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Conserved domains on  [gi|2117900674|ref|NP_990368|]
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photoreceptor outer segment membrane glycoprotein 2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
peripherin_like_LEL cd03162
Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. ...
 120-262 2.25e-102

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.


:

Pssm-ID: 239415  Cd Length: 143  Bit Score: 298.19  E-value: 2.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 120 YTMRNELEESLYLGLRDAIKFYKDTDIPGRCFLKKTVDMLQIGFQCCGNNGFRDWFEVQWVSARYLNMASKEVMDRFKSN 199
Cdd:cd03162     1 FIMRGSLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSSKEVKDRIKSN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2117900674 200 VDGKFLVDGVPFSCCNPSSPRPCIQYHLTNNSAHYNYDFLTEELNIWVKGCREALLEYYTAIM 262
Cdd:cd03162    81 VDGRYLTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYTSKM 143
Tetraspanin pfam00335
Tetraspanin family;
16-188 1.77e-15

Tetraspanin family;


:

Pssm-ID: 459767  Cd Length: 183  Bit Score: 73.89  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674  16 LAQILWILNWVSVVSGIILFSLGLFLkIEIKKRNEVMAKGDINSVPNMLISVGVIACVVNFLGgkiCYDCSDANKFsrwk 95
Cdd:pfam00335   1 LKYLLFLFNLLFWLLGLLLLGVGVWL-LSAFSLLLLGLSEASAYIPILLIVLGAVIFLVGFLG---CCGALKENRC---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674  96 lIMLPYIICTFCFTFCILLGALMCYTMRNELEESLYLGLRDAIKFYKDTDIPGRCFLKKTVDMLQIGFQCCGN--NGFRD 173
Cdd:pfam00335  73 -LLLTYFVLLLLLFLAELAAGILAFVYRDKLSGLLSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCGGckEKLLE 151

                         170
                  ....*....|....*
gi 2117900674 174 WFEVQWVSARYLNMA 188
Cdd:pfam00335 152 WLRKNLKIIGAGVIA 166
 
Name Accession Description Interval E-value
peripherin_like_LEL cd03162
Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. ...
 120-262 2.25e-102

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.


Pssm-ID: 239415  Cd Length: 143  Bit Score: 298.19  E-value: 2.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 120 YTMRNELEESLYLGLRDAIKFYKDTDIPGRCFLKKTVDMLQIGFQCCGNNGFRDWFEVQWVSARYLNMASKEVMDRFKSN 199
Cdd:cd03162     1 FIMRGSLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSSKEVKDRIKSN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2117900674 200 VDGKFLVDGVPFSCCNPSSPRPCIQYHLTNNSAHYNYDFLTEELNIWVKGCREALLEYYTAIM 262
Cdd:cd03162    81 VDGRYLTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYTSKM 143
Tetraspanin pfam00335
Tetraspanin family;
16-188 1.77e-15

Tetraspanin family;


Pssm-ID: 459767  Cd Length: 183  Bit Score: 73.89  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674  16 LAQILWILNWVSVVSGIILFSLGLFLkIEIKKRNEVMAKGDINSVPNMLISVGVIACVVNFLGgkiCYDCSDANKFsrwk 95
Cdd:pfam00335   1 LKYLLFLFNLLFWLLGLLLLGVGVWL-LSAFSLLLLGLSEASAYIPILLIVLGAVIFLVGFLG---CCGALKENRC---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674  96 lIMLPYIICTFCFTFCILLGALMCYTMRNELEESLYLGLRDAIKFYKDTDIPGRCFLKKTVDMLQIGFQCCGN--NGFRD 173
Cdd:pfam00335  73 -LLLTYFVLLLLLFLAELAAGILAFVYRDKLSGLLSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCGGckEKLLE 151

                         170
                  ....*....|....*
gi 2117900674 174 WFEVQWVSARYLNMA 188
Cdd:pfam00335 152 WLRKNLKIIGAGVIA 166
 
Name Accession Description Interval E-value
peripherin_like_LEL cd03162
Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. ...
 120-262 2.25e-102

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.


