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Conserved domains on  [gi|519008854|ref|WP_020164729|]
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MULTISPECIES: SPFH domain-containing protein [Methyloversatilis]

Protein Classification

SPFH domain-containing protein( domain architecture ID 11417211)

SPFH (stomatin, prohibitin, flotillin, and HflK/C) domain-containing protein similar to Homo sapiens mitochondrial stomatin-like protein 2, and Escherichia coli protein QmcA

CATH:  3.30.479.30
Gene Ontology:  GO:0016020
PubMed:  16101677|17766116|10542406|21501885|24782879
TCDB:  8.A.21

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 3-282 5.28e-77

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


:

Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 235.50  E-value: 5.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   3 SGLIVVIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNA 82
Cdd:COG0330    1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  83 VIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIADEAIDWGLTVKSVE 161
Cdd:COG0330   80 IVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 162 IQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQSMILEAEARLESAKRDA----AAQVTLAEASAESIRRVTASLGE 237
Cdd:COG0330  160 IKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAeayrEAQILRAEGEAEAFRIVAEAYSA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 519008854 238 QQlpmmYLLGEKYIAALNKLGeSPNAKVVVLPADLQDAVAGIFAR 282
Cdd:COG0330  240 AP----FVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 3-282 5.28e-77

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 235.50  E-value: 5.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   3 SGLIVVIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNA 82
Cdd:COG0330    1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  83 VIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIADEAIDWGLTVKSVE 161
Cdd:COG0330   80 IVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 162 IQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQSMILEAEARLESAKRDA----AAQVTLAEASAESIRRVTASLGE 237
Cdd:COG0330  160 IKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAeayrEAQILRAEGEAEAFRIVAEAYSA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 519008854 238 QQlpmmYLLGEKYIAALNKLGeSPNAKVVVLPADLQDAVAGIFAR 282
Cdd:COG0330  240 AP----FVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 59-169 2.60e-49

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 158.79  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  59 AYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKI 138
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 519008854 139 KVRLRESIADEAIDWGLTVKSVEIQDINPSD 169
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
PHB smart00244
prohibitin homologues; prohibitin homologues
 21-179 2.01e-40

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 137.79  E-value: 2.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854    21 KGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKA 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   101 VYGVTDFSEA-IRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQ 178
Cdd:smart00244  80 VYRVLDADYAvIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 519008854   179 A 179
Cdd:smart00244 160 Q 160
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 24-196 1.58e-33

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: 120.50  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   24 RVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKV--TDPVKAV 101
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  102 YGVTDFS---EAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQ 178
Cdd:pfam01145  80 QNVFGSDdlqELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 519008854  179 ASAERERKAMVTRSEGQK 196
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 24-229 1.92e-21

HflK 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.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 90.92  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   24 RVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYG 103
Cdd:TIGR01933   2 YTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  104 VTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-----RDKIKVRLRESIadEAIDWGLTVKSVEIQDINPSDSMQRAMEQQ 178
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgrsqiREDTKERLNEII--DNYDLGITVTDVNFQSARPPEEVKEAFDDV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 519008854  179 ASAERERKAMVTRSEGQKQSMILEAEARLESAKRDAAA--QVTLAEASAESIR 229
Cdd:TIGR01933 159 IIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGykERRINRAKGDVAR 211
PRK10930 PRK10930
FtsH protease activity modulator HflK;
3-237 9.06e-13

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 67.93  E-value: 9.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   3 SGLIVVIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVayKVVTKDIILDVQEQEV-ITRDN 81
Cdd:PRK10930  77 GGRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEV--KPVNVEAVRELAASGVmLTSDE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  82 AVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-----RDKIKVRLRESIadEAIDWGLT 156
Cdd:PRK10930 155 NVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgrtviRSDTQRELEETI--RPYDMGIT 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 157 VKSVEIQDINPSDSMQRAMEqQASAERErkamvtrsegQKQSMILEAEARLESAKRDA--AAQVTLAEASAESIRRVTAS 234
Cdd:PRK10930 233 LLDVNFQAARPPEEVKAAFD-DAIAARE----------NEQQYIREAEAYTNEVQPRAngQAQRILEEARAYKAQTILEA 301


