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Conserved domains on  [gi|124504959|ref|XP_001351221|]
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circumsporozoite- and TRAP-related protein [Plasmodium falciparum 3D7]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 304-494 7.58e-95

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


:

Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 304.63  E-value: 7.58e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  304 YDLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELKDKYG 383
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  384 YGGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGNETSKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAG 463
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  464 C-TENEECLRVIKCEWNDLTNITKILTDKICN 494
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 848-1039 1.01e-92

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


:

Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 298.46  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  848 YDLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIHDLKKYYK 927
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  928 SGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLYKKENVKLLLIGIGGPTIHKLRLLGG 1007
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959 1008 CDKSDGDCPYVVKAEWNNLKYTSNLIIDKICH 1039
Cdd:cd01473   161 CDINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 568-757 4.25e-90

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


:

Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 291.14  E-value: 4.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  568 YDITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLKRDYR 647
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  648 SGKKTYIIQALQYALTYYSKLSN-RKEAPKVTMLFTDGNDSYESEKGLQDIALLYRKENVKLLVVGVSTASENKLKMLVG 726
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNrRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  727 C-APNVVCPFVIKTEWGLLKNVSEVFVKKICD 757
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 84-274 6.39e-89

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


:

Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 287.68  E-value: 6.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   84 YDLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLKKDYY 163
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDGNENSASNKQLLEMGLTYRRERVKLLVLGVAAAEDNKLKLIAG 243
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  244 C-EENTNCPYSMKAEWETINDITKRLTNKICH 274
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1066-1255 3.52e-68

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.


The actual alignment was detected with superfamily member cd01473:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 192  Bit Score: 228.36  E-value: 3.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1066 FDLTYIEVPTLNSTYT-WRSDFMDCSKNIMNSLVIDKNKVHVSLIISLEKKSVHQGFDDVNSYNKNELIKTLGKLENSTV 1144
Cdd:cd01473     1 YDLTLILDESASIGYSnWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1145 -LNKTNILDSLVYGIQQSFGKGNREN-APKVTMLLTNSNSDISDEKALQDIYLNYKEKSIKLLIIGIGITNTGKLFNAGG 1222
Cdd:cd01473    81 sGGETYIVEALKYGLKNYTKHGNRRKdAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124504959 1223 CNMNGDNCPHVYASKsFSYIGGVDTFLEVNKCD 1255
Cdd:cd01473   161 CDINNDNCPNVIKTE-WNNLNGISKFLTDKICD 192
VWA pfam00092
von Willebrand factor type A domain;
1303-1460 5.40e-21

von Willebrand factor type A domain;


:

Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.34  E-value: 5.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEInkLPISYSK 1382
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFE-KVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDN--LRYLGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1383 KKDIAKSLKYVRTKVFKKSE---TNRKKLIIMLVEGKSNsnMNDLRKEVGLLKVNNIDFFAYAIDNIDETEYKILGDCEG 1459
Cdd:pfam00092   78 TTNTGKALKYALENLFSSAAgarPGAPKVVVLLTDGRSQ--DGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155


                   .
gi 124504959  1460 S 1460
Cdd:pfam00092  156 E 156
PspC_subgroup_2 super family cl41463
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 1.05e-10

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.


The actual alignment was detected with superfamily member NF033839:

Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 66.72  E-value: 1.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  359 EKPKPEVKPQP-EKPKPEVKPQP-ETPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPEK 415
Cornifin super family cl25524
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 752-837 1.19e-09

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


The actual alignment was detected with superfamily member pfam02389:

Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 58.53  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   752 VKKICDNGVVLP-------PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPS 824
Cdd:pfam02389   21 TKEPCHSKVPEPcnpkvpePCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHPKAPEPCHPK 100

                           90
                   ....*....|...
gi 124504959   825 ESTPGSPSESTPC 837
Cdd:pfam02389  101 VPEPCYPKAPEPC 113
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1597-1646 1.94e-09

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.29  E-value: 1.94e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1597 CGDFGEWSECSATCGEGIRVRNR----DNSLDNDDKCKLfNSTEMEACNIQECD 1646
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRsccsPPPQNGGGPCTG-EDVETRACNEQPCP 53
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1806-1863 1.73e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 1.73e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959   1806 CGDWSDWSECDRTCNVGVRIRHFISHMFDmvGDEDEKECLEyyNKVETQDClHLPPCD 1863
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPP--PQNGGGPCTG--EDVETRAC-NEQPCP 53
TSP1_spondin super family cl46269
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1654-1703 4.08e-07

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


The actual alignment was detected with superfamily member pfam19028:

Pssm-ID: 480609  Cd Length: 52  Bit Score: 48.43  E-value: 4.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 124504959  1654 CEdIGEWSDWSSCSKTCGYSTRSRTFTIL--PEYIGEypNCKifERSETEVC 1703
Cdd:pfam19028    1 CV-VSEWSEWSECSVTCGGGVQTRTRTVIvePQNGGR--PCP--ELLERRPC 47
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1939-2002 4.97e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


:

Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 4.97e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1939 CNEWEEWGDCSSTCGEGsfkIRKRKEPLELIPASQDingniGLTCAQQNikvEEREACIVPACE 2002
Cdd:smart00209    1 WSEWSEWSPCSVTCGGG---VQTRTRSCCSPPPQNG-----GGPCTGED---VETRACNEQPCP 53
 
Name Accession Description Interval E-value
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 304-494 7.58e-95

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 304.63  E-value: 7.58e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  304 YDLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELKDKYG 383
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  384 YGGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGNETSKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAG 463
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  464 C-TENEECLRVIKCEWNDLTNITKILTDKICN 494
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 848-1039 1.01e-92

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 298.46  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  848 YDLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIHDLKKYYK 927
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  928 SGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLYKKENVKLLLIGIGGPTIHKLRLLGG 1007
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959 1008 CDKSDGDCPYVVKAEWNNLKYTSNLIIDKICH 1039
Cdd:cd01473   161 CDINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 568-757 4.25e-90

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 291.14  E-value: 4.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  568 YDITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLKRDYR 647
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  648 SGKKTYIIQALQYALTYYSKLSN-RKEAPKVTMLFTDGNDSYESEKGLQDIALLYRKENVKLLVVGVSTASENKLKMLVG 726
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNrRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  727 C-APNVVCPFVIKTEWGLLKNVSEVFVKKICD 757
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 84-274 6.39e-89

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 287.68  E-value: 6.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   84 YDLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLKKDYY 163
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDGNENSASNKQLLEMGLTYRRERVKLLVLGVAAAEDNKLKLIAG 243
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  244 C-EENTNCPYSMKAEWETINDITKRLTNKICH 274
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1066-1255 3.52e-68

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 228.36  E-value: 3.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1066 FDLTYIEVPTLNSTYT-WRSDFMDCSKNIMNSLVIDKNKVHVSLIISLEKKSVHQGFDDVNSYNKNELIKTLGKLENSTV 1144
Cdd:cd01473     1 YDLTLILDESASIGYSnWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1145 -LNKTNILDSLVYGIQQSFGKGNREN-APKVTMLLTNSNSDISDEKALQDIYLNYKEKSIKLLIIGIGITNTGKLFNAGG 1222
Cdd:cd01473    81 sGGETYIVEALKYGLKNYTKHGNRRKdAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124504959 1223 CNMNGDNCPHVYASKsFSYIGGVDTFLEVNKCD 1255
Cdd:cd01473   161 CDINNDNCPNVIKTE-WNNLNGISKFLTDKICD 192
VWA pfam00092
von Willebrand factor type A domain;
305-486 6.90e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 6.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELkdKYGY 384
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEK-VKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSS--KEELLSAVDNL--RYLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   385 GGATHLVDALQYSLKTFTRHPNN-RVDAPKVTILFTDGNETSkkeKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAg 463
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGaRPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVGNADDEELRKIA- 151

                          170       180
                   ....*....|....*....|...
gi 124504959   464 cTENEECLRVIKCEWNDLTNITK 486
Cdd:pfam00092  152 -SEPGEGHVFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
849-1027 7.38e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 7.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQkeSYDKNNLVRRIHDLKkyYKS 928
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEK-VKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLND--YSSKEELLSAVDNLR--YLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   929 GGFSYIVEALKYGLYSYAKSTS-SRLNVPKVNILLTDGNNTDTSdfiLTEVSSLYKKENVKLLLIGIGGPTIHKLRLLGG 1007
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGRSQDGD---PEEVARELKSAGVTVFAVGVGNADDEELRKIAS 152

                          170       180
                   ....*....|....*....|
gi 124504959  1008 CdksDGDCPYVVKAEWNNLK 1027
Cdd:pfam00092  153 E---PGEGHVFTVSDFEALE 169
VWA pfam00092
von Willebrand factor type A domain;
569-749 1.28e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.91  E-value: 1.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   569 DITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFydNARYEKGTLQTKINDLKrdYRS 648
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNF-EKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPL--NDYSSKEELLSAVDNLR--YLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   649 GKKTYIIQALQYALTYY--SKLSNRKEAPKVTMLFTDGNDSYESekgLQDIALLYRKENVKLLVVGVSTASENKLKMLvG 726
Cdd:pfam00092   76 GGTTNTGKALKYALENLfsSAAGARPGAPKVVVLLTDGRSQDGD---PEEVARELKSAGVTVFAVGVGNADDEELRKI-A 151

                          170       180
                   ....*....|....*....|...
gi 124504959   727 CAPNvVCPFVIKTEWGLLKNVSE 749
Cdd:pfam00092  152 SEPG-EGHVFTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 569-736 9.24e-27

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: 108.70  E-value: 9.24e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    569 DITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFydNARYEKGTLQTKINDLKrdYRS 648
Cdd:smart00327    1 DVVFLLDGSGSMGGNRF-ELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLS--YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    649 GKKTYIIQALQYALTYYSKLSN--RKEAPKVTMLFTDGNdSYESEKGLQDIALLYRKENVKLLVVGVSTA-SENKLKMLV 725
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAgsRRGAPKVVILITDGE-SNDGPKDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLA 154

                           170
                    ....*....|.
gi 124504959    726 GCAPNVVCPFV 736
Cdd:smart00327  155 SAPGGVYVFLP 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 305-468 1.23e-26

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: 108.31  E-value: 1.23e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKdkYGY 384
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFEL-AKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS--KDALLEALASLS--YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    385 GGATHLVDALQYSLKT-FTRHPNNRVDAPKVTILFTDGNETSkKEKDIRDVGLLYRKENVKLIVVGV-NLATEKSLKLLA 462
Cdd:smart00327   76 GGGTNLGAALQYALENlFSKSAGSRRGAPKVVILITDGESND-GPKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLA 154


                    ....*.
gi 124504959    463 GCTENE 468
Cdd:smart00327  155 SAPGGV 160
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 85-268 1.79e-25

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: 105.23  E-value: 1.79e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959     85 DLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDElryqKDELLKKVEKLKKDYYC 164
Cdd:smart00327    1 DVVFLLDGSGSMGGNRF-ELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSYKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    165 GGGTKILGALKYSLENY-TKHKNIRYDAPKVTILFTDGNENSASnKQLLEMGLTYRRERVKLLVLGVAAAED-NKLKLIA 242
Cdd:smart00327   76 GGGTNLGAALQYALENLfSKSAGSRRGAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVGNDVDeEELKKLA 154

                           170       180
                    ....*....|....*....|....*.
gi 124504959    243 GCEENTNCPYSmkaewETINDITKRL 268
Cdd:smart00327  155 SAPGGVYVFLP-----ELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 849-1014 3.55e-25

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: 104.46  E-value: 3.55e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQkeSYDKNNLVRRIHDLKkyYKS 928
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFEL-AKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLND--SRSKDALLEALASLS--YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    929 GGFSYIVEALKYGL-YSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLyKKENVKLLLIGIGGPT-IHKLRLLG 1006
Cdd:smart00327   76 GGGTNLGAALQYALeNLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKEL-KRSGVKVFVVGVGNDVdEEELKKLA 154


                    ....*...
gi 124504959   1007 GCDKSDGD 1014
Cdd:smart00327  155 SAPGGVYV 162
VWA pfam00092
von Willebrand factor type A domain;
85-267 1.54e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.35  E-value: 1.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    85 DLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSS------KNRDYVTYG------DELRYQkdell 152
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNF-EKVKEFLKKLVESLDIGPDGTRVGLVQYSSdvrtefPLNDYSSKEellsavDNLRYL----- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   153 kkveklkkdyycGGGTKILG-ALKYSLENYTKHK-NIRYDAPKVTILFTDGNENSasnKQLLEMGLTYRRERVKLLVLGV 230
Cdd:pfam00092   75 ------------GGGTTNTGkALKYALENLFSSAaGARPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGV 139

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 124504959   231 AAAEDNKLKLIAGceENTNCPYSMKAEWETINDITKR 267
Cdd:pfam00092  140 GNADDEELRKIAS--EPGEGHVFTVSDFEALEDLQDQ 174
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 841-1055 1.60e-24

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 110.82  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  841 ECLCHNTYDLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIH 920
Cdd:PTZ00441   36 EEVCNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  921 DLKKYYKSGGFSYIVEALKyglySYAKSTSSRLNVPKVN---ILLTDGNNTDTSDFIltEVSSLYKKENVKLLLIGIGGP 997
Cdd:PTZ00441  116 SLRKTYLPYGKTNMTDALL----EVRKHLNDRVNRENAIqlvILMTDGIPNSKYRAL--EESRKLKDRNVKLAVIGIGQG 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  998 TIHKL-RLLGGCDKSDGDCPYVVKAEWNNLKYTSNLIIDKICHTDKPVEN--PGDNSSVCN 1055
Cdd:PTZ00441  190 INHQFnRLLAGCRPREGKCKFYSDADWEEAKNLIKPFIAKVCTEVERTAScgPWDEWTPCS 250
VWA pfam00092
von Willebrand factor type A domain;
1303-1460 5.40e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.34  E-value: 5.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEInkLPISYSK 1382
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFE-KVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDN--LRYLGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1383 KKDIAKSLKYVRTKVFKKSE---TNRKKLIIMLVEGKSNsnMNDLRKEVGLLKVNNIDFFAYAIDNIDETEYKILGDCEG 1459
Cdd:pfam00092   78 TTNTGKALKYALENLFSSAAgarPGAPKVVVLLTDGRSQ--DGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155


                   .
gi 124504959  1460 S 1460
Cdd:pfam00092  156 E 156
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1303-1461 2.15e-17

