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Conserved domains on  [gi|1622829693|ref|XP_028683442|]
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brevican core protein isoform X3 [Macaca mulatta]

Protein Classification

immunoglobulin domain-containing protein; fibroblast growth factor receptor 1( domain architecture ID 10308784)

immunoglobulin (Ig) domain-containing protein adopts a fold comprised of a sandwich of two beta sheets and may function in cell adhesion and pattern recognition; similar to Drosophila melanogaster DIP/Dpr cell recognition proteins, which are members of the Wirin family of IgSF proteins with neuronal wiring functions, and human IgLON proteins, a family of cell adhesion molecules| fibroblast growth factor receptor 1 (FGFR1) is a receptor tyrosine-protein kinase contains an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain that catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates; it binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 157-251 4.79e-59

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: 193.39  E-value: 4.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMDGFPGVRN 236
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 1622829693 237 YGVVDPDDLYDVYCY 251
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
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 ...
 258-353 5.14e-58

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: 190.60  E-value: 5.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 258 ELFLGDPPEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLFLFPN 337
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 1622829693 338 QTGFPNKHSRFNVYCF 353
Cdd:cd03520    81 QTGFPDPHSRFDAYCF 96
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 39-159 1.66e-34

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


The actual alignment was detected with superfamily member cd05900:

Pssm-ID: 472250  Cd Length: 123  Bit Score: 127.36  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  39 ISGHAPLQGVLGGALTIPCH--VHYLRPPPSRRAVLGSPRVKWTFLSGGREAEVLVARGVRVKVNEAYRFRVALPAYPAS 116
Cdd:cd05900     1 IPLESPLRVVLGSSLLIPCYfqDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622829693 117 LTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05900    81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 353-631 7.67e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  353 FRDSAQPSAIPEASNPASDPASDGLEAIVTVTETLEELQLPQEAMESESRGAIYSIPIMEDGGGGSSTPEDPAEAPR--- 429
Cdd:PHA03247  2608 PRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRrra 2687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  430 ---TV----------PEFETQSMVPPTVFSEEEGKALEEEEKYEDEEEKEEEEEEEEVEDEALWAWPSEFNSPgPEVSLP 496
Cdd:PHA03247  2688 arpTVgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-PTTAGP 2766

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  497 TEPAAQESLSQAPARAVLQPGVSPLPDGESETPRPPRVHGPPTETLPS----PRERNLASPSPSTLAGAREAGEETGGPE 572
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPaaalPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622829693  573 LSGVPRGESEETG------SSEGAPSLLPATRAPEGTRELEAPSEDNSGRTAPAGTSVQAQPVLP 631
Cdd:PHA03247  2847 PPSLPLGGSVAPGgdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP 2911
 
Name Accession Description Interval E-value
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 157-251 4.79e-59

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: 193.39  E-value: 4.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMDGFPGVRN 236
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 1622829693 237 YGVVDPDDLYDVYCY 251
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
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 ...
 258-353 5.14e-58

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: 190.60  E-value: 5.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 258 ELFLGDPPEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLFLFPN 337
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 1622829693 338 QTGFPNKHSRFNVYCF 353
Cdd:cd03520    81 QTGFPDPHSRFDAYCF 96
LINK smart00445
Link (Hyaluronan-binding);
155-252 1.67e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 148.64  E-value: 1.67e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  155 KGVVFLYREGsARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGdmdGFPGV 234
Cdd:smart00445   1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                           90
                   ....*....|....*...
gi 1622829693  235 RNYGVVDPDDLYDVYCYA 252
Cdd:smart00445  77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
157-251 9.67e-42

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 146.18  E-value: 9.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYReGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMdgfPGVRN 236
Cdd:pfam00193   1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                          90
                  ....*....|....*.
gi 1622829693 237 YGVVDP-DDLYDVYCY 251
Cdd:pfam00193  77 YGFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
256-354 2.90e-41

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 145.18  E-value: 2.90e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  256 NGELFLGDP--PEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKtlf 333
Cdd:smart00445   1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                           90       100
                   ....*....|....*....|.
gi 1622829693  334 lfpnQTGFPNKHSRFNVYCFR 354
Cdd:smart00445  78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
267-353 7.87e-37

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 132.70  E-value: 7.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 267 KLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVktlflfpNQTGFPNKHS 346
Cdd:pfam00193  12 KLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGV-------RQYGFRDPLS 84


                  ....*...
gi 1622829693 347 -RFNVYCF 353
Cdd:pfam00193  85 eRYDAYCY 92
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 39-159 1.66e-34

