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Conserved domains on  [gi|1333603193|ref|XP_023481308|]
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neurocan core protein [Equus caballus]

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 ...
 1132-1255 9.51e-67

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: 220.53  E-value: 9.51e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSFGRENTWIGLNDRIVERDFQWTDNTGLQYE 1211
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1333603193 1212 NWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKG 1255
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig super family cl11960
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 44-165 5.59e-62

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 cd05902:

Pssm-ID: 472250  Cd Length: 121  Bit Score: 207.00  E-value: 5.59e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   44 KVGSGSVRAALAELVALPCLFTLRPQQSAAREAPRIKWTKVRTaSGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYPRHR 123
Cdd:cd05902      1 RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLST-SGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1333603193  124 ANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
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 ...
 264-359 6.61e-56

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: 188.68  E-value: 6.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 343
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1333603193  344 RTGFPAPGARFDAYCF 359
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 ...
 163-257 2.50e-55

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: 186.84  E-value: 2.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRRSLPGVRS 242
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1333603193  243 YGRRDPRELYDVYCF 257
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1259-1315 4.07e-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: 62.48  E-value: 4.07e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193 1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1090-1126 3.10e-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: 56.49  E-value: 3.10e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1333603193 1090 DIDDCVS-SPCENGGTCIDEVNTFICLCLPSYGGSLCE 1126
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1056-1086 6.31e-08

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: 49.69  E-value: 6.31e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1333603193 1056 CENNPCLHGGTCKANGTMYGCSCDQGFTGEN 1086
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 355-775 1.37e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 56.33  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  355 DAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDFQEPLVSSGEEEPlilaeRQESQETPSP 434
Cdd:PHA03307    16 EGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP-----ANESRSTPTW 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  435 ASGGPMLASRPALEAEEvwlstvAPSRSSmEAGTARTTHREATPASATPRKRGRFK--GLNGRHFQEQEPQQGLEGGLEA 512
Cdd:PHA03307    91 SLSTLAPASPAREGSPT------PPGPSS-PDPPPPTPPPASPPPSPAPDLSEMLRpvGSPGPPPAASPPAAGASPAAVA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  513 SAHAPTSEAAgnqvePPLAVeTTDALRTGPNQSPwavltnevDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSRALGLE 592
Cdd:PHA03307   164 SDAASSRQAA-----LPLSS-PEETARAPSSPPA--------EPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  593 LEEVEGPSVRPATPNL--PWSPLEATalgPRPSEGPSTIPweappmiSSPDLPVVAMLRAPKLGllphptpfttqangik 670
Cdd:PHA03307   230 DDAGASSSDSSSSESSgcGWGPENEC---PLPRPAPITLP-------TRIWEASGWNGPSSRPG---------------- 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  671 rhgeamvTAPPSPASEIEASPQDPIHPELYSLPPSLDLKEQGGEATSSTLSGHGAGIPTAPLQAASDAQGGASPNSPRAD 750
Cdd:PHA03307   284 -------PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356

                          410       420
                   ....*....|....*....|....*
gi 1333603193  751 LGETGGTSPtglSKAEHPRSSPQAS 775
Cdd:PHA03307   357 PPPADPSSP---RKRPRPSRAPSSP 378
DUF5585 super family cl39316
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 683-1022 4.98e-05

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


The actual alignment was detected with superfamily member pfam17823:

Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 47.65  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  683 PASEIEASPQDPIHPELYSLPPSLDLKEQGGEA-------TSSTLSGHGAGIPTAPLqAASDAQGGASPNSPR------- 748
Cdd:pfam17823   14 PLSESHAAPADPRHFVLNKMWNGAGKQNASGDAvpradnkSSEQ*NFCAATAAPAPV-TLTKGTSAAHLNSTEvtaehtp 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  749 --ADLGE---TGGTSPTGLSKA-EHPRSSPQASVDGNEVVDFA--PTETATEPTGV---TGILGSESGVFSTAESPTFSS 817
Cdd:pfam17823   93 hgTDLSEpatREGAADGAASRAlAAAASSSPSSAAQSLPAAIAalPSEAFSAPRAAacrANASAAPRAAIAAASAPHAAS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  818 QATVDEAQGTWPSLHSGGLDLHPPFASSGGPGVslmprVTPSLEPWAATEATVGPTDSVATLGPRN---AGGIWDSGSYA 894
Cdd:pfam17823  173 PAPRTAASSTTAASSTTAASSAPTTAASSAPAT-----LTPARGISTAATATGHPAAGTALAAVGNsspAAGTVTAAVGT 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  895 VEGADSPTLSLQVAVDTSVVTSLMSLDPGDKVRVLAMSTVAFSNSQSHLELEGQMvTQGT---LGASAPRHEGSPlgEPT 971
Cdd:pfam17823  248 VTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQ-AQGPiiqVSTDQPVHNTAG--EPT 324

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333603193  972 fPPWTPTAASMDEPVSVSSGEPTV----------PWDSHSTLLPASLGPdefelEVLASSP 1022
Cdd:pfam17823  325 -PSPSNTTLEPNTPKSVASTNLAVvtttkaqakePSASPVPVLHTSMIP-----EVEATSP 379
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1132-1255 9.51e-67

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: 220.53  E-value: 9.51e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSFGRENTWIGLNDRIVERDFQWTDNTGLQYE 1211
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1333603193 1212 NWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKG 1255
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 44-165 5.59e-62

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: 207.00  E-value: 5.59e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   44 KVGSGSVRAALAELVALPCLFTLRPQQSAAREAPRIKWTKVRTaSGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYPRHR 123
Cdd:cd05902      1 RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLST-SGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1333603193  124 ANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
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 ...
 264-359 6.61e-56

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: 188.68  E-value: 6.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 343
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1333603193  344 RTGFPAPGARFDAYCF 359
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 ...
 163-257 2.50e-55

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: 186.84  E-value: 2.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRRSLPGVRS 242
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1333603193  243 YGRRDPRELYDVYCF 257
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
LINK smart00445
Link (Hyaluronan-binding);
162-258 3.75e-43

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 152.11  E-value: 3.75e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   162 GVVFHYRAaQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDrrsLPGVR 241
Cdd:smart00445    2 GGVFHVEK-NGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGN---LPGVR 77

                            90
                    ....*....|....*..
gi 1333603193   242 SYGRRDPRELYDVYCFA 258
Cdd:smart00445   78 QYGFPDPTSRYDAYCFN 94
LINK smart00445
Link (Hyaluronan-binding);
263-360 1.75e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 1.75e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   263 GEVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRtvyr 340
Cdd:smart00445    2 GGVFHVEKNGRykLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR---- 77

                            90       100
                    ....*....|....*....|
gi 1333603193   341 fanRTGFPAPGARFDAYCFR 360
Cdd:smart00445   78 ---QYGFPDPTSRYDAYCFN 94
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1132-1253 1.58e-40

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: 145.82  E-value: 1.58e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF-----GRENTWIGLNDRIVERDFQWTDNT 1206
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLlknsgSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1333603193  1207 GL-QYENWRENQPDNffaGGEDCVVMVAHeSGRWNDVPCNYNLPYVCK 1253
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVLSTS-GGKWNDVSCTSKLPFVCE 124
Xlink pfam00193
Extracellular link domain;
163-257 8.36e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 139.63  E-value: 8.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAaQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRrslPGVRS 242
Cdd:pfam00193    1 GVFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1333603193  243 YGRRDP-RELYDVYCF 257
Cdd:pfam00193   77 YGFRDPlSERYDAYCY 92
Xlink pfam00193
Extracellular link domain;
264-359 2.76e-38

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 138.09  E-value: 2.76e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTvyrf 341
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQ---- 76

                           90
                   ....*....|....*....
gi 1333603193  342 anrTGFPAP-GARFDAYCF 359
Cdd:pfam00193   77 ---YGFRDPlSERYDAYCY 92
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1153-1254 9.19e-28

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 108.72  E-value: 9.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1153 WEDAERDCRHRAGHLTSIHSPEEHGFINSFGR---ENTWIGLNDRIVERDFQWTDNTGLQYENWRENQPDNffAGGEDCV 1229
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKksnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENEDCV 81

