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Conserved domains on  [gi|1849067162|ref|XP_034802198|]
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neurocan core protein isoform X2 [Pan paniscus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1088-1211 5.16e-66

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


The actual alignment was detected with superfamily member cd03588:

Pssm-ID: 470576  Cd Length: 124  Bit Score: 218.60  E-value: 5.16e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSFGHENTWIGLNDRIVERDFQWTDNTGLQFE 1167
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1849067162 1168 NWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKG 1211
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 41-162 1.27e-63

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 409483  Cd Length: 121  Bit Score: 211.62  E-value: 1.27e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   41 KLGSGSVQAALAELVALPCLFTLQPQPSAARDAPRIKWTKVRTaSGQRQDLPILVAKDNVVKVAKSWQGRVSLPSYPRRR 120
Cdd:cd05902      1 RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLST-SGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1849067162  121 ANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05902     80 YNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 261-356 4.71e-57

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239597  Cd Length: 96  Bit Score: 191.76  E-value: 4.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 340
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1849067162  341 RTGFPSPAERFDAYCF 356
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 160-254 5.06e-56

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


:

Pssm-ID: 239594  Cd Length: 95  Bit Score: 188.77  E-value: 5.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRS 239
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1849067162  240 YGRRNPQELYDVYCF 254
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1215-1271 1.95e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


:

Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 63.25  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162 1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1046-1082 3.31e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.11  E-value: 3.31e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1849067162 1046 DIDDCL-CSPCENGGTCIDEVNGFVCLCLPSYGGSFCE 1082
Cdd:cd00054      1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
 568-1007 6.01e-08

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 57.30  E-value: 6.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  568 PPTMVPPSISGHSRAPVLELEKAEGPSARPATPdlfwSPLEATVSAPSPAPWEAFPVATSPDLPMMAMLRGPKEWMLPHP 647
Cdd:PRK07764   393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP----AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAP 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  648 TPISTEANRVEAHGEATTTAPPSPAAEtkvyslplsltptgqggEAMPTTPESPGADFRETGETSPAQVNKAEHSSSSPW 727
Cdd:PRK07764   469 APAAAPEPTAAPAPAPPAAPAPAAAPA-----------------APAAPAAPAGADDAATLRERWPEILAAVPKRSRKTW 531

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  728 PSVNRNVAVGFV--PTETATEPTGL---RGISGSESGVFDTAESPTSGLQATVDEVQDPWPSvySKGLGASSPSAPLGSP 802
Cdd:PRK07764   532 AILLPEATVLGVrgDTLVLGFSTGGlarRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG--AAGGEGPPAPASSGPP 609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  803 GVFLVPKVTPSLEPWVATDEGPTvnpmdstvTPAPSDASGIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKv 882
Cdd:PRK07764   610 EEAARPAAPAAPAAPAAPAPAGA--------AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA- 680

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  883 gvPAMSTLGSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSSTLLPV 962
Cdd:PRK07764   681 --PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1849067162  963 TLGIEDFELEVLAGSPGVESFWEEVASGEEPALPGTPMKAGAEEV 1007
Cdd:PRK07764   759 PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEE 803
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1012-1042 1.83e-07

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


:

Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.53  E-value: 1.83e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1849067162 1012 CENNPCLHGGTCNANGTMYGCSCDQGFAGEN 1042
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1088-1211 5.16e-66

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 218.60  E-value: 5.16e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSFGHENTWIGLNDRIVERDFQWTDNTGLQFE 1167
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1849067162 1168 NWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKG 1211
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 41-162 1.27e-63

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409483  Cd Length: 121  Bit Score: 211.62  E-value: 1.27e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   41 KLGSGSVQAALAELVALPCLFTLQPQPSAARDAPRIKWTKVRTaSGQRQDLPILVAKDNVVKVAKSWQGRVSLPSYPRRR 120
Cdd:cd05902      1 RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLST-SGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1849067162  121 ANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05902     80 YNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 261-356 4.71e-57

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 191.76  E-value: 4.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 340
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1849067162  341 RTGFPSPAERFDAYCF 356
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 160-254 5.06e-56

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239594  Cd Length: 95  Bit Score: 188.77  E-value: 5.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRS 239
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1849067162  240 YGRRNPQELYDVYCF 254
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
LINK smart00445
Link (Hyaluronan-binding);
159-255 1.73e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 1.73e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   159 GVVFHYRsARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDrssLPGVR 238
Cdd:smart00445    2 GGVFHVE-KNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGN---LPGVR 77

                            90
                    ....*....|....*..
gi 1849067162   239 SYGRRNPQELYDVYCFA 255
Cdd:smart00445   78 QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
260-357 2.41e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 149.80  E-value: 2.41e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   260 GEVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRtvyr 337
Cdd:smart00445    2 GGVFHVEKNGRykLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR---- 77

                            90       100
                    ....*....|....*....|
gi 1849067162   338 fanRTGFPSPAERFDAYCFR 357
Cdd:smart00445   78 ---QYGFPDPTSRYDAYCFN 94
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1088-1209 2.66e-41

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 147.75  E-value: 2.66e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF-----GHENTWIGLNDRIVERDFQWTDNT 1162
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLlknsgSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1849067162  1163 GL-QFENWRENQPDNffaGGEDCVVMVAHeSGRWNDVPCNYNLPYVCK 1209
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVLSTS-GGKWNDVSCTSKLPFVCE 124
Xlink pfam00193
Extracellular link domain;
261-356 6.10e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 140.02  E-value: 6.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTvyrf 338
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQ---- 76

                           90
                   ....*....|....*....
gi 1849067162  339 anrTGFPSP-AERFDAYCF 356
Cdd:pfam00193   77 ---YGFRDPlSERYDAYCY 92
Xlink pfam00193
Extracellular link domain;
160-254 2.75e-38

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 138.09  E-value: 2.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSaRDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRsslPGVRS 239
Cdd:pfam00193    1 GVFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1849067162  240 YGRR-NPQELYDVYCF 254
Cdd:pfam00193   77 YGFRdPLSERYDAYCY 92
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1109-1210 1.21e-29

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 113.73  E-value: 1.21e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1109 WEDAERDCRRRSGHLTSVHSSEEHSFINSF---GHENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPDNffAGGEDCV 1185
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTlkkSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENEDCV 81

                           90       100
                   ....*....|....*....|....*
gi 1849067162 1186 VMvAHESGRWNDVPCNYNLPYVCKK 1210
Cdd:pfam00059   82 EL-SSSSGKWNDENCNSKNPFVCEK 105
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1215-1271 1.95e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 63.25  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162 1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1046-1082 3.31e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.11  E-value: 3.31e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1849067162 1046 DIDDCL-CSPCENGGTCIDEVNGFVCLCLPSYGGSFCE 1082
Cdd:cd00054      1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1215-1271 6.79e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 56.00  E-value: 6.79e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162  1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
1215-1271 1.13e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.20  E-value: 1.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162 1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:pfam00084    1 CPPPPDIPNGKVSA-TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
1046-1082 1.64e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.18  E-value: 1.64e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1849067162  1046 DIDDCL-CSPCENGGTCIDEVNGFVCLCLPSY-GGSFCE 1082
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-158 2.68e-09

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 55.93  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   43 GSGSVQAALAELVALPCLFTlqpqPSAARDAPRIKWTKVRTasGQRQDLPILVAKDNVVKVAKswQGRVSLPSYPRRRaN 122
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTYS----SSMSEASTSVYWYRQPP--GKGPTFLIAYYSNGSEEGVK--KGRFSGRGDPSNG-D 72

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1849067162  123 ATLLLGPLRASDSGLYRCQVV-RGIEDEQDLVPLEVT 158
Cdd:pfam07686   73 GSLTIQNLTLSDSGTYTCAVIpSGEGVFGKGTRLTVL 109
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 568-1007 6.01e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 57.30  E-value: 6.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  568 PPTMVPPSISGHSRAPVLELEKAEGPSARPATPdlfwSPLEATVSAPSPAPWEAFPVATSPDLPMMAMLRGPKEWMLPHP 647
Cdd:PRK07764   393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP----AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAP 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  648 TPISTEANRVEAHGEATTTAPPSPAAEtkvyslplsltptgqggEAMPTTPESPGADFRETGETSPAQVNKAEHSSSSPW 727
Cdd:PRK07764   469 APAAAPEPTAAPAPAPPAAPAPAAAPA-----------------APAAPAAPAGADDAATLRERWPEILAAVPKRSRKTW 531

