLHVSGQLLGAPSRPSHKDQTRTYFHIITITSdKPRAYNITISRSSISV-QGESTLSLSWNQRALVKKPHLELHVASA 1165
Cdd:pfam06668 1 GSGVTVNGQLIGAKKPPGSHKKLRTYFGTIGIVV-KPLGVKIEVTPEKITLkDGEKRLVLSWSDTASVKQPGLTVSVVKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 1166 ALLTVRLGPHLNFFILRHQYRHPSTLQLPHLGFYVANGSGLSPSARGLMGQFQY-TDIRLVTGPSGS------YLQKHHG 1238
Cdd:pfam06668 80 SNVTVTIGDGISFVVLLHRVWKPHPYQVDHLGFYIVNSKGLSPSVHGLLGQFLHePEVEVTDVRPGSdpekpdATMKVKG 159
|
170 180 190
....*....|....*....|....*....|
gi 2208424302 1239 LDVPVVLGKRLLKESPRLLPRWTSCWIVKR 1268
Cdd:pfam06668 160 HKLPVTRGWQKDYRGDRKHGTNVPCWFVHN 189
|
|
| VIT |
smart00609 |
Vault protein Inter-alpha-Trypsin domain; |
40-150 |
3.02e-46 |
|
Vault protein Inter-alpha-Trypsin domain;
Pssm-ID: 197803 [Multi-domain] Cd Length: 130 Bit Score: 162.14 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:smart00609 20 LKVNSKVTSRFAHTVVTSRVVNRAVPAQEVTFDVELPKTAFISNFAMTIDGKTYVGEIKEKEVAQKQYEKAVSQGKTAGL 99
|
90 100 110
....*....|....*....|....*....|.
gi 2208424302 120 VGIRDRESENFRISTMLAAGTKATFALAYEE 150
Cdd:smart00609 100 VRASGRSMEQFTVSVNVAPGSKVTFELTYEE 130
|
|
| marine_srt_targ |
TIGR03788 |
marine proteobacterial sortase target protein; Members of this protein family are restricted ... |
51-630 |
2.74e-38 |
|
marine proteobacterial sortase target protein; Members of this protein family are restricted to the Proteobacteria. Each contains a C-terminal sortase-recognition motif, transmembrane domain, and basic residues cluster at the the C-terminus, and is encoded adjacent to a sortase gene. This protein is frequently the only sortase target in its genome, which is as unusual its occurrence in Gram-negative rather than Gram-positive genomes. Many bacteria with this system are marine. In addition to the LPXTG signal, members carry a vault protein inter-alpha-trypsin inhibitor domain (pfam08487) and a von Willebrand factor type A domain (pfam00092).
Pssm-ID: 274782 [Multi-domain] Cd Length: 596 Bit Score: 152.54 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 51 ANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAHVgirDRESENF 130
Cdd:TIGR03788 14 ARTEVTQTFRNPSQFWVEGRYVFPLPENAAVDSLTMHIGERVIVGQIMPKAAARAIYEQAKAEGKKAALV---EQQRPNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 131 RISTM--LAAGTKATFALAYEELLQRHQG----RYQLVVGLR--PGQLVrklNVEITVSERT-GIAYVHIP-PLRTSQVC 200
Cdd:TIGR03788 91 FTNKVanIGPGETVVVTIEYQQPVSYSSGtfslRLPLTVTPRyiPGSTV---NTVTDVNNSGwAIPTTQVPdADKISAPR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 201 TnnqTSEGDLPPSTR------IQRGETCVHITfSPT------LRDQSAFSSS----GIMADFTihYDVSMEDIIGDV--- 261
Cdd:TIGR03788 168 V---LDPDDDAPSSQasinvdLNAGLPLDSIT-SPShpiqieQQGQSGYTISlaqgQVIADRD--FVLTWRPAQGEApsa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 262 ----QVYGGYfiHY--------FAPRGLQPLEKNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN 329