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: 81.73  E-value: 2.15e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEInkLPISYSK 1382
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFE-LAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALAS--LSYKLGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   1383 KKDIAKSLKYVRTKVFKKSETNR---KKLIIMLVEGKSNSNMNDLRKEVGLLKVNNIDFFAYAIDN-IDETEYKILGDCE 1458
Cdd:smart00327   78 GTNLGAALQYALENLFSKSAGSRrgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157


                    ...
gi 124504959   1459 GSV 1461
Cdd:smart00327  158 GGV 160
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 564-756 2.48e-17

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 88.10  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  564 CKDFYDITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLK 643
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  644 RDYRSGKKTYIIQALQYALTYYSKLSNRKEAPKVTMLFTDG--NDSYESEKglqdIALLYRKENVKLLVVGVSTASENKL 721
Cdd:PTZ00441  119 KTYLPYGKTNMTDALLEVRKHLNDRVNRENAIQLVILMTDGipNSKYRALE----ESRKLKDRNVKLAVIGIGQGINHQF 194

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 124504959  722 -KMLVGCAP-NVVCPFVIKTEWGLLKNVSEVFVKKIC 756
Cdd:PTZ00441  195 nRLLAGCRPrEGKCKFYSDADWEEAKNLIKPFIAKVC 231
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 300-555 7.07e-17

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 86.56  E-value: 7.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  300 CEDYYDLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELK 379
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  380 DKYGYGGATHLVDALQYSLKtftrHPNNRVDAPK---VTILFTDGNETSKKekDIRDVGLLYRKENVKLIVVGVNLATEK 456
Cdd:PTZ00441  119 KTYLPYGKTNMTDALLEVRK----HLNDRVNRENaiqLVILMTDGIPNSKY--RALEESRKLKDRNVKLAVIGIGQGINH 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  457 SL-KLLAGCTENE-ECLRVIKCEWNDLTNITKILTDKIC-------NTG--------SVE-------------------- 499
Cdd:PTZ00441  193 QFnRLLAGCRPREgKCKFYSDADWEEAKNLIKPFIAKVCtevertaSCGpwdewtpcSVTcgkgthsrsrpilhegctth 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  500 ----------LPKPEENPEPVEKPNPEENPNPveKPTPEENPNP-----VEKPTPEENPNPVEKPEPEKNP 555
Cdd:PTZ00441  273 mveeceeeecPVEPEPLPVPAPVPPTPEDDNP--RPTDDEFAVPnfnegLDVPDNPQDPVPPPNEGKDGNP 341
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 80-273 9.98e-16

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 83.09  E-value: 9.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   80 CQNYYDLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLK 159
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  160 KDYYCGGGTKILGALKySLENYTKHKNIRYDAPKVTILFTDGNENSASNKqlLEMGLTYRRERVKLLVLGVAAAEDNKL- 238
Cdd:PTZ00441  119 KTYLPYGKTNMTDALL-EVRKHLNDRVNRENAIQLVILMTDGIPNSKYRA--LEESRKLKDRNVKLAVIGIGQGINHQFn 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 124504959  239 KLIAGCE-ENTNCPYSMKAEWETINDITKRLTNKIC 273
Cdd:PTZ00441  196 RLLAGCRpREGKCKFYSDADWEEAKNLIKPFIAKVC 231
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1302-1460 3.45e-14

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: 72.21  E-value: 3.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1302 LDIAVVLDQSSNISKDQWNVyIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISyqKKKIIKEINKLPISYS 1381
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDK-AKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTD--KADLLEAIDALKKGLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1382 KKKDIAKSLKYVRTKVFKKSETNRKKLIIMLVEGKSNSNMNDLRKEVGLLKVNNIDFFAYAI-DNIDETEYKILGDCEGS 1460
Cdd:cd00198    78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTTG 157
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 1.05e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 66.72  E-value: 1.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  359 EKPKPEVKPQP-EKPKPEVKPQP-ETPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPEK 415
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 2.65e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 65.56  E-value: 2.65e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  403 EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPET 459
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 4.64e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 64.79  E-value: 4.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  414 EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-ETPKPEVKP 466
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 4.76e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 64.79  E-value: 4.76e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  381 ETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPEK 437
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 497-553 7.50e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 64.02  E-value: 7.50e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  497 SVELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  324 QLEKPKPEVKPQP-EKPKPEVKPQL-ETPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPET 382
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 752-837 1.19e-09

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 58.53  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   752 VKKICDNGVVLP-------PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPS 824
Cdd:pfam02389   21 TKEPCHSKVPEPcnpkvpePCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHPKAPEPCHPK 100

                           90
                   ....*....|...
gi 124504959   825 ESTPGSPSESTPC 837
Cdd:pfam02389  101 VPEPCYPKAPEPC 113
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1597-1646 1.94e-09

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.29  E-value: 1.94e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1597 CGDFGEWSECSATCGEGIRVRNR----DNSLDNDDKCKLfNSTEMEACNIQECD 1646
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRsccsPPPQNGGGPCTG-EDVETRACNEQPCP 53
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 3.63e-09

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 61.71  E-value: 3.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPV-----EKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  392 EKPKPEVKPQP-EKPKPEvkpqpEKPKPEvkpqpEKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKP 455
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 5.86e-09

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 60.94  E-value: 5.86e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPE-----ENPNPVEKPTPEEnPNPVEKPEPEK 553
Cdd:NF033839  425 EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEvkpqpETPKPEVKPQPEK-PKPEVKPQPEK 481
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 1.15e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 60.17  E-value: 1.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPV-----EKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  348 ETPKPEVKPQP-EKPKPEvkpqpEKPKPEvkpqpETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKP 411
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 1.56e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.78  E-value: 1.56e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPV-----EKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  315 ETPKPEVKPQL-EKPKPEvkpqpEKPKPEvkpqlETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKP 378
TSP_1 pfam00090
Thrombospondin type 1 domain;
1598-1645 1.60e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 1.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 124504959  1598 GDFGEWSECSATCGEGIRVRNR--DNSLDNDDKCKLfNSTEMEACNIQEC 1645
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRtcKSPFPGGEPCTG-DDIETQACKMDKC 49
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 2.31e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.01  E-value: 2.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPVEKPTPEE-----NPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  370 EKPKPEVKPQP-ETPKPEvkpqpEKPKPEVKPQPEKpkpevKPQP-EKPKPEVKPQP-EKPKPEVKP 433
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 497-553 2.81e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.01  E-value: 2.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  497 SVELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  302 SPQPEKKEVKPEP-ETPKPEVKPQL-EKPKPEVKPQP-EKPKPEvkpqlETPKPEVKPQPEK 360
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 5.20e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 57.86  E-value: 5.20e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  293 SAPKPGMQPSP-QPEKKEVKPEP-ETPKPEVKPQL-EKPKPEVKPQP-EKPKPEVKP 345
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 1.50e-07

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 56.70  E-value: 1.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPVEKPTPeENPNPVEKPTPEEnPNPVEKPEPEK 553
Cdd:NF033839  337 EKPKPEVKPQL-ETPKPEvkpqpEKPKPEVKPQP-EKPKPEVKPQPET-PKPEVKPQPEK 393
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1806-1863 1.73e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 1.73e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959   1806 CGDWSDWSECDRTCNVGVRIRHFISHMFDmvGDEDEKECLEyyNKVETQDClHLPPCD 1863
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPP--PQNGGGPCTG--EDVETRAC-NEQPCP 53
PRK10819 PRK10819
transport protein TonB; Provisional
 501-555 2.01e-07

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 54.30  E-value: 2.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124504959  501 PKPEENPEPVEKPNPEENPnPVEKPTPEENPNPVEKPTPEENPNPVEK----PEPEKNP 555
Cdd:PRK10819   66 PPPEPVVEPEPEPEPIPEP-PKEAPVVIPKPEPKPKPKPKPKPKPVKKveeqPKREVKP 123
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 498-719 2.48e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 54.17  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  498 VELPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEENPNPVEKPEPEKNPCINMEDCYCKDFYDITLVLDES 577
Cdd:COG1240    23 LLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDAS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  578 ASISDLIWRNEVIPFSLEIIKRINisyKNVHMGVLLFSEYTRDIVRFydnaRYEKGTLQTKINDLKrdyrSGKKTYIIQA 657
Cdd:COG1240   103 GSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL----TRDREALKRALDELP----PGGGTPLGDA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  658 LQYALTYYSklSNRKEAPKVTMLFTDGNDSyESEKGLQDIALLYRKENVKLLVVGVSTASEN 719
Cdd:COG1240   172 LALALELLK--RADPARRKVIVLLTDGRDN-AGRIDPLEAAELAAAAGIRIYTIGVGTEAVD 230
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1654-1703 4.08e-07

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 48.43  E-value: 4.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 124504959  1654 CEdIGEWSDWSSCSKTCGYSTRSRTFTIL--PEYIGEypNCKifERSETEVC 1703
Cdd:pfam19028    1 CV-VSEWSEWSECSVTCGGGVQTRTRTVIvePQNGGR--PCP--ELLERRPC 47
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 763-838 1.27e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  763 PPGSPSESTPGSPSESTPgSPSESTPGSPSESTP-------GNPSESTPGSPSESTPGNPSESTPGSPSES---TPGSPS 832
Cdd:PHA03307  279 SSRPGPASSSSSPRERSP-SPSPSSPGSGPAPSSprassssSSSRESSSSSTSSSSESSRGAAVSPGPSPSrspSPSRPP 357


                  ....*.
gi 124504959  833 ESTPCS 838
Cdd:PHA03307  358 PPADPS 363
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 765-870 1.68e-06

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 52.59  E-value: 1.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   765 GSPSESTPGSPSESTPgSPSESTPGSPSESTPGNPSEST-PGSPSESTPGNPSESTPgSPSESTPGSPSESTPCSGTEcl 843
Cdd:TIGR00601   80 GTGKVAPPAATPTSAP-TPTPSPPASPASGMSAAPASAVeEKSPSEESATATAPESP-STSVPSSGSDAASTLVVGSE-- 155

                           90       100
                   ....*....|....*....|....*..
gi 124504959   844 chntYDLTliIDESASIGYsnwEKEVV 870
Cdd:TIGR00601  156 ----RETT--IEEIMEMGY---EREEV 173
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 497-555 2.50e-06

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 52.46  E-value: 2.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124504959  497 SVELPKPEENPEPvEKPNPE-----ENPNPVEKPTPEEnPNPVEKPTPEENPNPVEKPEPE-KNP 555
Cdd:NF033839  434 QPEKPKPEVKPQP-EKPKPEvkpqpETPKPEVKPQPEK-PKPEVKPQPEKPKPDNSKPQADdKKP 496
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1939-2002 4.97e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 4.97e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1939 CNEWEEWGDCSSTCGEGsfkIRKRKEPLELIPASQDingniGLTCAQQNikvEEREACIVPACE 2002
Cdd:smart00209    1 WSEWSEWSPCSVTCGGG---VQTRTRSCCSPPPQNG-----GGPCTGED---VETRACNEQPCP 53
Neisseria_TspB pfam05616
Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis ...
 500-555 4.98e-06

Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis TspB virulence factor proteins.


Pssm-ID: 283306 [Multi-domain]  Cd Length: 517  Bit Score: 51.63  E-value: 4.98e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959   500 LPKPEENPEPVEKPN----PEENP--NPVEKPTPEENPNPVEKPTPEENPNPVEKPEPEKNP 555
Cdd:pfam05616  325 IPRPDLTPASAEAPHaqplPEVSPaeNPANNPDPDENPGTRPNPEPDPDLNPDANPDTDGQP 386
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1658-1710 8.44e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.89  E-value: 8.44e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1658 GEWSDWSSCSKTCGYSTRSRT-FTILPEYIGEYPNCKIfERSETEVCaFIPACS 1710
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTrSCCSPPPQNGGGPCTG-EDVETRAC-NEQPCP 53
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 368-462 8.79e-06

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 49.55  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  368 KNDLIKLVRELKdkygYGGATHLVDALQYSLKTFTRHPNNRvdaPKVTILFTDGNETSKKEkDIRDVGLLYRKENVKLIV 447
Cdd:COG1240   150 REALKRALDELP----PGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGRDNAGRI-DPLEAAELAAAAGIRIYT 221

                          90
                  ....*....|....*..
gi 124504959  448 VGVNLAT--EKSLKLLA 462
Cdd:COG1240   222 IGVGTEAvdEGLLREIA 238
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1297-1523 4.58e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 48.42  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1297 ICTKVLDIAVVLDQSSNISKDQWNVYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEINKL 1376
Cdd:PTZ00441   38 VCNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1377 PISYSK--KKDIAKSLKYVRTKVfkKSETNRKK---LIIMLVEGKSNSNMNDLrKEVGLLKVNNIDFFAYAI-DNIDETE 1450
Cdd:PTZ00441  118 RKTYLPygKTNMTDALLEVRKHL--NDRVNRENaiqLVILMTDGIPNSKYRAL-EESRKLKDRNVKLAVIGIgQGINHQF 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124504959 1451 YKILGDCEgsvdmglmgnsppsPSYLPCKNIVKVSWDTLLSSTDIHMKYICNGYPEDAECSEWEEWSPCPETC 1523
Cdd:PTZ00441  195 NRLLAGCR--------------PREGKCKFYSDADWEEAKNLIKPFIAKVCTEVERTASCGPWDEWTPCSVTC 253
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1807-1827 6.85e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 42.27  E-value: 6.85e-05
                           10        20
                   ....*....|....*....|.
gi 124504959  1807 GDWSDWSECDRTCNVGVRIRH 1827
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRT 24
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 762-999 4.43e-04

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.16  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  762 LPPGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTPCSGTe 841
Cdd:COG1240    15 LALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGR- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  842 clchntyDLTLIIDESASIGYSN-WE--KEVVpftIGLASNLEiseKKVNMGILLFSDKIREFIKYgqkeSYDKNNLVRR 918
Cdd:COG1240    94 -------DVVLVVDASGSMAAENrLEaaKGAL---LDFLDDYR---PRDRVGLVAFGGEAEVLLPL----TRDREALKRA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  919 IHDLKkyykSGGFSYIVEALKYGLYSYAKSTSSRlnvPKVNILLTDG-NNTDTSDfiLTEVSSLYKKENVKLLLIGIGGP 997
Cdd:COG1240   157 LDELP----PGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGrDNAGRID--PLEAAELAAAAGIRIYTIGVGTE 227