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  728 PSVNRNVAVGFV--PTETATEPTGL---RGISGSESGVFDTAESPTSGLQATVDEVQDPWPSvySKGLGASSPSAPLGSP 802
Cdd:PRK07764   532 AILLPEATVLGVrgDTLVLGFSTGGlarRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG--AAGGEGPPAPASSGPP 609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  803 GVFLVPKVTPSLEPWVATDEGPTvnpmdstvTPAPSDASGIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKv 882
Cdd:PRK07764   610 EEAARPAAPAAPAAPAAPAPAGA--------AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA- 680

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  883 gvPAMSTLGSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSSTLLPV 962
Cdd:PRK07764   681 --PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1849067162  963 TLGIEDFELEVLAGSPGVESFWEEVASGEEPALPGTPMKAGAEEV 1007
Cdd:PRK07764   759 PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEE 803
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1012-1042 1.83e-07

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.53  E-value: 1.83e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1849067162 1012 CENNPCLHGGTCNANGTMYGCSCDQGFAGEN 1042
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 665-998 3.13e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 51.50  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  665 TTAPPSP-----------------AAETKVYSLPLSlTPTGQGGEAMPTTPESPGAdfreTGETSPAQVNKAEHSSSSPW 727
Cdd:pfam17823   63 ATAAPAPvtltkgtsaahlnstevTAEHTPHGTDLS-EPATREGAADGAASRALAA----AASSSPSSAAQSLPAAIAAL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  728 PSVNRNVAVGFVPTETATeptglrgisGSESGVFDTAESPTSGLQATVDevqdpwpsvyskglGASSPSAPLGSPGVFLV 807
Cdd:pfam17823  138 PSEAFSAPRAAACRANAS---------AAPRAAIAAASAPHAASPAPRT--------------AASSTTAASSTTAASSA 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  808 PKVTPSLEPWVATDEGPTVNPMDSTVTPAPSDAS---GIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKVGV 884
Cdd:pfam17823  195 PTTAASSAPATLTPARGISTAATATGHPAAGTALaavGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGD 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  885 PAMSTLGSSSSQP------HPEPEDQVETQG-TSGASV--PPHQSSPLGKPA-----VPPGTPTAASVGESASVSSGEPT 950
Cdd:pfam17823  275 PHARRLSPAKHMPsdtmarNPAAPMGAQAQGpIIQVSTdqPVHNTAGEPTPSpsnttLEPNTPKSVASTNLAVVTTTKAQ 354

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1849067162  951 VPwDPSSTLLPVTLGIEDFELEVL--------------AGSPGVESFWEEVASgeePALPGT 998
Cdd:pfam17823  355 AK-EPSASPVPVLHTSMIPEVEATspttqpspllptqgAAGPGILLAPEQVAT---EATAGT 412
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1010-1044 3.23e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 3.23e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1849067162 1010 DPCE-NNPCLHGGTC-NANGTmYGCSCDQGFAGENCE 1044
Cdd:cd00054      3 DECAsGNPCQNGGTCvNTVGS-YRCSCPPGYTGRNCE 38
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1055-1074 3.13e-05

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 41.94  E-value: 3.13e-05
                           10        20
                   ....*....|....*....|
gi 1849067162 1055 CENGGTCIDEVNGFVCLCLP 1074
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPP 20
EGF_CA smart00179
Calcium-binding EGF-like domain;
1010-1044 2.37e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.54  E-value: 2.37e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1849067162  1010 DPCE-NNPCLHGGTC-NANGTmYGCSCDQGF-AGENCE 1044
Cdd:smart00179    3 DECAsGNPCQNGGTCvNTVGS-YRCECPPGYtDGRNCE 39
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1088-1162 3.32e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 43.57  E-value: 3.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF-GHENTWIGLNDRIVERDFQWTDNT 1162
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYkDSSDHWIGLNRESSNHPWKWADNS 163
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 110-625 3.16e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.17  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  110 RVSLPSYP-RRRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVFHYRSARDRYALTFAEAQEACRLSSAI 188
Cdd:COG3321    860 RVPLPTYPfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  189 IAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRSYGRRNPQELYDVYCFARELGGEVFYVGPA 268
Cdd:COG3321    940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  269 RRLTLAGARAqcrRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGFPSPA 348
Cdd:COG3321   1020 ALLALAALLA---AAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  349 ERFDAYCFRAHHPTSQHGDLETPSSGDEGEILSAEGPPVRELEPTLEEEEVVTPDFQEPLVSSGEEEPLILEEKQEsqqt 428
Cdd:COG3321   1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAA---- 1172

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  429 lsPTPGDPMLASWPTGEVWLSTVAPSPSDMGAGTAASSHTEVAPTDPMPRRRGRFKGLNGRYFQQQEPEPGLQGGMEASA 508
Cdd:COG3321   1173 --LLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  509 QPPTSEAAGNQMEPPLAMAVTEMLGSGQSRSPWADLTNEVDMPGAGSAGGKSSPEPWLWPPTMVPPSISGHSRAPVLELE 588
Cdd:COG3321   1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAAL 1330

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1849067162  589 KAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVA 625
Cdd:COG3321   1331 AALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAA 1367
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1088-1211 5.16e-66

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 218.60  E-value: 5.16e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSFGHENTWIGLNDRIVERDFQWTDNTGLQFE 1167
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1849067162 1168 NWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKG 1211
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 41-162 1.27e-63

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), neurocan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Unlike aggrecan which is widely distributed in connective tissue and extracellular matrices, neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409483  Cd Length: 121  Bit Score: 211.62  E-value: 1.27e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   41 KLGSGSVQAALAELVALPCLFTLQPQPSAARDAPRIKWTKVRTaSGQRQDLPILVAKDNVVKVAKSWQGRVSLPSYPRRR 120
Cdd:cd05902      1 RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLST-SGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1849067162  121 ANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05902     80 YNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 41-162 2.70e-62

Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in chondroitin sulfate proteoglycans (CSPGs) and human cartilage link protein (LP). Included in this group are the CSPGs aggrecan, versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. There is considerable evidence that HA-binding CSPGs are involved in developmental processes in the central nervous system. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409379  Cd Length: 123  Bit Score: 207.83  E-value: 2.70e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   41 KLGSGSVQAALAELVALPCLFTLQPQP-SAARDAPRIKWTKVRTASGQRQDLPILVAKDNVVKVAKSWQGRVSLPSYPRR 119
Cdd:cd05714      1 EAESAKVFSHLGGNVTLPCKFYRDPTAfGSGIHKIRIKWTKLTSDSGYLKEVDVLVAMGNVVYHKKTYGGRVSVPLKPGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1849067162  120 RANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05714     81 DSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 41-162 3.48e-62

Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core protein (CSPG); The members here are composed of the immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core proteins (CSPGs). Included in this group are the Ig domains of other CSPGs: versican, and neurocan. In CSPGs, this Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggrecan and versican have a wide distribution in connective tissue and extracellular matrices. Neurocan is localized almost exclusively in nervous tissue. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409462  Cd Length: 125  Bit Score: 207.86  E-value: 3.48e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   41 KLGSGSVQAALAELVALPCLFTLQPQP---SAARDAPRIKWTKVRTASGQRQDLPILVAKDNVVKVAKSWQGRVSLPSYP 117
Cdd:cd05878      1 IPQSSPVRVLLGTSVTLPCYFIDPPHPvtpSTAPLAPRIKWSKVSVDGKKEKEVVLLVATEGRVRVNSAYQGRVSLPNYP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1849067162  118 RRRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05878     81 AIPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Link_domain_CSPGs_modules_2_4 cd03520
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules ...
 261-356 4.71e-57

Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239597  Cd Length: 96  Bit Score: 191.76  E-value: 4.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 340
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1849067162  341 RTGFPSPAERFDAYCF 356
Cdd:cd03520     81 QTGFPDPHSRFDAYCF 96
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 160-254 5.06e-56

Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan. In addition, it is found in the first link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. In addition, aggrecan contains a second globular domain (G2) which contains link modules 3 and 4. G2 appears to lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 239594  Cd Length: 95  Bit Score: 188.77  E-value: 5.06e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRS 239
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1849067162  240 YGRRNPQELYDVYCF 254
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 160-254 8.69e-43

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 151.03  E-value: 8.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRsslPGVRS 239
Cdd:cd01102      1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRS 77

                           90
                   ....*....|....*
gi 1849067162  240 YGRRNPQELYDVYCF 254
Cdd:cd01102     78 YGNPAPSGRYDAYCF 92
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 1088-1210 8.81e-43

