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Conserved domains on  [gi|164429152|ref|XP_001728514|]
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hypothetical protein NCU11185 [Neurospora crassa OR74A]

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List of domain hits

Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
121-603 1.53e-145

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


:

Pssm-ID: 253817  Cd Length: 347  Bit Score: 435.18  E-value: 1.53e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  121 LLAFSYRPPpNSPESKINGWDLYDVRAEFRRQGISEKSRelgWRISTINKDYSFSPTYPALLIVPSKISDATLKYAASYR 200
Cdd:pfam06602   2 LFAFSYNPK-FSELERLDGWKIFDPEREYKRLGLPNSNA---WRISSVNENYEICPSYPAKLIVPKSISDDELKKVAKFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  201 SRQRIPTLTYRHPVNNCTISRCSQPLPGISFKRNIQDESLVSacfsastefaggtsldmpvespppstadlMIESENtdg 280
Cdd:pfam06602  78 SGGRFPVLSWRHKENGAVIVRCSQPLVGIMGKRCKEDEKLLA-----------------------------AIRKSN--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  281 smsdiqkaedeltvggtilydgktgkrliyGAQQQNLIVDARPVINSYAMQAIGYGTENMEHYKFAKKEYLNIDNIHVMR 360
Cdd:pfam06602 126 ------------------------------PQSKKLYIVDARPRLNALANKAKGGGYENEDNYPNAELIFLGIPNIHVMR 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  361 ESLEKVISAIKDADVSPfPPNKELLAKSKWLKHISGILSGSALIAQRVGIQHSNVLIHCSDGWDRTSQLSALSQLMLDPY 440
Cdd:pfam06602 176 ESLQKLREACVTNEPDE-SSWLSSLESSGWLQHISAILAGAALIADAVDSEGSSVLVHCSDGWDRTAQVTSLAQLLLDPY 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  441 YRTLEGFIVLVEKDWLSFGHMFHLRSGHLSHedwftvdgdalagtavkpgendgradhfenaiagakrfwskktasgkea 520
Cdd:pfam06602 255 YRTIEGFQVLVEKEWLSFGHKFADRCGHLNN------------------------------------------------- 285
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  521 vtdadgtpietgvepavaenmATRPKDISPVFHQFLDATYQLLRQHPTRFEFNERFLRRLYYHVYSCQYGTFLFNNERQR 600
Cdd:pfam06602 286 ---------------------NGDSKERSPVFLQFLDCVWQLMRQFPCAFEFNEFFLIFLADHLYSCQFGTFLCNSEKER 344

                  ...
gi 164429152  601 HEA 603
Cdd:pfam06602 345 EEL 347
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
17-177 1.11e-05

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13211:

Pssm-ID: 266526  Cd Length: 159  Bit Score: 44.94  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  17 RGGKPEL-GDLALSDYHLVFRfppesltaadpSLKKSVKQVWFaFH--IISQCTlRPTPPSSGvpSSIRIRFRDFTYVSF 93
Cdd:cd13211   19 RPPRPNVeGTLCLTGHHLILS-----------SRQDNAEELWL-LHsnIDSIEK-KFVGQSSG--GTIILKCKDFRIIQL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  94 NFAGDKEAREAFEFIKSRTCkLGSVDKLLAFSYRPPPNSPEskiNGWDLYDVRAEFRRqgISEKSRElgWRISTINKDYS 173
Cdd:cd13211   84 DIPGMEECLNIASSIEALSS-LESITLYYPFFYRPMFEVLE---DGWTAFDPESEFAR--LLAETDD--WRRSSVNNKFS 155

                 ....
gi 164429152 174 FSPT 177
Cdd:cd13211  156 VCCS 159
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
121-603 1.53e-145