Cdd:TIGR03788 242 alfrEQIGGE--RYglamvmppTEAAVAQVLPRELVFVIDTSGSMAGESIEQAKSALLLALDQLRPGDRFNIIQFDSDVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 330 -IWKaeGSIQATVQNIHSAKNYVSRMEADGWTDInaALLAAASVLNHSNQEPGKGRGVgqipliMFLTDGEpTAGEttpS 408
Cdd:TIGR03788 320 lLFP--VPVPATAHNLARARQFVAGLQADGGTEM--AGALSAALRDDGPESSGALRQV------VFLTDGA-VGNE---D 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 409 VILSNIRQALAHRvSLFSLAFGDDADFSLLRRLSLENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDYLGGWVGA 488
Cdd:TIGR03788 386 ALFQLIRTKLGDS-RLFTVGIGSAPNSYFMRKAAQFGRGSFTFIGSTDEVQRKMSQLFAKLEQPALTDIALTFDNGNAAD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 489 SSRAHFPNYFHGSELVVAGKVQPGEQELGIhlAARGPNGHLLVAHHSEEASNSSQkafgcpgkpalnvthfIHRLWAYVT 568
Cdd:TIGR03788 465 VYPSPIPDLYRGEPLQIAIKLQQAAGELQL--TGRTGSQPWSQQLDLDSAAPGKG----------------IDKLWARRK 526
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2208424302 569 IGELLKARFQAKDTTtrrllAAKA--LNLSLEYNFVTPLTSLVVVHLEKTNEEAMTQPSTTAKT 630
Cdd:TIGR03788 527 IDSLEDSLRYGANEE-----KVKDqvTALALNHHLVSPFTSFVAVEETPIRPAAESLNSEASPN 585
|
|
| VIT |
pfam08487 |
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one ... |
40-148 |
2.04e-32 |
|
Vault protein inter-alpha-trypsin domain; Inter-alpha-trypsin inhibitors (ITIs) consist of one light chain and a variable set of heavy chains. ITIs play a role in extracellular matrix (ECM) stabilisation and tumor metastasis as well as in plasma protease inhibition. The vault protein inter-alpha-trypsin (VIT) domain described here is found to the N-terminus of a von Willebrand factor type A domain (pfam00092) in ITI heavy chains (ITIHs) and their precursors.
Pssm-ID: 430025 [Multi-domain] Cd Length: 111 Bit Score: 121.86 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 40 YSIRSTVVSRYANTLVTSVLFNPHDEAHEAIFDLNLPRIAFISNFTMTIDDKIYVAEIKEKHQAKKMYEKAYQQGKTAAH 119
Cdd:pfam08487 4 VSVEATITGRIARTTVTQTFVNPSSEALEAVYVFPLPEGAAVSGFTMTIGGKVIVGEVKEKEEAKKEYEEAVARGKTAGL 83
|
90 100 110
....*....|....*....|....*....|
gi 2208424302 120 VgiRDRESENFRIST-MLAAGTKATFALAY 148
Cdd:pfam08487 84 L--EQDDPDVFTTSVgNIPPGEKVTVELTY 111
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
283-458 |
7.12e-22 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 94.06 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQAS---DSFNIITFSDTVNIWKAEGSIqatvQNIHSAKNYVSRME--AD 357
Cdd:smart00327 1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIGpdgDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSykLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 358 GWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGettPSVILSNIRQALAHRVSLFSLAFGDDADFSL 437
Cdd:smart00327 77 GGTNLGAALQYALENLFSKSA--GSRRGAPKV--VILITDGESNDG---PKDLLKAAKELKRSGVKVFVVGVGNDVDEEE 149
|
170 180
....*....|....*....|.
gi 2208424302 438 LRRLSLENQGEARRIYEDADA 458
Cdd:smart00327 150 LKKLASAPGGVYVFLPELLDL 170
|
|
| vWA_subgroup |
cd01465 |
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
283-459 |
1.06e-21 |
|
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.