                  ..
gi 124504959  998 TI 999
Cdd:COG1240   228 AV 229
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1941-2001 6.02e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 6.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124504959  1941 EWEEWGDCSSTCGEGsFKIRKR---KEPLelipasqdiNGniGLTCAQQnikvEEREACIVPAC 2001
Cdd:pfam19028    5 EWSEWSECSVTCGGG-VQTRTRtviVEPQ---------NG--GRPCPEL----LERRPCNLPPC 52
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 764-832 9.27e-04

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 42.72  E-value: 9.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124504959  764 PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPgNPSESTPGSPSESTPGSPS 832
Cdd:cd21577    32 PPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLP-PPVAPPPLSPGSVPGGLPV 99
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 164-242 1.05e-03

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 43.00  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLEnytKHKNIRYDAPKVTILFTDGNENsASNKQLLEMGLTYRRERVKLLVLGVAAAEDNK--LKLI 241
Cdd:COG1240   162 PGGGTPLGDALALALE---LLKRADPARRKVIVLLTDGRDN-AGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREI 237


                  .
gi 124504959  242 A 242
Cdd:COG1240   238 A 238
VWA pfam00092
von Willebrand factor type A domain;
1091-1186 2.65e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 40.72  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1091 KNIMNSLVIDKNKVHVSLI---------ISLekksvhqgfddvNSY-NKNELIKTLGKLENSTVlNKTNILDSLVYGIQQ 1160
Cdd:pfam00092   25 KKLVESLDIGPDGTRVGLVqyssdvrteFPL------------NDYsSKEELLSAVDNLRYLGG-GTTNTGKALKYALEN 91

                           90       100
                   ....*....|....*....|....*...
gi 124504959  1161 SFGK--GNRENAPKVTMLLTNSNSDISD 1186
Cdd:pfam00092   92 LFSSaaGARPGAPKVVVLLTDGRSQDGD 119
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1091-1191 3.88e-03

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: 40.52  E-value: 3.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   1091 KNIMNSLVIDKNKVHVSLI-ISlekKSVHQGFDDVNSYNKNELIKTLGKLENSTvLNKTNILDSLVYGIQQSFGK--GNR 1167
Cdd:smart00327   25 LKLVEQLDIGPDGDRVGLVtFS---DDARVLFPLNDSRSKDALLEALASLSYKL-GGGTNLGAALQYALENLFSKsaGSR 100

                            90       100
                    ....*....|....*....|....
gi 124504959   1168 ENAPKVTMLLTNSNSDISDEKALQ 1191
Cdd:smart00327  101 RGAPKVVILITDGESNDGPKDLLK 124
 
Name Accession Description Interval E-value
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 304-494 7.58e-95

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 304.63  E-value: 7.58e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  304 YDLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELKDKYG 383
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  384 YGGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGNETSKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAG 463
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  464 C-TENEECLRVIKCEWNDLTNITKILTDKICN 494
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 848-1039 1.01e-92

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 298.46  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  848 YDLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIHDLKKYYK 927
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  928 SGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLYKKENVKLLLIGIGGPTIHKLRLLGG 1007
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959 1008 CDKSDGDCPYVVKAEWNNLKYTSNLIIDKICH 1039
Cdd:cd01473   161 CDINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 568-757 4.25e-90

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 291.14  E-value: 4.25e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  568 YDITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLKRDYR 647
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  648 SGKKTYIIQALQYALTYYSKLSN-RKEAPKVTMLFTDGNDSYESEKGLQDIALLYRKENVKLLVVGVSTASENKLKMLVG 726
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNrRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  727 C-APNVVCPFVIKTEWGLLKNVSEVFVKKICD 757
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 84-274 6.39e-89

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 287.68  E-value: 6.39e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   84 YDLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLKKDYY 163
Cdd:cd01473     1 YDLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDGNENSASNKQLLEMGLTYRRERVKLLVLGVAAAEDNKLKLIAG 243
Cdd:cd01473    81 SGGETYIVEALKYGLKNYTKHGNRRKDAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 124504959  244 C-EENTNCPYSMKAEWETINDITKRLTNKICH 274
Cdd:cd01473   161 CdINNDNCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1066-1255 3.52e-68

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 228.36  E-value: 3.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1066 FDLTYIEVPTLNSTYT-WRSDFMDCSKNIMNSLVIDKNKVHVSLIISLEKKSVHQGFDDVNSYNKNELIKTLGKLENSTV 1144
Cdd:cd01473     1 YDLTLILDESASIGYSnWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1145 -LNKTNILDSLVYGIQQSFGKGNREN-APKVTMLLTNSNSDISDEKALQDIYLNYKEKSIKLLIIGIGITNTGKLFNAGG 1222
Cdd:cd01473    81 sGGETYIVEALKYGLKNYTKHGNRRKdAPKVTMLFTDGNDTSASKKELQDISLLYKEENVKLLVVGVGAASENKLKLLAG 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124504959 1223 CNMNGDNCPHVYASKsFSYIGGVDTFLEVNKCD 1255
Cdd:cd01473   161 CDINNDNCPNVIKTE-WNNLNGISKFLTDKICD 192
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 304-466 1.98e-37

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: 138.96  E-value: 1.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  304 YDLTLILDESRSITLDkWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKdkYG 383
Cdd:cd01450     1 LDIVFLLDGSESVGPE-NFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKS--KDDLLKAVKNLK--YL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  384 YGGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGNetSKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAG 463
Cdd:cd01450    76 GGGGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153


                  ...
gi 124504959  464 CTE 466
Cdd:cd01450   154 CPS 156
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 568-733 3.64e-37

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: 138.19  E-value: 3.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  568 YDITLVLDESASISDLiWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNarYEKGTLQTKINDLKrdYR 647
Cdd:cd01450     1 LDIVFLLDGSESVGPE-NFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDY--KSKDDLLKAVKNLK--YL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  648 SGKKTYIIQALQYALTYYSKLSN-RKEAPKVTMLFTDGNDSYESekGLQDIALLYRKENVKLLVVGVSTASENKLKMLVG 726
Cdd:cd01450    76 GGGGTNTGKALQYALEQLFSESNaRENVPKVIIVLTDGRSDDGG--DPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153


                  ....*..
gi 124504959  727 CAPNVVC 733
Cdd:cd01450   154 CPSERHV 160
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 84-244 9.32e-36

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: 133.96  E-value: 9.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   84 YDLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDElryqKDELLKKVEKLKKDYY 163
Cdd:cd01450     1 LDIVFLLDGSESVGPENF-EKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDY----KSKDDLLKAVKNLKYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDGNENSASNkqLLEMGLTYRRERVKLLVLGVAAAEDNKLKLIAG 243
Cdd:cd01450    76 GGGGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGD--PKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153


                  .
gi 124504959  244 C 244
Cdd:cd01450   154 C 154
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 848-1019 5.07e-35

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: 132.03  E-value: 5.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  848 YDLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYgqKESYDKNNLVRRIHDLKkyYK 927
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEK-VKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSL--NDYKSKDDLLKAVKNLK--YL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  928 SGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTDTSDFIltEVSSLYKKENVKLLLIGIGGPTIHKLRLLGG 1007
Cdd:cd01450    76 GGGGTNTGKALQYALEQLFSESNARENVPKVIIVLTDGRSDDGGDPK--EAAAKLKDEGIKVFVVGVGPADEEELREIAS 153

                         170
                  ....*....|..
gi 124504959 1008 CdksdGDCPYVV 1019
Cdd:cd01450   154 C----PSERHVF 161
VWA pfam00092
von Willebrand factor type A domain;
305-486 6.90e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 6.90e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELkdKYGY 384
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEK-VKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSS--KEELLSAVDNL--RYLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   385 GGATHLVDALQYSLKTFTRHPNN-RVDAPKVTILFTDGNETSkkeKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAg 463
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGaRPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGVGNADDEELRKIA- 151

                          170       180
                   ....*....|....*....|...
gi 124504959   464 cTENEECLRVIKCEWNDLTNITK 486
Cdd:pfam00092  152 -SEPGEGHVFTVSDFEALEDLQD 173
VWA pfam00092
von Willebrand factor type A domain;
849-1027 7.38e-33

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 126.24  E-value: 7.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQkeSYDKNNLVRRIHDLKkyYKS 928
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEK-VKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLND--YSSKEELLSAVDNLR--YLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   929 GGFSYIVEALKYGLYSYAKSTS-SRLNVPKVNILLTDGNNTDTSdfiLTEVSSLYKKENVKLLLIGIGGPTIHKLRLLGG 1007
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAgARPGAPKVVVLLTDGRSQDGD---PEEVARELKSAGVTVFAVGVGNADDEELRKIAS 152

                          170       180
                   ....*....|....*....|
gi 124504959  1008 CdksDGDCPYVVKAEWNNLK 1027
Cdd:pfam00092  153 E---PGEGHVFTVSDFEALE 169
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 849-1027 9.21e-31

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 120.57  E-value: 9.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIHDLKKYYKS 928
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  929 GGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGnnTDTSDFILTEVSSLYKKENVKLLLIGIG-GPTIHKLRLLGG 1007
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDG--IPDSKFRTLKEARKLRERGVIIAVLGVGqGVNHEENRSLVG 159

                         170       180
                  ....*....|....*....|
gi 124504959 1008 CDKSDGDCPYVVKAEWNNLK 1027
Cdd:cd01471   160 CDPDDSPCPLYLQSSWSEVQ 179
VWA pfam00092
von Willebrand factor type A domain;
569-749 1.28e-28

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 113.91  E-value: 1.28e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   569 DITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFydNARYEKGTLQTKINDLKrdYRS 648
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNF-EKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPL--NDYSSKEELLSAVDNLR--YLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   649 GKKTYIIQALQYALTYY--SKLSNRKEAPKVTMLFTDGNDSYESekgLQDIALLYRKENVKLLVVGVSTASENKLKMLvG 726
Cdd:pfam00092   76 GGTTNTGKALKYALENLfsSAAGARPGAPKVVVLLTDGRSQDGD---PEEVARELKSAGVTVFAVGVGNADDEELRKI-A 151

                          170       180
                   ....*....|....*....|...
gi 124504959   727 CAPNvVCPFVIKTEWGLLKNVSE 749
Cdd:pfam00092  152 SEPG-EGHVFTVSDFEALEDLQD 173
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 569-736 9.24e-27

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: 108.70  E-value: 9.24e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    569 DITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFydNARYEKGTLQTKINDLKrdYRS 648
Cdd:smart00327    1 DVVFLLDGSGSMGGNRF-ELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPL--NDSRSKDALLEALASLS--YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    649 GKKTYIIQALQYALTYYSKLSN--RKEAPKVTMLFTDGNdSYESEKGLQDIALLYRKENVKLLVVGVSTA-SENKLKMLV 725
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAgsRRGAPKVVILITDGE-SNDGPKDLLKAAKELKRSGVKVFVVGVGNDvDEEELKKLA 154

                           170
                    ....*....|.
gi 124504959    726 GCAPNVVCPFV 736
Cdd:smart00327  155 SAPGGVYVFLP 165
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 305-468 1.23e-26

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: 108.31  E-value: 1.23e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKdkYGY 384
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFEL-AKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRS--KDALLEALASLS--YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    385 GGATHLVDALQYSLKT-FTRHPNNRVDAPKVTILFTDGNETSkKEKDIRDVGLLYRKENVKLIVVGV-NLATEKSLKLLA 462
Cdd:smart00327   76 GGGTNLGAALQYALENlFSKSAGSRRGAPKVVILITDGESND-GPKDLLKAAKELKRSGVKVFVVGVgNDVDEEELKKLA 154


                    ....*.
gi 124504959    463 GCTENE 468
Cdd:smart00327  155 SAPGGV 160
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 85-259 3.15e-26

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 107.86  E-value: 3.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLKKDYYC 164
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  165 GGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDGNENS-----ASNKQLLEMGltyrrerVKLLVLGVAAAEDNKL- 238
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDGIPDSkfrtlKEARKLRERG-------VIIAVLGVGQGVNHEEn 154

                         170       180
                  ....*....|....*....|..
gi 124504959  239 KLIAGCEENT-NCPYSMKAEWE 259
Cdd:cd01471   155 RSLVGCDPDDsPCPLYLQSSWS 176
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 85-268 1.79e-25

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: 105.23  E-value: 1.79e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959     85 DLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDElryqKDELLKKVEKLKKDYYC 164
Cdd:smart00327    1 DVVFLLDGSGSMGGNRF-ELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDS----RSKDALLEALASLSYKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    165 GGGTKILGALKYSLENY-TKHKNIRYDAPKVTILFTDGNENSASnKQLLEMGLTYRRERVKLLVLGVAAAED-NKLKLIA 242
Cdd:smart00327   76 GGGTNLGAALQYALENLfSKSAGSRRGAPKVVILITDGESNDGP-KDLLKAAKELKRSGVKVFVVGVGNDVDeEELKKLA 154

                           170       180
                    ....*....|....*....|....*.
gi 124504959    243 GCEENTNCPYSmkaewETINDITKRL 268
Cdd:smart00327  155 SAPGGVYVFLP-----ELLDLLIDLL 175
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 849-1014 3.55e-25

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: 104.46  E-value: 3.55e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQkeSYDKNNLVRRIHDLKkyYKS 928
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFEL-AKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLND--SRSKDALLEALASLS--YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    929 GGFSYIVEALKYGL-YSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLyKKENVKLLLIGIGGPT-IHKLRLLG 1006
Cdd:smart00327   76 GGGTNLGAALQYALeNLFSKSAGSRRGAPKVVILITDGESNDGPKDLLKAAKEL-KRSGVKVFVVGVGNDVdEEELKKLA 154


                    ....*...
gi 124504959   1007 GCDKSDGD 1014
Cdd:smart00327  155 SAPGGVYV 162
VWA pfam00092
von Willebrand factor type A domain;
85-267 1.54e-24

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 102.35  E-value: 1.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959    85 DLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSS------KNRDYVTYG------DELRYQkdell 152
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNF-EKVKEFLKKLVESLDIGPDGTRVGLVQYSSdvrtefPLNDYSSKEellsavDNLRYL----- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   153 kkveklkkdyycGGGTKILG-ALKYSLENYTKHK-NIRYDAPKVTILFTDGNENSasnKQLLEMGLTYRRERVKLLVLGV 230
Cdd:pfam00092   75 ------------GGGTTNTGkALKYALENLFSSAaGARPGAPKVVVLLTDGRSQD---GDPEEVARELKSAGVTVFAVGV 139