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


Pssm-ID: 253817  Cd Length: 347  Bit Score: 435.18  E-value: 1.53e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  121 LLAFSYRPPpNSPESKINGWDLYDVRAEFRRQGISEKSRelgWRISTINKDYSFSPTYPALLIVPSKISDATLKYAASYR 200
Cdd:pfam06602   2 LFAFSYNPK-FSELERLDGWKIFDPEREYKRLGLPNSNA---WRISSVNENYEICPSYPAKLIVPKSISDDELKKVAKFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  201 SRQRIPTLTYRHPVNNCTISRCSQPLPGISFKRNIQDESLVSacfsastefaggtsldmpvespppstadlMIESENtdg 280
Cdd:pfam06602  78 SGGRFPVLSWRHKENGAVIVRCSQPLVGIMGKRCKEDEKLLA-----------------------------AIRKSN--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  281 smsdiqkaedeltvggtilydgktgkrliyGAQQQNLIVDARPVINSYAMQAIGYGTENMEHYKFAKKEYLNIDNIHVMR 360
Cdd:pfam06602 126 ------------------------------PQSKKLYIVDARPRLNALANKAKGGGYENEDNYPNAELIFLGIPNIHVMR 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  361 ESLEKVISAIKDADVSPfPPNKELLAKSKWLKHISGILSGSALIAQRVGIQHSNVLIHCSDGWDRTSQLSALSQLMLDPY 440
Cdd:pfam06602 176 ESLQKLREACVTNEPDE-SSWLSSLESSGWLQHISAILAGAALIADAVDSEGSSVLVHCSDGWDRTAQVTSLAQLLLDPY 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  441 YRTLEGFIVLVEKDWLSFGHMFHLRSGHLSHedwftvdgdalagtavkpgendgradhfenaiagakrfwskktasgkea 520
Cdd:pfam06602 255 YRTIEGFQVLVEKEWLSFGHKFADRCGHLNN------------------------------------------------- 285
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  521 vtdadgtpietgvepavaenmATRPKDISPVFHQFLDATYQLLRQHPTRFEFNERFLRRLYYHVYSCQYGTFLFNNERQR 600
Cdd:pfam06602 286 ---------------------NGDSKERSPVFLQFLDCVWQLMRQFPCAFEFNEFFLIFLADHLYSCQFGTFLCNSEKER 344

                  ...
gi 164429152  601 HEA 603
Cdd:pfam06602 345 EEL 347
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
17-177 1.11e-05

Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR9 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR9 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 241365  Cd Length: 159  Bit Score: 44.94  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  17 RGGKPEL-GDLALSDYHLVFRfppesltaadpSLKKSVKQVWFaFH--IISQCTlRPTPPSSGvpSSIRIRFRDFTYVSF 93
Cdd:cd13211   19 RPPRPNVeGTLCLTGHHLILS-----------SRQDNAEELWL-LHsnIDSIEK-KFVGQSSG--GTIILKCKDFRIIQL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  94 NFAGDKEAREAFEFIKSRTCkLGSVDKLLAFSYRPPPNSPEskiNGWDLYDVRAEFRRqgISEKSRElgWRISTINKDYS 173
Cdd:cd13211   84 DIPGMEECLNIASSIEALSS-LESITLYYPFFYRPMFEVLE---DGWTAFDPESEFAR--LLAETDD--WRRSSVNNKFS 155

                 ....
gi 164429152 174 FSPT 177
Cdd:cd13211  156 VCCS 159
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
411-445 4.31e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649  Cd Length: 105  Bit Score: 42.73  E-value: 4.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 164429152   411 QHSNVLIHCSDGWDRTSQLSALSQLMLDPYYRTLE 445
Cdd:smart00404  38 SSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PRK12495 PRK12495
hypothetical protein; Provisional
661-774 9.38e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 40.24  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152 661 DDEMNGDLNALAATAERVAAYQQASSSSELSRPVDAGTIDvNSNPPSSGAPSRTSVSPTRsplPPGLAATAAGGSVHAGV 740
Cdd:PRK12495  71 DGAAGDDAGDGAEATAPSDAGSQASPDDDAQPAAEAEAAD-QSAPPEASSTSATDEAATD---PPATAAARDGPTPDPTA 146
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 164429152 741 ESA--HEVLTPGTRSPAPPNRNVAAGDPTGTFAALQ 774
Cdd:PRK12495 147 QPAtpDERRSPRQRPPVSGEPPTPSTPDAHVAGTLQ 182
 
Name Accession Description Interval E-value
Myotub-related pfam06602
Myotubularin-like phosphatase domain; This family represents the phosphatase domain within ...
121-603 1.53e-145

Myotubularin-like phosphatase domain; This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.


