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Conserved domains on  [gi|52545872|emb|CAD38899|]
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hypothetical protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02688 super family cl31919
pyrroline-5-carboxylate reductase
1-138 1.60e-42

pyrroline-5-carboxylate reductase


The actual alignment was detected with superfamily member PLN02688:

Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 142.79  E-value: 1.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqPAPKVIRCMTNTPV 80
Cdd:PLN02688  46 SLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPC 121
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 52545872   81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMA 138
Cdd:PLN02688 122 LVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLA 179
 
Name Accession Description Interval E-value
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
1-138 1.60e-42

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 142.79  E-value: 1.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqPAPKVIRCMTNTPV 80
Cdd:PLN02688  46 SLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPC 121
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 52545872   81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMA 138
Cdd:PLN02688 122 LVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLA 179
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
1-137 4.52e-40

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 135.85  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872     1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTNTPV 80
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 52545872    81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFM 137
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFL 161
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];
1-137 9.37e-40

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];


Pssm-ID: 223422 [Multi-domain]  Cd Length: 266  Bit Score: 135.79  E-value: 9.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872   1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIgADVQARHIVVSCAAGVTISSVEKKLmafqPAPKVIRCMTNTPV 80
Cdd:COG0345  47 EYGVVTTTDNQEAVEEADVVFLAVKPQDLEEVLSKL-KPLTKDKLVISIAAGVSIETLERLL----GGLRVVRVMPNTPA 121
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 52545872  81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFM 137
Cdd:COG0345 122 LVGAGVTAISANANVSEEDKAFVEALLSAVGKVVEVEESLMDAVTALSGSGPAYVFL 178
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
1-52 3.15e-10

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 281759 [Multi-domain]  Cd Length: 92  Bit Score: 54.18  E-value: 3.15e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 52545872     1 KMGVNLT-RSNKETVKHSDVLFLAVKPHIIPFILDEIGADvQARHIVVSCAAG 52
Cdd:pfam03807  41 ELGVGATaVDNEEAAEEADVVFLAVKPEDAPDVLSELKDL-LKGKIVISITAG 92
 
Name Accession Description Interval E-value
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
1-138 1.60e-42

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 142.79  E-value: 1.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqPAPKVIRCMTNTPV 80
Cdd:PLN02688  46 SLGVKTAASNTEVVKSSDVIILAVKPQVVKDVLTELRPLLSKDKLLVSVAAGITLADLQEWA----GGRRVVRVMPNTPC 121
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 52545872   81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMA 138
Cdd:PLN02688 122 LVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVDEKLLDAVTGLSGSGPAYIFLA 179
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
1-137 4.52e-40

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 135.85  E-value: 4.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872     1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTNTPV 80
Cdd:TIGR00112  28 ELGIVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGVTLEKLSQLLGGTRR---VVRVMPNTPA 104
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 52545872    81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFM 137
Cdd:TIGR00112 105 KVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVFL 161
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];
1-137 9.37e-40

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism];


Pssm-ID: 223422 [Multi-domain]  Cd Length: 266  Bit Score: 135.79  E-value: 9.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872   1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIgADVQARHIVVSCAAGVTISSVEKKLmafqPAPKVIRCMTNTPV 80
Cdd:COG0345  47 EYGVVTTTDNQEAVEEADVVFLAVKPQDLEEVLSKL-KPLTKDKLVISIAAGVSIETLERLL----GGLRVVRVMPNTPA 121
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 52545872  81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFM 137
Cdd:COG0345 122 LVGAGVTAISANANVSEEDKAFVEALLSAVGKVVEVEESLMDAVTALSGSGPAYVFL 178
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
3-137 2.01e-36

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 127.18  E-value: 2.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    3 GVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGAdvQARHIVVSCAAGVTISSVEKKLMAFQPapkVIRCMTNTPVVV 82
Cdd:PRK11880  49 GVRAATDNQEAAQEADVVVLAVKPQVMEEVLSELKG--QLDKLVVSIAAGVTLARLERLLGADLP---VVRAMPNTPALV 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 52545872   83 QEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVE-EDLIDAVTGLSGSGPAYAFM 137
Cdd:PRK11880 124 GAGMTALTANALVSAEDRELVENLLSAFGKVVWVDdEKQMDAVTAVSGSGPAYVFL 179
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
1-136 9.48e-24

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 94.45  E-value: 9.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKklmAFQPAPKVIRCMTNTPV 80
Cdd:PRK07679  50 KYGVKGTHNKKELLTDANILFLAMKPKDVAEALIPFKEYIHNNQLIISLLAGVSTHSIRN---LLQKDVPIIRAMPNTSA 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 52545872   81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAF 136
Cdd:PRK07679 127 AILKSATAISPSKHATAEHIQTAKALFETIGLVSVVEEEDMHAVTALSGSGPAYIY 182
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
5-137 4.19e-19

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 81.54  E-value: 4.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    5 NLTRSNKETVKHSDVLFLAVKPHIIPFILDEIgADVQARHIVVSCAAGVTISSVEKklMAFQPApKVIRCMTNTPVVVQE 84
Cdd:PTZ00431  46 VYLQSNEELAKTCDIIVLAVKPDLAGKVLLEI-KPYLGSKLLISICGGLNLKTLEE--MVGVEA-KIVRVMPNTPSLVGQ 121
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 52545872   85 GATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFM 137
Cdd:PTZ00431 122 GSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKEKDMDIATAISGCGPAYVFL 174
PRK12491 PRK12491
pyrroline-5-carboxylate reductase; Reviewed
1-137 2.36e-18

