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Conserved domains on  [gi|64085083|ref|NP_808807|]
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transmembrane prolyl 4-hydroxylase isoform c [Homo sapiens]

Protein Classification

transmembrane prolyl 4-hydroxylase( domain architecture ID 12145460)

transmembrane prolyl 4-hydroxylase (P4H-TM) catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins 1 which plays a crucial role in cellular adaptation to low oxygen levels (hypoxia)

CATH:  2.60.120.620
EC:  1.14.11.-

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 246-519 2.24e-19

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


:

Pssm-ID: 214780  Cd Length: 165  Bit Score: 85.52  E-value: 2.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    246 LQEFSNMDLRDfHKYMRSHKAESSELVRNSHHTWlYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHY 325
Cdd:smart00702   9 LEEAEPLGWRG-EVTRGIGNPNETSQYRQSNGTW-LELLERDLVIERIRQRLADFLGLLAGLPLSAEDAQVARYGPGGHY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    326 HAHVDSgpvypeticshtklvanesvpFETSCRQVspnwglpsilrpgtpmtqaqpctvgvplgmgpgdhwvipvspweh 405
Cdd:smart00702  87 GPHVDN---------------------FLYGDRIA--------------------------------------------- 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    406 pqlgtcsvpplpysymTVLFYLNNVTGGGETVFPvadnrtydemsliqddvdlrDTRRHCdkgNLRVKPQQGTAVFWYNy 485
Cdd:smart00702 101 ----------------TFILYLNDVEEGGELVFP--------------------GLRLMV---VATVKPKKGDLLFFPS- 140

                          250       260       270
                   ....*....|....*....|....*....|....
gi 64085083    486 lpdgqgwvgdVDDYSLHGGCLVTRGTKWIANNWI 519
Cdd:smart00702 141 ----------GHGRSLHGVCPVTRGSRWAITGWI 164
EF-hand_7 pfam13499
EF-hand domain pair;
192-252 2.77e-08

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 2.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64085083   192 DLFRLLDQNRDGHL---QLREVLAQTRLGNGwwMTPESIQEMYAaiKADPDGDGVLSLQEFSNM 252
Cdd:pfam13499   6 EAFKLLDSDGDGYLdveELKKLLRKLEEGEP--LSDEEVEELFK--EFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 246-519 2.24e-19

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 85.52  E-value: 2.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    246 LQEFSNMDLRDfHKYMRSHKAESSELVRNSHHTWlYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHY 325
Cdd:smart00702   9 LEEAEPLGWRG-EVTRGIGNPNETSQYRQSNGTW-LELLERDLVIERIRQRLADFLGLLAGLPLSAEDAQVARYGPGGHY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    326 HAHVDSgpvypeticshtklvanesvpFETSCRQVspnwglpsilrpgtpmtqaqpctvgvplgmgpgdhwvipvspweh 405
Cdd:smart00702  87 GPHVDN---------------------FLYGDRIA--------------------------------------------- 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    406 pqlgtcsvpplpysymTVLFYLNNVTGGGETVFPvadnrtydemsliqddvdlrDTRRHCdkgNLRVKPQQGTAVFWYNy 485
Cdd:smart00702 101 ----------------TFILYLNDVEEGGELVFP--------------------GLRLMV---VATVKPKKGDLLFFPS- 140

                          250       260       270
                   ....*....|....*....|....*....|....
gi 64085083    486 lpdgqgwvgdVDDYSLHGGCLVTRGTKWIANNWI 519
Cdd:smart00702 141 ----------GHGRSLHGVCPVTRGSRWAITGWI 164
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 418-521 1.39e-12

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 68.93  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083  418 YSYMTVLFYLNNVTGGGETVFPVA---DNRTYDemsliqddvdlrDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGwvg 494
Cdd:PLN00052 163 HRYATVLMYLSTVDKGGETVFPNAegwENQPKD------------DTFSECAHKGLAVKPVKGDAVLFFSLHIDGVP--- 227