Pssm-ID: 253817  Cd Length: 347  Bit Score: 435.18  E-value: 1.53e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  121 LLAFSYRPPpNSPESKINGWDLYDVRAEFRRQGISEKSRelgWRISTINKDYSFSPTYPALLIVPSKISDATLKYAASYR 200
Cdd:pfam06602   2 LFAFSYNPK-FSELERLDGWKIFDPEREYKRLGLPNSNA---WRISSVNENYEICPSYPAKLIVPKSISDDELKKVAKFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  201 SRQRIPTLTYRHPVNNCTISRCSQPLPGISFKRNIQDESLVSacfsastefaggtsldmpvespppstadlMIESENtdg 280
Cdd:pfam06602  78 SGGRFPVLSWRHKENGAVIVRCSQPLVGIMGKRCKEDEKLLA-----------------------------AIRKSN--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  281 smsdiqkaedeltvggtilydgktgkrliyGAQQQNLIVDARPVINSYAMQAIGYGTENMEHYKFAKKEYLNIDNIHVMR 360
Cdd:pfam06602 126 ------------------------------PQSKKLYIVDARPRLNALANKAKGGGYENEDNYPNAELIFLGIPNIHVMR 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  361 ESLEKVISAIKDADVSPfPPNKELLAKSKWLKHISGILSGSALIAQRVGIQHSNVLIHCSDGWDRTSQLSALSQLMLDPY 440
Cdd:pfam06602 176 ESLQKLREACVTNEPDE-SSWLSSLESSGWLQHISAILAGAALIADAVDSEGSSVLVHCSDGWDRTAQVTSLAQLLLDPY 254
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  441 YRTLEGFIVLVEKDWLSFGHMFHLRSGHLSHedwftvdgdalagtavkpgendgradhfenaiagakrfwskktasgkea 520
Cdd:pfam06602 255 YRTIEGFQVLVEKEWLSFGHKFADRCGHLNN------------------------------------------------- 285
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  521 vtdadgtpietgvepavaenmATRPKDISPVFHQFLDATYQLLRQHPTRFEFNERFLRRLYYHVYSCQYGTFLFNNERQR 600
Cdd:pfam06602 286 ---------------------NGDSKERSPVFLQFLDCVWQLMRQFPCAFEFNEFFLIFLADHLYSCQFGTFLCNSEKER 344

                  ...
gi 164429152  601 HEA 603
Cdd:pfam06602 345 EEL 347
PH-GRAM_MTMR9 cd13211
Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, ...
17-177 1.11e-05

Myotubularian (MTM) related 9 protein (MTMR9) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; MTMR9 is a catalytically inactive phosphatase that plays a role as an adapter for the phosphatase myotubularin to regulate myotubularintracellular location. It contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase. MTMR9 contains an N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, an inactive PTP domain, a SET interaction domain, and a C-terminal coiled-coil region. Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold. The PH domain family possesses multiple functions including the ability to bind phosphoinositides via its beta1/beta2, beta3/beta4, and beta6/beta7 connecting loops and to other proteins. However, no phosphoinositide binding sites have been found for the MTMRs to date.


Pssm-ID: 241365  Cd Length: 159  Bit Score: 44.94  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  17 RGGKPEL-GDLALSDYHLVFRfppesltaadpSLKKSVKQVWFaFH--IISQCTlRPTPPSSGvpSSIRIRFRDFTYVSF 93
Cdd:cd13211   19 RPPRPNVeGTLCLTGHHLILS-----------SRQDNAEELWL-LHsnIDSIEK-KFVGQSSG--GTIILKCKDFRIIQL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152  94 NFAGDKEAREAFEFIKSRTCkLGSVDKLLAFSYRPPPNSPEskiNGWDLYDVRAEFRRqgISEKSRElgWRISTINKDYS 173
Cdd:cd13211   84 DIPGMEECLNIASSIEALSS-LESITLYYPFFYRPMFEVLE---DGWTAFDPESEFAR--LLAETDD--WRRSSVNNKFS 155

                 ....
gi 164429152 174 FSPT 177
Cdd:cd13211  156 VCCS 159
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
411-445 4.31e-05

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649  Cd Length: 105  Bit Score: 42.73  E-value: 4.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 164429152   411 QHSNVLIHCSDGWDRTSQLSALSQLMLDPYYRTLE 445
Cdd:smart00404  38 SSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
411-445 4.31e-05

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469  Cd Length: 105  Bit Score: 42.73  E-value: 4.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 164429152   411 QHSNVLIHCSDGWDRTSQLSALSQLMLDPYYRTLE 445
Cdd:smart00012  38 SSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGE 72
PRK12495 PRK12495
hypothetical protein; Provisional
661-774 9.38e-04

hypothetical protein; Provisional


Pssm-ID: 183558 [Multi-domain]  Cd Length: 226  Bit Score: 40.24  E-value: 9.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164429152 661 DDEMNGDLNALAATAERVAAYQQASSSSELSRPVDAGTIDvNSNPPSSGAPSRTSVSPTRsplPPGLAATAAGGSVHAGV 740
Cdd:PRK12495  71 DGAAGDDAGDGAEATAPSDAGSQASPDDDAQPAAEAEAAD-QSAPPEASSTSATDEAATD---PPATAAARDGPTPDPTA 146
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 164429152 741 ESA--HEVLTPGTRSPAPPNRNVAAGDPTGTFAALQ 774
Cdd:PRK12495 147 QPAtpDERRSPRQRPPVSGEPPTPSTPDAHVAGTLQ 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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