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Conserved domains on  [gi|390608669|ref|NP_001254629|]
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prohibitin-2 isoform 3 [Homo sapiens]

Protein Classification

prohibitin family protein( domain architecture ID 10130412)

prohibitin family protein similar to Homo sapiens prohibitin, a lipid raft-associated integral membrane protein that inhibits DNA synthesis and has a role in regulating proliferation

CATH:  3.30.479.30
Gene Ontology:  GO:0005743|GO:0035632|GO:0016020
PubMed:  31522117|17766116|10542406|16101677
SCOP:  4003722

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 40-203 1.39e-76

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


:

Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 230.48  E-value: 1.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  40 VFTVEGGHRAIFFNRiGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:cd03401    1 FYTVDAGEVGVVFRR-GKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669 120 MYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA 199
Cdd:cd03401   80 LYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159


                 ....
gi 390608669 200 KQVA 203
Cdd:cd03401  160 KQVA 163
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 40-203 1.39e-76

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 230.48  E-value: 1.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  40 VFTVEGGHRAIFFNRiGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:cd03401    1 FYTVDAGEVGVVFRR-GKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669 120 MYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA 199
Cdd:cd03401   80 LYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159


                 ....
gi 390608669 200 KQVA 203
Cdd:cd03401  160 KQVA 163
PHB smart00244
prohibitin homologues; prohibitin homologues
 39-201 1.35e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 124.70  E-value: 1.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669    39 SVFTVEGGHRAIFFNRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKI-SSPTGSKDLQMVNISLRVLSRpNAQEL 117
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669   118 PSMYQRLglDYEERVLPSIVNEVLKSVVAKFNASQLIT-QRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAA 196
Cdd:smart00244  78 RAVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 390608669   197 VEAKQ 201
Cdd:smart00244 156 MEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-203 1.28e-23

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 93.93  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669   41 FTVEGGHRAIFFNriGGVQQDTILAeGLHFRIPWFQYPIIYDIRARPRKISSPT-GSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:pfam01145   1 IIVPPGEVGVVTR--FGKLSRVLEP-GLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  120 MYQRL-GLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVE 198
Cdd:pfam01145  78 LVQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIE 157


                  ....*
gi 390608669  199 AKQVA 203
Cdd:pfam01145 158 AKQTA 162
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 25-203 2.48e-18

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 81.81  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  25 LLLGAGAVAYGVRESVFTVEGGHRAIFFnRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKI-SSPTGSKDLQMVN 103
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669 104 ISLRVLSRPNaqELPSMYQRLGlDYEERVLPsIVNEVLKSVVAKFNASQLI-TQRAQVSLLIRRELTERAKDFSLILDDV 182
Cdd:COG0330   83 VDAVVQYRIT--DPAKFLYNVE-NAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDV 158

                        170       180
                 ....*....|....*....|.
gi 390608669 183 AITELSFSREYTAAVEAKQVA 203
Cdd:COG0330  159 EIKDIDPPEEVQDAMEDRMKA 179
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 39-171 3.04e-03

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 38.23  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669   39 SVFTVEGGHRAIFFnRIGGVQQD-----TILAEGLHFRIPWFQYPIIYDIR-----ARPRKIssPTGSKDLQMVNISlrv 108
Cdd:TIGR01932  19 PFFIIKEGERGIIT-RFGKILKDnnhhvLVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRI--PTKEKKDIIIDTY--- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 390608669  109 lSRPNAQELPSMYQRLGLD---YEERVLPSIVNEVLKSVVAKFNASQLITQ-RAQVSLLIRRELTER 171
Cdd:TIGR01932  93 -IRWRIEDFKKYYLSTGGGtisAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNR 158
 
Name Accession Description Interval E-value
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 40-203 1.39e-76

Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prohibitin (a lipid raft-associated integral membrane protein). Individual proteins of the SPFH (band 7) domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. These microdomains, in addition to being stable scaffolds, may also be dynamic units with their own regulatory functions. Prohibitin is a mitochondrial inner-membrane protein which may act as a chaperone for the stabilization of mitochondrial proteins. Human prohibitin forms a hetero-oligomeric complex with Bap-37 (prohibitin 2, an SPFH domain carrying homolog). This complex may protect non-assembled membrane proteins against proteolysis by the m-AAA protease. Prohibitin and Bap-37 yeast homologs have been implicated in yeast longevity and in the maintenance of mitochondrial morphology.


Pssm-ID: 259799 [Multi-domain]  Cd Length: 195  Bit Score: 230.48  E-value: 1.39e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  40 VFTVEGGHRAIFFNRiGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:cd03401    1 FYTVDAGEVGVVFRR-GKGVKDEVLGEGLHFKIPWIQVVIIYDVRTQPREITLTVLSKDGQTVNIDLSVLYRPDPEKLPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669 120 MYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEA 199
Cdd:cd03401   80 LYQNLGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDEYEKAIEA 159


                 ....
gi 390608669 200 KQVA 203
Cdd:cd03401  160 KQVA 163
PHB smart00244
prohibitin homologues; prohibitin homologues
 39-201 1.35e-35

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 124.70  E-value: 1.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669    39 SVFTVEGGHRAIFFNRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKI-SSPTGSKDLQMVNISLRVLSRpNAQEL 117
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLR--VLGPGLHFLIPFIDDVKKVDLRAQTDDVpPQETITKDNVKVSVDAVVYYR-VLDPL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669   118 PSMYQRLglDYEERVLPSIVNEVLKSVVAKFNASQLIT-QRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAA 196
Cdd:smart00244  78 RAVYRVL--DADYAVIEQLAQTTLRSVIGKRTLDELLTdQREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEA 155


                   ....*
gi 390608669   197 VEAKQ 201
Cdd:smart00244 156 MEAQQ 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 41-203 1.28e-23

SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent phylogenetic analysis has shown this domain to be a slipin or Stomatin-like integral membrane domain conserved from protozoa to mammals.