                           90       100
                   ....*....|....*....|....*
gi 1333603193 1230 VMvAHESGRWNDVPCNYNLPYVCKK 1254
Cdd:pfam00059   82 EL-SSSSGKWNDENCNSKNPFVCEK 105
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1259-1315 4.07e-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: 62.48  E-value: 4.07e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193 1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
Sushi pfam00084
Sushi repeat (SCR repeat);
1259-1315 2.74e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 57.12  E-value: 2.74e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193 1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:pfam00084    1 CPPPPDIPNGKVSA-TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1090-1126 3.10e-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: 56.49  E-value: 3.10e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1333603193 1090 DIDDCVS-SPCENGGTCIDEVNTFICLCLPSYGGSLCE 1126
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1259-1315 9.60e-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: 55.61  E-value: 9.60e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193  1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
1090-1126 2.14e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.18  E-value: 2.14e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1333603193  1090 DIDDCVS-SPCENGGTCIDEVNTFICLCLPSY-GGSLCE 1126
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 45-161 1.29e-08

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: 54.00  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   45 VGSGSVRAALAELVALPCLFTLrpqqSAAREAPRIKWTKVRTasGQRQDLPILVAKDNVVRVAKgwQGRVSLPAYPRhRA 124
Cdd:pfam07686    1 QTPREVTVALGGSVTLPCTYSS----SMSEASTSVYWYRQPP--GKGPTFLIAYYSNGSEEGVK--KGRFSGRGDPS-NG 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1333603193  125 NATLLLGPLRASDSGLYRCQVV-RGIEDEQDLVPLEVT 161
Cdd:pfam07686   72 DGSLTIQNLTLSDSGTYTCAVIpSGEGVFGKGTRLTVL 109
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1056-1086 6.31e-08

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: 49.69  E-value: 6.31e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1333603193 1056 CENNPCLHGGTCKANGTMYGCSCDQGFTGEN 1086
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 355-775 1.37e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 56.33  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  355 DAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDFQEPLVSSGEEEPlilaeRQESQETPSP 434
Cdd:PHA03307    16 EGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP-----ANESRSTPTW 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  435 ASGGPMLASRPALEAEEvwlstvAPSRSSmEAGTARTTHREATPASATPRKRGRFK--GLNGRHFQEQEPQQGLEGGLEA 512
Cdd:PHA03307    91 SLSTLAPASPAREGSPT------PPGPSS-PDPPPPTPPPASPPPSPAPDLSEMLRpvGSPGPPPAASPPAAGASPAAVA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  513 SAHAPTSEAAgnqvePPLAVeTTDALRTGPNQSPwavltnevDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSRALGLE 592
Cdd:PHA03307   164 SDAASSRQAA-----LPLSS-PEETARAPSSPPA--------EPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  593 LEEVEGPSVRPATPNL--PWSPLEATalgPRPSEGPSTIPweappmiSSPDLPVVAMLRAPKLGllphptpfttqangik 670
Cdd:PHA03307   230 DDAGASSSDSSSSESSgcGWGPENEC---PLPRPAPITLP-------TRIWEASGWNGPSSRPG---------------- 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  671 rhgeamvTAPPSPASEIEASPQDPIHPELYSLPPSLDLKEQGGEATSSTLSGHGAGIPTAPLQAASDAQGGASPNSPRAD 750
Cdd:PHA03307   284 -------PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356

                          410       420
                   ....*....|....*....|....*
gi 1333603193  751 LGETGGTSPtglSKAEHPRSSPQAS 775
Cdd:PHA03307   357 PPPADPSSP---RKRPRPSRAPSSP 378
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1054-1088 1.25e-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: 46.09  E-value: 1.25e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1333603193 1054 DPCE-NNPCLHGGTCK--ANGtmYGCSCDQGFTGENCE 1088
Cdd:cd00054      3 DECAsGNPCQNGGTCVntVGS--YRCSCPPGYTGRNCE 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1094-1123 3.33e-06

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: 44.68  E-value: 3.33e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333603193 1094 CVSSPCENGGTCIDEVNTFICLCLPSYGGS 1123
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 113-604 4.11e-05

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 48.33  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  113 RVSLPAYP-RHRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVFHYRAAQDRYALTFAEAQEACRLSSAT 191
Cdd:COG3321    860 RVPLPTYPfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  192 IAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRRSLPGVRSYGRRDPRELYDVYCFARELGGEVFY---- 267
Cdd:COG3321    940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAaaaa 1019

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  268 VGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGF 347
Cdd:COG3321   1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  348 PAPGARFDAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDFQEPLVSSGEEEPLILAERQE 427
Cdd:COG3321   1100 AALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  428 SQETPSPASGGPMLASRPALEAEEVWLSTVAPSRSSMEAGTARTTHREATPASATPRKRGRFKGLNGRHFQEQEPQQGLE 507
Cdd:COG3321   1180 ALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAAL 1259

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  508 GGLEASAHAPTSEAAGNQVEPPLAVETTDALRTGPNQSPWAVLTNEVDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSR 587
Cdd:COG3321   1260 AALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAA 1339

                          490
                   ....*....|....*..
gi 1333603193  588 ALGLELEEVEGPSVRPA 604
Cdd:COG3321   1340 ALALAAAAAAAAAAAAA 1356
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 683-1022 4.98e-05

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: 47.65  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  683 PASEIEASPQDPIHPELYSLPPSLDLKEQGGEA-------TSSTLSGHGAGIPTAPLqAASDAQGGASPNSPR------- 748
Cdd:pfam17823   14 PLSESHAAPADPRHFVLNKMWNGAGKQNASGDAvpradnkSSEQ*NFCAATAAPAPV-TLTKGTSAAHLNSTEvtaehtp 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  749 --ADLGE---TGGTSPTGLSKA-EHPRSSPQASVDGNEVVDFA--PTETATEPTGV---TGILGSESGVFSTAESPTFSS 817
Cdd:pfam17823   93 hgTDLSEpatREGAADGAASRAlAAAASSSPSSAAQSLPAAIAalPSEAFSAPRAAacrANASAAPRAAIAAASAPHAAS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  818 QATVDEAQGTWPSLHSGGLDLHPPFASSGGPGVslmprVTPSLEPWAATEATVGPTDSVATLGPRN---AGGIWDSGSYA 894
Cdd:pfam17823  173 PAPRTAASSTTAASSTTAASSAPTTAASSAPAT-----LTPARGISTAATATGHPAAGTALAAVGNsspAAGTVTAAVGT 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  895 VEGADSPTLSLQVAVDTSVVTSLMSLDPGDKVRVLAMSTVAFSNSQSHLELEGQMvTQGT---LGASAPRHEGSPlgEPT 971
Cdd:pfam17823  248 VTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQ-AQGPiiqVSTDQPVHNTAG--EPT 324

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333603193  972 fPPWTPTAASMDEPVSVSSGEPTV----------PWDSHSTLLPASLGPdefelEVLASSP 1022
Cdd:pfam17823  325 -PSPSNTTLEPNTPKSVASTNLAVvtttkaqakePSASPVPVLHTSMIP-----EVEATSP 379
EGF_CA smart00179
Calcium-binding EGF-like domain;
1054-1088 2.31e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.92  E-value: 2.31e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1333603193  1054 DPCE-NNPCLHGGTC--KANGtmYGCSCDQGFT-GENCE 1088
Cdd:smart00179    3 DECAsGNPCQNGGTCvnTVGS--YRCECPPGYTdGRNCE 39
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1132-1206 5.29e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 43.18  E-value: 5.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF-GRENTWIGLNDRIVERDFQWTDNT 1206
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYkDSSDHWIGLNRESSNHPWKWADNS 163
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1124-1253 6.05e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 44.69  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1124 LCEKDTEgcdrgWHKFQGHCYRYFAHRRAWEDAERDCRHRA-GHLTSIHSPEEHGFI-----NSFGReNTWIGLND--RI 1195
Cdd:TIGR00864  317 HCPKDGE-----IFEENGHCFQIVPEEAAWLDAQEQCLARAgAALAIVDNDALQNFLarkvtHSLDR-GVWIGFSDvnGA 390

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333603193 1196 VERDFQWTDNTGLQY-ENWRENQPDnfFAGGEDCVVMvaHESGRWNDVPCNYNLPYVCK 1253
Cdd:TIGR00864  391 EKGPAHQGEAFEAEEcEEGLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
 
Name Accession Description Interval E-value
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 1132-1255 9.51e-67

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: 220.53  E-value: 9.51e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSFGRENTWIGLNDRIVERDFQWTDNTGLQYE 1211
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQWIGLNDRTIEGDFRWSDGHPLQFE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1333603193 1212 NWRENQPDNFFAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKKG 1255
Cdd:cd03588     81 NWRPNQPDNFFATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKKG 124
Ig_Neurocan cd05902
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 44-165 5.59e-62