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: 127.36  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  39 ISGHAPLQGVLGGALTIPCH--VHYLRPPPSRRAVLGSPRVKWTFLSGGREAEVLVARGVRVKVNEAYRFRVALPAYPAS 116
Cdd:cd05900     1 IPLESPLRVVLGSSLLIPCYfqDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622829693 117 LTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05900    81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 44-154 6.51e-12

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: 62.48  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  44 PLQGVLGGALTIPCHVhylrpppSRRAVLGSPRVKWTFLSGGREAEVLVARGVRVKVNEAYRFRVALPAYPaSLTDVSLA 123
Cdd:pfam07686   5 EVTVALGGSVTLPCTY-------SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNGDGSLT 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622829693 124 LSELRPNDSGIYRCEV-QHGIDDSSDAVEVKV 154
Cdd:pfam07686  77 IQNLTLSDSGTYTCAViPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
53-139 2.38e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 51.61  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693   53 LTIPCHVHYLRpppsrravLGSPRVKWTFLSGGREAEVLVARGVRVKV--NEAYRFRVALPAYPaSLTDVSLALSELRPN 130
Cdd:smart00406   2 VTLSCKFSGST--------FSSYYVSWVRQPPGKGLEWLGYIGSNGSSyyQESYKGRFTISKDT-SKNDVSLTISNLRVE 72


                   ....*....
gi 1622829693  131 DSGIYRCEV 139
Cdd:smart00406  73 DTGTYYCAV 81
PHA03247 PHA03247
large tegument protein UL36; Provisional
 353-631 7.67e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  353 FRDSAQPSAIPEASNPASDPASDGLEAIVTVTETLEELQLPQEAMESESRGAIYSIPIMEDGGGGSSTPEDPAEAPR--- 429
Cdd:PHA03247  2608 PRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRrra 2687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  430 ---TV----------PEFETQSMVPPTVFSEEEGKALEEEEKYEDEEEKEEEEEEEEVEDEALWAWPSEFNSPgPEVSLP 496
Cdd:PHA03247  2688 arpTVgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-PTTAGP 2766

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  497 TEPAAQESLSQAPARAVLQPGVSPLPDGESETPRPPRVHGPPTETLPS----PRERNLASPSPSTLAGAREAGEETGGPE 572
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPaaalPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622829693  573 LSGVPRGESEETG------SSEGAPSLLPATRAPEGTRELEAPSEDNSGRTAPAGTSVQAQPVLP 631
Cdd:PHA03247  2847 PPSLPLGGSVAPGgdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP 2911
 
Name Accession Description Interval E-value
Link_domain_CSPGs_modules_1_3 cd03517
Link_domain_CSPGs_modules_1_3; this extracellular link domain is found in the first and third ...
 157-251 4.79e-59

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: 193.39  E-value: 4.79e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMDGFPGVRN 236
Cdd:cd03517     1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                          90
                  ....*....|....*
gi 1622829693 237 YGVVDPDDLYDVYCY 251
Cdd:cd03517    81 YGVRDPDELYDVYCY 95
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 ...
 258-353 5.14e-58

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: 190.60  E-value: 5.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 258 ELFLGDPPEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLFLFPN 337
Cdd:cd03520     1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                          90
                  ....*....|....*.
gi 1622829693 338 QTGFPNKHSRFNVYCF 353
Cdd:cd03520    81 QTGFPDPHSRFDAYCF 96
LINK smart00445
Link (Hyaluronan-binding);
155-252 1.67e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 148.64  E-value: 1.67e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  155 KGVVFLYREGsARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGdmdGFPGV 234
Cdd:smart00445   1 DGGVFHVEKN-GRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGG---NLPGV 76

                           90
                   ....*....|....*...
gi 1622829693  235 RNYGVVDPDDLYDVYCYA 252
Cdd:smart00445  77 RQYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
157-251 9.67e-42

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 146.18  E-value: 9.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYReGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMdgfPGVRN 236
Cdd:pfam00193   1 GVFHLE-SPGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                          90
                  ....*....|....*.
gi 1622829693 237 YGVVDP-DDLYDVYCY 251
Cdd:pfam00193  77 YGFRDPlSERYDAYCY 92
LINK smart00445
Link (Hyaluronan-binding);
256-354 2.90e-41

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 145.18  E-value: 2.90e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  256 NGELFLGDP--PEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKtlf 333
Cdd:smart00445   1 DGGVFHVEKngRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR--- 77