Pssm-ID: 238742 [Multi-domain] Cd Length: 170 Bit Score: 93.49 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTvniwkAEGSIQATVQNIHSA-KNYVSRMEADGWTD 361
Cdd:cd01465 2 NLVFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGA-----AETVLPATPVRDKAAiLAAIDRLTAGGSTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 362 InaallaaASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLRRL 441
Cdd:cd01465 77 G-------GAGIQLGYQEAQKHFVPGGVNRILLATDGDFNVGETDPDELARLVAQKRESGITLSTLGFGDNYNEDLMEAI 149
|
170
....*....|....*...
gi 2208424302 442 SLENQGEARRIYEDADAA 459
Cdd:cd01465 150 ADAGNGNTAYIDNLAEAR 167
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
283-449 |
2.59e-20 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 89.16 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQAS---DSFNIITFSDTVNIWkAEGSIQATVQNIHSAKNYVsRMEADGW 359
Cdd:cd00198 2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSASppgDRVGLVTFGSNARVV-LPLTTDTDKADLLEAIDAL-KKGLGGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 360 TDInaallaaASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQAlahRVSLFSLAFGDDADFSLLR 439
Cdd:cd00198 80 TNI-------GAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKL---GITVYTIGIGDDANEDELK 149
|
170
....*....|
gi 2208424302 440 RLSLENQGEA 449
Cdd:cd00198 150 EIADKTTGGA 159
|
|
| VWA |
pfam00092 |
von Willebrand factor type A domain; |
283-468 |
6.56e-16 |
|
von Willebrand factor type A domain;
Pssm-ID: 425461 [Multi-domain] Cd Length: 174 Bit Score: 76.93 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQA---SDSFNIITFSDTVNIWkaegsIQ-ATVQNIHSAKNYVSRME--A 356
Cdd:pfam00092 1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDIgpdGTRVGLVQYSSDVRTE-----FPlNDYSSKEELLSAVDNLRylG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 357 DGWTDINAALLAAASVLNHSNQepGKGRGVGQIplIMFLTDGEPTAGEttpsvILSNIRQALAHRVSLFSLAFGdDADFS 436
Cdd:pfam00092 76 GGTTNTGKALKYALENLFSSAA--GARPGAPKV--VVLLTDGRSQDGD-----PEEVARELKSAGVTVFAVGVG-NADDE 145
|
170 180 190
....*....|....*....|....*....|..
gi 2208424302 437 LLRRLSLENqgEARRIYEDADAAlQLEGLYAE 468
Cdd:pfam00092 146 ELRKIASEP--GEGHVFTVSDFE-ALEDLQDQ 174
|
|
| vWA_VGCC_like |
cd01463 |
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ... |
282-447 |
4.61e-14 |
|
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.
Pssm-ID: 238740 [Multi-domain] Cd Length: 190 Bit Score: 72.04 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 282 KNVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVN--IWKAEGS-IQATVQNIHSAKNYVSRMEADG 358
Cdd:cd01463 14 KDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNpvVPCFNDTlVQATTSNKKVLKEALDMLEAKG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 359 WTDINAALLAAASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPtagETTPSVI-LSNIRQALAHRVSLFSLAFGDDA-DFS 436
Cdd:cd01463 94 IANYTKALEFAFSLLLKNLQSNHSGSRSQCNQAIMLITDGVP---ENYKEIFdKYNWDKNSEIPVRVFTYLIGREVtDRR 170
|
170
....*....|.
gi 2208424302 437 LLRRLSLENQG 447
Cdd:cd01463 171 EIQWMACENKG 181
|
|
| vWA_C3HC4_type |
cd01466 |
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
284-400 |
5.57e-11 |
|
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.
Pssm-ID: 238743 [Multi-domain] Cd Length: 155 Bit Score: 62.02 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 284 VVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNiwKAEGSIQATVQNIHSAKNYVSRMEADGWTDIN 363
Cdd:cd01466 3 LVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAK--RLSPLRRMTAKGKRSAKRVVDGLQAGGGTNVV 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2208424302 364 AALLAAASVLnhsnqepGKGRGVGQIPLIMFLTDGEP 400
Cdd:cd01466 81 GGLKKALKVL-------GDRRQKNPVASIMLLSDGQD 110
|
|
| VWA_3 |
pfam13768 |
von Willebrand factor type A domain; |
282-450 |
1.57e-07 |
|
von Willebrand factor type A domain;
Pssm-ID: 372716 [Multi-domain] Cd Length: 155 Bit Score: 52.01 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 282 KNVVFVIDVSGSMFGTKLQQtKKAMDTILSDLQASDSFNIITFSDTVNIWKAEGsiqatvQNIHSAknyvSRMEADGWTD 361
Cdd:pfam13768 1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGW------RVVSPR----SLQEAFQFIK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 362 INAALLAAASVLNHSNQEPGKGRGVGQIPLIMFLTDGEPTAGETTpsvILSNIRQALAHrVSLFSLAFGDDADFSLLRRL 441
Cdd:pfam13768 70 TLQPPLGGSDLLGALKEAVRAPASPGYIRHVLLLTDGSPMQGETR---VSDLISRAPGK-IRFFAYGLGASISAPMLQLL 145
|
....*....