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 152.07  E-value: 8.81e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYrYFAH-RRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF--GHENTWIGLNDRIVERDFQWTDNTGL 1164
Cdd:cd03590      1 CPTNWKSFQSSCY-FFSTeKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIlsGNRSYWIGLSDEETEGEWKWVDGTPL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1849067162 1165 Q--FENWRENQPDNFFAGGEDCVVMVaHESGRWNDVPCNYNLPYVCKK 1210
Cdd:cd03590     80 NssKTFWHPGEPNNWGGGGEDCAELV-YDSGGWNDVPCNLEYRWICEK 126
LINK smart00445
Link (Hyaluronan-binding);
159-255 1.73e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 1.73e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   159 GVVFHYRsARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDrssLPGVR 238
Cdd:smart00445    2 GGVFHVE-KNGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGN---LPGVR 77

                            90
                    ....*....|....*..
gi 1849067162   239 SYGRRNPQELYDVYCFA 255
Cdd:smart00445   78 QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
260-357 2.41e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 149.80  E-value: 2.41e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   260 GEVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRtvyr 337
Cdd:smart00445    2 GGVFHVEKNGRykLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR---- 77

                            90       100
                    ....*....|....*....|
gi 1849067162   338 fanRTGFPSPAERFDAYCFR 357
Cdd:smart00445   78 ---QYGFPDPTSRYDAYCFN 94
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1088-1209 2.66e-41

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 147.75  E-value: 2.66e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF-----GHENTWIGLNDRIVERDFQWTDNT 1162
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLlknsgSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1849067162  1163 GL-QFENWRENQPDNffaGGEDCVVMVAHeSGRWNDVPCNYNLPYVCK 1209
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVLSTS-GGKWNDVSCTSKLPFVCE 124
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 1088-1209 5.51e-40

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 144.81  E-value: 5.51e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCR-----RRSGHLTSVHSSEEHSFINSF------GHENT--WIGLNDRIVER 1154
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVYDLfessrgPDTPYglWIGLHDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162 1155 DFQWTDNTGLQFENWRENQPDNFFaGGEDCVVMVAHES--GRWNDVPCNYNLPYVCK 1209
Cdd:cd03589     81 PFEWTDGSPVDFTKWAGGQPDNYG-GNEDCVQMWRRGDagQSWNDMPCDAVFPYICK 136
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1098-1210 8.36e-40

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 143.14  E-value: 8.36e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1098 HCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF----GHENTWIGLNDRIVERDFQWTDNTG-LQFENWREN 1172
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLlkksSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1849067162 1173 QPDNffAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKK 1210
Cdd:cd00037     81 EPNP--GGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
Xlink pfam00193
Extracellular link domain;
261-356 6.10e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 140.02  E-value: 6.10e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTvyrf 338
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQ---- 76

                           90
                   ....*....|....*....
gi 1849067162  339 anrTGFPSP-AERFDAYCF 356
Cdd:pfam00193   77 ---YGFRDPlSERYDAYCY 92
Xlink pfam00193
Extracellular link domain;
160-254 2.75e-38

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 138.09  E-value: 2.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSaRDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRsslPGVRS 239
Cdd:pfam00193    1 GVFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1849067162  240 YGRR-NPQELYDVYCF 254
Cdd:pfam00193   77 YGFRdPLSERYDAYCY 92
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 1088-1209 3.18e-32

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 122.10  E-value: 3.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRR--SGHLTSVHSSEEHSFINSF------GHENTWIGLNDRIVERDFQWT 1159
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLissyqkAYQPVWIGLHDPQQSRGWEWS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1849067162 1160 DNTGLQFENWRENQPdnfFAGGEDCVVMVAhESG--RWNDVPCNYNLPYVCK 1209
Cdd:cd03594     81 DGSKLDYRSWDRNPP---YARGGYCAELSR-STGflKWNDANCEERNPFICK 128
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 261-356 1.91e-31

The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It is found in the CD44 receptor and in human TSG-6. TSG-6 is the protein product of the tumor necrosis factor-stimulated gene-6. TSG-6 has a strong anti-inflammatory effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. This group also contains the link domains of the chondroitin sulfate proteoglycan core proteins (CSPG) including aggrecan, versican, neurocan, and brevican and the link domains of the vertebrate HAPLN (HA and proteoglycan binding link) protein family. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates in which other CSPGs substitute for aggregan might contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN gene family are physically linked adjacent to CSPG genes. TSG-6 contains a single link module which supports high affinity binding with HA. The functional HA-binding domain of CD44 is an extended domain comprised of a link module flanked with N-and C- extensions. These extensions are essential for folding and functional activity. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of the CSPG aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) which contains link modules 3 and 4 which lack HA-binding activity. HAPLNs contain two contiguous link modules.


Pssm-ID: 238534  Cd Length: 92  Bit Score: 118.68  E-value: 1.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPAR---RLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVyr 337
Cdd:cd01102      1 VVFHLESQNgryKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-- 78

                           90
                   ....*....|....*....
gi 1849067162  338 fanrtGFPSPAERFDAYCF 356
Cdd:cd01102     79 -----GNPAPSGRYDAYCF 92
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 261-356 2.38e-31

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 118.29  E-value: 2.38e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  261 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWH-EGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVyrfa 339
Cdd:cd03519      1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                           90
                   ....*....|....*...
gi 1849067162  340 nrtGFPSP-AERFDAYCF 356
Cdd:cd03519     77 ---GFPDKkHKLYGVYCY 91
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 160-254 4.62e-31

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 117.53  E-value: 4.62e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  160 VVFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCyGDRSSLPGVRS 239
Cdd:cd03518      1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                           90
                   ....*....|....*.
gi 1849067162  240 YGRRNPQE-LYDVYCF 254
Cdd:cd03518     80 YGERDKMLsRYDAFCF 95
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1109-1210 1.21e-29

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 113.73  E-value: 1.21e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1109 WEDAERDCRRRSGHLTSVHSSEEHSFINSF---GHENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPDNffAGGEDCV 1185
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTlkkSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENEDCV 81

                           90       100
                   ....*....|....*....|....*
gi 1849067162 1186 VMvAHESGRWNDVPCNYNLPYVCKK 1210
Cdd:pfam00059   82 EL-SSSSGKWNDENCNSKNPFVCEK 105
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 44-162 6.57e-28

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), versican. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, the CSPG aggrecan (not included in this group) forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Like aggrecan, versican has a wide distribution in connective tissue and extracellular matrices. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409482  Cd Length: 128  Bit Score: 109.66  E-value: 6.57e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   44 SGSVQAALAELVALPCLF----TLQPQPSAARDAPRIKWTKVRTASGQR--QDLPILVAKDNVVKVAKSWQGRVSLPSYP 117
Cdd:cd05901      4 SSRVHGSLSGSVVLPCRFstlpTLPPSYNITSEFLRIKWTKIQVDKNGKdhKETTVLVAQNGIIKIGQEYMGRVSVPSHP 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1849067162  118 RRRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05901     84 EDQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 270-356 2.19e-24

Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239595  Cd Length: 95  Bit Score: 98.65  E-value: 2.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  270 RLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGP--APGVRTVyrfanrtGFPSP 347
Cdd:cd03518     13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKrtVPGLRSY-------GERDK 85

                           90
                   ....*....|
gi 1849067162  348 AE-RFDAYCF 356
Cdd:cd03518     86 MLsRYDAFCF 95
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 1110-1208 2.77e-23

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 96.21  E-value: 2.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1110 EDAERDCRRRSGHLTSVHSSEEHSFINSF---GHENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPDNfFAGGEDCVV 1186
Cdd:cd03591     14 DDAQKLCSEAGGTLAMPRNAAENAAIASYvkkGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNN-AGGGEDCVE 92

                           90       100
                   ....*....|....*....|..
gi 1849067162 1187 MVAheSGRWNDVPCNYNLPYVC 1208
Cdd:cd03591     93 MYT--SGKWNDVACNLTRLFVC 112
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 51-162 3.46e-21

Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan; The members here are composed of the immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), aggrecan. In CSPGs, the Ig-like domain is followed by hyaluronan (HA)-binding tandem repeats, and a C-terminal region with epidermal growth factor-like, lectin-like, and complement regulatory protein-like domains. Separating these N- and C-terminal regions is a nonhomologous glycosaminoglycan attachment region. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggrecan has a wide distribution in connective tissue and extracellular matrices. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409481  Cd Length: 123  Bit Score: 90.38  E-value: 3.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   51 LAELVALPCLFTL-----QPQPSAARDAPRIKWTKVrtasGQRQDLPILVAKDNVVKVAKSWQGRVSLPSYPRRRANATL 125
Cdd:cd05900     11 LGSSLLIPCYFQDpiakdPGAPTVAPLSPRIKWSFI----SKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAIPSDATL 86

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1849067162  126 LLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05900     87 EITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 55-162 7.81e-20

Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The members here are composed of the immunoglobulin (Ig)-like domain similar to that found in human cartilage link protein (LP; also called hyaluronan and proteoglycan link protein). In cartilage, chondroitin-keratan sulfate proteoglycan (CSPG), aggrecan, forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.