                 ...
gi 519008854 235 LGE 237
Cdd:PRK10930 302 QGE 304
 
Name Accession Description Interval E-value
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
 3-282 5.28e-77

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


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 235.50  E-value: 5.28e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   3 SGLIVVIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNA 82
Cdd:COG0330    1 NKLILLLILLVLVLVLLFSSVYIVPQGERGVVLRFGKYVRTLEPGLHFKIPFIDRV-RKVDVREQVLDVPPQEVLTKDNN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  83 VIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIADEAIDWGLTVKSVE 161
Cdd:COG0330   80 IVDVDAVVQYRITDPAKFLYNVENAEEALRQLAESALREVIGKMTLDEVLSTgRDEINAEIREELQEALDPYGIEVVDVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 162 IQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQSMILEAEARLESAKRDA----AAQVTLAEASAESIRRVTASLGE 237
Cdd:COG0330  160 IKDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAIIEAeayrEAQILRAEGEAEAFRIVAEAYSA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 519008854 238 QQlpmmYLLGEKYIAALNKLGeSPNAKVVVLPADLQDAVAGIFAR 282
Cdd:COG0330  240 AP----FVLFYRSLEALEEVL-SPNSKVIVLPPDGNGFLKYLLKS 279
SPFH_paraslipin cd08829
Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; ...
 59-169 2.60e-49

Paraslipin or slipin-2 (SLP-2, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in all three kingdoms of life. The conserved domain common to these families has also been referred to as the Band 7 domain. Individual proteins of the SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This subgroup of the SLPs remains largely uncharacterized. It includes human SLP-2 which is upregulated and involved in the progression and development in several types of cancer, including esophageal squamous cell carcinoma, endometrial adenocarcinoma, breast cancer, and glioma.


Pssm-ID: 259811 [Multi-domain]  Cd Length: 111  Bit Score: 158.79  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  59 AYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKI 138
Cdd:cd08829    1 AYKVDLREQVLDIPPQEVITKDNVTVTVDAVLYYRVVDPYKASYGVEDLEYAIENLAQTTLRSEIGKMELDETLSSREEI 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 519008854 139 KVRLRESIADEAIDWGLTVKSVEIQDINPSD 169
Cdd:cd08829   81 NAKLLEALDEATDPWGVKVTRVEIKDITPPE 111
SPFH_eoslipins_u1 cd08826
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 61-226 5.52e-46

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized. This subgroup contains PH1511 from the hyperthermophilic archaeon Pyrococcus horikoshi.


Pssm-ID: 259808 [Multi-domain]  Cd Length: 178  Bit Score: 152.67  E-value: 5.52e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  61 KVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKV 140
Cdd:cd08826    8 RVDLRTVTLDVPPQEVITKDNVTVKVNAVVYFRVVDPEKAVLAVEDYRYATSQLAQTTLRSVVGQVELDELLSEREEINK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 141 RLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQS--MILEAEARLESAKrdAAAQV 218
Cdd:cd08826   88 RIQEIIDEQTEPWGIKVTAVEIKDVDLPESMQRAMARQAEAERERRAKIIKAEGELQAaeKLAEAAEILAKSP--GALQL 165

                        170
                 ....*....|..
gi 519008854 219 ----TLAEASAE 226
Cdd:cd08826  166 rylqTLSEIASE 177
PHB smart00244
prohibitin homologues; prohibitin homologues
 21-179 2.01e-40

prohibitin homologues; prohibitin homologues


Pssm-ID: 214581 [Multi-domain]  Cd Length: 160  Bit Score: 137.79  E-value: 2.01e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854    21 KGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKA 100
Cdd:smart00244   1 AAIKVVGEGERGVVERLGRVLRVLGPGLHFLIPFIDDV-KKVDLRAQTDDVPPQETITKDNVKVSVDAVVYYRVLDPLRA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   101 VYGVTDFSEA-IRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQ 178
Cdd:smart00244  80 VYRVLDADYAvIEQLAQTTLRSVIGKRTLDELLTDqREKISENIREELNEAAEAWGIKVEDVEIKDIRLPEEIKEAMEAQ 159


                   .
gi 519008854   179 A 179
Cdd:smart00244 160 Q 160
SPFH_alloslipin cd13437
Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 26-271 6.40e-38

Alloslipin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in some eukaryotes and viruses. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. This diverse subgroup of the SLPs remains largely uncharacterized.