gi 2208424302 442 SLENQGEAR 450
Cdd:pfam13768 146 AEASNGTYE 154
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
655-996 |
1.80e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 655 KVFSKSRPTKPTSTIIAPTMKvtsskelgALGWWSNSLTTSVQPKPQ------IPGQDSSTLALPTLKMKPLAHVPSNSN 728
Cdd:PHA03247 2666 RARRLGRAAQASSPPQRPRRR--------AARPTVGSLTSLADPPPPpptpepAPHALVSATPLPPGPAAARQASPALPA 2737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 729 DPLPRKPSTSTHQNPGITSLVNSGTYILPLNPVSPSQPKGGTMKHFNSFSPFKLPASSDAHPTPDTPS-----YLQPVSQ 803
Cdd:PHA03247 2738 APAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAdppaaVLAPAAA 2817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 804 EPISQS-SQSVPQPkyisTFQIPKHPlhlsskdlaPKTSPNLPHSKP--GNVLPKSP---KIPSSHEPSVSSHQTSP--S 875
Cdd:PHA03247 2818 LPPAASpAGPLPPP----TSAQPTAP---------PPPPGPPPPSLPlgGSVAPGGDvrrRPPSRSPAAKPAAPARPpvR 2884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 876 LLLSKSRTPTTYSTQIPLPARPRPLVPQSlntfsntlssstspsstvatsiPGEPLPSPFTPTLTSLLPTARRWHQQDPL 955
Cdd:PHA03247 2885 RLARPAVSRSTESFALPPDQPERPPQPQA----------------------PPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2208424302 956 LGPKS-TSTLPEAITLHLLPEKLHLLSESVEESKFVESLNPP 996
Cdd:PHA03247 2943 LAPTTdPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
628-949 |
4.11e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.94 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 628 AKTSTVTPSSSNRLGLGTGTAQPASvlkvfsksrPTKPTSTIIAPTMKVTSSKELgalgwwSNSLTTSVQPKPQIPGqDS 707
Cdd:PHA03247 2744 VPAGPATPGGPARPARPPTTAGPPA---------PAPPAAPAAGPPRRLTRPAVA------SLSESRESLPSPWDPA-DP 2807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 708 STLALPTLKMKPLAHVPSNsndPLPrKPSTSTHQNPGitslvnsgtyiLPLNPVSPSQPKGGTMKHFNSFSpfKLPASSD 787
Cdd:PHA03247 2808 PAAVLAPAAALPPAASPAG---PLP-PPTSAQPTAPP-----------PPPGPPPPSLPLGGSVAPGGDVR--RRPPSRS 2870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 788 AHPTPDTPSY--LQPVSQEPISQSSQSVPQPkyistfqiPKHPLHLSSKDLAPKTSPNLPHSKPGNVLPKSPKIPSSHEP 865
Cdd:PHA03247 2871 PAAKPAAPARppVRRLARPAVSRSTESFALP--------PDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 866 SVSSHQTSPSLLLSKSRTPTTYSTQIP-LPARPRPLVPQSLntfsntlssstspsstvatsiPGEPLPSPFTPTLTSL-L 943
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPgRVAVPRFRVPQPA---------------------PSREAPASSTPPLTGHsL 3001
|
....*.
gi 2208424302 944 PTARRW 949
Cdd:PHA03247 3002 SRVSSW 3007
|
|
| vWA_subfamily |
cd01464 |
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
284-442 |
6.71e-07 |
|
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.