Pssm-ID: 409461  Cd Length: 117  Bit Score: 86.23  E-value: 7.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   55 VALPCLFTLQPQPSAARDApRIKWTKVRTASGQRQDlpILVAKDNVVKVAKSWQGRVSLpsyprRRA---NATLLLGPLR 131
Cdd:cd05877     15 VTLPCRYHYEPELSAPRKI-RVKWTKLEVDYAKEED--VLVAIGTRHKSYGSYQGRVFL-----RRAddlDASLVITDLR 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1849067162  132 ASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 162
Cdd:cd05877     87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 173-254 8.76e-19

Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins similar to the vertebrate HAPLN (hyaluronan/HA and proteoglycan binding link) protein family which includes cartilage link protein. The link domain is a HA-binding domain. HAPLNs contain two contiguous link modules. Both link modules of cartilage link protein are involved in interaction with HA. In cartilage, a chondroitin sulfate proteoglycan core protein (CSPG) aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates with other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HAPLN gene family are physically linked adjacent to CSPG genes.


Pssm-ID: 239596  Cd Length: 91  Bit Score: 82.47  E-value: 8.76e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  173 LTFAEAQEACRLSSAIIAAPRHLQAAFE-DGFDNCDAGWLSDRTVRYPITQSRPGCYGDRsslPGVRSYGRRNPQE-LYD 250
Cdd:cd03519     11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGFPDKKHkLYG 87


                   ....
gi 1849067162  251 VYCF 254
Cdd:cd03519     88 VYCY 91
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 161-254 7.75e-18

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 79.82  E-value: 7.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  161 VFHYRSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSslpGVRSY 240
Cdd:cd03515      2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHV---GIVDY 78

                           90
                   ....*....|....*
gi 1849067162  241 G-RRNPQELYDVYCF 254
Cdd:cd03515     79 GpRLNLSERWDAYCY 93
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 1098-1207 1.39e-17

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 79.78  E-value: 1.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1098 HCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFI--NSFGHENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPD 1175
Cdd:cd03603      1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLlsNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1849067162 1176 NFFAGGEDCVVM--VAHESGRWNDVPCNYNLPYV 1207
Cdd:cd03603     81 NNGGGNEDYAAInhFPGISGKWNDLANSYNTLGY 114
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 1100-1208 1.89e-17

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 79.34  E-value: 1.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1100 YRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSFG----HENTWIGLNDRIVERDFQWTDNTGLQFENWRENQPD 1175
Cdd:cd03592      3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAlkynLGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1849067162 1176 NffAGGEDCVVMVAHESGRWNDVPCNYNLPYVC 1208
Cdd:cd03592     83 N--GRNENCLEIYIKDNGKWNDEPCSKKKSAIC 113
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 1088-1210 6.43e-15

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 72.36  E-value: 6.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF-GHENTWIGLNDRIVERDFQWTDNTglQF 1166
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQiGSSSYWIGLSREKSEKPWKWIDGS--PL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1849067162 1167 ENWRENQPDNffaGGEDCVVMvahESGRWNDVPCNYNLPYVCKK 1210
Cdd:cd03593     79 NNLFNIRGST---KSGNCAYL---SSTGIYSEDCSTKKRWICEK 116
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 1097-1208 5.25e-14

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 69.79  E-value: 5.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1097 GHCYRYFAHRRAWEDAERDCRR-RSGHLTSVHSSEEH----SFINSFGHENTWIG--LNDRIVERDFQWTDNTGLQFENW 1169
Cdd:cd03598      1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNyrvqRLVSTLNQAQVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1849067162 1170 RENQPDNffaGGEDCVVMVAHEsGRWNDVPCNYNLPYVC 1208
Cdd:cd03598     81 APGQPGN---RRGHCVELCTRG-GHWRRAHCKLRRPFIC 115
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 1088-1208 2.74e-13

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 68.18  E-value: 2.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGwHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFI-----NSFGHEN-TWIGLNDRIVERdfQWTDN 1161
Cdd:cd03596      1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALrdyvkASVPGNWeVWLGINDMVAEG--KWVDV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1849067162 1162 TGLQ--FENWREN---QPDnffaGG--EDCVVMVAHESGRWNDVPCNYNLPYVC 1208
Cdd:cd03596     78 NGSPisYFNWEREitaQPD----GGkrENCVALSSSAQGKWFDEDCRREKPYVC 127
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 1088-1209 8.12e-13

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 67.22  E-value: 8.12e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1088 CDRGwhkFQGHCYR--YF--AHRRA-WEDAERDCRRRSGHLTSVHSSEEHSFINSFGHE------NTWIGL---NDRIVE 1153
Cdd:cd03595      4 CRRG---TEKPCYKiaYFqdSRRRLnFEEARQACREDGGELLSIESENEQKLIERFIQTlrasdgDFWIGLrrsSQYNVT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1849067162 1154 RD-----FQWTDNTGLQFENWRENQPDnffAGGEDCVVMVAHESG----------RWNDVPCNYNLPYVCK 1209
Cdd:cd03595     81 SSacsslYYWLDGSISTFRNWYVDEPS---CGSEVCVVMYHQPSApagqggpylfQWNDDNCNMKNNFICK 148
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1215-1271 1.95e-12

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056 [Multi-domain]  Cd Length: 57  Bit Score: 63.25  E-value: 1.95e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162 1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Link_domain_TSG_6_like cd03515
This is the extracellular link domain of the type found in human TSG-6. The link domain is a ...
 270-356 9.82e-12

This is the extracellular link domain of the type found in human TSG-6. The link domain is a hyaluronan (HA)-binding domain. TSG-6 is the protein product of tumor necrosis factor-stimulated gene-6. TSG-6 is up-regulated in inflammatory lesions and in the ovary during ovulation. It has a strong anti-inflammatory and chondroprotective effect in models of acute inflammation and autoimmune arthritis and plays an essential role in female fertility. Also included in this group are the stabilins: stabilin-1 (FEEL-1, CLEVER-1) and stabilin-2 (FEEL-2). Stabilin-2 functions as the major liver and lymph node-scavenging receptor for HA and related glycosaminoglycans. Stabilin-2 is a scavenger receptor with a broad range of ligands including advanced glycation end (AGE) products, acetylated low density lipoprotein and procollagen peptides. In contrast, stabilin-1 does not bind HA, but binds acetylated low density lipoprotein and AGEs with lower affinity. As AGEs accumulate in vascular tissues during aging and diabetes, these receptors may be implicated in the pathologies of these states. Both stabilins are present in the early endocytic pathway in hepatic sinusoidal epithelium associating with clathrin/AP-2. Stabilin-1 is expressed in macrophages. Stabilin-2 is absent from the latter. In macrophages: stabilin-1 is involved in trafficking between early/sorting endosomes and the trans-Golgi network. Stabilin-1 has also been implicated in angiogenesis and possibly leucocyte trafficking. Both stabilins bind gram-positive and gram-negative bacteria. TSG-6 and stabilins contain a single link module which supports high affinity binding to HA.