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 124504959   231 AAAEDNKLKLIAGceENTNCPYSMKAEWETINDITKR 267
Cdd:pfam00092  140 GNADDEELRKIAS--EPGEGHVFTVSDFEALEDLQDQ 174
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 841-1055 1.60e-24

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 110.82  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  841 ECLCHNTYDLTLIIDESASIGYSNWEKEVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIH 920
Cdd:PTZ00441   36 EEVCNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  921 DLKKYYKSGGFSYIVEALKyglySYAKSTSSRLNVPKVN---ILLTDGNNTDTSDFIltEVSSLYKKENVKLLLIGIGGP 997
Cdd:PTZ00441  116 SLRKTYLPYGKTNMTDALL----EVRKHLNDRVNRENAIqlvILMTDGIPNSKYRAL--EESRKLKDRNVKLAVIGIGQG 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  998 TIHKL-RLLGGCDKSDGDCPYVVKAEWNNLKYTSNLIIDKICHTDKPVEN--PGDNSSVCN 1055
Cdd:PTZ00441  190 INHQFnRLLAGCRPREGKCKFYSDADWEEAKNLIKPFIAKVCTEVERTAScgPWDEWTPCS 250
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 305-486 3.86e-23

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 98.61  E-value: 3.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELKDKYGY 384
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  385 GGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGnETSKKEKDIRDVGLLyRKENVKLIVVGVNLATEKSL-KLLAG 463
Cdd:cd01471    82 NGSTNTTSALLVVEKHLFDTRGNRENAPQLVIIMTDG-IPDSKFRTLKEARKL-RERGVIIAVLGVGQGVNHEEnRSLVG 159

                         170       180
                  ....*....|....*....|....
gi 124504959  464 CTENE-ECLRVIKCEWNDLTNITK 486
Cdd:cd01471   160 CDPDDsPCPLYLQSSWSEVQNVIK 183
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 569-747 5.83e-22

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 95.53  E-value: 5.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLKRDYRS 648
Cdd:cd01471     2 DLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYYP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  649 GKKTYIIQALQYALT-YYSKLSNRKEAPKVTMLFTDG--NDSYESEKGLQDIallyRKENVKLLVVGVSTA---SENKLk 722
Cdd:cd01471    82 NGSTNTTSALLVVEKhLFDTRGNRENAPQLVIIMTDGipDSKFRTLKEARKL----RERGVIIAVLGVGQGvnhEENRS- 156

                         170       180
                  ....*....|....*....|....*.
gi 124504959  723 mLVGCAPNVV-CPFVIKTEWGLLKNV 747
Cdd:cd01471   157 -LVGCDPDDSpCPLYLQSSWSEVQNV 181
VWA pfam00092
von Willebrand factor type A domain;
1303-1460 5.40e-21

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 92.34  E-value: 5.40e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEInkLPISYSK 1382
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFE-KVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDN--LRYLGGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1383 KKDIAKSLKYVRTKVFKKSE---TNRKKLIIMLVEGKSNsnMNDLRKEVGLLKVNNIDFFAYAIDNIDETEYKILGDCEG 1459
Cdd:pfam00092   78 TTNTGKALKYALENLFSSAAgarPGAPKVVVLLTDGRSQ--DGDPEEVARELKSAGVTVFAVGVGNADDEELRKIASEPG 155


                   .
gi 124504959  1460 S 1460
Cdd:pfam00092  156 E 156
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 304-467 5.35e-18

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: 83.38  E-value: 5.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  304 YDLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKdkYG 383
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDK-AKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTD--KADLLEAIDALK--KG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  384 YGGATHLVDALQYSLKTFTRhpNNRVDAPKVTILFTDGNETSKKEKDIRDVGLLyRKENVKLIVVGV-NLATEKSLKLLA 462
Cdd:cd00198    76 LGGGTNIGAALRLALELLKS--AKRPNARRVIILLTDGEPNDGPELLAEAAREL-RKLGITVYTIGIgDDANEDELKEIA 152


                  ....*
gi 124504959  463 GCTEN 467
Cdd:cd00198   153 DKTTG 157
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1303-1461 2.15e-17

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: 81.73  E-value: 2.15e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEInkLPISYSK 1382
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFE-LAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALAS--LSYKLGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   1383 KKDIAKSLKYVRTKVFKKSETNR---KKLIIMLVEGKSNSNMNDLRKEVGLLKVNNIDFFAYAIDN-IDETEYKILGDCE 1458
Cdd:smart00327   78 GTNLGAALQYALENLFSKSAGSRrgaPKVVILITDGESNDGPKDLLKAAKELKRSGVKVFVVGVGNdVDEEELKKLASAP 157


                    ...
gi 124504959   1459 GSV 1461
Cdd:smart00327  158 GGV 160
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 564-756 2.48e-17

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 88.10  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  564 CKDFYDITLVLDESASISDLIWRNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLK 643
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  644 RDYRSGKKTYIIQALQYALTYYSKLSNRKEAPKVTMLFTDG--NDSYESEKglqdIALLYRKENVKLLVVGVSTASENKL 721
Cdd:PTZ00441  119 KTYLPYGKTNMTDALLEVRKHLNDRVNRENAIQLVILMTDGipNSKYRALE----ESRKLKDRNVKLAVIGIGQGINHQF 194

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 124504959  722 -KMLVGCAP-NVVCPFVIKTEWGLLKNVSEVFVKKIC 756
Cdd:PTZ00441  195 nRLLAGCRPrEGKCKFYSDADWEEAKNLIKPFIAKVC 231
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 848-1002 3.22e-17

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: 81.07  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  848 YDLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIREFIKYGqkESYDKNNLVRRIHDLKKYYk 927
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDK-AKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLT--TDTDKADLLEAIDALKKGL- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124504959  928 sGGFSYIVEALKYGLYSYAKSTSSrlNVPKVNILLTDGNNTDtSDFILTEVSSLYKKENVKLLLIGIGGPTIHKL 1002
Cdd:cd00198    77 -GGGTNIGAALRLALELLKSAKRP--NARRVIILLTDGEPND-GPELLAEAARELRKLGITVYTIGIGDDANEDE 147
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 568-730 4.14e-17

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: 80.69  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  568 YDITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFydNARYEKGTLQTKINDLKRDYR 647
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKL-DKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPL--TTDTDKADLLEAIDALKKGLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  648 SGkkTYIIQALQYALTYYSKlSNRKEAPKVTMLFTDGnDSYESEKGLQDIALLYRKENVKLLVVGVST-ASENKLKMLVG 726
Cdd:cd00198    78 GG--TNIGAALRLALELLKS-AKRPNARRVIILLTDG-EPNDGPELLAEAARELRKLGITVYTIGIGDdANEDELKEIAD 153


                  ....
gi 124504959  727 CAPN 730
Cdd:cd00198   154 KTTG 157
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 300-555 7.07e-17

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 86.56  E-value: 7.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  300 CEDYYDLTLILDESRSITLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELK 379
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  380 DKYGYGGATHLVDALQYSLKtftrHPNNRVDAPK---VTILFTDGNETSKKekDIRDVGLLYRKENVKLIVVGVNLATEK 456
Cdd:PTZ00441  119 KTYLPYGKTNMTDALLEVRK----HLNDRVNRENaiqLVILMTDGIPNSKY--RALEESRKLKDRNVKLAVIGIGQGINH 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  457 SL-KLLAGCTENE-ECLRVIKCEWNDLTNITKILTDKIC-------NTG--------SVE-------------------- 499
Cdd:PTZ00441  193 QFnRLLAGCRPREgKCKFYSDADWEEAKNLIKPFIAKVCtevertaSCGpwdewtpcSVTcgkgthsrsrpilhegctth 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  500 ----------LPKPEENPEPVEKPNPEENPNPveKPTPEENPNP-----VEKPTPEENPNPVEKPEPEKNP 555
Cdd:PTZ00441  273 mveeceeeecPVEPEPLPVPAPVPPTPEDDNP--RPTDDEFAVPnfnegLDVPDNPQDPVPPPNEGKDGNP 341
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 305-463 5.43e-16

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 77.33  E-value: 5.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKDKygy 384
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFNL-VRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNAYTS--KEDVLAAIKNLPYK--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  385 GGATHLVDALQYSL-KTFTRHPNNRVDAPKVTILFTDGnetsKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLAG 463
Cdd:cd01482    76 GGNTRTGKALTHVReKNFTPDAGARPGVPKVVILITDG----KSQDDVELPARVLRNLGVNVFAVGVKDADESELKMIAS 151
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 80-273 9.98e-16

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 83.09  E-value: 9.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   80 CQNYYDLTLILDESASIGSKNWKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLK 159
Cdd:PTZ00441   39 CNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSLR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  160 KDYYCGGGTKILGALKySLENYTKHKNIRYDAPKVTILFTDGNENSASNKqlLEMGLTYRRERVKLLVLGVAAAEDNKL- 238
Cdd:PTZ00441  119 KTYLPYGKTNMTDALL-EVRKHLNDRVNRENAIQLVILMTDGIPNSKYRA--LEESRKLKDRNVKLAVIGIGQGINHQFn 195

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 124504959  239 KLIAGCE-ENTNCPYSMKAEWETINDITKRLTNKIC 273
Cdd:PTZ00441  196 RLLAGCRpREGKCKFYSDADWEEAKNLIKPFIAKVC 231
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 85-242 4.07e-15

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 74.96  E-value: 4.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNwKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNR------DYVTYGD------ELRYQkdell 152
Cdd:cd01472     2 DIVFLVDGSESIGLSN-FNLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPRtefylnTYRSKDDvleavkNLRYI----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  153 kkveklkkdyycGGGTKILGALKYSLENY-TKHKNIRYDAPKVTILFTDGNensaSNKQLLEMGLTYRRERVKLLVLGVA 231
Cdd:cd01472    76 ------------GGGTNTGKALKYVRENLfTEASGSREGVPKVLVVITDGK----SQDDVEEPAVELKQAGIEVFAVGVK 139

                         170
                  ....*....|.
gi 124504959  232 AAEDNKLKLIA 242
Cdd:cd01472   140 NADEEELKQIA 150
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1066-1201 5.74e-15

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: 74.64  E-value: 5.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1066 FDLTYIEVPTLNSTYTWRSDFMDCSKNIMNSLVIDKNKVHVSLIISLEKKSVHQGFDDVNSynKNELIKTLGKLENSTVL 1145
Cdd:cd01450     1 LDIVFLLDGSESVGPENFEKVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKS--KDDLLKAVKNLKYLGGG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959 1146 NkTNILDSLVYGIQQSFGKGN-RENAPKVTMLLTNSNSDisDEKALQDIYLNYKEKS 1201
Cdd:cd01450    79 G-TNTGKALQYALEQLFSESNaRENVPKVIIVLTDGRSD--DGGDPKEAAAKLKDEG 132
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 85-243 1.27e-14

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 73.47  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNwKNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNR---DYVTYGD---------ELRYQkdell 152
Cdd:cd01482     2 DIVFLVDGSWSIGRSN-FNLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRtefDLNAYTSkedvlaaikNLPYK----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  153 kkveklkkdyycGGGTKILGALKYSLEN-YTKHKNIRYDAPKVTILFTDGNensaSNKQLLEMGLTYRRERVKLLVLGVA 231
Cdd:cd01482    76 ------------GGNTRTGKALTHVREKnFTPDAGARPGVPKVVILITDGK----SQDDVELPARVLRNLGVNVFAVGVK 139

                         170
                  ....*....|..
gi 124504959  232 AAEDNKLKLIAG 243
Cdd:cd01482   140 DADESELKMIAS 151
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 84-249 2.35e-14

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: 72.60  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   84 YDLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVtygdELRYQKDELLKKVEKLKKDYY 163
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKL-DKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVL----PLTTDTDKADLLEAIDALKKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLENYTKHKniRYDAPKVTILFTDGNENSaSNKQLLEMGLTYRRERVKLLVLGVAAAEDNK-LKLIA 242
Cdd:cd00198    76 LGGGTNIGAALRLALELLKSAK--RPNARRVIILLTDGEPND-GPELLAEAARELRKLGITVYTIGIGDDANEDeLKEIA 152


                  ....*..
gi 124504959  243 GCEENTN 249
Cdd:cd00198   153 DKTTGGA 159
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1302-1460 3.45e-14

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: 72.21  E-value: 3.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1302 LDIAVVLDQSSNISKDQWNVyIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISyqKKKIIKEINKLPISYS 1381
Cdd:cd00198     1 ADIVFLLDVSGSMGGEKLDK-AKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTD--KADLLEAIDALKKGLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1382 KKKDIAKSLKYVRTKVFKKSETNRKKLIIMLVEGKSNSNMNDLRKEVGLLKVNNIDFFAYAI-DNIDETEYKILGDCEGS 1460
Cdd:cd00198    78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAARELRKLGITVYTIGIgDDANEDELKEIADKTTG 157
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 305-462 9.17e-13

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 68.02  E-value: 9.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKDKygy 384
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNL-VKDFVKRVVERLDIGPDGVRVGVVQYSDDPRTEFYLNTYRS--KDDVLEAVKNLRYI--- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124504959  385 GGATHLVDALQYSLKT-FTRHPNNRVDAPKVTILFTDGnetsKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLLA 462
Cdd:cd01472    76 GGGTNTGKALKYVRENlFTEASGSREGVPKVLVVITDG----KSQDDVEEPAVELKQAGIEVFAVGVKNADEEELKQIA 150
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 849-997 2.44e-12

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 66.87  E-value: 2.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIR-EFikyGQKESYDKNNLVRRIHDLKkyYK 927
Cdd:cd01472     2 DIVFLVDGSESIGLSNFNL-VKDFVKRVVERLDIGPDGVRVGVVQYSDDPRtEF---YLNTYRSKDDVLEAVKNLR--YI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  928 SGGfSYIVEALKYGLYSYAKSTS-SRLNVPKVNILLTDGNNTDTsdfiLTEVSSLYKKENVKLLLIGIGGP 997
Cdd:cd01472    76 GGG-TNTGKALKYVRENLFTEASgSREGVPKVLVVITDGKSQDD----VEEPAVELKQAGIEVFAVGVKNA 141
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 849-994 2.71e-12

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 66.93  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIGYSNWeKEVVPFTIGLASNLEISEKKVNMGILLFSDKIRefIKYGQKESYDKNNLVRRIHDLKkyYKs 928
Cdd:cd01482     2 DIVFLVDGSWSIGRSNF-NLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPR--TEFDLNAYTSKEDVLAAIKNLP--YK- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  929 GGFSYIVEALKYGL-YSYAKSTSSRLNVPKVNILLTDGNNTDTsdfiLTEVSSLYKKENVKLLLIGI 994
Cdd:cd01482    76 GGNTRTGKALTHVReKNFTPDAGARPGVPKVVILITDGKSQDD----VELPARVLRNLGVNVFAVGV 138
vWA_collagen cd01472
von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This ...
 569-735 2.38e-11

von Willebrand factor (vWF) type A domain; equivalent to the I-domain of integrins. This domain has a variety of functions including: intermolecular adhesion, cell migration, signalling, transcription, and DNA repair. In integrins these domains form heterodimers while in vWF it forms homodimers and multimers. There are different interaction surfaces of this domain as seen by its complexes with collagen with either integrin or human vWFA. In integrins collagen binding occurs via the metal ion-dependent adhesion site (MIDAS) and involves three surface loops located on the upper surface of the molecule. In human vWFA, collagen binding is thought to occur on the bottom of the molecule and does not involve the vestigial MIDAS motif.