Pssm-ID: 238741 [Multi-domain] Cd Length: 176 Bit Score: 50.80 E-value: 6.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 284 VVFVIDVSGSMFGTKLQQTKKAMDTILSDLQ----ASDS--FNIITFsdtvniwkaeGSIQATVQNIHSAKN-YVSRMEA 356
Cdd:cd01464 6 IYLLLDTSGSMAGEPIEALNQGLQMLQSELRqdpyALESveISVITF----------DSAARVIVPLTPLESfQPPRLTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 357 DGWTDINAALLAAASVLNHSNQEPgKGRGVGQI-PLIMFLTDGEPTaGETTPSVilSNIRQALAHRVSLFSLAFGDDADF 435
Cdd:cd01464 76 SGGTSMGAALELALDCIDRRVQRY-RADQKGDWrPWVFLLTDGEPT-DDLTAAI--ERIKEARDSKGRIVACAVGPKADL 151
|
....*..
gi 2208424302 436 SLLRRLS 442
Cdd:cd01464 152 DTLKQIT 158
|
|
| VWA_2 |
pfam13519 |
von Willebrand factor type A domain; |
284-330 |
1.08e-06 |
|
von Willebrand factor type A domain;
Pssm-ID: 433277 [Multi-domain] Cd Length: 103 Bit Score: 48.44 E-value: 1.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2208424302 284 VVFVIDVSGSM-----FGTKLQQTKKAMDTILSDLqASDSFNIITFSDTVNI 330
Cdd:pfam13519 1 LVFVLDTSGSMrngdyLPTRLEAAKDAVLALLKSL-PGDRVGLVTFGDGPEV 51
|
|
| vWA_ywmD_type |
cd01456 |
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
280-434 |
2.22e-06 |
|
VWA ywmD type:Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Not much is known about the function of the members of this subgroup. All members of this subgroup however have a conserved MIDAS motif.
Pssm-ID: 238733 [Multi-domain] Cd Length: 206 Bit Score: 49.74 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 280 LEKNVVFVIDVSGSM------FGTKLQQTKKAMDTILSDLQASDSFNIITFS---DTVNIWKAEGSIQATVQNIH----- 345
Cdd:cd01456 19 LPPNVAIVLDNSGSMrevdggGETRLDNAKAALDETANALPDGTRLGLWTFSgdgDNPLDVRVLVPKGCLTAPVNgfpsa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 346 ---SAKNYVSRM-EADGWTDINAALlaaasvlnhsnQEPGKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNI-RQALAH 420
Cdd:cd01456 99 qrsALDAALNSLqTPTGWTPLAAAL-----------AEAAAYVDPGRVNVVVLITDGEDTCGPDPCEVARELAkRRTPAP 167
|
170
....*....|....
gi 2208424302 421 RVSLFSLAFGDDAD 434
Cdd:cd01456 168 PIKVNVIDFGGDAD 181
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
283-481 |
4.19e-06 |
|
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];
Pssm-ID: 225187 [Multi-domain] Cd Length: 399 Bit Score: 50.72 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDLQASDSFNIITFSDTVNiWKAEGSIQATVQNIHSAKNYVSRmeADGWTDI 362
Cdd:COG2304 39 NLTLAIDTSGSMTGALLELAKSAAIELVNGLNPGDLLSIVTFAGSAD-VLIPPTGATNKESITAAIDQSLQ--AGGATAV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 363 naALLAAASVLNHSnqepgKGRGVGQIPLIMFLTDGEPTAGETTPSVILSNIRQALAHRVSLFSLAFGDDADFSLLRRLS 442
Cdd:COG2304 116 --EASLSLAVELAA-----KALPRGTLNRILLLTDGENNLGLVDPSRLSALAKLAAGKGIVLDTLGLGDDVNEDELTGIA 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 2208424302 443 LENQGEARRIYEDADAALQLEGLYAEISRPLLADVHLDY 481
Cdd:COG2304 189 AAANGNLAFIYLSSLSEAQFVIALEKSQTVLLVIGVTDA 227
|
|
| ChlD |
COG1240 |
Mg-chelatase subunit ChlD [Coenzyme transport and metabolism]; |
284-407 |
8.84e-06 |
|
Mg-chelatase subunit ChlD [Coenzyme transport and metabolism];