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: 207.00  E-value: 5.59e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   44 KVGSGSVRAALAELVALPCLFTLRPQQSAAREAPRIKWTKVRTaSGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYPRHR 123
Cdd:cd05902      1 RVTAPPVRRPLSSSVLLPCVFTLPPSASSPPEGPRIKWTKLST-SGGQQQRPVLVARDNVVRVAKAFQGRVSLPGYPKNR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1333603193  124 ANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
Cdd:cd05902     80 YNASLVLSRLRYSDSGTYRCEVVLGINDEQDTVPLEVTGVVF 121
Ig_Aggrecan_like cd05878
Immunoglobulin (Ig)-like domain of the aggrecan-like chondroitin sulfate proteoglycan core ...
 44-165 5.89e-59

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: 198.61  E-value: 5.89e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   44 KVGSGSVRAALAELVALPCLFTLRPQ---QSAAREAPRIKWTKVRTASGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYP 120
Cdd:cd05878      1 IPQSSPVRVLLGTSVTLPCYFIDPPHpvtPSTAPLAPRIKWSKVSVDGKKEKEVVLLVATEGRVRVNSAYQGRVSLPNYP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1333603193  121 RHRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
Cdd:cd05878     81 AIPSDATLEVQSLRASDSGLYRCEVMHGIEDSQDTVELVVKGVVF 125
Ig_CSPGs_LP_like cd05714
Immunoglobulin (Ig)-like domain of chondroitin sulfate proteoglycans (CSPGs), human cartilage ...
 44-165 1.48e-58

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: 197.43  E-value: 1.48e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   44 KVGSGSVRAALAELVALPCLFTLRPQ-QSAAREAPRIKWTKVRTASGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYPRH 122
Cdd:cd05714      1 EAESAKVFSHLGGNVTLPCKFYRDPTaFGSGIHKIRIKWTKLTSDSGYLKEVDVLVAMGNVVYHKKTYGGRVSVPLKPGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1333603193  123 RANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
Cdd:cd05714     81 DSDASLVITDLTASDYGLYRCEVIEGIEDDQDVVALDVQGVVF 123
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 ...
 264-359 6.61e-56

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: 188.68  E-value: 6.61e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 343
Cdd:cd03520      1 EVFYATAPEKFTFQEARAECRSLGAVLATTGQLYAAWRQGLDQCDPGWLADGSVRYPISTPRPQCGGGLPGVRTLYRFPN 80

                           90
                   ....*....|....*.
gi 1333603193  344 RTGFPAPGARFDAYCF 359
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 ...
 163-257 2.50e-55

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: 186.84  E-value: 2.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRRSLPGVRS 242
Cdd:cd03517      1 VVFHYRDATARYALTFPRAQRACLDISAQIATPEQLLAAYEDGFEQCDAGWLADQTVRYPIQTPREGCYGDMDGFPGVRN 80

                           90
                   ....*....|....*
gi 1333603193  243 YGRRDPRELYDVYCF 257
Cdd:cd03517     81 YGVRDPDELYDVYCY 95
LINK smart00445
Link (Hyaluronan-binding);
162-258 3.75e-43

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 152.11  E-value: 3.75e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   162 GVVFHYRAaQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDrrsLPGVR 241
Cdd:smart00445    2 GGVFHVEK-NGRYKLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGN---LPGVR 77

                            90
                    ....*....|....*..
gi 1333603193   242 SYGRRDPRELYDVYCFA 258
Cdd:smart00445   78 QYGFPDPTSRYDAYCFN 94
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 1132-1254 5.15e-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: 152.84  E-value: 5.15e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYrYFAH-RRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF--GRENTWIGLNDRIVERDFQWTDNTGL 1208
Cdd:cd03590      1 CPTNWKSFQSSCY-FFSTeKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIlsGNRSYWIGLSDEETEGEWKWVDGTPL 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1333603193 1209 Q--YENWRENQPDNFFAGGEDCVVMVaHESGRWNDVPCNYNLPYVCKK 1254
Cdd:cd03590     80 NssKTFWHPGEPNNWGGGGEDCAELV-YDSGGWNDVPCNLEYRWICEK 126
LINK smart00445
Link (Hyaluronan-binding);
263-360 1.75e-42

Link (Hyaluronan-binding);


Pssm-ID: 214667  Cd Length: 94  Bit Score: 150.19  E-value: 1.75e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   263 GEVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRtvyr 340
Cdd:smart00445    2 GGVFHVEKNGRykLTFAEAREACRAQGATLATVGQLYAAWQDGFDTCDAGWLADGSVRYPIITPRPRCGGNLPGVR---- 77

                            90       100
                    ....*....|....*....|
gi 1333603193   341 fanRTGFPAPGARFDAYCFR 360
Cdd:smart00445   78 ---QYGFPDPTSRYDAYCFN 94
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 163-257 9.50e-42

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: 147.95  E-value: 9.50e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRrslPGVRS 242
Cdd:cd01102      1 VVFHLESQNGRYKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRN---PGVRS 77

                           90
                   ....*....|....*
gi 1333603193  243 YGRRDPRELYDVYCF 257
Cdd:cd01102     78 YGNPAPSGRYDAYCF 92
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 1132-1253 1.33e-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: 146.35  E-value: 1.33e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCR-----HRAGHLTSIHSPEEHGFI----NSFGRENT----WIGLNDRIVER 1198
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVydlfESSRGPDTpyglWIGLHDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193 1199 DFQWTDNTGLQYENWRENQPDNFFaGGEDCVVMVAHES--GRWNDVPCNYNLPYVCK 1253
Cdd:cd03589     81 PFEWTDGSPVDFTKWAGGQPDNYG-GNEDCVQMWRRGDagQSWNDMPCDAVFPYICK 136
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 1132-1253 1.58e-40

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: 145.82  E-value: 1.58e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF-----GRENTWIGLNDRIVERDFQWTDNT 1206
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLlknsgSSDYYWIGLSDPDSNGSWQWSDGS 80

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1333603193  1207 GL-QYENWRENQPDNffaGGEDCVVMVAHeSGRWNDVPCNYNLPYVCK 1253
Cdd:smart00034   81 GPvSYSNWAPGEPNN---SSGDCVVLSTS-GGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 1142-1254 2.26e-39

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: 141.99  E-value: 2.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1142 HCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF----GRENTWIGLNDRIVERDFQWTDNTG-LQYENWREN 1216
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLlkksSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1333603193 1217 QPDNffAGGEDCVVMVAHESGRWNDVPCNYNLPYVCKK 1254
Cdd:cd00037     81 EPNP--GGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
Xlink pfam00193
Extracellular link domain;
163-257 8.36e-39

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 139.63  E-value: 8.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAaQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRrslPGVRS 242
Cdd:pfam00193    1 GVFHLES-PGRYKLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNM---PGVRQ 76

                           90
                   ....*....|....*.
gi 1333603193  243 YGRRDP-RELYDVYCF 257
Cdd:pfam00193   77 YGFRDPlSERYDAYCY 92
Xlink pfam00193
Extracellular link domain;
264-359 2.76e-38

Extracellular link domain;


Pssm-ID: 459706  Cd Length: 92  Bit Score: 138.09  E-value: 2.76e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPARR--LTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTvyrf 341
Cdd:pfam00193    1 GVFHLESPGRykLTFQEAQAACAALGATLATPEQLYAAWKAGLDTCDAGWLADGTVRYPITTPRPNCGGNMPGVRQ---- 76

                           90
                   ....*....|....*....
gi 1333603193  342 anrTGFPAP-GARFDAYCF 359
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 ...
 1132-1253 7.00e-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: 121.32  E-value: 7.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCR-HRAG-HLTSIHSPEEHGFINSF------GRENTWIGLNDRIVERDFQWT 1203
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCQkYGPGaHLASIHSPAEAAAIASLissyqkAYQPVWIGLHDPQQSRGWEWS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333603193 1204 DNTGLQYENWRENQPdnfFAGGEDCVVMVAhESG--RWNDVPCNYNLPYVCK 1253
Cdd:cd03594     81 DGSKLDYRSWDRNPP---YARGGYCAELSR-STGflKWNDANCEERNPFICK 128
Link_Domain cd01102
The link domain is a hyaluronan (HA)-binding domain. It functions to mediate adhesive ...
 264-359 1.54e-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: 1.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPAR---RLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVyr 340
Cdd:cd01102      1 VVFHLESQNgryKLTFAEAALACKARGAHLATPGQLEAAWQDGFDVCTAGWLADGSVRYPIVTSRPNCGGRNPGVRSY-- 78