                         90       100
                 ....*....|....*....|....*..
gi 64085083  495 dvDDYSLHGGCLVTRGTKWIANNWINV 521
Cdd:PLN00052 228 --DPLSLHGSCPVIEGEKWSAPKWIHI 252
EF-hand_7 pfam13499
EF-hand domain pair;
192-252 2.77e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 2.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64085083   192 DLFRLLDQNRDGHL---QLREVLAQTRLGNGwwMTPESIQEMYAaiKADPDGDGVLSLQEFSNM 252
Cdd:pfam13499   6 EAFKLLDSDGDGYLdveELKKLLRKLEEGEP--LSDEEVEELFK--EFDLDKDGRISFEEFLEL 65
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
177-258 4.46e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 4.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083 177 EEYEEAMSTMQVSQL-----DLFRLLDQNRDGHLQLREVlaqTRLGNGWWMTPESIQEMYAAIkaDPDGDGVLSLQEFSN 251
Cdd:COG5126  53 EEFVAGMESLFEATVepfarAAFDLLDTDGDGKISADEF---RRLLTALGVSEEEADELFARL--DTDGDGKISFEEFVA 127


                ....*..
gi 64085083 252 MdLRDFH 258
Cdd:COG5126 128 A-VRDYY 133
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 422-519 6.22e-07

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 47.76  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083   422 TVLFYLNNVT--GGGETVFpvadnrtydemsliqddvdlrdtrrHCDKGNLRVKPQQGTAVFWYNylpdgqgwvgdvDDY 499
Cdd:pfam13640  31 TVVLYLNDWEeeEGGELVL-------------------------YDGDGVEDIKPKKGRLVLFPS------------SEL 73

                          90       100
                  ....*....|....*....|
gi 64085083   500 SLHGGCLVTRGTKWIANNWI 519
Cdd:pfam13640  74 SLHEVLPVTGGERWSITGWF 93
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 194-252 2.19e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.23  E-value: 2.19e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 64085083 194 FRLLDQNRDGHLQ---LREVLAQTrlgnGWWMTPESIQEMYAaiKADPDGDGVLSLQEFSNM 252
Cdd:cd00051   6 FRLFDKDGDGTISadeLKAALKSL----GEGLSEEEIDEMIR--EVDKDGDGKIDFEEFLEL 61
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 182-250 1.54e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 38.03  E-value: 1.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 64085083    182 AMSTMQVSQLD-LFRLLDQNRDGHL---QLREVLAQTRLGNgwwMTPESIQEMyaaikADPDGDGVLSLQEFS 250
Cdd:smart00027   3 AISPEDKAKYEqIFRSLDKNQDGTVtgaQAKPILLKSGLPQ---TLLAKIWNL-----ADIDNDGELDKDEFA 67
 
Name Accession Description Interval E-value
P4Hc smart00702
Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of ...
 246-519 2.24e-19

Prolyl 4-hydroxylase alpha subunit homologues; Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.


Pssm-ID: 214780  Cd Length: 165  Bit Score: 85.52  E-value: 2.24e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    246 LQEFSNMDLRDfHKYMRSHKAESSELVRNSHHTWlYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHY 325
Cdd:smart00702   9 LEEAEPLGWRG-EVTRGIGNPNETSQYRQSNGTW-LELLERDLVIERIRQRLADFLGLLAGLPLSAEDAQVARYGPGGHY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    326 HAHVDSgpvypeticshtklvanesvpFETSCRQVspnwglpsilrpgtpmtqaqpctvgvplgmgpgdhwvipvspweh 405
Cdd:smart00702  87 GPHVDN---------------------FLYGDRIA--------------------------------------------- 100

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083    406 pqlgtcsvpplpysymTVLFYLNNVTGGGETVFPvadnrtydemsliqddvdlrDTRRHCdkgNLRVKPQQGTAVFWYNy 485
Cdd:smart00702 101 ----------------TFILYLNDVEEGGELVFP--------------------GLRLMV---VATVKPKKGDLLFFPS- 140

                          250       260       270
                   ....*....|....*....|....*....|....
gi 64085083    486 lpdgqgwvgdVDDYSLHGGCLVTRGTKWIANNWI 519
Cdd:smart00702 141 ----------GHGRSLHGVCPVTRGSRWAITGWI 164
PLN00052 PLN00052
prolyl 4-hydroxylase; Provisional
 418-521 1.39e-12

prolyl 4-hydroxylase; Provisional


Pssm-ID: 177683 [Multi-domain]  Cd Length: 310  Bit Score: 68.93  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083  418 YSYMTVLFYLNNVTGGGETVFPVA---DNRTYDemsliqddvdlrDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGwvg 494
Cdd:PLN00052 163 HRYATVLMYLSTVDKGGETVFPNAegwENQPKD------------DTFSECAHKGLAVKPVKGDAVLFFSLHIDGVP--- 227