Pssm-ID: 224161 [Multi-domain] Cd Length: 261 Bit Score: 48.90 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 284 VVFVIDVSGSMFG-TKLQQTKKAMDTILSD-LQASDSFNIITFSDTvniwKAEGSIQATvQNIHSAKNYVSRMEADGWTD 361
Cdd:COG1240 81 IVFVVDASGSMAArRRMAAAKGAALSLLRDaYQRRDKVAVIAFRGE----KAELLLPPT-SSVELAERALERLPTGGKTP 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2208424302 362 INAALLAAASVLNHSnqepgKGRGVGQIPLIMFLTDGEPTAGETTP 407
Cdd:COG1240 156 LADALRQAYEVLARE-----KRRGPDRRPVMVVITDGRANVPIPLG 196
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
690-905 |
1.78e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 427171 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 690 NSLTTSVQPKPQIPGQDS-STLALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPgiTSLVNSGTYILPLNPVSP-SQPK 767
Cdd:pfam03154 141 NRSTSPSIPSPQDNESDSdSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA--TAGPTPSAPSVPPQGSPAtSQPP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 768 GGTMKHFNSFSPFKLPASSDAHPTPDTPSYLQPVSQE--PISQSSQSVPQPKYISTFQIPKHPLHLSskdlapktSPNLP 845
Cdd:pfam03154 219 NQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPppPSQVSPQPLPQPSLHGQMPPMPHSLQTG--------PSHMQ 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 846 HSKPGNVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARPRPLVPQSL 905
Cdd:pfam03154 291 HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
699-945 |
2.44e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 45.45 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 699 KPQIPGQDSSTLALPTLKMKPLAHVPSNSNDPL----PRKPSTsthqnpgitslvnsgtyilPLNPVSPSQPKGGtmkhf 774
Cdd:PTZ00449 596 KPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPEspksPKRPPP-------------------PQRPSSPERPEGP----- 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 775 nsfspfKLPASSDAHPTPDTPsyLQPVSQEPISQS-SQSVPQPKYISTFQIPKHPLHLSSKDLAPKTsPNLPHSKPGNVL 853
Cdd:PTZ00449 652 ------KIIKSPKPPKSPKPP--FDPKFKEKFYDDyLDAAAKSKETKTTVVLDESFESILKETLPET-PGTPFTTPRPLP 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 854 PKSPKIPSS-HEP--SVSSHQTSPSLLLSKSRTPTTYSTQIPLPARPRPLVPQSLNTFSNTLSSSTspsstvatsiPGEP 930
Cdd:PTZ00449 723 PKLPRDEEFpFEPigDPDAEQPDDIEFFTPPEEERTFFHETPADTPLPDILAEEFKEEDIHAETGE----------PDEA 792
|
250
....*....|....*
gi 2208424302 931 LPSPFTPTLTSLLPT 945
Cdd:PTZ00449 793 MKRPDSPSEHEDKPP 807
|
|
| vWFA_subfamily_ECM |
cd01450 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
283-442 |
2.55e-04 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains
Pssm-ID: 238727 [Multi-domain] Cd Length: 161 Bit Score: 43.05 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 283 NVVFVIDVSGSMFGTKLQQTKKAMDTILSDL-QASDS--FNIITFSDTVNIW------KAEGSIQATVQNIHSaknyvsr 353
Cdd:cd01450 2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdIGPDKtrVGLVQYSDDVRVEfslndyKSKDDLLKAVKNLKY------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 354 MEADGwTDINAALLAaasVLNHSNQEPGKGRGVGQIplIMFLTDGEPTAGeTTPSVILSNIRQalaHRVSLFSLAFGdDA 433
Cdd:cd01450 75 LGGGG-TNTGKALQY---ALEQLFSESNARENVPKV--IIVLTDGRSDDG-GDPKEAAAKLKD---EGIKVFVVGVG-PA 143
|
....*....