                           90       100
                   ....*....|....*....|.
gi 1622829693  334 lfpnQTGFPNKHSRFNVYCFR 354
Cdd:smart00445  78 ----QYGFPDPTSRYDAYCFN 94
Xlink pfam00193
Extracellular link domain;
267-353 7.87e-37

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 132.70  E-value: 7.87e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 267 KLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVktlflfpNQTGFPNKHS 346
Cdd:pfam00193  12 KLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGV-------RQYGFRDPLS 84


                  ....*...
gi 1622829693 347 -RFNVYCF 353
Cdd:pfam00193  85 eRYDAYCY 92
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 39-159 1.66e-34

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: 127.36  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  39 ISGHAPLQGVLGGALTIPCH--VHYLRPPPSRRAVLGSPRVKWTFLSGGREAEVLVARGVRVKVNEAYRFRVALPAYPAS 116
Cdd:cd05900     1 IPLESPLRVVLGSSLLIPCYfqDPIAKDPGAPTVAPLSPRIKWSFISKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622829693 117 LTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05900    81 PSDATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 157-251 6.34e-32

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: 119.06  E-value: 6.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACYGDMdgfPGVRN 236
Cdd:cd01102     1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRS 77

                          90
                  ....*....|....*
gi 1622829693 237 YGVVDPDDLYDVYCY 251
Cdd:cd01102    78 YGNPAPSGRYDAYCF 92
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 39-159 9.15e-32

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: 119.65  E-value: 9.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  39 ISGHAPLQGVLGGALTIPCH-VHYLRPPPSRRAVLgSPRVKWTFLS--GGREAE--VLVARGVRVKVNEAYRFRVALPAY 113
Cdd:cd05878     1 IPQSSPVRVLLGTSVTLPCYfIDPPHPVTPSTAPL-APRIKWSKVSvdGKKEKEvvLLVATEGRVRVNSAYQGRVSLPNY 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622829693 114 PASLTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05878    80 PAIPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 260-353 5.31e-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: 116.37  E-value: 5.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 260 FLGDPPEKLTLEEARAYCQERGAEIATTGQLYAAWD-GGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLflfpnq 338
Cdd:cd03519     3 FYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF------ 76

                          90
                  ....*....|....*.
gi 1622829693 339 tGFPNK-HSRFNVYCF 353
Cdd:cd03519    77 -GFPDKkHKLYGVYCY 91
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 263-353 3.67e-30

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: 114.05  E-value: 3.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 263 DPPEKLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLflfpnqtGFP 342
Cdd:cd01102     9 NGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-------GNP 81

                          90
                  ....*....|.
gi 1622829693 343 NKHSRFNVYCF 353
Cdd:cd01102    82 APSGRYDAYCF 92
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 157-251 9.45e-29

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: 110.21  E-value: 9.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 157 VVFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACyGDMDGFPGVRN 236
Cdd:cd03518     1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                          90
                  ....*....|....*.
gi 1622829693 237 YGVVDPD-DLYDVYCY 251
Cdd:cd03518    80 YGERDKMlSRYDAFCF 95
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 41-159 9.94e-25

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: 99.52  E-value: 9.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  41 GHAPLQGVLGGALTIPChVHYLrpPPSRRAVLGSPRVKWTFLSGG---REAEVLVARGVRVKVNEAYRFRVALPAYPASL 117
Cdd:cd05902     3 TAPPVRRPLSSSVLLPC-VFTL--PPSASSPPEGPRIKWTKLSTSggqQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622829693 118 TDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05902    80 YNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 43-159 1.03e-24

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: 99.65  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  43 APLQGVLGGALTIPCHVHYLRP-PPSRRAVLGSPRVKWTFLSGGR------EAEVLVARGVRVKVNEAYRFRVALPAYPA 115
Cdd:cd05901     5 SRVHGSLSGSVVLPCRFSTLPTlPPSYNITSEFLRIKWTKIQVDKngkdhkETTVLVAQNGIIKIGQEYMGRVSVPSHPE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622829693 116 SLTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05901    85 DQGDASLTIVKLRASDAGVYRCEVMHGIEDTQDTVSLDVSGVVF 128
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 41-159 1.95e-24

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: 98.82  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  41 GHAPLQGVLGGALTIPCHvhYLRPPPSRRAVLGSPRVKWTFLSGG----REAEVLVARGVRVKVNEAYRFRVALPAYPAS 116
Cdd:cd05714     3 ESAKVFSHLGGNVTLPCK--FYRDPTAFGSGIHKIRIKWTKLTSDsgylKEVDVLVAMGNVVYHKKTYGGRVSVPLKPGS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622829693 117 LTDVSLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05714    81 DSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 267-353 3.20e-23