Pssm-ID: 239592  Cd Length: 93  Bit Score: 62.48  E-value: 9.82e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  270 RLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVrTVYRF-ANRTgfpspa 348
Cdd:cd03515     13 KLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGI-VDYGPrLNLS------ 85


                   ....*...
gi 1849067162  349 ERFDAYCF 356
Cdd:cd03515     86 ERWDAYCY 93
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 1109-1208 1.62e-11

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 62.39  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1109 WEDAERDCRRRSGHLTSVHSSEEH----SFINSFGHEnTWIGLNDRIVErdFQWTDNTGLQFENWRENQPDnffaGGEDC 1184
Cdd:cd03602     12 WSEAQQYCRENYTDLATVQNQEDNallsNLSRVSNSA-AWIGLYRDVDS--WRWSDGSESSFRNWNTFQPF----GQGDC 84

                           90       100
                   ....*....|....*....|....
gi 1849067162 1185 VVMvaHESGRWNDVPCNYNLPYVC 1208
Cdd:cd03602     85 ATM--YSSGRWYAALCSALKPFIC 106
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1046-1082 3.31e-10

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 56.11  E-value: 3.31e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1849067162 1046 DIDDCL-CSPCENGGTCIDEVNGFVCLCLPSYGGSFCE 1082
Cdd:cd00054      1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1215-1271 6.79e-10

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478 [Multi-domain]  Cd Length: 56  Bit Score: 56.00  E-value: 6.79e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162  1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
1215-1271 1.13e-09

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 55.20  E-value: 1.13e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162 1215 CGPPPAVENASLIGaRKAKYNVHATVRYQCNEGFAQHHVATIRCRSNGKWDRPQIVC 1271
Cdd:pfam00084    1 CPPPPDIPNGKVSA-TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
1046-1082 1.64e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.18  E-value: 1.64e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1849067162  1046 DIDDCL-CSPCENGGTCIDEVNGFVCLCLPSY-GGSFCE 1082
Cdd:smart00179    1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 43-158 2.68e-09

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 55.93  E-value: 2.68e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   43 GSGSVQAALAELVALPCLFTlqpqPSAARDAPRIKWTKVRTasGQRQDLPILVAKDNVVKVAKswQGRVSLPSYPRRRaN 122
Cdd:pfam07686    2 TPREVTVALGGSVTLPCTYS----SSMSEASTSVYWYRQPP--GKGPTFLIAYYSNGSEEGVK--KGRFSGRGDPSNG-D 72

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1849067162  123 ATLLLGPLRASDSGLYRCQVV-RGIEDEQDLVPLEVT 158
Cdd:pfam07686   73 GSLTIQNLTLSDSGTYTCAVIpSGEGVFGKGTRLTVL 109
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 1096-1209 1.45e-08

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 54.74  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162 1096 QGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF----------GHENTWIGLNDRIVE--------RDFQ 1157
Cdd:cd03600      3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLlaagpgrhgrGSLRLWIGLQREPRQcsdpslplRGFS 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1849067162 1158 W-TDNTGLQFENWRENQPDNffAGGEDCVVMVAHESG----RWNDVPCNYNLP-YVCK 1209
Cdd:cd03600     83 WvTGDQDTDFSNWLQEPAGT--CTSPRCVALSAAGSTpdnlKWKDGPCSARADgYLCK 138
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 568-1007 6.01e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 57.30  E-value: 6.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  568 PPTMVPPSISGHSRAPVLELEKAEGPSARPATPdlfwSPLEATVSAPSPAPWEAFPVATSPDLPMMAMLRGPKEWMLPHP 647
Cdd:PRK07764   393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP----AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAP 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  648 TPISTEANRVEAHGEATTTAPPSPAAEtkvyslplsltptgqggEAMPTTPESPGADFRETGETSPAQVNKAEHSSSSPW 727
Cdd:PRK07764   469 APAAAPEPTAAPAPAPPAAPAPAAAPA-----------------APAAPAAPAGADDAATLRERWPEILAAVPKRSRKTW 531

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  728 PSVNRNVAVGFV--PTETATEPTGL---RGISGSESGVFDTAESPTSGLQATVDEVQDPWPSvySKGLGASSPSAPLGSP 802
Cdd:PRK07764   532 AILLPEATVLGVrgDTLVLGFSTGGlarRFASPGNAEVLVTALAEELGGDWQVEAVVGPAPG--AAGGEGPPAPASSGPP 609

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  803 GVFLVPKVTPSLEPWVATDEGPTvnpmdstvTPAPSDASGIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKv 882
Cdd:PRK07764   610 EEAARPAAPAAPAAPAAPAPAGA--------AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA- 680

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  883 gvPAMSTLGSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSSTLLPV 962
Cdd:PRK07764   681 --PPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQP 758

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1849067162  963 TLGIEDFELEVLAGSPGVESFWEEVASGEEPALPGTPMKAGAEEV 1007
Cdd:PRK07764   759 PPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEE 803
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1012-1042 1.83e-07

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 48.53  E-value: 1.83e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1849067162 1012 CENNPCLHGGTCNANGTMYGCSCDQGFAGEN 1042
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
PHA03247 PHA03247
large tegument protein UL36; Provisional
 421-964 2.15e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.71  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  421 EKQESQQTLSPTPGDPMLASWPTGEVWLSTVAPSPSDMGAGTAASSHTEVAPTDPMprrRGRFKGlngryfqqqePEPGL 500
Cdd:PHA03247  2541 EELASDDAGDPPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSA---RPRAPV----------DDRGD 2607

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  501 QGGMEASAQPPTSEAAGNQMEPPLAMAVTEMLGSGQSRSPwadltnEVDMPGAGSAGGKSSPepwlwpptmvPPSISGHS 580
Cdd:PHA03247  2608 PRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVP------PPERPRDDPAPGRVSR----------PRRARRLG 2671

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  581 RAPvleleKAEGPSARPATPDL--FWSPLEATVSAPSPAPW-EAFPVATSPDLPMMAmlrGPKEWMLPHPTPISTEANRv 657
Cdd:PHA03247  2672 RAA-----QASSPPQRPRRRAArpTVGSLTSLADPPPPPPTpEPAPHALVSATPLPP---GPAAARQASPALPAAPAPP- 2742

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  658 eahgeATTTAPPSPAAETKVYSLPLSLTPTGQGGEAMPTTPESPGAdfretgeTSPAQVNKAEHSSSSPWPSVNRNVAVG 737
Cdd:PHA03247  2743 -----AVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL-------TRPAVASLSESRESLPSPWDPADPPAA 2810

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  738 fVPTETATEPTGLRGISGSesgvfdtaESPTSGLQATVDEVQDPWPSVYSKGlGASSPSAPLGSPGvflvpkvtPSLEPw 817
Cdd:PHA03247  2811 -VLAPAAALPPAASPAGPL--------PPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPGGDVRRRP--------PSRSP- 2871

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  818 VATDEGPTVNPMDSTVTPAPSDASgiwEPGSQVFEEAESttlSPQVALDTSIVTPLTTLEQGDKVGVPAMSTLGSSSSQP 897
Cdd:PHA03247  2872 AAKPAAPARPPVRRLARPAVSRST---ESFALPPDQPER---PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP 2945

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1849067162  898 HPEPEDQVETQGTS-----GASVP-----PHQSSPLGKPAVP-PGTPTAASVGESAS-VSSGEPTVPWDPSSTLLPVTL 964
Cdd:PHA03247  2946 TTDPAGAGEPSGAVpqpwlGALVPgrvavPRFRVPQPAPSREaPASSTPPLTGHSLSrVSSWASSLALHEETDPPPVSL 3024
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 161-254 4.70e-07

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 50.54  E-value: 4.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  161 VFHYrSARDRYALTFAEAQEACRLSSAIIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCygdRSSLPGVrsY 240
Cdd:cd03516      8 VFLV-EKNGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLC---GKNGTGV--Y 81

                           90
                   ....*....|....*
gi 1849067162  241 GRRNP-QELYDVYCF 254
Cdd:cd03516     82 ILNSNlSSRYDAYCY 96
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 46-143 1.94e-06

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 47.83  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   46 SVQAALAELVALPCLFTlqpqPSAARDAPRIKWTKVRTasGQRQDLPILVAKDNVVkVAKSWQGRVSLPSYPRRRANATL 125
Cdd:cd05718      8 EVTGFLGGSVTLPCSLT----SPGTTKITQVTWMKIGA--GSSQNVAVFHPQYGPS-VPNPYAERVEFLAARLGLRNATL 80

                           90
                   ....*....|....*...
gi 1849067162  126 LLGPLRASDSGLYRCQVV 143
Cdd:cd05718     81 RIRNLRVEDEGNYICEFA 98
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 665-998 3.13e-06

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 51.50  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  665 TTAPPSP-----------------AAETKVYSLPLSlTPTGQGGEAMPTTPESPGAdfreTGETSPAQVNKAEHSSSSPW 727
Cdd:pfam17823   63 ATAAPAPvtltkgtsaahlnstevTAEHTPHGTDLS-EPATREGAADGAASRALAA----AASSSPSSAAQSLPAAIAAL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  728 PSVNRNVAVGFVPTETATeptglrgisGSESGVFDTAESPTSGLQATVDevqdpwpsvyskglGASSPSAPLGSPGVFLV 807
Cdd:pfam17823  138 PSEAFSAPRAAACRANAS---------AAPRAAIAAASAPHAASPAPRT--------------AASSTTAASSTTAASSA 194