Pssm-ID: 238749 [Multi-domain]  Cd Length: 164  Bit Score: 64.17  E-value: 2.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASISDliwRN--EVIPFSLEIIKRINISYKNVHMGVLLFSEYTRdiVRFYDNARYEKGTLQTKINDLKrdY 646
Cdd:cd01472     2 DIVFLVDGSESIGL---SNfnLVKDFVKRVVERLDIGPDGVRVGVVQYSDDPR--TEFYLNTYRSKDDVLEAVKNLR--Y 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  647 RsGKKTYIIQALQYAL-TYYSKLSN-RKEAPKVTMLFTDGndsYESEKGLQDiALLYRKENVKLLVVGVSTASENKLKMl 724
Cdd:cd01472    75 I-GGGTNTGKALKYVReNLFTEASGsREGVPKVLVVITDG---KSQDDVEEP-AVELKQAGIEVFAVGVKNADEEELKQ- 148

                         170
                  ....*....|...
gi 124504959  725 VGCAPNV--VCPF 735
Cdd:cd01472   149 IASDPKElyVFNV 161
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 569-734 6.99e-11

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 62.80  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASISDLIwrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQTKINDLKRdyRS 648
Cdd:cd01476     2 DLLFVLDSSGSVRGKF--EKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLRF--IG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  649 GkKTYIIQALQYALTYYSKLSNRKEA-PKVTMLFTDGNdSYESEKGLQDIalLYRKENVKLLVVGV---STASENKLKML 724
Cdd:cd01476    78 G-TTATGAAIEVALQQLDPSEGRREGiPKVVVVLTDGR-SHDDPEKQARI--LRAVPNIETFAVGTgdpGTVDTEELHSI 153

                         170
                  ....*....|
gi 124504959  725 VGCAPNVVCP 734
Cdd:cd01476   154 TGNEDHIFTD 163
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 1.05e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 66.72  E-value: 1.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  359 EKPKPEVKPQP-EKPKPEVKPQP-ETPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPEK 415
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 569-724 2.09e-10

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 61.53  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEYTRdiVRFYDNARYEKGTLQTKINDLKrdYRS 648
Cdd:cd01482     2 DIVFLVDGSWSIGRSNF-NLVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPR--TEFDLNAYTSKEDVLAAIKNLP--YKG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959  649 GKkTYIIQALQYAL-TYYSKLSN-RKEAPKVTMLFTDGndsyESEKGLQDIALLYRKENVKLLVVGVSTASENKLKML 724
Cdd:cd01482    77 GN-TRTGKALTHVReKNFTPDAGaRPGVPKVVILITDG----KSQDDVELPARVLRNLGVNVFAVGVKDADESELKMI 149
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 2.65e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 65.56  E-value: 2.65e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  403 EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPET 459
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 1302-1460 2.65e-10

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: 61.15  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1302 LDIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEInkLPISYS 1381
Cdd:cd01450     1 LDIVFLLDGSESVGPENFE-KVKDFIEKLVEKLDIGPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKN--LKYLGG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1382 KKKDIAKSLKYVRTKVFKKSET--NRKKLIIMLVEGKSNSNmNDLRKEVGLLKVNNIDFFAYAIDNIDETEYKILGDCEG 1459
Cdd:cd01450    78 GGTNTGKALQYALEQLFSESNAreNVPKVIIVLTDGRSDDG-GDPKEAAAKLKDEGIKVFVVGVGPADEEELREIASCPS 156


                  .
gi 124504959 1460 S 1460
Cdd:cd01450   157 E 157
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 4.64e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 64.79  E-value: 4.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  414 EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-ETPKPEVKP 466
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 4.76e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 64.79  E-value: 4.76e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  381 ETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPEK 437
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 497-553 7.50e-10

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 64.02  E-value: 7.50e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  497 SVELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  324 QLEKPKPEVKPQP-EKPKPEVKPQL-ETPKPEVKPQP-EKPKPEvkpqpEKPKPEVKPQPET 382
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 752-837 1.19e-09

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 58.53  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   752 VKKICDNGVVLP-------PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPS 824
Cdd:pfam02389   21 TKEPCHSKVPEPcnpkvpePCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHPKAPEPCHPK 100

                           90
                   ....*....|...
gi 124504959   825 ESTPGSPSESTPC 837
Cdd:pfam02389  101 VPEPCYPKAPEPC 113
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1597-1646 1.94e-09

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 55.29  E-value: 1.94e-09
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1597 CGDFGEWSECSATCGEGIRVRNR----DNSLDNDDKCKLfNSTEMEACNIQECD 1646
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRsccsPPPQNGGGPCTG-EDVETRACNEQPCP 53
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 85-273 2.11e-09

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 59.71  E-value: 2.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNWKNhVIPFTDKIIKDLTISKNEVHVGILLFSS--KN----RDYVTYGDELRYQKDELlkkvekl 158
Cdd:cd01475     4 DLVFLIDSSRSVRPENFEL-VKQFLNQIIDSLDVGPDATRVGLVQYSStvKQefplGRFKSKADLKRAVRRME------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  159 kkdyYCGGGTKILGALKYSLEN-YTKHKNIR---YDAPKVTILFTDGNensaSNKQLLEMGLTYRRERVKLLVLGVAAAE 234
Cdd:cd01475    76 ----YLETGTMTGLAIQYAMNNaFSEAEGARpgsERVPRVGIVVTDGR----PQDDVSEVAAKARALGIEMFAVGVGRAD 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 124504959  235 DNKLKLIAgcEENTNCPYSMKAEWETINDITKRLTNKIC 273
Cdd:cd01475   148 EEELREIA--SEPLADHVFYVEDFSTIEELTKKFQGKIC 184
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 3.63e-09

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 61.71  E-value: 3.63e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPV-----EKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  392 EKPKPEVKPQP-EKPKPEvkpqpEKPKPEvkpqpEKPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKP 455
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 5.86e-09

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 60.94  E-value: 5.86e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPE-----ENPNPVEKPTPEEnPNPVEKPEPEK 553
Cdd:NF033839  425 EKPKPEVKPQP-EKPKPEVKPQP-EKPKPEvkpqpETPKPEVKPQPEK-PKPEVKPQPEK 481
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 849-996 9.93e-09

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 56.98  E-value: 9.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIRefIKYGQKESYDKNNLVRRIHDLKKYyks 928
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQK-VKNFLSTVMKKLDIGPTKTQFGLVQYSESFR--TEFTLNEYRTKEEPLSLVKHISQL--- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124504959  929 GGFSYIVEALKYGL-YSYAKSTSSRLNVPKVNILLTDGNNTDTSDfiLTEVSSLYKKENVKLLLIGIGG 996
Cdd:cd01469    76 LGLTNTATAIQYVVtELFSESNGARKDATKVLVVITDGESHDDPL--LKDVIPQAEREGIIRYAIGVGG 142
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 1.15e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 60.17  E-value: 1.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPV-----EKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  348 ETPKPEVKPQP-EKPKPEvkpqpEKPKPEvkpqpETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKP 411
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 1.56e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.78  E-value: 1.56e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPV-----EKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  315 ETPKPEVKPQL-EKPKPEvkpqpEKPKPEvkpqlETPKPEVKPQP-EKPKPEVKPQP-EKPKPEVKP 378
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 764-840 1.57e-08

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 55.06  E-value: 1.57e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959   764 PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTPCSGT 840
Cdd:pfam02389   48 PCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPCHPKAPEPCHPKVPEPCYPKAPEPCQPKVPEPCPST 124
TSP_1 pfam00090
Thrombospondin type 1 domain;
1598-1645 1.60e-08

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 52.42  E-value: 1.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 124504959  1598 GDFGEWSECSATCGEGIRVRNR--DNSLDNDDKCKLfNSTEMEACNIQEC 1645
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQRtcKSPFPGGEPCTG-DDIETQACKMDKC 49
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 2.31e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.01  E-value: 2.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPVEKPTPEE-----NPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  370 EKPKPEVKPQP-ETPKPEvkpqpEKPKPEVKPQPEKpkpevKPQP-EKPKPEVKPQP-EKPKPEVKP 433
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 497-553 2.81e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 59.01  E-value: 2.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  497 SVELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPE-----ENPNPVEKPEPEK 553
Cdd:NF033839  302 SPQPEKKEVKPEP-ETPKPEVKPQL-EKPKPEVKPQP-EKPKPEvkpqlETPKPEVKPQPEK 360
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 305-461 3.23e-08

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 55.44  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKDkygY 384
Cdd:cd01469     2 DIVFVLDGSGSIYPDDFQK-VKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNEYRT--KEEPLSLVKHISQ---L 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  385 GGATHLVDALQYSLKTFTRHPNN-RVDAPKVTILFTDGNetSKKEKDIRDVGLLYRKENVKLIVVGVNLA--TEKSLKLL 461
Cdd:cd01469    76 LGLTNTATAIQYVVTELFSESNGaRKDATKVLVVITDGE--SHDDPLLKDVIPQAEREGIIRYAIGVGGHfqRENSREEL 153
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 305-493 4.22e-08

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 55.85  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRymKNDLIKLVRELKdKYGY 384
Cdd:cd01475     4 DLVFLIDSSRSVRPENFEL-VKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQEFPLGRFKS--KADLKRAVRRME-YLET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  385 GGATHLvdALQYSL-KTFTRHPNNR---VDAPKVTILFTDGnetsKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKL 460
Cdd:cd01475    80 GTMTGL--AIQYAMnNAFSEAEGARpgsERVPRVGIVVTDG----RPQDDVSEVAAKARALGIEMFAVGVGRADEEELRE 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 124504959  461 LAGCTENEECLRVikCEWNDLTNITKILTDKIC 493
Cdd:cd01475   154 IASEPLADHVFYV--EDFSTIEELTKKFQGKIC 184
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-555 5.20e-08

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 57.86  E-value: 5.20e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  499 ELPKPEENPEPvEKPNPEENPNPvEKPTPEENPNPvEKPTPEENPNPvEKPEPEKNP 555
Cdd:NF033839  293 SAPKPGMQPSP-QPEKKEVKPEP-ETPKPEVKPQL-EKPKPEVKPQP-EKPKPEVKP 345
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1598-1645 5.57e-08

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 51.13  E-value: 5.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 124504959  1598 GDFGEWSECSATCGEGIRVRNRD---NSLDNDDKCKlfNSTEMEACNIQEC 1645
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRTRTvivEPQNGGRPCP--ELLERRPCNLPPC 52
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
 763-835 1.30e-07

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 53.80  E-value: 1.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959   763 PPgsPSESTPGSPSESTPGSPSESTPGSPS-ESTPGNPSES-TPGSPSESTPGNPSESTPG-SPSESTPGSPSEST 835
Cdd:pfam09595   68 PP--LNEAAKEAPSESEDAPDIDPNNQHPSqDRSEAPPLEPaAKTKPSEHEPANPPDASNRlSPPDASTAAIREAR 141
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 849-969 1.42e-07

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 53.17  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIG-----YSNWEKEVVpftiglaSNLEISEKKVNMGILLFSDKIREFIKYGQKESYDKNNLVRRIHDLK 923
Cdd:cd01476     2 DLLFVLDSSGSVRgkfekYKKYIERIV-------EGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLR 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 124504959  924 KYyksGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTD 969
Cdd:cd01476    75 FI---GGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDGRSHD 117
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 763-837 1.43e-07

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 52.36  E-value: 1.43e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959   763 PPGSPSESTPGSPSEST---PGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTPC 837
Cdd:pfam02389   12 PPQEPCVPTTKEPCHSKvpePCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCYPKVPEPCSPKVPEPC 89
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 499-553 1.50e-07

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 56.70  E-value: 1.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  499 ELPKPEENPEPvEKPNPE-----ENPNPVEKPTPeENPNPVEKPTPEEnPNPVEKPEPEK 553
Cdd:NF033839  337 EKPKPEVKPQL-ETPKPEvkpqpEKPKPEVKPQP-EKPKPEVKPQPET-PKPEVKPQPEK 393
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 85-242 1.56e-07

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 53.54  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNW---KNHVIPFTDKIIKD--LTISKNEVHVGILLFSSKNRDYVTYGDELRYQKDELLKKVEKLk 159
Cdd:cd01480     4 DITFVLDSSESVGLQNFditKNFVKRVAERFLKDyyRKDPAGSWRVGVVQYSDQQEVEAGFLRDIRNYTSLKEAVDNLE- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  160 kdyYCGGGTKILGALKYSLENYTKHKniRYDAPKVTILFTDGNENSASNKQLLEMGLTYRRERVKLLVLGVAAAEDNKLK 239
Cdd:cd01480    83 ---YIGGGTFTDCALKYATEQLLEGS--HQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQNEEPLS 157


                  ...
gi 124504959  240 LIA 242
Cdd:cd01480   158 RIA 160
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1806-1863 1.73e-07

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 49.51  E-value: 1.73e-07
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959   1806 CGDWSDWSECDRTCNVGVRIRHFISHMFDmvGDEDEKECLEyyNKVETQDClHLPPCD 1863
Cdd:smart00209    1 WSEWSEWSPCSVTCGGGVQTRTRSCCSPP--PQNGGGPCTG--EDVETRAC-NEQPCP 53
PRK10819 PRK10819
transport protein TonB; Provisional
 501-555 2.01e-07

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 54.30  E-value: 2.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 124504959  501 PKPEENPEPVEKPNPEENPnPVEKPTPEENPNPVEKPTPEENPNPVEK----PEPEKNP 555
Cdd:PRK10819   66 PPPEPVVEPEPEPEPIPEP-PKEAPVVIPKPEPKPKPKPKPKPKPVKKveeqPKREVKP 123
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 498-719 2.48e-07