Pssm-ID: 426078 [Multi-domain]  Cd Length: 177  Bit Score: 93.93  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669   41 FTVEGGHRAIFFNriGGVQQDTILAeGLHFRIPWFQYPIIYDIRARPRKISSPT-GSKDLQMVNISLRVLSRPNAQELPS 119
Cdd:pfam01145   1 IIVPPGEVGVVTR--FGKLSRVLEP-GLHFIIPFIQRVVTVDVRVQTLEVSVQTvLTKDGVPVNVDVTVIYRVNPDDPPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  120 MYQRL-GLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVE 198
Cdd:pfam01145  78 LVQNVfGSDDLQELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIE 157


                  ....*
gi 390608669  199 AKQVA 203
Cdd:pfam01145 158 AKQTA 162
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 25-203 2.48e-18

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 81.81  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  25 LLLGAGAVAYGVRESVFTVEGGHRAIFFnRIGGVQQdtILAEGLHFRIPWFQYPIIYDIRARPRKI-SSPTGSKDLQMVN 103
Cdd:COG0330    6 LLILLVLVLVLLFSSVYIVPQGERGVVL-RFGKYVR--TLEPGLHFKIPFIDRVRKVDVREQVLDVpPQEVLTKDNNIVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669 104 ISLRVLSRPNaqELPSMYQRLGlDYEERVLPsIVNEVLKSVVAKFNASQLI-TQRAQVSLLIRRELTERAKDFSLILDDV 182
Cdd:COG0330   83 VDAVVQYRIT--DPAKFLYNVE-NAEEALRQ-LAESALREVIGKMTLDEVLsTGRDEINAEIREELQEALDPYGIEVVDV 158

                        170       180
                 ....*....|....*....|.
gi 390608669 183 AITELSFSREYTAAVEAKQVA 203
Cdd:COG0330  159 EIKDIDPPEEVQDAMEDRMKA 179
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 91-189 1.32e-09

core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons, and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease, and in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259797 [Multi-domain]  Cd Length: 110  Bit Score: 54.29  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  91 SSPTGSKDLQMVNISLRVLSRP-NAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELT 169
Cdd:cd02106    9 VEPVGTADGVPVAVDLVVQFRItDYNALPAFYLVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVKEDLE 88

                         90       100
                 ....*....|....*....|
gi 390608669 170 ERAKDFSLILDDVAITELSF 189
Cdd:cd02106   89 EDLENFGVVISDVDITSIEP 108
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 39-197 3.55e-09

High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.


Pssm-ID: 259803 [Multi-domain]  Cd Length: 249  Bit Score: 55.57  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669  39 SVFTVEGGHRAIFFnRIGGVQQdTILAEGLHFRIPWFQYPIIYDIR-----ARPRKIssPTgsKDLQMVNISLRVLSRPN 113
Cdd:cd03405    1 SVFIVDETEQAVVL-QFGKPVR-VITEPGLHFKLPFIQNVRKFDKRiltldGPPEEV--LT--KDKKRLIVDSYARWRIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669 114 AQELpsMYQRLGLDYE-ERVLPSIVNEVLKSVVAKFNASQLI-TQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSR 191
Cdd:cd03405   75 DPLR--FYQSVGGEEGaESRLDDIVDSALRNEIGKRTLAEVVsGGRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPE 152


                 ....*.
gi 390608669 192 EYTAAV 197
Cdd:cd03405  153 EVSESV 158
hflC TIGR01932
HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 39-171 3.04e-03

HflC protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described. [Protein fate, Degradation of proteins, peptides, and glycopeptides, Regulatory functions, Protein interactions]


Pssm-ID: 273883 [Multi-domain]  Cd Length: 317  Bit Score: 38.23  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 390608669   39 SVFTVEGGHRAIFFnRIGGVQQD-----TILAEGLHFRIPWFQYPIIYDIR-----ARPRKIssPTGSKDLQMVNISlrv 108
Cdd:TIGR01932  19 PFFIIKEGERGIIT-RFGKILKDnnhhvLVYEPGLHFKIPFIEHVKIFDAKiqtmdGRPDRI--PTKEKKDIIIDTY--- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 390608669  109 lSRPNAQELPSMYQRLGLD---YEERVLPSIVNEVLKSVVAKFNASQLITQ-RAQVSLLIRRELTER 171
Cdd:TIGR01932  93 -IRWRIEDFKKYYLSTGGGtisAAEVLIKRKIDDRLRSEIGVLGLKEIVRSsNDQLDTLVSKLALNR 158
 
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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