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  808 PKVTPSLEPWVATDEGPTVNPMDSTVTPAPSDAS---GIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKVGV 884
Cdd:pfam17823  195 PTTAASSAPATLTPARGISTAATATGHPAAGTALaavGNSSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGD 274

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  885 PAMSTLGSSSSQP------HPEPEDQVETQG-TSGASV--PPHQSSPLGKPA-----VPPGTPTAASVGESASVSSGEPT 950
Cdd:pfam17823  275 PHARRLSPAKHMPsdtmarNPAAPMGAQAQGpIIQVSTdqPVHNTAGEPTPSpsnttLEPNTPKSVASTNLAVVTTTKAQ 354

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1849067162  951 VPwDPSSTLLPVTLGIEDFELEVL--------------AGSPGVESFWEEVASgeePALPGT 998
Cdd:pfam17823  355 AK-EPSASPVPVLHTSMIPEVEATspttqpspllptqgAAGPGILLAPEQVAT---EATAGT 412
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1010-1044 3.23e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.94  E-value: 3.23e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1849067162 1010 DPCE-NNPCLHGGTC-NANGTmYGCSCDQGFAGENCE 1044
Cdd:cd00054      3 DECAsGNPCQNGGTCvNTVGS-YRCSCPPGYTGRNCE 38
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 583-958 1.80e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 49.14  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  583 PVLELEKAEGPSArpaTPDLFWS---------PLEATVSAPSPAPWE----AFPVATSPDLPMMAMLRGPKEWMLPHPTP 649
Cdd:pfam05109  334 PMVTSEDANSPNV---TVTAFWAwpnntetdfKCKWTLTSGTPSGCEnisgAFASNRTFDITVSGLGTAPKTLIITRTAT 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  650 ISTEANRVEAHGEATTTAPPSPAAETKVYSLPLSLT--PTGQGGEAMPTTPESPGADFRETGETSPAQVNKAEHSSS-SP 726
Cdd:pfam05109  411 NATTTTHKVIFSKAPESTTTSPTLNTTGFAAPNTTTglPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPvTP 490

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  727 WPSVNRNVAVGFVPTETAtePTglrgisgsesgvfDTAESPTSGLQATVDEVQDPWPSVYSKGLGASSPSAPLGSPgvfl 806
Cdd:pfam05109  491 SPSPRDNGTESKAPDMTS--PT-------------SAVTTPTPNATSPTPAVTTPTPNATSPTLGKTSPTSAVTTP---- 551

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  807 VPKVTpSLEPWVATdegPTVNPMDSTVtpapsdasGIWEPGSQVFEEAESTTlSPQVAlDTSIVTPLTTLEQGDKVGVPA 886
Cdd:pfam05109  552 TPNAT-SPTPAVTT---PTPNATIPTL--------GKTSPTSAVTTPTPNAT-SPTVG-ETSPQANTTNHTLGGTSSTPV 617

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1849067162  887 MSTLGSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSST 958
Cdd:pfam05109  618 VTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISETLSPSTSDNSTSHMPLLTSAHPTGGENITQVTPAST 689
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1053-1082 2.51e-05

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 42.46  E-value: 2.51e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1849067162 1053 SPCENGGTCIDEVNGFVCLCLPSYGGSF-CE 1082
Cdd:cd00053      6 NPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1055-1074 3.13e-05

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.


Pssm-ID: 463660  Cd Length: 22  Bit Score: 41.94  E-value: 3.13e-05
                           10        20
                   ....*....|....*....|
gi 1849067162 1055 CENGGTCIDEVNGFVCLCLP 1074
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPP 20
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 548-863 4.89e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.16  E-value: 4.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  548 VDMPGAGSAGGKSSPEPWLWPPTMVPPSisghsrAPVLelekaeGPSARPATPDLFWSPLEAT-----VSAPSPAPWEAF 622
Cdd:PRK10263   316 ITEPVAVAAAATTATQSWAAPVEPVTQT------PPVA------SVDVPPAQPTVAWQPVPGPqtgepVIAPAPEGYPQQ 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  623 PVATSPDLPMMAmlrgpkEWMLPHPTPISTEANRVEAHGEATTTAPPSPAAETKVYSLPLSLTPTGQGgeamPTTPESPG 702
Cdd:PRK10263   384 SQYAQPAVQYNE------PLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGN----AWQAEEQQ 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  703 ADFRETGETSPAQVNK---AEHSSSSPWPSVNRNVAVGFVPTETATEPT--GLRGISGSESGVFDTAESPTSGLQATVDE 777
Cdd:PRK10263   454 STFAPQSTYQTEQTYQqpaAQEPLYQQPQPVEQQPVVEPEPVVEETKPArpPLYYFEEVEEKRAREREQLAAWYQPIPEP 533

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  778 VQDPWPSvyskglgasSPSAPLGSPGVflVPKVTPSlepwvatdegPTVNPMDSTVTPAPSDASGIWEPGSQVFEEAEST 857
Cdd:PRK10263   534 VKEPEPI---------KSSLKAPSVAA--VPPVEAA----------AAVSPLASGVKKATLATGAAATVAAPVFSLANSG 592


                   ....*.
gi 1849067162  858 TLSPQV 863
Cdd:PRK10263   593 GPRPQV 598
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1050-1080 7.29e-05

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 40.83  E-value: 7.29e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1849067162 1050 CLCSPCENGGTCIDEVNGFVCLCLPSYGGSF 1080
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 470-679 1.91e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  470 VAPTDPMPRRRGRFKGLNGRYFQQQEPEPGLQGGMEASAQPPTSEAAGNQMEPPLAMAVTEMLGSGQSRSPWADLTNEVD 549
Cdd:PRK07764   587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  550 MPGAGSAGGKSSPEPWLWPPTMVPPSISGHSRAPVLELEKAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVATSPD 629
Cdd:PRK07764   667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1849067162  630 LPmmamLRGPKEWMLPHPTPISTEANRVEAHGEATTTAPPSPAAETKVYS 679
Cdd:PRK07764   747 DP----PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPS 792
EGF_CA smart00179
Calcium-binding EGF-like domain;
1010-1044 2.37e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.54  E-value: 2.37e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1849067162  1010 DPCE-NNPCLHGGTC-NANGTmYGCSCDQGF-AGENCE 1044
Cdd:smart00179    3 DECAsGNPCQNGGTCvNTVGS-YRCECPPGYtDGRNCE 39
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1088-1162 3.32e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 43.57  E-value: 3.32e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1849067162 1088 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRRRSGHLTSVHSSEEHSFINSF-GHENTWIGLNDRIVERDFQWTDNT 1162
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYkDSSDHWIGLNRESSNHPWKWADNS 163
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 594-964 3.82e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 44.57  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  594 SARPATPDLFWSPLEATVSAPSPAPWEAfPVATSPDLPMMAMLRGPKEWMLPHPTPISTEANRVEAHGEATTTAPPSPAA 673
Cdd:pfam17823  117 AAASSSPSSAAQSLPAAIAALPSEAFSA-PRAAACRANASAAPRAAIAAASAPHAASPAPRTAASSTTAASSTTAASSAP 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  674 ETKVYSLPLSLTP-TGQGGEAMPTTPESPGADFRETGETSPA-QVNKAEHSSSSPWPSVNRNVAVGFVPTETATEPTG-- 749
Cdd:pfam17823  196 TTAASSAPATLTPaRGISTAATATGHPAAGTALAAVGNSSPAaGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGdp 275

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  750 -LRGISGSESGVFDTAES---PTSGLQA--TVDEVQDPWPSVYSKGLGASSPSAPLGSPGVFLVPKVTPSLEpwVATDEG 823
Cdd:pfam17823  276 hARRLSPAKHMPSDTMARnpaAPMGAQAqgPIIQVSTDQPVHNTAGEPTPSPSNTTLEPNTPKSVASTNLAV--VTTTKA 353

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  824 PTVNPMDSTVtPAPSdasgiwepgsqvfeeaesTTLSPQVALdTSIVTPLTTLEQGDKVGVPAMstlgssssqphPEPED 903
Cdd:pfam17823  354 QAKEPSASPV-PVLH------------------TSMIPEVEA-TSPTTQPSPLLPTQGAAGPGI-----------LLAPE 402