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 105695 [Multi-domain]  Cd Length: 272  Bit Score: 79.73  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    1 KMGVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKlmaFQPAPKVIRCMTNTPV 80
Cdd:PRK12491  48 KYGITITTNNNEVANSADILILSIKPDLYTSVINQIKDQIKNDVIVVTIAAGKSIKSTENE---FDRKLKVIRVMPNTPV 124
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 52545872   81 VVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFM 137
Cdd:PRK12491 125 LVGEGMSALSFNEMVTEKDIKEVLNIFNIFGQTEVVNEKLMDVVTSISGSSPAYVYM 181
PRK07680 PRK07680
late competence protein ComER; Validated
3-179 1.96e-12

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 63.45  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    3 GVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIGADVQARHIVVSCAAGVTISSVEKKLmafqP--APKVIRCMTNTpv 80
Cdd:PRK07680  49 GIHVAKTIEEVISQSDLIFICVKPLDIYPLLQKLAPHLTDEHCLVSITSPISVEQLETLV----PcqVARIIPSITNR-- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872   81 vVQEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYAFMADQEKISpAALKKTLLDrvKLES 160
Cdd:PRK07680 123 -ALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVIEEDITRVSSDIVSCGPAFFSYLLQRFID-AAVEETNIS--KEEA 198
                        170
                 ....*....|....*....
gi 52545872  161 PTVSTLTPSSPGKLLTRSL 179
Cdd:PRK07680 199 TTLASEMLIGMGKLLEKGL 217
PRK07634 PRK07634
pyrroline-5-carboxylate reductase; Reviewed
3-134 8.10e-12

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181063 [Multi-domain]  Cd Length: 245  Bit Score: 61.69  E-value: 8.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    3 GVNLTRSNKETVKHSDVLFLAVKPHIIPFILDEIgADVQARHIVVSCAAGVTISSVEKKLMAFQPAPKVircMTNTPVVV 82
Cdd:PRK07634  53 NVSTTTDWKQHVTSVDTIVLAMPPSAHEELLAEL-SPLLSNQLVVTVAAGIGPSYLEERLPKGTPVAWI---MPNTAAEI 128
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 52545872   83 QEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAY 134
Cdd:PRK07634 129 GKSISLYTMGQSVNETHKETLQLILKGIGTSQLCTEEEVHQLTAVTGSAPAF 180
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
1-52 3.15e-10

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 281759 [Multi-domain]  Cd Length: 92  Bit Score: 54.18  E-value: 3.15e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 52545872     1 KMGVNLT-RSNKETVKHSDVLFLAVKPHIIPFILDEIGADvQARHIVVSCAAG 52
Cdd:pfam03807  41 ELGVGATaVDNEEAAEEADVVFLAVKPEDAPDVLSELKDL-LKGKIVISITAG 92
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
4-153 4.29e-08

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 51.31  E-value: 4.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    4 VNLTRSNKETVKHSDVLFLAVKP-HIIPfILDEIGADVQARHIVVSCAAGVTISsvekKLMAFQPAPKVIRCMTNTPVVV 82
Cdd:PRK06928  52 VELADNEAEIFTKCDHSFICVPPlAVLP-LLKDCAPVLTPDRHVVSIAAGVSLD----DLLEITPGLQVSRLIPSLTSAV 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52545872   83 QEGATVYATGTHALVEDGQLLEQLMSSVGFCTEVEEDLIDAVTGLSGSGPAYaFMADQEKISPAALKKTLL 153
Cdd:PRK06928 127 GVGTSLVAHAETVNEANKSRLEETLSHFSHVMTIREENMDIASNLTSSSPGF-IAAIFEEFAEAAVRNSSL 196
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
118-137 2.92e-06

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 339361  Cd Length: 105  Bit Score: 43.91  E-value: 2.92e-06
                          10        20
                  ....*....|....*....|
gi 52545872   118 EDLIDAVTGLSGSGPAYAFM 137
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFL 20
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
4-140 3.26e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812  Cd Length: 258  Bit Score: 40.00  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    4 VNLTRSNKETVKHSDVLFLAVKPhiipfildEIGADV------QARHIVVSCAAGVTISSVEKklmAFQPAPKVIRCMTN 77
Cdd:PRK06476  49 VRIAKDNQAVVDRSDVVFLAVRP--------QIAEEVlralrfRPGQTVISVIAATDRAALLE---WIGHDVKLVRAIPL 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52545872   78 TPVVVQEGAT-VYAtgTHALVEDgqLLEQLMSSVGFCTEVEEDLIDAVTGLsgSGPAYAFMADQ 140
Cdd:PRK06476 118 PFVAERKGVTaIYP--PDPFVAA--LFDALGTAVECDSEEEYDLLAAASAL--MATYFGILETA 175
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
32-167 7.63e-03

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 333984  Cd Length: 294  Bit Score: 35.74  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52545872    32 ILDEIGADVqaRHIVVSCAAGVTISSVEKKLMAFQPAPKVIrcmtntpvVVQ-EGATVYATGTHALVEDGQLLEQLMSSV 110
Cdd:pfam00291 150 ILEQLGGKP--DAVVVPVGGGGLIAGIARGLKELGPDVRII--------GVEpEGAPALARSLAARPVTLPVSDTIADGL 219
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52545872   111 GFCTEVEEDLIDAVTGLSGSG---------PAYAFMADQEKISP--------AALKKTLLDRVKLESPTVSTLT 167
Cdd:pfam00291 220 GVGDVPGALALDLLDEYVGEVvtvsdeealEAMRLLARREGIVVepssaaalAALKLALAGELKGGDRVVVVLT 293
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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