                           90
                   ....*....|....*....
gi 1333603193  341 fanrtGFPAPGARFDAYCF 359
Cdd:cd01102     79 -----GNPAPSGRYDAYCF 92
Link_domain_HAPLN_module_1 cd03518
Link_domain_HAPLN_module_1; this link domain is found in the first link module of proteins ...
 163-257 2.03e-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: 118.68  E-value: 2.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  163 VVFHYRAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCyGDRRSLPGVRS 242
Cdd:cd03518      1 VVFPYQPRLGRYNLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPC-GGKRTVPGLRS 79

                           90
                   ....*....|....*.
gi 1333603193  243 YGRRDP-RELYDVYCF 257
Cdd:cd03518     80 YGERDKmLSRYDAFCF 95
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 264-359 3.85e-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: 117.52  E-value: 3.85e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  264 EVFYVGPARRLTLAGARAQCRRQGAALASVGQLHLAWH-EGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVyrfa 342
Cdd:cd03519      1 GVFYLLHPGKLTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLEPGVRSF---- 76

                           90
                   ....*....|....*...
gi 1333603193  343 nrtGFPAPGAR-FDAYCF 359
Cdd:cd03519     77 ---GFPDKKHKlYGVYCY 91
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 1153-1254 9.19e-28

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 108.72  E-value: 9.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1153 WEDAERDCRHRAGHLTSIHSPEEHGFINSFGR---ENTWIGLNDRIVERDFQWTDNTGLQYENWRENQPDNffAGGEDCV 1229
Cdd:pfam00059    4 WDEAREACRKLGGHLVSINSAEELDFLSSTLKksnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNN--GENEDCV 81

                           90       100
                   ....*....|....*....|....*
gi 1333603193 1230 VMvAHESGRWNDVPCNYNLPYVCKK 1254
Cdd:pfam00059   82 EL-SSSSGKWNDENCNSKNPFVCEK 105
Ig_Versican cd05901
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 47-165 1.98e-27

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: 108.51  E-value: 1.98e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   47 SGSVRAALAELVALPCLF----TLRPQQSAAREAPRIKWTKVRTASGQR--QDLPILVAKDNVVRVAKGWQGRVSLPAYP 120
Cdd:cd05901      4 SSRVHGSLSGSVVLPCRFstlpTLPPSYNITSEFLRIKWTKIQVDKNGKdhKETTVLVAQNGIIKIGQEYMGRVSVPSHP 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1333603193  121 RHRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
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 ...
 273-359 4.02e-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: 97.88  E-value: 4.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  273 RLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGP--APGVRTVyrfanrtGFPAP 350
Cdd:cd03518     13 NLNFHEAQQACEEQDATLASFEQLYQAWTEGLDWCNAGWLSDGTVQYPITKPREPCGGKrtVPGLRSY-------GERDK 85

                           90
                   ....*....|
gi 1333603193  351 G-ARFDAYCF 359
Cdd:cd03518     86 MlSRYDAFCF 95
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 1154-1252 2.19e-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: 2.19e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1154 EDAERDCRHRAGHLTSIHSPEEHGFINSF---GRENTWIGLNDRIVERDFQWTDNTGLQYENWRENQPDNfFAGGEDCVV 1230
Cdd:cd03591     14 DDAQKLCSEAGGTLAMPRNAAENAAIASYvkkGNTYAFIGITDLETEGQFVYLDGGPLTYTNWKPGEPNN-AGGGEDCVE 92

                           90       100
                   ....*....|....*....|..
gi 1333603193 1231 MVAheSGRWNDVPCNYNLPYVC 1252
Cdd:cd03591     93 MYT--SGKWNDVACNLTRLFVC 112
Ig_Aggrecan cd05900
Immunoglobulin (Ig)-like domain of the chondroitin sulfate proteoglycan core protein (CSPG), ...
 50-165 8.09e-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: 89.23  E-value: 8.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   50 VRAALAELVALPCLFTLRPQQ-----SAAREAPRIKWTKVrtasGQRQDLPILVAKDNVVRVAKGWQGRVSLPAYPRHRA 124
Cdd:cd05900      7 LRVVLGSSLLIPCYFQDPIAKdpgapTVAPLSPRIKWSFI----SKEKESVLLVATEGKVRVNTEYLDRVSLPNYPAIPS 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1333603193  125 NATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
Cdd:cd05900     83 DATLEITELRSNDSGTYRCEVMHGIEDNYDTVEVQVKGIVF 123
Link_domain_HAPLN_module_2 cd03519
Link_domain_HAPLN_module_2; this link domain is found in the second link module of proteins ...
 176-257 1.41e-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: 84.78  E-value: 1.41e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  176 LTFAEAQEACRLSSATIAAPRHLQAAFE-DGFDNCDAGWLSDRTVRYPITQSRPGCYGDRrslPGVRSYGRRDP-RELYD 253
Cdd:cd03519     11 LTFSEAVAACQRDGAQIAKVGQLFAAWKfHGLDRCDAGWLADGSVRYPISRPRPRCGPLE---PGVRSFGFPDKkHKLYG 87


                   ....
gi 1333603193  254 VYCF 257
Cdd:cd03519     88 VYCY 91
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 1144-1252 1.62e-19

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: 85.50  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1144 YRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSFGR----ENTWIGLNDRIVERDFQWTDNTGLQYENWRENQPD 1219
Cdd:cd03592      3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALkynlGYYWIDGNDINNEGTWVDTDKKELEYKNWAPGEPN 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1333603193 1220 NffAGGEDCVVMVAHESGRWNDVPCNYNLPYVC 1252
Cdd:cd03592     83 N--GRNENCLEIYIKDNGKWNDEPCSKKKSAIC 113
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 1142-1251 2.21e-19

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: 85.17  E-value: 2.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1142 HCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFI--NSFGRENTWIGLNDRIVERDFQWTDNTGLQYENWRENQPD 1219
Cdd:cd03603      1 HFYKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLlsNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPH 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1333603193 1220 NFFAGGEDCVVM--VAHESGRWNDVPCNYNLPYV 1251
Cdd:cd03603     81 NNGGGNEDYAAInhFPGISGKWNDLANSYNTLGY 114
Ig_LP_like cd05877
Immunoglobulin (Ig)-like domain of human cartilage link protein (LP), and similar domains; The ...
 58-165 1.03e-18

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: 83.14  E-value: 1.03e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   58 VALPCLFTLRPQQSAAREApRIKWTKVRTASGQRQDlpILVAKDNVVRVAKGWQGRVSLpayprHRA---NATLLLGPLR 134
Cdd:cd05877     15 VTLPCRYHYEPELSAPRKI-RVKWTKLEVDYAKEED--VLVAIGTRHKSYGSYQGRVFL-----RRAddlDASLVITDLR 86

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1333603193  135 ASDSGLYRCQVVRGIEDEQDLVPLEVTGVVF 165
Cdd:cd05877     87 LEDYGRYRCEVIDGLEDESVVVALRLRGVVF 117
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 ...
 164-257 5.95e-17

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: 77.12  E-value: 5.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  164 VFHYRAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCyGDRRSlpGVRSY 243
Cdd:cd03515      2 VFHLRSRSGKYKLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANC-GFGHV--GIVDY 78

                           90
                   ....*....|....*
gi 1333603193  244 G-RRDPRELYDVYCF 257
Cdd:cd03515     79 GpRLNLSERWDAYCY 93
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 1132-1254 2.24e-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: 73.52  E-value: 2.24e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSFGRENT-WIGLNDRIVERDFQWTDNTglQY 1210
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSSyWIGLSREKSEKPWKWIDGS--PL 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1333603193 1211 ENWRENQPDNffaGGEDCVVMvahESGRWNDVPCNYNLPYVCKK 1254
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 ...
 1141-1252 1.13e-13