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 54.17  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  498 VELPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEENPNPVEKPEPEKNPCINMEDCYCKDFYDITLVLDES 577
Cdd:COG1240    23 LLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDAS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  578 ASISDLIWRNEVIPFSLEIIKRINisyKNVHMGVLLFSEYTRDIVRFydnaRYEKGTLQTKINDLKrdyrSGKKTYIIQA 657
Cdd:COG1240   103 GSMAAENRLEAAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPL----TRDREALKRALDELP----PGGGTPLGDA 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  658 LQYALTYYSklSNRKEAPKVTMLFTDGNDSyESEKGLQDIALLYRKENVKLLVVGVSTASEN 719
Cdd:COG1240   172 LALALELLK--RADPARRKVIVLLTDGRDN-AGRIDPLEAAELAAAAGIRIYTIGVGTEAVD 230
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1654-1703 4.08e-07

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 48.43  E-value: 4.08e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 124504959  1654 CEdIGEWSDWSSCSKTCGYSTRSRTFTIL--PEYIGEypNCKifERSETEVC 1703
Cdd:pfam19028    1 CV-VSEWSEWSECSVTCGGGVQTRTRTVIvePQNGGR--PCP--ELLERRPC 47
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 849-1003 4.11e-07

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 53.16  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIGYSNWEKeVVPFTIGLASNLEISEKKVNMGILLFSDKIR-EFI--KYGQKESYDKnnLVRRIHDLKKY 925
Cdd:cd01475     4 DLVFLIDSSRSVRPENFEL-VKQFLNQIIDSLDVGPDATRVGLVQYSSTVKqEFPlgRFKSKADLKR--AVRRMEYLETG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  926 YKSGgfsyivEALKYGL---YSYAK-STSSRLNVPKVNILLTDGNNTDTsdfiLTEVSSLYKKENVKLLLIGIGGPTIHK 1001
Cdd:cd01475    81 TMTG------LAIQYAMnnaFSEAEgARPGSERVPRVGIVVTDGRPQDD----VSEVAAKARALGIEMFAVGVGRADEEE 150


                  ..
gi 124504959 1002 LR 1003
Cdd:cd01475   151 LR 152
PRK11633 PRK11633
cell division protein DedD; Provisional
 500-555 1.14e-06

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 51.93  E-value: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959  500 LPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEenPNPVEKPEPEKNP 555
Cdd:PRK11633   90 VAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPA--PKPEPKPVVEEKA 143
PRK10819 PRK10819
transport protein TonB; Provisional
 501-553 1.16e-06

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 51.99  E-value: 1.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 124504959  501 PKPEENPEPVEKPNPEenPNPVEKPtPEENPNPVEKPTPEENPNPVEKPEPEK 553
Cdd:PRK10819   62 QAVQPPPEPVVEPEPE--PEPIPEP-PKEAPVVIPKPEPKPKPKPKPKPKPVK 111
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 763-838 1.27e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.02  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  763 PPGSPSESTPGSPSESTPgSPSESTPGSPSESTP-------GNPSESTPGSPSESTPGNPSESTPGSPSES---TPGSPS 832
Cdd:PHA03307  279 SSRPGPASSSSSPRERSP-SPSPSSPGSGPAPSSprassssSSSRESSSSSTSSSSESSRGAAVSPGPSPSrspSPSRPP 357


                  ....*.
gi 124504959  833 ESTPCS 838
Cdd:PHA03307  358 PPADPS 363
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 305-450 1.46e-06

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 50.09  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSitLDKWKKDVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDIGYEQETRYMKNDLIKLVRELKdkyGY 384
Cdd:cd01476     2 DLLFVLDSSGS--VRGKFEKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVRFNLPKHNDGEELLEKVDNLR---FI 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959  385 GGATHLVDALQYSLKTFTRHPNNRVDAPKVTILFTDGnETSKKEKDIRDVglLYRKENVKLIVVGV 450
Cdd:cd01476    77 GGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDG-RSHDDPEKQARI--LRAVPNIETFAVGT 139
Metaviral_G pfam09595
Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. ...
 753-835 1.65e-06

Metaviral_G glycoprotein; This is a viral attachment glycoprotein from region G of metaviruses. It is high in serine and threonine suggesting it is highly glycosylated.


Pssm-ID: 462833 [Multi-domain]  Cd Length: 183  Bit Score: 50.72  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   753 KKICDNGVVLPPGSPSESTPGSPSESTPgSPSESTPGSPSESTPG---NPSESTPG-SPSESTPGNPSESTpgSPSESTP 828
Cdd:pfam09595   41 KEAALIITDIIDININKQHPEQEHHENP-PLNEAAKEAPSESEDApdiDPNNQHPSqDRSEAPPLEPAAKT--KPSEHEP 117


                   ....*..
gi 124504959   829 GSPSEST 835
Cdd:pfam09595  118 ANPPDAS 124
rad23 TIGR00601
UV excision repair protein Rad23; All proteins in this family for which functions are known ...
 765-870 1.68e-06

UV excision repair protein Rad23; All proteins in this family for which functions are known are components of a multiprotein complex used for targeting nucleotide excision repair to specific parts of the genome. In humans, Rad23 complexes with the XPC protein. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273167 [Multi-domain]  Cd Length: 378  Bit Score: 52.59  E-value: 1.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   765 GSPSESTPGSPSESTPgSPSESTPGSPSESTPGNPSEST-PGSPSESTPGNPSESTPgSPSESTPGSPSESTPCSGTEcl 843
Cdd:TIGR00601   80 GTGKVAPPAATPTSAP-TPTPSPPASPASGMSAAPASAVeEKSPSEESATATAPESP-STSVPSSGSDAASTLVVGSE-- 155

                           90       100
                   ....*....|....*....|....*..
gi 124504959   844 chntYDLTliIDESASIGYsnwEKEVV 870
Cdd:TIGR00601  156 ----RETT--IEEIMEMGY---EREEV 173
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 497-555 2.50e-06

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: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 52.46  E-value: 2.50e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124504959  497 SVELPKPEENPEPvEKPNPE-----ENPNPVEKPTPEEnPNPVEKPTPEENPNPVEKPEPE-KNP 555
Cdd:NF033839  434 QPEKPKPEVKPQP-EKPKPEvkpqpETPKPEVKPQPEK-PKPEVKPQPEKPKPDNSKPQADdKKP 496
TSP1_ADAMTS pfam19030
Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found ...
 1601-1645 3.80e-06

Thrombospondin type 1 domain; This subfamily of thrombospondin type 1 repeats are mainly found in ADAMTS proteins.


Pssm-ID: 465950 [Multi-domain]  Cd Length: 55  Bit Score: 45.91  E-value: 3.80e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 124504959  1601 GEWSECSATCGEGIRVRN------RDNSLDNDDKCKLFNS-TEMEACNIQEC 1645
Cdd:pfam19030    4 GPWGECSVTCGGGVQTRLvqcvqkGGGSIVPDSECSAQKKpPETQSCNLKPC 55
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1939-2002 4.97e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 45.66  E-value: 4.97e-06
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1939 CNEWEEWGDCSSTCGEGsfkIRKRKEPLELIPASQDingniGLTCAQQNikvEEREACIVPACE 2002
Cdd:smart00209    1 WSEWSEWSPCSVTCGGG---VQTRTRSCCSPPPQNG-----GGPCTGED---VETRACNEQPCP 53
Neisseria_TspB pfam05616
Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis ...
 500-555 4.98e-06

Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis TspB virulence factor proteins.


Pssm-ID: 283306 [Multi-domain]  Cd Length: 517  Bit Score: 51.63  E-value: 4.98e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959   500 LPKPEENPEPVEKPN----PEENP--NPVEKPTPEENPNPVEKPTPEENPNPVEKPEPEKNP 555
Cdd:pfam05616  325 IPRPDLTPASAEAPHaqplPEVSPaeNPANNPDPDENPGTRPNPEPDPDLNPDANPDTDGQP 386
Cornifin pfam02389
Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small ...
 772-837 6.68e-06

Cornifin (SPRR) family; SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteriztic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.


Pssm-ID: 280537 [Multi-domain]  Cd Length: 135  Bit Score: 47.74  E-value: 6.68e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959   772 PGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTPC 837
Cdd:pfam02389    8 PCQPPPQEPCVPTTKEPCHSKVPEPCNPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPCCPKVPEPC 73
TSP1 smart00209
Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.
 1658-1710 8.44e-06

Thrombospondin type 1 repeats; Type 1 repeats in thrombospondin-1 bind and activate TGF-beta.


Pssm-ID: 214559 [Multi-domain]  Cd Length: 53  Bit Score: 44.89  E-value: 8.44e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 124504959   1658 GEWSDWSSCSKTCGYSTRSRT-FTILPEYIGEYPNCKIfERSETEVCaFIPACS 1710
Cdd:smart00209    2 SEWSEWSPCSVTCGGGVQTRTrSCCSPPPQNGGGPCTG-EDVETRAC-NEQPCP 53
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 368-462 8.79e-06

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 49.55  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  368 KNDLIKLVRELKdkygYGGATHLVDALQYSLKTFTRHPNNRvdaPKVTILFTDGNETSKKEkDIRDVGLLYRKENVKLIV 447
Cdd:COG1240   150 REALKRALDELP----PGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGRDNAGRI-DPLEAAELAAAAGIRIYT 221

                          90
                  ....*....|....*..
gi 124504959  448 VGVNLAT--EKSLKLLA 462
Cdd:COG1240   222 IGVGTEAvdEGLLREIA 238
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 564-756 9.75e-06

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 48.28  E-value: 9.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  564 CKDFYDITLVLDESASISDlIWrNEVIPFSLEIIKRINISykNVHMGVLLFSEYTRDIVRFYDNARYEKGTLQtkinDLK 643
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVAA-NW-IEIYDFVEQLVDRFNSP--GLRFSFITFSTRATKILPLTDDSSAIIKGLE----VLK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  644 RDYRSGkKTYIIQALQYA--LTYYSKLSNRKEApKVTMLFTDGNDSYESEKGLQDIALLYRKENVKLLVVGVSTASENKL 721
Cdd:cd01474    73 KVTPSG-QTYIHEGLENAneQIFNRNGGGRETV-SVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQL 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 124504959  722 KMLVGCAPNVvcpFVIKTEWGLLKNVSEVFVKKIC 756
Cdd:cd01474   151 INIADSKEYV---FPVTSGFQALSGIIESVVKKAC 182
vWA_CTRP cd01473
CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an ...
 1303-1502 1.26e-05

CTRP for CS protein-TRAP-related protein: Adhesion of Plasmodium to host cells is an important phenomenon in parasite invasion and in malaria associated pathology.CTRP encodes a protein containing a putative signal sequence followed by a long extracellular region of 1990 amino acids, a transmembrane domain, and a short cytoplasmic segment. The extracellular region of CTRP contains two separated adhesive domains. The first domain contains six 210-amino acid-long homologous VWA domain repeats. The second domain contains seven repeats of 87-60 amino acids in length, which share similarities with the thrombospondin type 1 domain found in a variety of adhesive molecules. Finally, CTRP also contains consensus motifs found in the superfamily of haematopoietin receptors. The VWA domains in these proteins likely mediate protein-protein interactions.


Pssm-ID: 238750 [Multi-domain]  Cd Length: 192  Bit Score: 48.08  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1303 DIAVVLDQSSNISKDQWNVYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEINKLPISY-- 1380
Cdd:cd01473     2 DLTLILDESASIGYSNWRKDVIPFTEKIINNLNISKDKVHVGILLFAEKNRDVVPFSDEERYDKNELLKKINDLKNSYrs 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1381 SKKKDIAKSLKYVRTKVFKK--SETNRKKLIIMLVEGKSNSNMNDLRKEVGLL-KVNNIDFFAYAIDNIDETEYKILGDC 1457
Cdd:cd01473    82 GGETYIVEALKYGLKNYTKHgnRRKDAPKVTMLFTDGNDTSASKKELQDISLLyKEENVKLLVVGVGAASENKLKLLAGC 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 124504959 1458 EgsvdmglMGNSppspsylPCKNIVKVSWDTLLSSTDIHMKYICN 1502
Cdd:cd01473   162 D-------INND-------NCPNVIKTEWNNLNGISKFLTDKICD 192
vWA_collagen_alphaI-XII-like cd01482
Collagen: The extracellular matrix represents a complex alloy of variable members of diverse ...
 1303-1456 1.60e-05

Collagen: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238759 [Multi-domain]  Cd Length: 164  Bit Score: 47.28  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKkisyqkkkiikeinklpisYSK 1382
Cdd:cd01482     2 DIVFLVDGSWSIGRSNFN-LVRSFLSSVVEAFEIGPDGVQVGLVQYSDDPRTEFDLNA-------------------YTS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1383 KKDI----------------AKSLKYVRTKVFKKSETNRK---KLIIMLVEGKSNSNMNDLRKEvglLKVNNIDFFAYAI 1443
Cdd:cd01482    62 KEDVlaaiknlpykggntrtGKALTHVREKNFTPDAGARPgvpKVVILITDGKSQDDVELPARV---LRNLGVNVFAVGV 138

                         170
                  ....*....|...
gi 124504959 1444 DNIDETEYKILGD 1456
Cdd:cd01482   139 KDADESELKMIAS 151
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 762-836 1.73e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124504959  762 LPPGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSEStpgnPSESTPGSPSESTPGSPSESTP 836
Cdd:PHA03307  308 APSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP----PPPADPSSPRKRPRPSRAPSSP 378
PRK11633 PRK11633
cell division protein DedD; Provisional
 501-548 1.88e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 48.08  E-value: 1.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 124504959  501 PKPEENPE--PVEKPNPEENPNPVEKPTPEenPNPVEKPTPEENPNPVEK 548
Cdd:PRK11633  101 PAPVEPPKpkPVEKPKPKPKPQQKVEAPPA--PKPEPKPVVEEKAAPTGK 148
PRK10819 PRK10819
transport protein TonB; Provisional
 497-555 1.96e-05

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 48.14  E-value: 1.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124504959  497 SVELPKPEE-------NPEPVEKPNPEE-NPNPVEKPTPEenPNPVEKPTPEE-------NPNPVEKPEPEKNP 555
Cdd:PRK10819   38 VIELPAPAQpisvtmvAPADLEPPQAVQpPPEPVVEPEPE--PEPIPEPPKEApvvipkpEPKPKPKPKPKPKP 109
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 85-201 2.72e-05