Pssm-ID: 239415  Cd Length: 143  Bit Score: 298.19  E-value: 2.25e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 120 YTMRNELEESLYLGLRDAIKFYKDTDIPGRCFLKKTVDMLQIGFQCCGNNGFRDWFEVQWVSARYLNMASKEVMDRFKSN 199
Cdd:cd03162     1 FIMRGSLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSSKEVKDRIKSN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2117900674 200 VDGKFLVDGVPFSCCNPSSPRPCIQYHLTNNSAHYNYDFLTEELNIWVKGCREALLEYYTAIM 262
Cdd:cd03162    81 VDGRYLTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYTSKM 143
Tetraspanin pfam00335
Tetraspanin family;
16-188 1.77e-15

Tetraspanin family;


Pssm-ID: 459767  Cd Length: 183  Bit Score: 73.89  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674  16 LAQILWILNWVSVVSGIILFSLGLFLkIEIKKRNEVMAKGDINSVPNMLISVGVIACVVNFLGgkiCYDCSDANKFsrwk 95
Cdd:pfam00335   1 LKYLLFLFNLLFWLLGLLLLGVGVWL-LSAFSLLLLGLSEASAYIPILLIVLGAVIFLVGFLG---CCGALKENRC---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674  96 lIMLPYIICTFCFTFCILLGALMCYTMRNELEESLYLGLRDAIKFYKDTDIPGRCFLKKTVDMLQIGFQCCGN--NGFRD 173
Cdd:pfam00335  73 -LLLTYFVLLLLLFLAELAAGILAFVYRDKLSGLLSNWLKKSLEDGYRDWLDLYSCLNSALDSLQSEFGCCGGckEKLLE 151

                         170
                  ....*....|....*
gi 2117900674 174 WFEVQWVSARYLNMA 188
Cdd:pfam00335 152 WLRKNLKIIGAGVIA 166
tetraspanin_LEL cd03127
Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are ...
 120-262 1.22e-11

Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. The tetraspanin family contains CD9, CD63, CD37, CD53, CD82, CD151, and CD81, amongst others. Tetraspanins are involved in diverse processes such as cell activation and proliferation, adhesion and motility, differentiation, cancer, and others. Their various functions may relate to their ability to act as molecular facilitators, grouping specific cell-surface proteins and affecting formation and stability of signaling complexes. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web", which may also include integrins.


Pssm-ID: 239401 [Multi-domain]  Cd Length: 90  Bit Score: 60.21  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 120 YTMRNELEESLYLGLRDAIKFYKDTDipgrcFLKKTVDMLQIGFQCCGNNGFRDWFEvqwvsarylnmaskevmdrfksn 199
Cdd:cd03127     1 FVYRDQLESLVSDTLNDAWDEYYVDD-----DFQEAMDALQSTFECCGVNGPTDYLD----------------------- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2117900674 200 vdgkfLVDGVPFSCCNPSSPRPCIqyhltnnsahynydflteelNIWVKGCREALLEYYTAIM 262
Cdd:cd03127    53 -----LRLLVPSSCCKGTDGNCGL--------------------NLYTEGCLEKLVDFLRSNL 90
CD151_like_LEL cd03155
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. ...
 120-230 2.90e-08

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD151strongly associates with integrins, especially alpha3beta1, alpha6beta1, alpha7beta1, and alpha6beta4; it may play roles in cell-cell adhesion, cell migration, platelet aggregation, and angiogenesis. For example, CD151 is is involved in regulation of migration of neutrophils, endothelial cells, and various tumor cell lines; it associates specifically with laminin-binding integrins and strengthens alpha6beta1 integrin-mediated adhesion to laminin-1; CD151 also specifically attenuates adhesion-dependent activation of Ras and correspdonding downstream effects, and is involved in epithelial cell-cell adhesion as a modulator of PKC- and Cdc42-dependent actin cytoskeletal reorganization.


Pssm-ID: 239408 [Multi-domain]  Cd Length: 110  Bit Score: 51.19  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 120 YTMRNELEESLYLGLRDAIKfyKDTDIPGRCFLKKTVDMLQIGFQCCGNNGFRDWFEVQWVSARYLNMASkevmdrfksn 199
Cdd:cd03155     1 YTYYQQLEDELKESLKRTMQ--ENYGQSGEEALTLTVDELQQEFKCCGSNNYTDWQDSEWINSNEANGRL---------- 68

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2117900674 200 vdgkflvdgVPFSCCNPSSPRPCIQYHLTNN 230
Cdd:cd03155    69 ---------VPDSCCKTVVDRCGCLRDHPSN 90
oculospanin_like_LEL cd03167
Tetraspanin, extracellular domain or large extracellular loop (LEL), oculospanin_like family. ...
 121-214 2.28e-07

Tetraspanin, extracellular domain or large extracellular loop (LEL), oculospanin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contains sequences similar to oculospanin, which is found to be expressed in retinal pigment epithelium, iris, ciliary body, and retinal ganglion cells.