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: 68.63  E-value: 1.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1141 GHCYRYFAHRRAWEDAERDCRH-RAGHLTSIHSPEEHGFINSF-GREN---TWIG--LNDRIVERDFQWTDNTGLQYENW 1213
Cdd:cd03598      1 GRCYRFVKSPRTFRDAQVICRRcYRGNLASIHSFAFNYRVQRLvSTLNqaqVWIGgiITGKGRCRRFSWVDGSVWNYAYW 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1333603193 1214 RENQPDNffaGGEDCVVMVAHEsGRWNDVPCNYNLPYVC 1252
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 ...
 1132-1252 8.08e-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: 66.64  E-value: 8.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGwHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSFGR------ENTWIGLNDRIVERdfQWTDN 1205
Cdd:cd03596      1 CLKG-TKIHKKCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKasvpgnWEVWLGINDMVAEG--KWVDV 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333603193 1206 TGLQ--YENWREN---QPDnffaGG--EDCVVMVAHESGRWNDVPCNYNLPYVC 1252
Cdd:cd03596     78 NGSPisYFNWEREitaQPD----GGkrENCVALSSSAQGKWFDEDCRREKPYVC 127
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
 1259-1315 4.07e-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: 62.48  E-value: 4.07e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193 1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:cd00033      1 CPPPPVPENGTVTG-SKGSYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTC 56
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 1132-1253 2.17e-11

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: 63.37  E-value: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1132 CDRGwhkFQGHCYR--YF--AHRRA-WEDAERDCRHRAGHLTSIHSPEEHGFINSFGRE------NTWIGL---NDRIVE 1197
Cdd:cd03595      4 CRRG---TEKPCYKiaYFqdSRRRLnFEEARQACREDGGELLSIESENEQKLIERFIQTlrasdgDFWIGLrrsSQYNVT 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333603193 1198 RD-----FQWTDNTGLQYENWRENQPDnffAGGEDCVVMVAHESG----------RWNDVPCNYNLPYVCK 1253
Cdd:cd03595     81 SSacsslYYWLDGSISTFRNWYVDEPS---CGSEVCVVMYHQPSApagqggpylfQWNDDNCNMKNNFICK 148
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 1153-1252 5.07e-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: 60.85  E-value: 5.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1153 WEDAERDCRHRAGHLTSIHSPEEHGFINSFGRENT---WIGLNDRIVErdFQWTDNTGLQYENWRENQPDnffaGGEDCV 1229
Cdd:cd03602     12 WSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNsaaWIGLYRDVDS--WRWSDGSESSFRNWNTFQPF----GQGDCA 85

                           90       100
                   ....*....|....*....|...
gi 1333603193 1230 VMvaHESGRWNDVPCNYNLPYVC 1252
Cdd:cd03602     86 TM--YSSGRWYAALCSALKPFIC 106
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 ...
 273-359 1.33e-10

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: 59.40  E-value: 1.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  273 RLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVrTVYRF-ANRTgfpapg 351
Cdd:cd03515     13 KLTYTEAKAACEAEGAHLATYSQLSAAQQLGFHLCAAGWLAKGRVGYPIVFPSANCGFGHVGI-VDYGPrLNLS------ 85


                   ....*...
gi 1333603193  352 ARFDAYCF 359
Cdd:cd03515     86 ERWDAYCY 93
Sushi pfam00084
Sushi repeat (SCR repeat);
1259-1315 2.74e-10

Sushi repeat (SCR repeat);


Pssm-ID: 459664 [Multi-domain]  Cd Length: 56  Bit Score: 57.12  E-value: 2.74e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193 1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:pfam00084    1 CPPPPDIPNGKVSA-TKNEYNYGASVSYECDPGYRLVGSPTITCQEDGTWSPPFPEC 56
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1090-1126 3.10e-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: 56.49  E-value: 3.10e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1333603193 1090 DIDDCVS-SPCENGGTCIDEVNTFICLCLPSYGGSLCE 1126
Cdd:cd00054      1 DIDECASgNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 1140-1253 8.33e-10

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: 58.60  E-value: 8.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1140 QGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF----------GRENTWIGLNDRIVE--------RDFQ 1201
Cdd:cd03600      3 SDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLlaagpgrhgrGSLRLWIGLQREPRQcsdpslplRGFS 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333603193 1202 W-TDNTGLQYENW-RENQPDnffAGGEDCVVMVAHESG----RWNDVPCNYNLP-YVCK 1253
Cdd:cd03600     83 WvTGDQDTDFSNWlQEPAGT---CTSPRCVALSAAGSTpdnlKWKDGPCSARADgYLCK 138
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
 1259-1315 9.60e-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: 55.61  E-value: 9.60e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333603193  1259 CGPPPTVENASPIGaRKAKYNVHATVRYQCDEGFAQRHVAIIRCRSNGKWDRPQIVC 1315
Cdd:smart00032    1 CPPPPDIENGTVTS-SSGTYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56
EGF_CA smart00179
Calcium-binding EGF-like domain;
1090-1126 2.14e-09

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 54.18  E-value: 2.14e-09
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1333603193  1090 DIDDCVS-SPCENGGTCIDEVNTFICLCLPSY-GGSLCE 1126
Cdd:smart00179    1 DIDECASgNPCQNGGTCVNTVGSYRCECPPGYtDGRNCE 39
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
 45-161 1.29e-08

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: 54.00  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   45 VGSGSVRAALAELVALPCLFTLrpqqSAAREAPRIKWTKVRTasGQRQDLPILVAKDNVVRVAKgwQGRVSLPAYPRhRA 124
Cdd:pfam07686    1 QTPREVTVALGGSVTLPCTYSS----SMSEASTSVYWYRQPP--GKGPTFLIAYYSNGSEEGVK--KGRFSGRGDPS-NG 71

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1333603193  125 NATLLLGPLRASDSGLYRCQVV-RGIEDEQDLVPLEVT 161
Cdd:pfam07686   72 DGSLTIQNLTLSDSGTYTCAVIpSGEGVFGKGTRLTVL 109
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1056-1086 6.31e-08

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: 49.69  E-value: 6.31e-08
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1333603193 1056 CENNPCLHGGTCKANGTMYGCSCDQGFTGEN 1086
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 355-775 1.37e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 56.33  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  355 DAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDFQEPLVSSGEEEPlilaeRQESQETPSP 434
Cdd:PHA03307    16 EGGEFFPRPPATPGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAP-----ANESRSTPTW 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  435 ASGGPMLASRPALEAEEvwlstvAPSRSSmEAGTARTTHREATPASATPRKRGRFK--GLNGRHFQEQEPQQGLEGGLEA 512
Cdd:PHA03307    91 SLSTLAPASPAREGSPT------PPGPSS-PDPPPPTPPPASPPPSPAPDLSEMLRpvGSPGPPPAASPPAAGASPAAVA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  513 SAHAPTSEAAgnqvePPLAVeTTDALRTGPNQSPwavltnevDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSRALGLE 592
Cdd:PHA03307   164 SDAASSRQAA-----LPLSS-PEETARAPSSPPA--------EPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAA 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  593 LEEVEGPSVRPATPNL--PWSPLEATalgPRPSEGPSTIPweappmiSSPDLPVVAMLRAPKLGllphptpfttqangik 670
Cdd:PHA03307   230 DDAGASSSDSSSSESSgcGWGPENEC---PLPRPAPITLP-------TRIWEASGWNGPSSRPG---------------- 283

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  671 rhgeamvTAPPSPASEIEASPQDPIHPELYSLPPSLDLKEQGGEATSSTLSGHGAGIPTAPLQAASDAQGGASPNSPRAD 750
Cdd:PHA03307   284 -------PASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356

                          410       420
                   ....*....|....*....|....*
gi 1333603193  751 LGETGGTSPtglSKAEHPRSSPQAS 775
Cdd:PHA03307   357 PPPADPSSP---RKRPRPSRAPSSP 378
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 164-257 3.07e-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: 51.31  E-value: 3.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  164 VFHYrAAQDRYALTFAEAQEACRLSSATIAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCygdRRSLPGVrsY 243
Cdd:cd03516      8 VFLV-EKNGRYSLNFTEAKEACRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLC---GKNGTGV--Y 81

                           90
                   ....*....|....*
gi 1333603193  244 GRRDPREL-YDVYCF 257
Cdd:cd03516     82 ILNSNLSSrYDAYCY 96
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 1054-1088 1.25e-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: 46.09  E-value: 1.25e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1333603193 1054 DPCE-NNPCLHGGTCK--ANGtmYGCSCDQGFTGENCE 1088
Cdd:cd00054      3 DECAsGNPCQNGGTCVntVGS--YRCSCPPGYTGRNCE 38
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
 49-146 3.17e-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: 47.44  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193   49 SVRAALAELVALPCLFTlrpqQSAAREAPRIKWTKVRTasGQRQDLPILVAKDNVVrVAKGWQGRVSLPAYPRHRANATL 128
Cdd:cd05718      8 EVTGFLGGSVTLPCSLT----SPGTTKITQVTWMKIGA--GSSQNVAVFHPQYGPS-VPNPYAERVEFLAARLGLRNATL 80