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1849067162  904 QVETQGTSGASvpphQSSPLGKPAVPPGTPTAASVGESAS----VSSGEPTVPWDPSSTLLPVTL 964
Cdd:pfam17823  403 QVATEATAGTA----SAGPTPRSSGDPKTLAMASCQLSTQgqylVVTTDPLTPALVDKMFLLVVL 463
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1011-1044 4.50e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 39.00  E-value: 4.50e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1849067162 1011 PCE-NNPCLHGGTCNANGTMYGCSCDQGFAGE-NCE 1044
Cdd:cd00053      1 ECAaSNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
498-752 5.53e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  498 PGLQGGmeaSAQPPTSEAAGNQMEPPLAMA---VTEMLGSGQSRSPWADLTNEVDMPGAGSAGGKSSPEPWLWPPTMVPP 574
Cdd:PRK12323   365 PGQSGG---GAGPATAAAAPVAQPAPAAAApaaAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASA 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  575 SISGHSRAPVLELEKAEGPSARPATPDLFWSPLEATVSAPSPAPwEAFPVATSPDLPmmamlrgPKEWM---LPHPTPIS 651
Cdd:PRK12323   442 RGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAP-AAAPAPADDDPP-------PWEELppeFASPAPAQ 513

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  652 TEANRVEAHGEATT---TAPPSPAAETKVYSLPLSLTPTGQGGEAMPTTPESPGADFRETGETSPAQvnkaehsssspWP 728
Cdd:PRK12323   514 PDAAPAGWVAESIPdpaTADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD-----------WP 582

                          250       260
                   ....*....|....*....|....*.
gi 1849067162  729 SVNRNVAVGFVPTETA--TEPTGLRG 752
Cdd:PRK12323   583 ALAARLPVRGLAQQLArqSELAGVEG 608
PHA03247 PHA03247
large tegument protein UL36; Provisional
 574-963 7.31e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 7.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  574 PSISGHSRAPvleleKAEGPSARPATPDLFWSPLE-----ATVSAPSPAPWEAFPVATSPDLPMMAMLRGPKEWMLPH-- 646
Cdd:PHA03247  2475 PGAPVYRRPA-----EARFPFAAGAAPDPGGGGPPdpdapPAPSRLAPAILPDEPVGEPVHPRMLTWIRGLEELASDDag 2549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  647 -PTPISTEANRVEAHGEATTTA-----PPSPAAETKvyslplSLTPTGQGGEAMPTTPESPGADFRETGETSPAQvnKAE 720
Cdd:PHA03247  2550 dPPPPLPPAAPPAAPDRSVPPPrpaprPSEPAVTSR------ARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP--PDT 2621

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  721 HSSSSPWPSvnrnvavgfvPTETATEPTGLRGISGSESGVFDtaesptsglqatvdevQDPWPSVYSKGLGASSPSAPlg 800
Cdd:PHA03247  2622 HAPDPPPPS----------PSPAANEPDPHPPPTVPPPERPR----------------DDPAPGRVSRPRRARRLGRA-- 2673

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  801 spgvflvPKVTPSLEPWVATDEGPTVNPMDSTVTPAPSDASGiwEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGd 880
Cdd:PHA03247  2674 -------AQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTP--EPAPHALVSATPLPPGPAAARQASPALPAAPAPPA- 2743

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  881 kvgvPAMSTLGSSSSQPHPEPedqvetQGTSGasvPPHQSSPLGKPAVPPGTPTAASVGeSASVSSGEPTVPWDPSSTLL 960
Cdd:PHA03247  2744 ----VPAGPATPGGPARPARP------PTTAG---PPAPAPPAAPAAGPPRRLTRPAVA-SLSESRESLPSPWDPADPPA 2809


                   ...
gi 1849067162  961 PVT 963
Cdd:PHA03247  2810 AVL 2812
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 262-385 1.00e-03

This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates adhesive interactions during inflammatory leukocyte homing and tumor metastasis. It also plays an important role in arteriogenesis. The functional HA-binding domain of CD44 is an extended domain comprised of a single link module flanked with N-and C- extensions. These extensions are essential for folding and for functional activity. This group also contains the cell surface retention sequence (CRS) binding protein-1 (CRSBP-1) and lymph vessel endothelial receptor-1 (LYVE-1). CRSBP-1 is a cell surface binding protein for the CRS motif of PDGF-BB (platelet-derived growth factor-BB) and is responsible for the cell surface retention of PDGF-BB in SSV-transformed cells. CRSBP-1 may play a role in autocrine regulation of cell growth mediated by CRS containing growth regulators. LYVE-1 is preferentially expressed on the lymphatic endothelium and is used as a molecular marker for the detection and characterization of lymphatic vessels in tumors.


Pssm-ID: 239593  Cd Length: 144  Bit Score: 40.91  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  262 VFYVGPARRLTLAGARAQ--CRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGgpAPGVRTVYRFA 339
Cdd:cd03516      8 VFLVEKNGRYSLNFTEAKeaCRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCG--KNGTGVYILNS 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1849067162  340 NRTGfpspaeRFDAYCFRAHhptsqhgdlETPSSGDEGEILSAEGP 385
Cdd:cd03516     86 NLSS------RYDAYCYNSS---------DTWINSCLPEILTTDDP 116
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 494-855 1.35e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  494 QEPEPGLQGGMEASAQPPTSEAAGNQMEPPLAMAVTEMLGSGQSRSPWADLTNEVDMPGAGSAGGKSSPEPWLWPPTMVP 573
Cdd:PRK07764   406 PAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPP 485

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  574 PSISGHSRAPVLELEKAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFpVATspdlPMMAMLRGPKEWmLPHPTP---- 649
Cdd:PRK07764   486 AAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAIL-LPE----ATVLGVRGDTLV-LGFSTGglar 559

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  650 ---------ISTEANRVEAHGEATTTA---PPSPAAETKVYSLPLSLTPTGQGGE-AMPTTPESPGADFRETGETSPAQV 716
Cdd:PRK07764   560 rfaspgnaeVLVTALAEELGGDWQVEAvvgPAPGAAGGEGPPAPASSGPPEEAARpAAPAAPAAPAAPAPAGAAAAPAEA 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  717 NKAEHSSSSPWPSVNRNVAVGFV-------------PTETATEPTGLRGISGSESGVFDTAESPTSGLQATVDEVQDPWP 783
Cdd:PRK07764   640 SAAPAPGVAAPEHHPKHVAVPDAsdggdgwpakaggAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAA 719

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1849067162  784 SVYSKGLGASSPSaPLGSPGVFLVPkvTPSLEPWVATDEGPtvnPMDSTVTPAPSDASGIWEPGSQVFEEAE 855
Cdd:PRK07764   720 QPPQAAQGASAPS-PAADDPVPLPP--EPDDPPDPAGAPAQ---PPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 110-625 3.16e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 42.17  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  110 RVSLPSYP-RRRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVFHYRSARDRYALTFAEAQEACRLSSAI 188
Cdd:COG3321    860 RVPLPTYPfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  189 IAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRSSLPGVRSYGRRNPQELYDVYCFARELGGEVFYVGPA 268
Cdd:COG3321    940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  269 RRLTLAGARAqcrRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGFPSPA 348
Cdd:COG3321   1020 ALLALAALLA---AAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  349 ERFDAYCFRAHHPTSQHGDLETPSSGDEGEILSAEGPPVRELEPTLEEEEVVTPDFQEPLVSSGEEEPLILEEKQEsqqt 428
Cdd:COG3321   1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAA---- 1172

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  429 lsPTPGDPMLASWPTGEVWLSTVAPSPSDMGAGTAASSHTEVAPTDPMPRRRGRFKGLNGRYFQQQEPEPGLQGGMEASA 508
Cdd:COG3321   1173 --LLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAA 1250

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  509 QPPTSEAAGNQMEPPLAMAVTEMLGSGQSRSPWADLTNEVDMPGAGSAGGKSSPEPWLWPPTMVPPSISGHSRAPVLELE 588
Cdd:COG3321   1251 AAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAAL 1330

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1849067162  589 KAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVA 625
Cdd:COG3321   1331 AALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAA 1367
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 271-355 3.68e-03

Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, it is highly similar to the link domain. The link domain is a hyaluronan-binding (HA) domain. KIAA0527 contains a single link module. The KIAA0527 gene was originally cloned from human brain tissue.