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: 94.42  E-value: 3.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 267 KLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGG--GLPGVKTLflfpnqtGFPNK 344
Cdd:cd03518    13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGkrTVPGLRSY-------GERDK 85

                          90
                  ....*....|
gi 1622829693 345 H-SRFNVYCF 353
Cdd:cd03518    86 MlSRYDAFCF 95
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 43-159 3.47e-22

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: 92.00  E-value: 3.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  43 APLQGVLGGALTIPCHVHYLRPPPSRRAVlgspRVKWTFLS--GGREAEVLVARGVRVKVNEAYRFRVALPAypASLTDV 120
Cdd:cd05877     5 AKVFSHRGGNVTLPCRYHYEPELSAPRKI----RVKWTKLEvdYAKEEDVLVAIGTRHKSYGSYQGRVFLRR--ADDLDA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622829693 121 SLALSELRPNDSGIYRCEVQHGIDDSSDAVEVKVKGVVF 159
Cdd:cd05877    79 SLVITDLRLEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 170-251 5.21e-21

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: 87.86  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 170 FSFVGAQEACARIGAHIATPEQLYAAY-LGGYEQCDAGWLSDQTVRYPIQTPREACYGDMdgfPGVRNYGVVDPDD-LYD 247
Cdd:cd03519    11 LTFSEAVAACQRDGAQIAKVGQLFAAWkFHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGFPDKKHkLYG 87


                  ....
gi 1622829693 248 VYCY 251
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 ...
 267-353 7.46e-16

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: 73.27  E-value: 7.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 267 KLTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLflfpnqtGF-PNKH 345
Cdd:cd03515    13 KLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGIVDY-------GPrLNLS 85


                  ....*...
gi 1622829693 346 SRFNVYCF 353
Cdd:cd03515    86 ERWDAYCY 93
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 ...
 158-251 4.30e-15

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: 70.96  E-value: 4.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 158 VFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACygdMDGFPGVRNY 237
Cdd:cd03515     2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC---GFGHVGIVDY 78

                          90
                  ....*....|....*
gi 1622829693 238 GV-VDPDDLYDVYCY 251
Cdd:cd03515    79 GPrLNLSERWDAYCY 93
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 44-154 6.51e-12

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: 62.48  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  44 PLQGVLGGALTIPCHVhylrpppSRRAVLGSPRVKWTFLSGGREAEVLVARGVRVKVNEAYRFRVALPAYPaSLTDVSLA 123
Cdd:pfam07686   5 EVTVALGGSVTLPCTY-------SSSMSEASTSVYWYRQPPGKGPTFLIAYYSNGSEEGVKKGRFSGRGDP-SNGDGSLT 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622829693 124 LSELRPNDSGIYRCEV-QHGIDDSSDAVEVKV 154
Cdd:pfam07686  77 IQNLTLSDSGTYTCAViPSGEGVFGKGTRLTV 108
IGv smart00406
Immunoglobulin V-Type;
53-139 2.38e-08

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 51.61  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693   53 LTIPCHVHYLRpppsrravLGSPRVKWTFLSGGREAEVLVARGVRVKV--NEAYRFRVALPAYPaSLTDVSLALSELRPN 130
Cdd:smart00406   2 VTLSCKFSGST--------FSSYYVSWVRQPPGKGLEWLGYIGSNGSSyyQESYKGRFTISKDT-SKNDVSLTISNLRVE 72


                   ....*....
gi 1622829693  131 DSGIYRCEV 139
Cdd:smart00406  73 DTGTYYCAV 81
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 36-139 3.89e-07

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: 48.98  E-value: 3.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  36 RVRISGHAPlqGVLGGALTIPCHVhylrPPPSRRAVlgsPRVKWTFLSGGREAEVLV---ARGVRVKvnEAYRFRVALPA 112
Cdd:cd05718     2 RVQVPTEVT--GFLGGSVTLPCSL----TSPGTTKI---TQVTWMKIGAGSSQNVAVfhpQYGPSVP--NPYAERVEFLA 70