                           90
                   ....*....|....*...
gi 1333603193  129 LLGPLRASDSGLYRCQVV 146
Cdd:cd05718     81 RIRNLRVEDEGNYICEFA 98
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 1094-1123 3.33e-06

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: 44.68  E-value: 3.33e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333603193 1094 CVSSPCENGGTCIDEVNTFICLCLPSYGGS 1123
Cdd:pfam00008    1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGK 30
PHA03247 PHA03247
large tegument protein UL36; Provisional
 429-771 4.67e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  429 QETPSPASGGPM----LASRPALEAEEVWLSTVAPsRSSMEAGTARTTHREATPASATPRKRGRFKGlngrhfqeQEPQQ 504
Cdd:PHA03247  2541 EELASDDAGDPPpplpPAAPPAAPDRSVPPPRPAP-RPSEPAVTSRARRPDAPPQSARPRAPVDDRG--------DPRGP 2611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  505 GLEGGLEASAHAPTSEAAGNQVEPPLAVETTDALRTGPNQSPWAVLTNEVDVPGAGSLGGRSPPE---PWLWPPTVAPPS 581
Cdd:PHA03247  2612 APPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQAsspPQRPRRRAARPT 2691

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  582 IpGPSRALGleleEVEGPSVRPATPNLPWSPLEATALGPRPSEGPStipweaPPMISSPDLPVVAMLRAPKLGLLPHPTP 661
Cdd:PHA03247  2692 V-GSLTSLA----DPPPPPPTPEPAPHALVSATPLPPGPAAARQAS------PALPAAPAPPAVPAGPATPGGPARPARP 2760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  662 FTTQANGIKRHGEAMVTAPP-----------SPASEIEASPQDPIHPELYSLPPSLDLKEQ----GGEATSSTLSGHGAG 726
Cdd:PHA03247  2761 PTTAGPPAPAPPAAPAAGPPrrltrpavaslSESRESLPSPWDPADPPAAVLAPAAALPPAaspaGPLPPPTSAQPTAPP 2840

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1333603193  727 IPTAPLQAASDAQGGASPNSPRADLGETGGTSPTGLSKAeHPRSS 771
Cdd:PHA03247  2841 PPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPA-RPPVR 2884
PHA03247 PHA03247
large tegument protein UL36; Provisional
 517-877 6.94e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  517 PTSEAAGNQVEPplAVETTDALRTGPNQSpwavltNEVDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSRA-------- 588
Cdd:PHA03247  2569 PPPRPAPRPSEP--AVTSRARRPDAPPQS------ARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSpaanepdp 2640

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  589 -LGLELEEVEGPSVRPATPNLPwSPLEATALGpRPSEGPSTIPWEAPPMISSPDLPVVAMLRAPKLGLLPHPTPFTTQAN 667
Cdd:PHA03247  2641 hPPPTVPPPERPRDDPAPGRVS-RPRRARRLG-RAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSA 2718

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  668 gikrhgeamVTAPPSPASEIEASPQDPIHPelyslppsldlkeqggeatsstlsghgagIPTAPLQAASDAQGGASPNSP 747
Cdd:PHA03247  2719 ---------TPLPPGPAAARQASPALPAAP-----------------------------APPAVPAGPATPGGPARPARP 2760

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  748 RADLGETGGTSPTGLSKAEHPRSSPQASVDGNEVVDFAPteTATEPTGVTGILGSESGVFSTAESPTfSSQATVDEAQGT 827
Cdd:PHA03247  2761 PTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLP--SPWDPADPPAAVLAPAAALPPAASPA-GPLPPPTSAQPT 2837

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333603193  828 WPSLHSGGLDLHPPFASSGGPGVSLMPRVTPSLEPWAATEATVGPTDSVA 877
Cdd:PHA03247  2838 APPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLA 2887
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1096-1126 2.61e-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: 2.61e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1333603193 1096 SSPCENGGTCIDEVNTFICLCLPSYGGSL-CE 1126
Cdd:cd00053      5 SNPCSNGGTCVNTPGSYRCVCPPGYTGDRsCE 36
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 1055-1088 3.00e-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: 42.08  E-value: 3.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1333603193 1055 PCE-NNPCLHGGTCKANGTMYGCSCDQGFTGE-NCE 1088
Cdd:cd00053      1 ECAaSNPCSNGGTCVNTPGSYRCVCPPGYTGDrSCE 36
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 113-604 4.11e-05

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


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 48.33  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  113 RVSLPAYP-RHRANATLLLGPLRASDSGLYRCQVVRGIEDEQDLVPLEVTGVVFHYRAAQDRYALTFAEAQEACRLSSAT 191
Cdd:COG3321    860 RVPLPTYPfQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAA 939

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  192 IAAPRHLQAAFEDGFDNCDAGWLSDRTVRYPITQSRPGCYGDRRSLPGVRSYGRRDPRELYDVYCFARELGGEVFY---- 267
Cdd:COG3321    940 AALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAaaaa 1019

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  268 VGPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFANRTGF 347
Cdd:COG3321   1020 ALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALAL 1099

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  348 PAPGARFDAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDFQEPLVSSGEEEPLILAERQE 427
Cdd:COG3321   1100 AALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  428 SQETPSPASGGPMLASRPALEAEEVWLSTVAPSRSSMEAGTARTTHREATPASATPRKRGRFKGLNGRHFQEQEPQQGLE 507
Cdd:COG3321   1180 ALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAAL 1259

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  508 GGLEASAHAPTSEAAGNQVEPPLAVETTDALRTGPNQSPWAVLTNEVDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSR 587
Cdd:COG3321   1260 AALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAA 1339

                          490
                   ....*....|....*..
gi 1333603193  588 ALGLELEEVEGPSVRPA 604
Cdd:COG3321   1340 ALALAAAAAAAAAAAAA 1356
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 683-1022 4.98e-05

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: 47.65  E-value: 4.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  683 PASEIEASPQDPIHPELYSLPPSLDLKEQGGEA-------TSSTLSGHGAGIPTAPLqAASDAQGGASPNSPR------- 748
Cdd:pfam17823   14 PLSESHAAPADPRHFVLNKMWNGAGKQNASGDAvpradnkSSEQ*NFCAATAAPAPV-TLTKGTSAAHLNSTEvtaehtp 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  749 --ADLGE---TGGTSPTGLSKA-EHPRSSPQASVDGNEVVDFA--PTETATEPTGV---TGILGSESGVFSTAESPTFSS 817
Cdd:pfam17823   93 hgTDLSEpatREGAADGAASRAlAAAASSSPSSAAQSLPAAIAalPSEAFSAPRAAacrANASAAPRAAIAAASAPHAAS 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  818 QATVDEAQGTWPSLHSGGLDLHPPFASSGGPGVslmprVTPSLEPWAATEATVGPTDSVATLGPRN---AGGIWDSGSYA 894
Cdd:pfam17823  173 PAPRTAASSTTAASSTTAASSAPTTAASSAPAT-----LTPARGISTAATATGHPAAGTALAAVGNsspAAGTVTAAVGT 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  895 VEGADSPTLSLQVAVDTSVVTSLMSLDPGDKVRVLAMSTVAFSNSQSHLELEGQMvTQGT---LGASAPRHEGSPlgEPT 971
Cdd:pfam17823  248 VTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQ-AQGPiiqVSTDQPVHNTAG--EPT 324

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333603193  972 fPPWTPTAASMDEPVSVSSGEPTV----------PWDSHSTLLPASLGPdefelEVLASSP 1022
Cdd:pfam17823  325 -PSPSNTTLEPNTPKSVASTNLAVvtttkaqakePSASPVPVLHTSMIP-----EVEATSP 379
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 1146-1254 8.27e-05

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 43.68  E-value: 8.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1146 YFAHRRA-WEDAERDCRHRAGHLTSIHSP--EEHGFINSF---GRENTWIGLND-RIVERDFQWTDNTGL--QYENWREN 1216
Cdd:cd03601      4 LCSDETMnYAKAGAFCRSRGMRLASLAMRdsEMRDAILAFtlvKGHGYWVGADNlQDGEYDFLWNDGVSLptDSDLWAPN 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1333603193 1217 QPDNfFAGGEDCVVMvAHESGRWNDVPCNYNLPYVCKK 1254
Cdd:cd03601     84 EPSN-PQSRQLCVQL-WSKYNLLDDEYCGRAKRVICEK 119
PHA03247 PHA03247
large tegument protein UL36; Provisional
 313-758 1.47e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  313 ADGSVryPIQTPRRRCGGPAPGVRtvyrfANRTGFPAPGARFDAycfrahhPTPQHGDPETPSS------GDEGEILSAE 386
Cdd:PHA03247  2564 PDRSV--PPPRPAPRPSEPAVTSR-----ARRPDAPPQSARPRA-------PVDDRGDPRGPAPpsplppDTHAPDPPPP 2629