                         90       100
                 ....*....|....*....|....*..
gi 64085083  495 dvDDYSLHGGCLVTRGTKWIANNWINV 521
Cdd:PLN00052 228 --DPLSLHGSCPVIEGEKWSAPKWIHI 252
EF-hand_7 pfam13499
EF-hand domain pair;
192-252 2.77e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 2.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 64085083   192 DLFRLLDQNRDGHL---QLREVLAQTRLGNGwwMTPESIQEMYAaiKADPDGDGVLSLQEFSNM 252
Cdd:pfam13499   6 EAFKLLDSDGDGYLdveELKKLLRKLEEGEP--LSDEEVEELFK--EFDLDKDGRISFEEFLEL 65
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
177-258 4.46e-08

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 52.10  E-value: 4.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083 177 EEYEEAMSTMQVSQL-----DLFRLLDQNRDGHLQLREVlaqTRLGNGWWMTPESIQEMYAAIkaDPDGDGVLSLQEFSN 251
Cdd:COG5126  53 EEFVAGMESLFEATVepfarAAFDLLDTDGDGKISADEF---RRLLTALGVSEEEADELFARL--DTDGDGKISFEEFVA 127


                ....*..
gi 64085083 252 MdLRDFH 258
Cdd:COG5126 128 A-VRDYY 133
2OG-FeII_Oxy_3 pfam13640
2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and ...
 422-519 6.22e-07

2OG-Fe(II) oxygenase superfamily; This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.


Pssm-ID: 463943  Cd Length: 94  Bit Score: 47.76  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 64085083   422 TVLFYLNNVT--GGGETVFpvadnrtydemsliqddvdlrdtrrHCDKGNLRVKPQQGTAVFWYNylpdgqgwvgdvDDY 499
Cdd:pfam13640  31 TVVLYLNDWEeeEGGELVL-------------------------YDGDGVEDIKPKKGRLVLFPS------------SEL 73

                          90       100
                  ....*....|....*....|
gi 64085083   500 SLHGGCLVTRGTKWIANNWI 519
Cdd:pfam13640  74 SLHEVLPVTGGERWSITGWF 93
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 194-252 2.19e-06

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 45.23  E-value: 2.19e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 64085083 194 FRLLDQNRDGHLQ---LREVLAQTrlgnGWWMTPESIQEMYAaiKADPDGDGVLSLQEFSNM 252
Cdd:cd00051   6 FRLFDKDGDGTISadeLKAALKSL----GEGLSEEEIDEMIR--EVDKDGDGKIDFEEFLEL 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
192-262 5.29e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 5.29e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 64085083 192 DLFRLLDQNRDGHLQLREVLAqtrLGNGWWmtpesiQEMYAaiKADPDGDGVLSLQEFSNMDLRDFHKYMR 262
Cdd:COG5126   9 RRFDLLDADGDGVLERDDFEA---LFRRLW------ATLFS--EADTDGDGRISREEFVAGMESLFEATVE 68
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 182-250 1.54e-03

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 38.03  E-value: 1.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 64085083    182 AMSTMQVSQLD-LFRLLDQNRDGHL---QLREVLAQTRLGNgwwMTPESIQEMyaaikADPDGDGVLSLQEFS 250
Cdd:smart00027   3 AISPEDKAKYEqIFRSLDKNQDGTVtgaQAKPILLKSGLPQ---TLLAKIWNL-----ADIDNDGELDKDEFA 67
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 193-249 1.74e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 40.38  E-value: 1.74e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 64085083 193 LFRLLDQNRDGHLQLREVLAQTRlgngwwmtPESIQEMYAAI------KADPDGDGVLSLQEF 249
Cdd:cd16227 127 MFEAADLNKDGKLDKTEFSAFQH--------PEEYPHMHPVLieqtlrDKDKDNDGFISFQEF 181
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 192-251 2.74e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 36.43  E-value: 2.74e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 64085083 192 DLFRLLDQNRDGHL---QLREVLAQTRLgngwwmtPesiQEMYAAI--KADPDGDGVLSLQEFSN 251
Cdd:cd00052   3 QIFRSLDPDGDGLIsgdEARPFLGKSGL-------P---RSVLAQIwdLADTDKDGKLDKEEFAI 57
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 198-253 9.36e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 38.05  E-value: 9.36e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 64085083 198 DQNRDGHLQLREVLAqtrlgngwWMTPE----SIQEMYAAI--KADPDGDGVLSLQEFSNMD 253
Cdd:cd16225 141 DEPEDGLLDVEEFLS--------FRHPEhsrgMLKNMVKEIlhDLDQDGDEKLTLDEFVSLP 194
 
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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