                          90       100
                  ....*....|....*....|....*..
gi 1622829693 113 YPASLTDVSLALSELRPNDSGIYRCEV 139
Cdd:cd05718    71 ARLGLRNATLRIRNLRVEDEGNYICEF 97
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 268-365 7.56e-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: 49.00  E-value: 7.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 268 LTLEEARAYCQERGAEIATTGQLYAAWDGGLDRCSPGWLADGSVRYPIVTPSQRCGGGLPGVKTLFLfpnqtgfpNKHSR 347
Cdd:cd03516    19 LNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCGKNGTGVYILNS--------NLSSR 90

                          90       100
                  ....*....|....*....|
gi 1622829693 348 FNVYCFRDSAQP--SAIPEA 365
Cdd:cd03516    91 YDAYCYNSSDTWinSCLPEI 110
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 158-251 2.05e-06

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: 47.84  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 158 VFLYREGSaRYAFSFVGAQEACARIGAHIATPEQLYAAYLGGYEQCDAGWLSDQTVRYPIQTPREACygdmdGFPGVRNY 237
Cdd:cd03516     8 VFLVEKNG-RYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLC-----GKNGTGVY 81

                          90
                  ....*....|....*
gi 1622829693 238 GVVDPDDL-YDVYCY 251
Cdd:cd03516    82 ILNSNLSSrYDAYCY 96
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 44-154 1.85e-05

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 43.26  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693   44 PLQGVLGGALTIPCHVHYLRPPpsrravlgspRVKWTflsggREAEVLVARGVRVKVNEayrfrvalpaypaSLTDVSLA 123
Cdd:smart00410   3 SVTVKEGESVTLSCEASGSPPP----------EVTWY-----KQGGKLLAESGRFSVSR-------------SGSTSTLT 54

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1622829693  124 LSELRPNDSGIYRCEVQHGIDDSSDAVEVKV 154
Cdd:smart00410  55 ISNVTPEDSGTYTCAATNSSGSASSGTTLTV 85
IgV_1_Nectin-2_NecL-5_like_CD112_CD155 cd20989
First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar ...
 36-138 2.93e-05

First immunoglobulin variable (IgV) domain of nectin-2, nectin-like protein 5, and similar domains; The members here are composed of the second immunoglobulin (Ig) domain of nectin-2 (also known as poliovirus receptor related protein 2 or Cluster of Differentiation 112 (CD112)), nectin-like protein 5 (CD155), and similar proteins. Nectins and Nectin-like molecules are a family of Ca(2+)-independent immunoglobulin-like transmembrane glycoproteins belonging to the class of adhesion receptors, consisting of nine members (nectins 1 through 4 and nectin-like proteins 1 through 5). Nectins are synaptic cell adhesion molecules (CAMs) which facilitate adhesion and signaling at various intracellular junctions. Nectins form homophilic cis-dimers, followed by homophilic and heterophilic trans-dimers involved in cell-cell adhesion. Nectin-2 and nectin-3 localize at Sertoli-spermatid junctions where they form heterophilic trans-interactions between the cells that are essential for the formation and maintenance of the junctions and for spermatid development. CD155 is the fifth member in the nectin-like molecule family, and functions as the receptor of poliovirus; therefore, CD155 is also referred to as Necl-5, or PVR. In contrast to all other family members, CD155 lacks self-adhesion capacity, yet it shares with nectins the feature to interact with other nectins. For instance, CD155 heterophilically trans-interacts with nectin-3, thereby contributing significantly to the establishment of adherens junctions between epithelial cells. This group belongs to the Constant 1 (C1)-set of IgSF domains, which has one beta-sheet that is formed by strands A-B-E-D and the other strands by G-F-C-C'.


Pssm-ID: 409581  Cd Length: 112  Bit Score: 43.72  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  36 RVRISGHAPlqGVLGGALTIPCHvhyLRPPPSRRAVlgsPRVKWTFL-SGGREAEVLVARGVRVKVNEAYRFRVALPAyp 114
Cdd:cd20989     2 RVQVPPEVR--GFLGGSVTLPCH---LLPPNMVTHV---SQVTWQRHdEHGSVAVFHPKQGPSFPESERLSFVAARLG-- 71

                          90       100
                  ....*....|....*....|....
gi 1622829693 115 ASLTDVSLALSELRPNDSGIYRCE 138
Cdd:cd20989    72 AELRNASLAMFGLRVEDEGNYTCE 95
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 158-213 3.68e-04