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  387 GPLARELEPSLGEEEVVTPDFQEPLVSSGEEepLILAERQESQETPSPASGGPMLASRPALEAEEVWLSTVA-------- 458
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGR--VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdppppppt 2707

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  459 ------PSRSSMEAGTARTTHREATPAS-ATPRKRGRFKGLNGRHFQEQEPQQGLEGGLEASAhAPTSEAAGNQVEPPLA 531
Cdd:PHA03247  2708 pepaphALVSATPLPPGPAAARQASPALpAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA-PPAAPAAGPPRRLTRP 2786

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  532 VETTDALRTGPNQSPWAVLTNEVDVPG-AGSLGGRSPPEPWLWPPT----VAPPSIPGPSR-ALGLELEEVEGPSVRPAT 605
Cdd:PHA03247  2787 AVASLSESRESLPSPWDPADPPAAVLApAAALPPAASPAGPLPPPTsaqpTAPPPPPGPPPpSLPLGGSVAPGGDVRRRP 2866

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  606 PNLPWSPLEATALGP------RPSEGPSTIPWEAPPMISSPdlpvvamLRAPKLGLLPHPTPfttqangikrhgEAMVTA 679
Cdd:PHA03247  2867 PSRSPAAKPAAPARPpvrrlaRPAVSRSTESFALPPDQPER-------PPQPQAPPPPQPQP------------QPPPPP 2927

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  680 PPSPASEIEASPQDPihpelysLPPSLDLKEQGGEATSSTLSGHGAGIP-------TAPLQAASDAQGGASPNSPRADLG 752
Cdd:PHA03247  2928 QPQPPPPPPPRPQPP-------LAPTTDPAGAGEPSGAVPQPWLGALVPgrvavprFRVPQPAPSREAPASSTPPLTGHS 3000


                   ....*.
gi 1333603193  753 ETGGTS 758
Cdd:PHA03247  3001 LSRVSS 3006
hEGF pfam12661
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ...
 1099-1118 1.69e-04

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: 40.01  E-value: 1.69e-04
                           10        20
                   ....*....|....*....|
gi 1333603193 1099 CENGGTCIDEVNTFICLCLP 1118
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPP 20
EGF_CA smart00179
Calcium-binding EGF-like domain;
1054-1088 2.31e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.92  E-value: 2.31e-04
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1333603193  1054 DPCE-NNPCLHGGTC--KANGtmYGCSCDQGFT-GENCE 1088
Cdd:smart00179    3 DECAsGNPCQNGGTCvnTVGS--YRCECPPGYTdGRNCE 39
Link_domain_KIAA0527_like cd03521
Link_domain_KIAA0527_like; this domain is found in the human protein KIAA0527. Sequence-wise, ...
 274-358 4.49e-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: 40.68  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  274 LTLAGARAQCRRQGAALASVGQL-HLAWHEGLDQCDPGWLADGSVRYPIQTPrrRCGGPAPGVRTVYRFANRtgfPAPGA 352
Cdd:cd03521     14 LGLRAARQSCASLGARLASAAELrRAVVECFFSACARGWLADGTVGTTVCNP--VVAEALKAVDVKVEIETN---PIPFA 88


                   ....*.
gi 1333603193  353 RFDAYC 358
Cdd:cd03521     89 HYNALC 94
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
500-697 4.84e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 4.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  500 QEPQQGLEGGLEASAHAPTSEAAGNQVEPPLAVETTDALRTGPNQSPWAVLTNEvdvPGAGSLGGRSPPEPWLWPPTVAP 579
Cdd:PRK12323   364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAAR---AVAAAPARRSPAPEALAAARQAS 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  580 PSIPGPSRALGLELEEVEGPSVRPATPNLPWSPLEATALGPRPSEGPS-------TIPWEAPPMISSPDLPVVAMLRAPK 652
Cdd:PRK12323   441 ARGPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAApapadddPPPWEELPPEFASPAPAQPDAAPAG 520

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1333603193  653 LGLLPHPTPFTTQANGIKRHGEAMVTAPPSPASEIEASPQDPIHP 697
Cdd:PRK12323   521 WVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 1132-1206 5.29e-04

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 43.18  E-value: 5.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333603193 1132 CDRGWHKFQGHCYRYFAHRRAWEDAERDCRHRAGHLTSIHSPEEHGFINSF-GRENTWIGLNDRIVERDFQWTDNT 1206
Cdd:PHA02642    88 CPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYkDSSDHWIGLNRESSNHPWKWADNS 163
Link_domain_CD44_like cd03516
This domain is a hyaluronan (HA)-binding domain. It is found in CD44 receptor and mediates ...
 265-391 6.03e-04

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: 41.68  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  265 VFYVGPARRLTLAGARAQ--CRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGgpAPGVRTVYRFA 342
Cdd:cd03516      8 VFLVEKNGRYSLNFTEAKeaCRALGLTLASKAQVETALKFGFETCRYGWVEDGFVVIPRIDPNPLCG--KNGTGVYILNS 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1333603193  343 NRTGfpapgaRFDAYCFRAhhptpqhgdPETPSSGDEGEILSAEGPLAR 391
Cdd:cd03516     86 NLSS------RYDAYCYNS---------SDTWINSCLPEILTTDDPIFI 119
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 1124-1253 6.05e-04

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 44.69  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193 1124 LCEKDTEgcdrgWHKFQGHCYRYFAHRRAWEDAERDCRHRA-GHLTSIHSPEEHGFI-----NSFGReNTWIGLND--RI 1195
Cdd:TIGR00864  317 HCPKDGE-----IFEENGHCFQIVPEEAAWLDAQEQCLARAgAALAIVDNDALQNFLarkvtHSLDR-GVWIGFSDvnGA 390

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333603193 1196 VERDFQWTDNTGLQY-ENWRENQPDnfFAGGEDCVVMvaHESGRWNDVPCNYNLPYVCK 1253
Cdd:TIGR00864  391 EKGPAHQGEAFEAEEcEEGLAGEPH--PARAEHCVRL--DPRGQCNSDLCNAPHAYVCE 445
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 554-817 9.47e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 9.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  554 VDVPGAGSLGGRSPPEPWLWPPTVAPPSIPGPSRALGLELEEVEGPSVRPATPNLPWSPLEATALGPRPSEGPSTIPWEA 633
Cdd:PHA03307    51 AAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSP 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  634 PPMISSPDLPVVAMLRAPKLGLLPHPTPFTTQANGIKRHGEAMVTAP-PSPASEIEASPQDPIHPELYSLPPSLDLKEQG 712
Cdd:PHA03307   131 APDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSsPEETARAPSSPPAEPPPSTPPAAASPRPPRRS 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  713 GEATSSTLSGHGAGIPTAPLQAASDAQGGASPNSPRADLGETGGTSPTGLSKAEHPRSSPQASVDGNEVVDFAPTETATE 792
Cdd:PHA03307   211 SPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS 290

                          250       260
                   ....*....|....*....|....*
gi 1333603193  793 PTGVTGILGSESGVFSTAESPTFSS 817
Cdd:PHA03307   291 PRERSPSPSPSSPGSGPAPSSPRAS 315
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
431-653 1.44e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.94  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  431 TPSPASGGPMLASRPALEAEEVwlSTVAPSRSSMEAGTARTTHREATPASATPRKRGrfkglNGRHFQEQEPQQGLEGGL 510
Cdd:PRK12323   373 GPATAAAAPVAQPAPAAAAPAA--AAPAPAAPPAAPAAAPAAAAAARAVAAAPARRS-----PAPEALAAARQASARGPG 445

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  511 EASAHAPTSEAAGNQVEPPLAVETTDALRTGPNQSPWAvltnevdVPGAGSLGGRSPPEPWL-WPPTVAPPSIPGPSRAL 589
Cdd:PRK12323   446 GAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARA-------APAAAPAPADDDPPPWEeLPPEFASPAPAQPDAAP 518