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 46.62  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNwkNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYV-------TYGDELRYQKDELLKKvek 157
Cdd:cd01476     2 DLLFVLDSSGSVRGKF--EKYKKYIERIVEGLEIGPTATRVALITYSGRGRQRVrfnlpkhNDGEELLEKVDNLRFI--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 124504959  158 lkkdyycGGGTKILGALKYSLENYTKHKNIRYDAPKVTILFTDG 201
Cdd:cd01476    77 -------GGTTATGAAIEVALQQLDPSEGRREGIPKVVVVLTDG 113
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 569-721 3.30e-05

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 46.61  E-value: 3.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASISDL---IWRN---EVIPFSLEIIKRiNISYKNVHMGVLLFSeytrdivrfyDNARYEKGTLQTKIN-- 640
Cdd:cd01480     4 DITFVLDSSESVGLQnfdITKNfvkRVAERFLKDYYR-KDPAGSWRVGVVQYS----------DQQEVEAGFLRDIRNyt 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  641 DLKRDYRS----GKKTYIIQALQYALTYYSKLSNRKEApKVTMLFTDGNDSYESEKGLQDIALLYRKENVKLLVVGVSTA 716
Cdd:cd01480    73 SLKEAVDNleyiGGGTFTDCALKYATEQLLEGSHQKEN-KFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVGSQ 151


                  ....*
gi 124504959  717 SENKL 721
Cdd:cd01480   152 NEEPL 156
PRK10819 PRK10819
transport protein TonB; Provisional
 501-555 3.44e-05

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 47.75  E-value: 3.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  501 PKPEENPEPVEKPNPEE-------NPNPVEKPTPEenPNPVEKptPEENPNPVEKPePEKNP 555
Cdd:PRK10819   72 VEPEPEPEPIPEPPKEApvvipkpEPKPKPKPKPK--PKPVKK--VEEQPKREVKP-VEPRP 128
PRK11633 PRK11633
cell division protein DedD; Provisional
 501-555 3.88e-05

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 47.30  E-value: 3.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 124504959  501 PKPEENPEPVEKPNPEENPNPVEKPTPEenPNPVEKPTPEENPNPVEKPEPEKNP 555
Cdd:PRK11633   81 AAPSLDPATVAPPNTPVEPEPAPVEPPK--PKPVEKPKPKPKPQQKVEAPPAPKP 133
PTZ00441 PTZ00441
sporozoite surface protein 2 (SSP2); Provisional
 1297-1523 4.58e-05

sporozoite surface protein 2 (SSP2); Provisional


Pssm-ID: 240420 [Multi-domain]  Cd Length: 576  Bit Score: 48.42  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1297 ICTKVLDIAVVLDQSSNISKDQWNVYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEINKL 1376
Cdd:PTZ00441   38 VCNEEVDLYLLVDGSGSIGYHNWITHVIPMLMGLIQQLNLSDDAINLYMSLFSNNTTELIRLGSGASKDKEQALIIVKSL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1377 PISYSK--KKDIAKSLKYVRTKVfkKSETNRKK---LIIMLVEGKSNSNMNDLrKEVGLLKVNNIDFFAYAI-DNIDETE 1450
Cdd:PTZ00441  118 RKTYLPygKTNMTDALLEVRKHL--NDRVNRENaiqLVILMTDGIPNSKYRAL-EESRKLKDRNVKLAVIGIgQGINHQF 194

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124504959 1451 YKILGDCEgsvdmglmgnsppsPSYLPCKNIVKVSWDTLLSSTDIHMKYICNGYPEDAECSEWEEWSPCPETC 1523
Cdd:PTZ00441  195 NRLLAGCR--------------PREGKCKFYSDADWEEAKNLIKPFIAKVCTEVERTASCGPWDEWTPCSVTC 253
PRK10819 PRK10819
transport protein TonB; Provisional
 498-554 6.80e-05

transport protein TonB; Provisional


Pssm-ID: 236768 [Multi-domain]  Cd Length: 246  Bit Score: 46.60  E-value: 6.80e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  498 VELPKPEENPEPVEKPNPEenpnPVEKptPEENPNPVEKPTPEENPNPVEKPEPEKN 554
Cdd:PRK10819   90 VVIPKPEPKPKPKPKPKPK----PVKK--VEEQPKREVKPVEPRPASPFENTAPARP 140
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1807-1827 6.85e-05

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 42.27  E-value: 6.85e-05
                           10        20
                   ....*....|....*....|.
gi 124504959  1807 GDWSDWSECDRTCNVGVRIRH 1827
Cdd:pfam19028    4 SEWSEWSECSVTCGGGVQTRT 24
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 305-476 7.24e-05

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 45.84  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITL---DKWKKDVVPFAEKVLNNLNIDK--DKIHVGIMRFAKSMKTDIGYEQETRYMKnDLIKLVRELK 379
Cdd:cd01480     4 DITFVLDSSESVGLqnfDITKNFVKRVAERFLKDYYRKDpaGSWRVGVVQYSDQQEVEAGFLRDIRNYT-SLKEAVDNLE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  380 dkyGYGGATHLVDALQYSLKTFTRHPnnRVDAPKVTILFTDGNETSKKEKDIRDVGLLYRKENVKLIVVGVNlatekslk 459
Cdd:cd01480    83 ---YIGGGTFTDCALKYATEQLLEGS--HQKENKFLLVITDGHSDGSPDGGIEKAVNEADHLGIKIFFVAVG-------- 149

                         170
                  ....*....|....*..
gi 124504959  460 llagcTENEECLRVIKC 476
Cdd:cd01480   150 -----SQNEEPLSRIAC 161
vWA_collagen_alpha_1-VI-type cd01480
VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable ...
 849-972 7.38e-05

VWA_collagen alpha(VI) type: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238757 [Multi-domain]  Cd Length: 186  Bit Score: 45.84  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  849 DLTLIIDESASIGYSNWE------KEVVPFTIGlASNLEISEKKVNMGILLFSDKIREFIKYGQkesydknnLVRRIHDL 922
Cdd:cd01480     4 DITFVLDSSESVGLQNFDitknfvKRVAERFLK-DYYRKDPAGSWRVGVVQYSDQQEVEAGFLR--------DIRNYTSL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 124504959  923 KKYYKS----GGFSYIVEALKYGLYSYAKstSSRLNVPKVNILLTDGnNTDTSD 972
Cdd:cd01480    75 KEAVDNleyiGGGTFTDCALKYATEQLLE--GSHQKENKFLLVITDG-HSDGSP 125
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 764-842 7.61e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.24  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  764 PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTP----GNPSESTPGSPSESTPGSPSESTPCSG 839
Cdd:PHA03307  266 PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRAssssSSSRESSSSSTSSSSESSRGAAVSPGP 345


                  ...
gi 124504959  840 TEC 842
Cdd:PHA03307  346 SPS 348
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 757-836 8.93e-05

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 47.31  E-value: 8.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  757 DNGVVLPPGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPsesTPGNPSESTPGSPSESTPGSPSESTP 836
Cdd:PHA03264  271 SGGSPAPPGDDRPEAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEP---KPGPPRPAPDADRPEGWPSLEAITFP 347
Neisseria_TspB pfam05616
Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis ...
 496-549 9.37e-05

Neisseria meningitidis TspB protein; This family consists of several Neisseria meningitidis TspB virulence factor proteins.


Pssm-ID: 283306 [Multi-domain]  Cd Length: 517  Bit Score: 47.40  E-value: 9.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 124504959   496 GSVELPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEENPNPVEKP 549
Cdd:pfam05616  333 ASAEAPHAQPLPEVSPAENPANNPDPDENPGTRPNPEPDPDLNPDANPDTDGQP 386
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 766-836 1.00e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 47.37  E-value: 1.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959  766 SPSESTPGSPSESTPGSPS----ESTPGSPSESTPGNPSESTPG-SPSESTPGNPSESTPGSPSESTPGSPSESTP 836
Cdd:PRK14959  415 TPSSAAPATPAPSAAPSPRvpwdDAPPAPPRSGIPPRPAPRMPEaSPVPGAPDSVASASDAPPTLGDPSDTAEHTP 490
PRK12495 PRK12495
hypothetical protein; Provisional
 764-840 1.19e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 45.63  E-value: 1.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959  764 PGSPSESTPgSPSESTPGSpSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSE-STPCSGT 840
Cdd:PRK12495  102 PAAEAEAAD-QSAPPEASS-TSATDEAATDPPATAAARDGPTPDPTAQPATPDERRSPRQRPPVSGEPPTpSTPDAHV 177
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 764-841 1.54e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 47.01  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  764 PGSPSESTPGS--PSESTPGSPSESTPGSPSESTPGNPSESTPGSPSE--STPGNPSESTPGSPSeSTPGSPSESTPCSG 839
Cdd:PLN02217  566 PGSTNSTPTGSaaSSNTTFSSDSPSTVVAPSTSPPAGHLGSPPATPSKivSPSTSPPASHLGSPS-TTPSSPESSIKVAS 644


                  ..
gi 124504959  840 TE 841
Cdd:PLN02217  645 TE 646
PLN02217 PLN02217
probable pectinesterase/pectinesterase inhibitor
 758-835 1.57e-04

probable pectinesterase/pectinesterase inhibitor


Pssm-ID: 215130 [Multi-domain]  Cd Length: 670  Bit Score: 47.01  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  758 NGVVLPPGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSE--STPGSPSESTPGNPSeSTPGSPSESTPGSPSEST 835
Cdd:PLN02217  570 NSTPTGSAASSNTTFSSDSPSTVVAPSTSPPAGHLGSPPATPSKivSPSTSPPASHLGSPS-TTPSSPESSIKVASTETA 648
PRK12495 PRK12495
hypothetical protein; Provisional
 766-836 2.51e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 44.86  E-value: 2.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  766 SPSESTPGSPSESTPGSPSESTPgSPSESTPGNpSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTP 836
Cdd:PRK12495   88 SDAGSQASPDDDAQPAAEAEAAD-QSAPPEASS-TSATDEAATDPPATAAARDGPTPDPTAQPATPDERRS 156
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 763-840 2.98e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  763 PPGSPSESTPGSPSESTPgsPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPG------------- 829
Cdd:PHA03307  100 PAREGSPTPPGPSSPDPP--PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASdaassrqaalpls 177

                          90
                  ....*....|.
gi 124504959  830 SPSESTPCSGT 840
Cdd:PHA03307  178 SPEETARAPSS 188
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 569-720 3.32e-04

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 43.50  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASISDLIWrNEVIPFSLEIIKRINISYKNVHMGVLLFSEytrDIVRFYDNARYEkgTLQTKINDLKRDYRS 648
Cdd:cd01469     2 DIVFVLDGSGSIYPDDF-QKVKNFLSTVMKKLDIGPTKTQFGLVQYSE---SFRTEFTLNEYR--TKEEPLSLVKHISQL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959  649 GKKTYIIQALQYALTYYSKLSN--RKEAPKVTMLFTDGN--DSYESEKGLQDIallyRKENVKLLVVGVSTASENK 720
Cdd:cd01469    76 LGLTNTATAIQYVVTELFSESNgaRKDATKVLVVITDGEshDDPLLKDVIPQA----EREGIIRYAIGVGGHFQRE 147
vWA_integrins_alpha_subunit cd01469
Integrins are a class of adhesion receptors that link the extracellular matrix to the ...
 85-242 3.35e-04

Integrins are a class of adhesion receptors that link the extracellular matrix to the cytoskeleton and cooperate with growth factor receptors to promote celll survival, cell cycle progression and cell migration. Integrins consist of an alpha and a beta sub-unit. Each sub-unit has a large extracellular portion, a single transmembrane segment and a short cytoplasmic domain. The N-terminal domains of the alpha and beta subunits associate to form the integrin headpiece, which contains the ligand binding site, whereas the C-terminal segments traverse the plasma membrane and mediate interaction with the cytoskeleton and with signalling proteins.The VWA domains present in the alpha subunits of integrins seem to be a chordate specific radiation of the gene family being found only in vertebrates. They mediate protein-protein interactions.


Pssm-ID: 238746 [Multi-domain]  Cd Length: 177  Bit Score: 43.50  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   85 DLTLILDESASIGSKNWkNHVIPFTDKIIKDLTISKNEVHVGILLFSSKNRDYVTYGDelrYQKDELLKKVEKLKKDYyc 164
Cdd:cd01469     2 DIVFVLDGSGSIYPDDF-QKVKNFLSTVMKKLDIGPTKTQFGLVQYSESFRTEFTLNE---YRTKEEPLSLVKHISQL-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  165 GGGTKILGALKYSL-ENYTKHKNIRYDAPKVTILFTDGN-ENSASNKQLLEMGltyRRERVKLLVLGVAAAEDNK----- 237
Cdd:cd01469    76 LGLTNTATAIQYVVtELFSESNGARKDATKVLVVITDGEsHDDPLLKDVIPQA---EREGIIRYAIGVGGHFQREnsree 152


                  ....*
gi 124504959  238 LKLIA 242
Cdd:cd01469   153 LKTIA 157
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 305-462 3.40e-04

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 43.47  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  305 DLTLILDESRSITLDKWKKdVVPFAEKVLNNLNIDKDKIHVGIMRFAKSMKTDigYEQETRYMKNDLIKLVRELKDKYGY 384
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFPA-IRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPE--FYLNTHSTKADVLGAVRRLRLRGGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  385 GGATHlvDALQYSLKT-FTRHPNNRVD--APKVTILFTDGnetsKKEKDIRDVGLLYRKENVKLIVVGVNLATEKSLKLL 461
Cdd:cd01481    79 QLNTG--SALDYVVKNlFTKSAGSRIEegVPQFLVLITGG----KSQDDVERPAVALKRAGIVPFAIGARNADLAELQQI 152


                  .
gi 124504959  462 A 462
Cdd:cd01481   153 A 153
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 762-999 4.43e-04

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 44.16  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  762 LPPGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTPCSGTe 841
Cdd:COG1240    15 LALLLLALLLPLLPLLLLPLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGR- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  842 clchntyDLTLIIDESASIGYSN-WE--KEVVpftIGLASNLEiseKKVNMGILLFSDKIREFIKYgqkeSYDKNNLVRR 918
Cdd:COG1240    94 -------DVVLVVDASGSMAAENrLEaaKGAL---LDFLDDYR---PRDRVGLVAFGGEAEVLLPL----TRDREALKRA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  919 IHDLKkyykSGGFSYIVEALKYGLYSYAKSTSSRlnvPKVNILLTDG-NNTDTSDfiLTEVSSLYKKENVKLLLIGIGGP 997
Cdd:COG1240   157 LDELP----PGGGTPLGDALALALELLKRADPAR---RKVIVLLTDGrDNAGRID--PLEAAELAAAAGIRIYTIGVGTE 227


                  ..
gi 124504959  998 TI 999
Cdd:COG1240   228 AV 229
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 765-836 5.65e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 5.65e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124504959  765 GSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSES---TPGNPSeSTPGSPSESTPGSPSESTP 836
Cdd:PHA03307   58 GAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREgspTPPGPS-SPDPPPPTPPPASPPPSPA 131
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 765-836 5.99e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 5.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124504959  765 GSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPGNPSESTPGSPSESTPGSPSESTP 836
Cdd:PHA03307  316 SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTR 387
TSP1_spondin pfam19028
Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an ...
 1941-2001 6.02e-04

Spondin-like TSP1 domain; This entry represents a sub-type of TSP1 domains that have an alternative disulphide binding pattern compared to the canonical TSP1 domain.