Pssm-ID: 239420  Cd Length: 120  Bit Score: 49.00  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 121 TMRNELEESLYLGLRDAIKFYKDTdiPGRCFLkktVDMLQIGFQCCGNNGFRDWfeVQWVsarYLNMASKEVMdrfksnv 200
Cdd:cd03167     2 ALWGPLQDGLEHTLRLAIAHYQDD--PDLRFL---IDQVQLGLQCCGASSYQDW--QQNL---YFNCSSPGVQ------- 64

                          90
                  ....*....|....
gi 2117900674 201 dgkflVDGVPFSCC 214
Cdd:cd03167    65 -----ACSLPASCC 73
NET-5_like_LEL cd03165
Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. ...
 120-254 3.28e-05

Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This sub-family contains proteins similar to human tetraspan NET-5.


Pssm-ID: 239418 [Multi-domain]  Cd Length: 98  Bit Score: 42.35  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 120 YTMRNELEESLYLGLRDAIKFYKDTDIPGrcfLKKTVDMLQIGFQCCGNNGFRDWFEVQWvsarylnmaskevmdrfksn 199
Cdd:cd03165     1 FVFREKVDLTAKDDLKEGLELYGTRNNRG---LTNAWDITQTEFRCCGVTNYTDWYEVLG-------------------- 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2117900674 200 vdgkflVDGVPFSCCNpSSPRPCIQyhltNNSAhynydflteelNIWVKGCREAL 254
Cdd:cd03165    58 ------ENRVPDSCCQ-EDSQDCGR----NPTE-----------LWWKTGCYEKV 90
TM4SF2_6_like_LEL cd03161
Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF2_6_like subfamily. ...
 123-215 5.60e-04

Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF2_6_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 2 (TM4SF2) or Tspan-7, transmembrane 4 superfamily 6 (TM4SF6) or Tspan-6, and related proteins. TM4SF2 has been identified as involved in some forms of X-linked mental retardation.


Pssm-ID: 239414  Cd Length: 104  Bit Score: 38.88  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 123 RNELEESLYLGLRDAIKFYKDTDipGRcflKKTVDMLQIGFQCCGNNGFRDWFEVQWvsarylnmaskevmdrfksnvdg 202
Cdd:cd03161     4 RHEIKGTFLRTYNEAVSNYNGDD--ER---SDAVDTVQRTLHCCGVENYTDWLNSPY----------------------- 55

                          90
                  ....*....|...
gi 2117900674 203 kFLVDGVPFSCCN 215
Cdd:cd03161    56 -FLEKGIPLSCCK 67
CD53_like_LEL cd03164
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD53_Like family. ...
 124-174 3.99e-03

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD53_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD53 is a tetraspanin of the lymphoid-myeloid lineage and has been implicated in apoptosis protection. It associates with integrin alpha4beta1. Some of the cellular responses modulated by CD53 may be mediated by JNK activation and/or via the AKT pathway.


Pssm-ID: 239417 [Multi-domain]  Cd Length: 86  Bit Score: 35.92  E-value: 3.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2117900674 124 NELEESLYLGLRDAIKFY-KDTDIpgrcflKKTVDMLQIGFQCCGNNGFRDW 174
Cdd:cd03164     5 KKLNNYVKEGLTDSLEQYhKDNNT------SEAWDMIQSNLQCCGINGTTDW 50
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 154-257 8.16e-03

Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Uroplakin Ia and Ib are components of the 16nm protein particles, which are packed hexagonally to form 2D crystals of asymmetric unit membranes, and cover the apical surface of mammalian urothelium, contributing to the urinay bladder's permeability barrier function. Uroplakins Ia and Ib are maturation facilitators. They trigger conformational changes in their single-transmembrane-domain binding partner proteins uroplakin II and IIIa, which in turn may lead to ER-exit, stabilization, and cell-surface expression.


Pssm-ID: 239409  Cd Length: 114  Bit Score: 35.97  E-value: 8.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2117900674 154 KTVDMLQIGFQCCGNNGFRDWFEVQWVSARYLNMASKevmdrfksnvdgkflvdgVPFSCCNPSSPRpCIQYHLTNNSAH 233
Cdd:cd03156    33 STWNRVMIELKCCGVNGPTDFVDSTSFFRQKNEPNSP------------------YPESCCKRNSNS-QIVDLDCPKLGS 93

                          90       100
                  ....*....|....*....|....
gi 2117900674 234 YNYDFlteelniwVKGCREALLEY 257
Cdd:cd03156    94 PNSYN--------KKGCYEKLSNP 109
 
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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