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333603193  590 -GLELEEVEGPSVRPATPNLPWSPLEATA-LGPRPSEGPSTIPWEAPPMISSPDLPVVAMLRAPKL 653
Cdd:PRK12323   519 aGWVAESIPDPATADPDDAFETLAPAPAAaPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPAL 584
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 255-753 1.82e-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: 42.94  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  255 YCFARELggevfyvgPARRLTLAGARAQCRRQGAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPG 334
Cdd:COG3321    866 YPFQRED--------AAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAA 937

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  335 VRTVYRFANRTGFPAPGARFDAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDFQEPLVSS 414
Cdd:COG3321    938 AAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAA 1017

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  415 GEEEPLILAERQESQETPSPASGGPMLASRPALEAEEVWLSTVAPSRSSMEAGTARTTHREATPASATPRKRGRFKGLNG 494
Cdd:COG3321   1018 AAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALAL 1097

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  495 RHFQEQEPQQGLEGGLEASAHAPTSEAAGNQVEPPLAVETTDALRTGPNQSPWAVLTNEVDVPGAGSLGGRSPPEPWLWP 574
Cdd:COG3321   1098 ALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLAL 1177

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  575 PTVAPPSIPGPSRALGLELEEVEGPSVRPATPNLPWSPLEATALG-------------PRPSEGPSTIPWEAPPMISSPD 641
Cdd:COG3321   1178 ALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAAllaaaaaaaalalLALAAAAAAVAALAAAAAALLA 1257

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  642 LPVVAMLRAPKLGLLPHPTPFTTQANGIKRHGEAMVTAPPSPASEIEASPQDPIHPELYSLPPSLDLKEQGGEATSSTLS 721
Cdd:COG3321   1258 ALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAV 1337

                          490       500       510
                   ....*....|....*....|....*....|..
gi 1333603193  722 GHGAGIPTAPLQAASDAQGGASPNSPRADLGE 753
Cdd:COG3321   1338 AAALALAAAAAAAAAAAAAAAAAAALAAAAGA 1369
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
574-771 3.12e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.79  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  574 PPTVAPPSIPGPSRALGLELEEVEGPSVRPATPNLPWSPLEATalgPRPSEGPSTIPWEAPPMISSPDLPVVAMLRAPKL 653
Cdd:PRK12323   374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAA---RAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  654 GLLPHPTPFTTQAN---GIKRHGEAMVTAPPSPASEIEASPQDPIHPELYSLPPslDLKEQGGEATSSTLSGHGAGIPTA 730
Cdd:PRK12323   451 APAPAAAPAAAARPaaaGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP--EFASPAPAQPDAAPAGWVAESIPD 528

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1333603193  731 PLQAASDAQGGASPNSPRADLGETGGTSPTGLSKAEHPRSS 771
Cdd:PRK12323   529 PATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRAS 569
EGF smart00181
Epidermal growth factor-like domain;
1055-1088 3.98e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.34  E-value: 3.98e-03
                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1333603193  1055 PC-ENNPCLHGgTCKANGTMYGCSCDQGFTG-ENCE 1088
Cdd:smart00181    1 ECaSGGPCSNG-TCINTPGSYTCSCPPGYTGdKRCE 35
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 565-788 4.14e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.45  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  565 RSPP-------EPWLWPPTVAPPSIPGPsralglelEEVEGPSVRPATPNLPWSPLEA-TALGPRPSEGPSTiPWEAPPm 636
Cdd:PLN03209   327 RVPPkesdaadGPKPVPTKPVTPEAPSP--------PIEEEPPQPKAVVPRPLSPYTAyEDLKPPTSPIPTP-PSSSPA- 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  637 iSSPDLPVVAMLRAPKLGLLPHPTPfttqangikrhgeamvTAPPSPASEIEASPQDPIHP----ELYSLPPSLDLKEQG 712
Cdd:PLN03209   397 -SSKSVDAVAKPAEPDVVPSPGSAS----------------NVPEVEPAQVEAKKTRPLSPyaryEDLKPPTSPSPTAPT 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  713 GEATSSTLSGHGAGIP-TAPLQAASDAQGGASPNS-------PRADLGETGGTSPTGLSKAEHPRSSPQASVDGNEVVDF 784
Cdd:PLN03209   460 GVSPSVSSTSSVPAVPdTAPATAATDAAAPPPANMrplspyaVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPT 539


                   ....
gi 1333603193  785 APTE 788
Cdd:PLN03209   540 ALAD 543
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 629-873 7.65e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 40.68  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  629 IPWEAPPmissPDLPVVAMLRAPKLGLLPHPTPFTTQANGIKRHGEAMVTAPPSP--ASEIEASPQDPIHPELYSLPP-- 704
Cdd:PLN03209   323 IPSQRVP----PKESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPytAYEDLKPPTSPIPTPPSSSPAss 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  705 -SLDLKEQGGEATSSTLSGHGAGIP-TAPLQAASDAQGGASPNSPRADLGETGGTSPTGLSKAEHPRSSPQA-SVDGNEV 781
Cdd:PLN03209   399 kSVDAVAKPAEPDVVPSPGSASNVPeVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSvPAVPDTA 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  782 VDFAPTETATEPTGvTGILGSESGVFSTAESPTFSSQATVDEAQGTWPSLHSGGLDLHPPFASSGGPGVSLMPRVTPsLE 861
Cdd:PLN03209   479 PATAATDAAAPPPA-NMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRP-LS 556

                          250
                   ....*....|..
gi 1333603193  862 PWAATEATVGPT 873
Cdd:PLN03209   557 PYTMYEDLKPPT 568
dnaA PRK14086
chromosomal replication initiator protein DnaA;
574-777 8.40e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 40.58  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  574 PPTVAPPSIPGPSRALGLElEEVEGPSVRPATPNLPWSPLEATALGPRPS-----EGPSTIPWEAPPMISSPDLPVVAml 648
Cdd:PRK14086    97 PPPPHARRTSEPELPRPGR-RPYEGYGGPRADDRPPGLPRQDQLPTARPAypayqQRPEPGAWPRAADDYGWQQQRLG-- 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  649 rapklglLPHPTPFTTqANGIKRHGEAMVTAPPSPASEIEASPQDPIHPELYSLPPSLDLKEQGGEATSSTLSGHGAGIP 728
Cdd:PRK14086   174 -------FPPRAPYAS-PASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPEPPPGAGHVHRGGPGP 245

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1333603193  729 TAPLQAASDAQGGASPNSPRADlgetggTSPTGLSKAEHPRSSPQASVD 777
Cdd:PRK14086   246 PERDDAPVVPIRPSAPGPLAAQ------PAPAPGPGEPTARLNPKYTFD 288
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 348-758 9.35e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  348 PAPGARFDAYCFRAHHPTPQHGDPETPSSGDEGEILSAEGPLARELEPSLGEEEVVTPDfqeplvSSGEEEPLILAERQE 427
Cdd:PRK07764   417 PAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPE------PTAAPAPAPPAAPAP 490

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  428 SQETPSPASGGPMLASRPALEAEEVW--LSTVAPSRSsmeagtaRTTHREATPASatprkrgRFKGLNGRHFQEQEPQQG 505
Cdd:PRK07764   491 AAAPAAPAAPAAPAGADDAATLRERWpeILAAVPKRS-------RKTWAILLPEA-------TVLGVRGDTLVLGFSTGG 556

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  506 LEGGLEASAHAPT-SEAAGNQVEPPLAVETTdalrTGPNqspwavltnevdvPGAGSLGGRSPPEPWLWPPTVAPPSIPG 584
Cdd:PRK07764   557 LARRFASPGNAEVlVTALAEELGGDWQVEAV----VGPA-------------PGAAGGEGPPAPASSGPPEEAARPAAPA 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  585 PsralglelEEVEGPSVRPATPNLPWSPLEATALGPRPSEGPSTIPWEAPPMISSPDLPVVAMLRAPKL-GLLPHPTPFT 663
Cdd:PRK07764   620 A--------PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAApPPAPAPAAPA 691

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333603193  664 TQANGIKRHGEAMVTAPPSPASEIEASPQDPIHPELYS-----------LPPSLDLKEQGGEATSSTLSGHGAGIPTAPL 732
Cdd:PRK07764   692 APAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASapspaaddpvpLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPA 771

                          410       420
                   ....*....|....*....|....*.
gi 1333603193  733 QAASDAQGGASPNSPRADLGETGGTS 758
Cdd:PRK07764   772 AAPPPSPPSEEEEMAEDDAPSMDDED 797
 
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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