gi 2208424302 434 DFSLLRRLS 442
Cdd:cd01450 144 DEEELREIA 152
|
|
| PLN03209 |
PLN03209 |
translocon at the inner envelope of chloroplast subunit 62; Provisional |
693-937 |
2.79e-04 |
|
translocon at the inner envelope of chloroplast subunit 62; Provisional
Pssm-ID: 178748 [Multi-domain] Cd Length: 576 Bit Score: 44.92 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 693 TTSVQPKPQIPGQDSSTLALPTLKMKPLAhvPSNSNDPLprKPSTSThqnpgitslvnsgtyilplnpvSPSQPKGGTMK 772
Cdd:PLN03209 344 TKPVTPEAPSPPIEEEPPQPKAVVPRPLS--PYTAYEDL--KPPTSP----------------------IPTPPSSSPAS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 773 HfNSFSPFKLPASSDAHPTPDTPSylqpvsqepisqssqSVPQPKYISTFQIPKHPL--HLSSKDLAPKTSPN------- 843
Cdd:PLN03209 398 S-KSVDAVAKPAEPDVVPSPGSAS---------------NVPEVEPAQVEAKKTRPLspYARYEDLKPPTSPSptaptgv 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 844 LPHSKPGNVLPKSPKIP-------SSHEPSVSSHQTSPSLLLSKSRTPTTystqiPLPARPRPLVPQSLNTFSNTLSSST 916
Cdd:PLN03209 462 SPSVSSTSSVPAVPDTApataatdAAAPPPANMRPLSPYAVYDDLKPPTS-----PSPAAPVGKVAPSSTNEVVKVGNSA 536
|
250 260
....*....|....*....|.
gi 2208424302 917 SPSSTVATSIPGEPLPSPFTP 937
Cdd:PLN03209 537 PPTALADEQHHAQPKPRPLSP 557
|
|
| vWA_Magnesium_chelatase |
cd01451 |
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). ... |
284-403 |
5.57e-04 |
|
Magnesium chelatase: Mg-chelatase catalyses the insertion of Mg into protoporphyrin IX (Proto). In chlorophyll biosynthesis, insertion of Mg2+ into protoporphyrin IX is catalysed by magnesium chelatase in an ATP-dependent reaction. Magnesium chelatase is a three sub-unit (BchI, BchD and BchH) enzyme with a novel arrangement of domains: the C-terminal helical domain is located behind the nucleotide binding site. The BchD domain contains a AAA domain at its N-terminus and a VWA domain at its C-terminus. The VWA domain has been speculated to be involved in mediating protein-protein interactions.
Pssm-ID: 238728 [Multi-domain] Cd Length: 178 Bit Score: 42.26 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 284 VVFVIDVSGSM-FGTKLQQTKKAMDTILSD-LQASDSFNIITFSDTvniwkaegsiQATV-----QNIHSAKNYVSRMEA 356
Cdd:cd01451 3 VIFVVDASGSMaARHRMAAAKGAVLSLLRDaYQRRDKVALIAFRGT----------EAEVllpptRSVELAKRRLARLPT 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2208424302 357 DGWTDINAALLAAASVLNHSnqepgkGRGVGQIPLIMFLTDGEPTAG 403
Cdd:cd01451 73 GGGTPLAAGLLAAYELAAEQ------ARDPGQRPLIVVITDGRANVG 113
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
579-864 |
5.65e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 436069 [Multi-domain] Cd Length: 480 Bit Score: 44.14 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 579 AKDTTTRRLLAAKALN--LSLEYNFVTPLTSLVVVHLEKTNEEAmtqPSTTAKTSTVTPSSSNrLGLGTGTAQPASVLKV 656
Cdd:pfam17823 102 AADGAASRALAAAASSspSSAAQSAPTTIAGLPSLASSAPMAAA---PRTNAASNAPTAAASS-TAAASGAPTTAASSAP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 657 fSKSRPTKPTSTIIAPTMKVTSSKELGALGwwsNSLTTSVQPKPQIPGQDSSTLALPTLKMKPLAHV--PSNSNDPLPRK 734
Cdd:pfam17823 178 -ATLTPASGISTAATATGHPAAGTALAAVG---NSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAagTINTGDPHARR 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 735 PSTSTHQNPGITSlvnsgtyilpLNPVSPSQPKG-GTMKHFNSFSPFklpASSDAHPTPD-TPSYLQPVSQEPISQSSQS 812
Cdd:pfam17823 254 LSPAKHMPSDTSA----------RNPAAPSGAQAqGLIIQVSTDQPV---HNTAGEPTPSpSNTTLEPNTPKSVASTNLA 320