Pssm-ID: 239598  Cd Length: 95  Bit Score: 37.99  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  271 LTLAGARAQCRRQGAALASVGQL-HLAWHEGLDQCDPGWLADGSVRYPIQTPrrRCGGPAPGVRTVYRFANRtgfPSPAE 349
Cdd:cd03521     14 LGLRAARQSCASLGARLASAAELrRAVVECFFSACARGWLADGTVGTTVCNP--VVAEALKAVDVKVEIETN---PIPFA 88


                   ....*.
gi 1849067162  350 RFDAYC 355
Cdd:cd03521     89 HYNALC 94
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 548-943 3.71e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  548 VDMPGAGSAGGKSSPEPWLWPPTMVPPSISGHSRAPVLELEkaeGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVATS 627
Cdd:PHA03307    51 AAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWS---LSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPP 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  628 PDLPMMAMLRGPKEWMLPHPTPISTEANRVEAHGEATTTAPPSPAAETkVYSLPLSLTPTGQGGEAMPTTPESPGADFRE 707
Cdd:PHA03307   128 PSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP-LSSPEETARAPSSPPAEPPPSTPPAAASPRP 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  708 TGETSPAQvnkaeHSSSSPWPSVNRNVAVGFVPTETateptglrgiSGSESGVFDTAESPTSglqatvdevqdpwpsvys 787
Cdd:PHA03307   207 PRRSSPIS-----ASASSPAPAPGRSAADDAGASSS----------DSSSSESSGCGWGPEN------------------ 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  788 kglgasspSAPLGSPGVFLVPKVTPSLEPWVATDEGPTvnpmDSTVTPAPSDASGIWEPGSQVFEEAEST-TLSPQVALD 866
Cdd:PHA03307   254 --------ECPLPRPAPITLPTRIWEASGWNGPSSRPG----PASSSSSPRERSPSPSPSSPGSGPAPSSpRASSSSSSS 321

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1849067162  867 TSIVTPlTTLEQGDKVGVPAMSTlgSSSSQPHPEPEDQVETQGTSGASVPPHQSSPLGKPAVPPGTPTAASVGESAS 943
Cdd:PHA03307   322 RESSSS-STSSSSESSRGAAVSP--GPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVA 395
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
554-804 3.94e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  554 GSAGGKSSPEPWLWPPTMVPPSISghsRAPVLELEKAEGPSARPATPDLFWSPLEATVSAPSPAPWEAFPVATSPDLPMM 633
Cdd:PRK12323   366 GQSGGGAGPATAAAAPVAQPAPAA---AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASAR 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  634 AMLRGPKEWMLPHPTPISTEANRVEAHGEATTTAPPSPAAETKVySLPLSLTPTGQGGEAMPTTPESPGADFRE------ 707
Cdd:PRK12323   443 GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPA-AAPAPADDDPPPWEELPPEFASPAPAQPDaapagw 521

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  708 ---------TGETSPAQVNKAEHSSSSPWPSVNRNVAVGFVPTETATEPTGLRGISGSESGVFdTAESPTSGLQATVdEV 778
Cdd:PRK12323   522 vaesipdpaTADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPAL-AARLPVRGLAQQL-AR 599

                          250       260
                   ....*....|....*....|....*.
gi 1849067162  779 QDPWPSVYSKGLGASSPSAPLGSPGV 804
Cdd:PRK12323   600 QSELAGVEGDTVRLRVPVPALAEAEV 625
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 592-930 4.40e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.68  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  592 GPSARPATPDLFWSPLEATV-----SAPSPAPweafpvATSPDLPMMAMLRGPKEWMLPHPTPISTEANRVEAHGEATTT 666
Cdd:pfam03154   20 GRKKQTASPDGRASPTNEDLrssgrNSPSAAS------TSSNDSKAESMKKSSKKIKEEAPSPLKSAKRQREKGASDTEE 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  667 APPSPAAETKVYSLPLSLTPTGQGGEAmpttpeSPGADFRETGETSPAQVNKAEHSSSSPWPSVNRNvavgfvptETATE 746
Cdd:pfam03154   94 PERATAKKSKTQEISRPNSPSEGEGES------SDGRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDN--------ESDSD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  747 PTGLRGISGSESGVFDTAESPTSglqatvdevqdPWPSVYSKGLGASSPSAPLGSPGVFLVPKVTPSLEPWVATDEGPTV 826
Cdd:pfam03154  160 SSAQQQILQTQPPVLQAQSGAAS-----------PPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPH 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  827 NPMDSTVTPAPSDASGIWEPGSQVFEEAESTTLSPQVALDTSIVTPLTTLEQGDKVGVPAMS----------TLGSSSSQ 896
Cdd:pfam03154  229 TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQhpvppqpfplTPQSSQSQ 308

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1849067162  897 PHPEPEDQVETQGTSGASVPPHQSSPlgKPAVPP 930
Cdd:pfam03154  309 VPPGPSPAAPGQSQQRIHTPPSQSQL--QSQQPP 340
IgV_CAR_like cd20960
Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and ...
 42-142 4.65e-03

Immunoglobulin Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins; The members here are composed of the Variable (V) domain of the Coxsackievirus and Adenovirus Receptor (CAR), and similar proteins. CAR, which is encoded by human CXADR gene, is a cell adhesion molecule of the Immunoglobulin (Ig) superfamily. The CAR acts as a type I membrane receptor for group B1-B6 coxsackie viruses and subgroup C adenoviruses. For instance, adenovirus interacts with the coxsackievirus and adenovirus receptor to enter epithelial airway cells. The CAR is also shown to be involved in physiological processes such as neuronal and heart development, epithelial tight junction integrity, and tumor suppression. The CAR is a component of the epithelial apical junction complex that may function as a homophilic cell adhesion molecule and is essential for tight junction integrity. The CAR is also involved in transepithelial migration of leukocytes through adhesive interactions with JAML a transmembrane protein of the plasma membrane of leukocytes. The interaction between both receptors also mediates the activation of gamma-delta T-cells, a subpopulation of T-cells residing in epithelia and involved in tissue homeostasis and repair. The CAR is composed of one V-set and one C2-set Ig module, a single transmembrane helix, and an intracellular domain. This group belongs to the V-set of IgSF domains, having A, B, E and D strands in one beta-sheet and A', G, F, C, C' and C" in the other


Pssm-ID: 409552  Cd Length: 114  Bit Score: 38.20  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162   42 LGSGSVQAALAELVALPCLFTLQPQPSAARDaprIKWtkVRTASGQRQDLPILVAKDNVVK-VAKSWQGRVSLPSyPRRR 120
Cdd:cd20960      5 SAQTEIKKVAGENVTLPCHHQLGLEDQGTLD---IEW--LLLPSDKVEKVVITYSGDRVYNhYYPALKGRVAFTS-NDLS 78

                           90       100
                   ....*....|....*....|..
gi 1849067162  121 ANATLLLGPLRASDSGLYRCQV 142
Cdd:cd20960     79 GDASLNISNLKLSDTGTYQCKV 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 596-961 5.28e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 5.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  596 RPATPDLFwSPLEATVSAPSPAPweafPVATSPDLPMMAMLRGPKEWMLPHPTPIST----EANRVEAHGEATTTAPPSP 671
Cdd:PHA03307     1 SDNAPDLY-DLIEAAAEGGEFFP----RPPATPGDAADDLLSGSQGQLVSDSAELAAvtvvAGAAACDRFEPPTGPPPGP 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  672 -AAETKVYSLPLSLTPTGQGGEAMPTTPESPGADFRETGETSPAQVNKAE--HSSSSPWPSVNRNVAVGFVPTETATEPT 748
Cdd:PHA03307    76 gTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASppPSPAPDLSEMLRPVGSPGPPPAASPPAA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  749 GlrgiSGSESGVFDTAESPTSGL-QATVDEVQDPWPSVYSKGLGASSPSAPLGSPGVFLVPKVTPSLEPwvatdegpTVN 827
Cdd:PHA03307   156 G----ASPAAVASDAASSRQAALpLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSP--------APA 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849067162  828 PMDSTVTPAPSDASGIWEPGSQVFEEA-ESTTLSPQVALDTSIVTPLTTLEQGDKVGVPAMSTLGSSSSQPHPEPEDqve 906
Cdd:PHA03307   224 PGRSAADDAGASSSDSSSSESSGCGWGpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSP--- 300

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1849067162  907 tqgtSGASVPPHQSSPLGKPAVPPGTPTAASVGESASVSSGEPTVPWDPSSTLLP 961
Cdd:PHA03307   301 ----SSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSP 351
 
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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