Pssm-ID: 465948  Cd Length: 52  Bit Score: 39.57  E-value: 6.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124504959  1941 EWEEWGDCSSTCGEGsFKIRKR---KEPLelipasqdiNGniGLTCAQQnikvEEREACIVPAC 2001
Cdd:pfam19028    5 EWSEWSECSVTCGGG-VQTRTRtviVEPQ---------NG--GRPCPEL----LERRPCNLPPC 52
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 764-831 6.92e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 44.67  E-value: 6.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124504959  764 PGSPSESTPGSPS----ESTPGSPSESTPGSPSESTPG-NPSESTPGSPSESTPGNPSESTPGSPSESTPGSP 831
Cdd:PRK14959  421 PATPAPSAAPSPRvpwdDAPPAPPRSGIPPRPAPRMPEaSPVPGAPDSVASASDAPPTLGDPSDTAEHTPSGP 493
PRK11633 PRK11633
cell division protein DedD; Provisional
 502-551 7.92e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 43.07  E-value: 7.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 124504959  502 KPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEENPNPVEKPEP 551
Cdd:PRK11633   86 DPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEP 135
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 764-832 9.27e-04

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 42.72  E-value: 9.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124504959  764 PGSPSESTPGSPSESTPGSPSESTPGSPSESTPGNPSESTPGSPSESTPgNPSESTPGSPSESTPGSPS 832
Cdd:cd21577    32 PPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPPQQRPLSPPLSLP-PPVAPPPLSPGSVPGGLPV 99
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 164-242 1.05e-03

vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];


Pssm-ID: 440853 [Multi-domain]  Cd Length: 262  Bit Score: 43.00  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  164 CGGGTKILGALKYSLEnytKHKNIRYDAPKVTILFTDGNENsASNKQLLEMGLTYRRERVKLLVLGVAAAEDNK--LKLI 241
Cdd:COG1240   162 PGGGTPLGDALALALE---LLKRADPARRKVIVLLTDGRDN-AGRIDPLEAAELAAAAGIRIYTIGVGTEAVDEglLREI 237


                  .
gi 124504959  242 A 242
Cdd:COG1240   238 A 238
VWA_2 pfam13519
von Willebrand factor type A domain;
308-418 1.15e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 40.35  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   308 LILDESRSIT---LDKWKKDVVP-FAEKVLNNLNIDKdkihVGIMRFAKSMKTDIGYeqetRYMKNDLIKLVRELKDKyg 383
Cdd:pfam13519    3 FVLDTSGSMRngdYGPTRLEAAKdAVLALLKSLPGDR----VGLVTFGDGPEVLIPL----TKDRAKILRALRRLEPK-- 72

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 124504959   384 yGGATHLVDALQYSLKTFtrhPNNRVDAPKVTILF 418
Cdd:pfam13519   73 -GGGTNLAAALQLARAAL---KHRRKNQPRRIVLI 103
TSP_1 pfam00090
Thrombospondin type 1 domain;
1807-1862 1.19e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.55  E-value: 1.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  1807 GDWSDWSECDRTCNVGVRIRH-FISHMFDmvgdeDEKECLEyyNKVETQDClHLPPC 1862
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQrTCKSPFP-----GGEPCTG--DDIETQAC-KMDKC 49
TSP_1 pfam00090
Thrombospondin type 1 domain;
1941-2001 1.45e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 38.55  E-value: 1.45e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124504959  1941 EWEEWGDCSSTCGEGSfKIRKRkepleLIPASQDINGNigltCAQqniKVEEREACIVPAC 2001
Cdd:pfam00090    2 PWSPWSPCSVTCGKGI-QVRQR-----TCKSPFPGGEP----CTG---DDIETQACKMDKC 49
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 763-839 1.63e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124504959  763 PPGSPSESTPGSPSESTPGSPSESTPGSPSEStpgnPSESTPGSPSESTPgnPSESTPGSPSESTPGSPSESTPCSG 839
Cdd:PHA03307   72 PPGPGTEAPANESRSTPTWSLSTLAPASPARE----GSPTPPGPSSPDPP--PPTPPPASPPPSPAPDLSEMLRPVG 142
vWA_micronemal_protein cd01471
Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a ...
 1302-1492 1.77e-03

Micronemal proteins: The Toxoplasma lytic cycle begins when the parasite actively invades a target cell. In association with invasion, T. gondii sequentially discharges three sets of secretory organelles beginning with the micronemes, which contain adhesive proteins involved in parasite attachment to a host cell. Deployed as protein complexes, several micronemal proteins possess vertebrate-derived adhesive sequences that function in binding receptors. The VWA domain likely mediates the protein-protein interactions of these with their interacting partners.


Pssm-ID: 238748 [Multi-domain]  Cd Length: 186  Bit Score: 41.60  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1302 LDIAVVLDQSSNISKDQWNVYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNKKISYQKKKIIKEINKLPISYS 1381
Cdd:cd01471     1 LDLYLLVDGSGSIGYSNWVTHVVPFLHTFVQNLNISPDEINLYLVTFSTNAKELIRLSSPNSTNKDLALNAIRALLSLYY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1382 KK--KDIAKSLKYVRTKVF--KKSETNRKKLIIMLVEGKSNsNMNDLRKEVGLLKVNNIDFFAYAIDN-IDETEYKILGD 1456
Cdd:cd01471    81 PNgsTNTTSALLVVEKHLFdtRGNRENAPQLVIIMTDGIPD-SKFRTLKEARKLRERGVIIAVLGVGQgVNHEENRSLVG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 124504959 1457 CegsvdmglmgnsppSPSYLPCKNIVKVSWDTLLSS 1492
Cdd:cd01471   160 C--------------DPDDSPCPLYLQSSWSEVQNV 181
PRK11633 PRK11633
cell division protein DedD; Provisional
 498-539 1.79e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 41.91  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 124504959  498 VELPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTP 539
Cdd:PRK11633  104 VEPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKPVVEEKAAP 145
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 844-996 2.35e-03

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 41.34  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  844 CHNTYDLTLIIDESASIGySNWeKEVVPFTIGLASnlEISEKKVNMGILLFSDkiREFIKYGQKEsyDKNNLVRRIHDLK 923
Cdd:cd01474     1 CAGHFDLYFVLDKSGSVA-ANW-IEIYDFVEQLVD--RFNSPGLRFSFITFST--RATKILPLTD--DSSAIIKGLEVLK 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124504959  924 KYyKSGGFSYIVEALKYGLYSYAKSTSSRLNVPKVNILLTDGNNTDTSDFILTEVSSLYKKENVKLLLIGIGG 996
Cdd:cd01474    73 KV-TPSGQTYIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTD 144
TSP1_CCN pfam19035
CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in ...
 1600-1645 2.48e-03

CCN3 Nov like TSP1 domain; This entry represents a sub-type of TSP1 domains found in matricellular CCN proteins that have an alternative disulphide binding pattern compared to the canonical TSP1 domains.


Pssm-ID: 465952  Cd Length: 44  Bit Score: 37.70  E-value: 2.48e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 124504959  1600 FGEWSECSATCGEGI--RVRNrdnsldNDDKCKLfnSTEMEACNIQEC 1645
Cdd:pfam19035    5 STEWSPCSKTCGMGVstRVSN------DNAECKL--VTETRLCQLRPC 44
VWA pfam00092
von Willebrand factor type A domain;
1091-1186 2.65e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 40.72  E-value: 2.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  1091 KNIMNSLVIDKNKVHVSLI---------ISLekksvhqgfddvNSY-NKNELIKTLGKLENSTVlNKTNILDSLVYGIQQ 1160
Cdd:pfam00092   25 KKLVESLDIGPDGTRVGLVqyssdvrteFPL------------NDYsSKEELLSAVDNLRYLGG-GTTNTGKALKYALEN 91

                           90       100
                   ....*....|....*....|....*...
gi 124504959  1161 SFGK--GNRENAPKVTMLLTNSNSDISD 1186
Cdd:pfam00092   92 LFSSaaGARPGAPKVVVLLTDGRSQDGD 119
VWA_integrin_invertebrates cd01476
VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have ...
 1084-1192 2.90e-03

VWA_integrin (invertebrates): Integrins are a family of cell surface receptors that have diverse functions in cell-cell and cell-extracellular matrix interactions. Because of their involvement in many biologically important adhesion processes, integrins are conserved across a wide range of multicellular animals. Integrins from invertebrates have been identified from six phyla. There are no data to date to suggest any immunological functions for the invertebrate integrins. The members of this sub-group have the conserved MIDAS motif that is charateristic of this domain suggesting the involvement of the integrins in the recognition and binding of multi-ligands.


Pssm-ID: 238753 [Multi-domain]  Cd Length: 163  Bit Score: 40.46  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1084 SDFMDCSKNIMNSLVIDKNKVHVSLII--SLEKKSVHQGFDDVNsyNKNELIKTLGKLEnsTVLNKTNILDSLVYGIQQ- 1160
Cdd:cd01476    18 EKYKKYIERIVEGLEIGPTATRVALITysGRGRQRVRFNLPKHN--DGEELLEKVDNLR--FIGGTTATGAAIEVALQQl 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 124504959 1161 SFGKGNRENAPKVTMLLTNSNSDISDEKALQD 1192
Cdd:cd01476    94 DPSEGRREGIPKVVVVLTDGRSHDDPEKQARI 125
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 569-782 3.59e-03

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 41.22  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  569 DITLVLDESASIsdliwRNE----VIPFSLEIIKRINISYKNVHMGVLLFSEYTRDivrfydnaRYEKGTLQTKiNDLKR 644
Cdd:cd01475     4 DLVFLIDSSRSV-----RPEnfelVKQFLNQIIDSLDVGPDATRVGLVQYSSTVKQ--------EFPLGRFKSK-ADLKR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959  645 DYRS----GKKTYIIQALQYALTY-YSKLSN----RKEAPKVTMLFTDGndsyESEKGLQDIALLYRKENVKLLVVGVST 715
Cdd:cd01475    70 AVRRmeylETGTMTGLAIQYAMNNaFSEAEGarpgSERVPRVGIVVTDG----RPQDDVSEVAAKARALGIEMFAVGVGR 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124504959  716 ASENKLKMLvgcAPNVVCPFVIKTE-WGLLKNVSEVFVKKICdngVVLPPGSPSESTPGSPSESTPGS 782
Cdd:cd01475   146 ADEEELREI---ASEPLADHVFYVEdFSTIEELTKKFQGKIC---VVPDLCATLSHVCQQVCISTPGS 207
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 1091-1191 3.88e-03

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: 40.52  E-value: 3.88e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959   1091 KNIMNSLVIDKNKVHVSLI-ISlekKSVHQGFDDVNSYNKNELIKTLGKLENSTvLNKTNILDSLVYGIQQSFGK--GNR 1167
Cdd:smart00327   25 LKLVEQLDIGPDGDRVGLVtFS---DDARVLFPLNDSRSKDALLEALASLSYKL-GGGTNLGAALQYALENLFSKsaGSR 100

                            90       100
                    ....*....|....*....|....
gi 124504959   1168 ENAPKVTMLLTNSNSDISDEKALQ 1191
Cdd:smart00327  101 RGAPKVVILITDGESNDGPKDLLK 124
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
483-558 4.62e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 41.87  E-value: 4.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124504959  483 NITKILTDKICNTGSVELPKPEENPEPVEKPNPEENPNPVEKPTPEENPNPVEKPTPEENPNPVEKPEPEKNPCIN 558
Cdd:PRK14948  364 FISEIANASAPANPTPAPNPSPPPAPIQPSAPKTKQAATTPSPPPAKASPPIPVPAEPTEPSPTPPANAANAPPSL 439
TSP_1 pfam00090
Thrombospondin type 1 domain;
1658-1678 5.44e-03

Thrombospondin type 1 domain;


Pssm-ID: 459668 [Multi-domain]  Cd Length: 49  Bit Score: 36.63  E-value: 5.44e-03
                           10        20
                   ....*....|....*....|.
gi 124504959  1658 GEWSDWSSCSKTCGYSTRSRT 1678
Cdd:pfam00090    1 SPWSPWSPCSVTCGKGIQVRQ 21
vWA_collagen_alpha3-VI-like cd01481
VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable ...
 1303-1450 7.96e-03

VWA_collagen alpha 3(VI) like: The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified thus far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. Some collagens have about 15-18 vWA domains in them. The VWA domains present in these collagens mediate protein-protein interactions.


Pssm-ID: 238758  Cd Length: 165  Bit Score: 39.23  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1303 DIAVVLDQSSNISKDQWNvYIKQFVINTVNQNYLSKYRSHITIVKMGKSTKEKWSLNkkisyqkkkiikeinklpiSYSK 1382
Cdd:cd01481     2 DIVFLIDGSDNVGSGNFP-AIRDFIERIVQSLDVGPDKIRVAVVQFSDTPRPEFYLN-------------------THST 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124504959 1383 KKDI-----------------AKSLKYVRTKVFKKSETNR-----KKLIIMLVEGKSnsnMNDLRKEVGLLKVNNIDFFA 1440
Cdd:cd01481    62 KADVlgavrrlrlrggsqlntGSALDYVVKNLFTKSAGSRieegvPQFLVLITGGKS---QDDVERPAVALKRAGIVPFA 138

                         170
                  ....*....|
gi 124504959 1441 YAIDNIDETE 1450
Cdd:cd01481   139 IGARNADLAE 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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