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2208424302 813 VPQPKYISTFQIPKHPLHLSSKDLAPKTSPNLPHSKPGNVLPKS----PKIPSSHE 864
Cdd:pfam17823 321 VVTTTKAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQgaagPGILLAPD 376
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
694-906 |
1.94e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 411408 [Multi-domain] Cd Length: 557 Bit Score: 42.45 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 694 TSVQPKPQIPGQDSST-LALPTLKMKPLAHVPSNSNDPLPRKPSTSTHQNPGITSlvnsgtyilPLNPVSPSQPKGGTMK 772
Cdd:NF033839 297 PGMQPSPQPEKKEVKPePETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK---------PEVKPQPEKPKPEVKP 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 773 HFNSFSPfklpassDAHPTPDTPSYL---QPVSQEPISQSSQSVPQPKYISTFQIPKHPLHLSSKDLAPKTSPNLPHSKP 849
Cdd:NF033839 368 QPEKPKP-------EVKPQPETPKPEvkpQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKP 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2208424302 850 G-NVLPKSPKIPSSHEPSVSSHQTSPSLLLSKSRTPTTYSTQIPLPARP-----RPLVPQSLN 906
Cdd:NF033839 441 EvKPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPDNSKPqaddkKPSTPNNLS 503
|
|
| TerY |
COG4245 |
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
284-442 |
9.10e-03 |
|
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
Pssm-ID: 226696 [Multi-domain] Cd Length: 207 Bit Score: 38.97 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 284 VVFVIDVSGSMFGTKLQQTKKAMDTILSDLQA------SDSFNIITFSDTVNiwkaegsiqaTVQNIHSAKN-YVSRMEA 356
Cdd:COG4245 6 CYLLLDTSGSMIGEPIEALNAGLQMMIDTLKQdpyaleRVELSIVTFGGPAR----------VIQPFTDAANfNPPILTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 357 DGWTDINAALLAAASVLNHSNQEPgKGRGVGQI-PLIMFLTDGEPTaGETTPSVILSNIRQALAHRVSLFSLAfGDDADF 435
Cdd:COG4245 76 QGGTPLGAALTLALDMIEERKRKY-DANGKGDYrPWVFLITDGEPT-DDWQAGAALVFQGERRAKSVAAFSVG-VQGADN 152
|
....*..
gi 2208424302 436 SLLRRLS 442
Cdd:COG4245 153 KTLNQIT 159
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
626-971 |
9.79e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 40.28 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 626 TTAKTSTVTPSSSNrlglGTGTAQPAsvlkVFSKSrptkPTSTIIAPTMKVTsskelgalGWWSNSLTTsvqpkpqipGQ 705
Cdd:pfam05109 398 TAPKTLIITRTATN----ATTTTHKV----IFSKA----PESTTTSPTLNTT--------GFAAPNTTT---------GL 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 706 DSSTlalptlkmkplaHVPSNSNDPLPRKPSTSTHQnpgITSLVNSGTY--ILPLNPvSPSQPKGGTmkhfNSFSP-FKL 782
Cdd:pfam05109 449 PSST------------HVPTNLTAPASTGPTVSTAD---VTSPTPAGTTsgASPVTP-SPSPRDNGT----ESKAPdMTS 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 783 PASSDAHPTPDTPSYLQPVSQEPISQSSQSVPQPKYISTFQIPKhPLHLSSKDLAPKTSPNLPHSKPGNVLPKSP-KIPS 861
Cdd:pfam05109 509 PTSAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTPT-PNATSPTPAVTTPTPNATIPTLGKTSPTSAvTTPT 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2208424302 862 SHEPSVSSHQTSPSLLLSKSRTPTTYSTqiPLPARPRPLVPQSLNTFSNTLSSSTSPSSTVATSIPGEPLPSPFTPTLTS 941
Cdd:pfam05109 588 PNATSPTVGETSPQANTTNHTLGGTSST--PVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTS 665
|
330 340 350
....*....|....*....|....*....|
gi 2208424302 942 LLPTARRWHqqdPLLGPKSTSTLPEAITLH 971
Cdd:pfam05109 666 HMPLLTSAH---PTGGENITQVTPASTSTH 692
|
|
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