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: 39.91  E-value: 3.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622829693 158 VFLYREGSARYAFSFVGAQEACARIGAHIATPEQLYAAYLG-GYEQCDAGWLSDQTV 213
Cdd:cd03521     2 LFVLELENGSQGLGLRAARQSCASLGARLASAAELRRAVVEcFFSACARGWLADGTV 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
 353-631 7.67e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  353 FRDSAQPSAIPEASNPASDPASDGLEAIVTVTETLEELQLPQEAMESESRGAIYSIPIMEDGGGGSSTPEDPAEAPR--- 429
Cdd:PHA03247  2608 PRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRrra 2687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  430 ---TV----------PEFETQSMVPPTVFSEEEGKALEEEEKYEDEEEKEEEEEEEEVEDEALWAWPSEFNSPgPEVSLP 496
Cdd:PHA03247  2688 arpTVgsltsladppPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARP-PTTAGP 2766

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  497 TEPAAQESLSQAPARAVLQPGVSPLPDGESETPRPPRVHGPPTETLPS----PRERNLASPSPSTLAGAREAGEETGGPE 572
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPaaalPPAASPAGPLPPPTSAQPTAPPPPPGPP 2846

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622829693  573 LSGVPRGESEETG------SSEGAPSLLPATRAPEGTRELEAPSEDNSGRTAPAGTSVQAQPVLP 631
Cdd:PHA03247  2847 PPSLPLGGSVAPGgdvrrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP 2911
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 259-311 8.51e-04

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: 39.14  E-value: 8.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622829693 259 LFLGDPPEKLTLEEARAYCQERGAEIATTGQL-YAAWDGGLDRCSPGWLADGSV 311
Cdd:cd03521     5 LELENGSQGLGLRAARQSCASLGARLASAAELrRAVVECFFSACARGWLADGTV 58
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
 40-141 1.25e-03

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 38.33  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  40 SGHAPLQGVLGGALTIPCHVHYLRPPPSrravlgsprVKWtFLSGGREAEvlvarGVRVKVNEAYRFRvalpaypASLTd 119
Cdd:pfam00047   1 SAPPTVTVLEGDSATLTCSASTGSPGPD---------VTW-SKEGGTLIE-----SLKVKHDNGRTTQ-------SSLL- 57

                          90       100
                  ....*....|....*....|..
gi 1622829693 120 vslaLSELRPNDSGIYRCEVQH 141
Cdd:pfam00047  58 ----ISNVTKEDAGTYTCVVNN 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
 496-646 3.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  496 PTEPAAQESLSQAPARAVLQPGVSPLPDGESETPRPPRVHGPPTETLP-SPRERNLASPSPSTLAGAREAGEETGGPELS 574
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPrAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622829693  575 GVPRGESEETGSSEGAPSLLPATRAPEGTRelEAPSEDNSGRTAPAGTSvqAQPVLPTDSASRGGVAVVPAS 646
Cdd:PHA03247  2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGR--VSRPRRARRLGRAAQAS--SPPQRPRRRAARPTVGSLTSL 2698
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 483-602 4.44e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.08  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 483 PSEFNSPGPEVSLPTEPAAQESLSQAPARAVLQPGVSPLPDGESETPRPPRVHGPPTETLPSPRERNLASPSPSTLAGAR 562
Cdd:PRK14951  375 PAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQ 454

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622829693 563 EAGEETGGPELSGVPRGESEETGSSEGAPSLLPATRAPEG 602
Cdd:PRK14951  455 AAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEEG 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
 488-647 4.67e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 4.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  488 SPGPEVSLPTEPAAQESLSQAPARAVLQPGVSPL------PDGESETPRPPRVHGPPTETLPSPRERNLASPSPSTLAGA 561
Cdd:PHA03247  2662 SRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLtsladpPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAP 2741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693  562 REAGEETGGPELSGVPRGESEETGSSEGAPSLLPATRAPEGTRELEAPSEDNSGRTAPAGTSVQAQPVLPTDSASRGGVA 641
Cdd:PHA03247  2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPA 2821


                   ....*.
gi 1622829693  642 VVPASG 647
Cdd:PHA03247  2822 ASPAGP 2827
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
499-631 6.99e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.47  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622829693 499 PAAQESLSQAPARAVLQPGVSPLPDGESETPRPPRVHGPPTETLPSPRERnlASPSPSTLAGAREAGEETGGPELSGVPR 578
Cdd:PRK12323  376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPAR--RSPAPEALAAARQASARGPGGAPAPAPA 453

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622829693 579 GeseetgssegAPSLLPATRAP-EGTRELEAPSEDNSGRTAPAGTSVQAQPVLP 631
Cdd:PRK12323  454 P----------AAAPAAAARPAaAGPRPVAAAAAAAPARAAPAAAPAPADDDPP 497
 
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.
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