Pssm-ID: 259815 [Multi-domain]  Cd Length: 222  Bit Score: 133.51  E-value: 6.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  26 VPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVT 105
Cdd:cd13437    9 VKQGSVGLVERFGKFYKTVDPGLHKVNPCTEKI-IQVDMKTQVIDLPRQSVMTKDNVSVTIDSVVYYRIIDPYKAIYRID 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 106 DFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMeqqasaerer 185
Cdd:cd13437   88 NVKQALIERTQTTLRSVIGERTLQDLLEKREEIADEIEEIVEEVAKEWGVYVESILIKDIVLSKDLQQSL---------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 186 kAMVTRSEGQKQSMILEAEARLESAK--RDAAAQvtLAEASAESIRrvtaslgeqqlpmmyllgekYIAALNKLGESPNA 263
Cdd:cd13437  158 -SSAAKAKRIGESKIISAKADVESAKlmREAADI--LDSKAAMQIR--------------------YLETLQAIAKSANS 214


                 ....*...
gi 519008854 264 KVVVLPAD 271
Cdd:cd13437  215 KVIFLPLD 222
SPFH_SLP-4 cd13435
Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 46-226 1.39e-35

Slipin-4 (SLP-4), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in arthropods. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this divergent slipin subgroup remain largely uncharacterized. It contains Drosophila Mec2, the gene for which was identified in a screen for genes required for nephrocyte function; it may function together with Sns in maintaining nephrocyte diaphragm.


Pssm-ID: 259813 [Multi-domain]  Cd Length: 208  Bit Score: 127.11  E-value: 1.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  46 PGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGE 125
Cdd:cd13435    7 PGVFFVLPCIDNY-CKVDLRTVSFDVPPQEVLTKDSVTVTVDAVVYYRISDPLNAVIQVANYSHSTRLLAATTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 126 MDLDQALSSRDKIKVRLRESIaDEAID-WGLTVKSVEIQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQSMILEAE 204
Cdd:cd13435   86 RNLSELLTERETISHSMQVTL-DEATDpWGVQVERVEIKDVSLPDSLQRAMAAEAEAAREARAKVIAAEGEMKSSRALKE 164

                        170       180
                 ....*....|....*....|....*.
gi 519008854 205 ARLESAKRDAAAQV----TLAEASAE 226
Cdd:cd13435  165 ASDIISASPSALQLrylqTLSSISGE 190
Band_7 pfam01145
SPFH domain / Band 7 family; This family has been called SPFH, Band 7 or PHB domain. Recent ...
 24-196 1.58e-33

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: 120.50  E-value: 1.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   24 RVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKV--TDPVKAV 101
Cdd:pfam01145   1 IIVPPGEVGVVTRFGKLSRVLEPGLHFIIPFIQRV-VTVDVRVQTLEVSVQTVLTKDGVPVNVDVTVIYRVnpDDPPKLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  102 YGVTDFS---EAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQ 178
Cdd:pfam01145  80 QNVFGSDdlqELLRRVLESALREIIARYTLEELLSNREELAEEIKNALQEELAKYGVEIIDVQITDIDPPPEIAEAIEAK 159

                         170
                  ....*....|....*...
gi 519008854  179 ASAERERKAMVTRSEGQK 196
Cdd:pfam01145 160 QTAEQEAEAEIARAEAEA 177
SPFH_HflK cd03404
High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and ...
 9-215 5.68e-30

High frequency of lysogenization K (HflK) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflK (High frequency of lysogenization K). 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 HflK is an integral membrane protein which may localize to the plasma membrane. HflK associates with another SPFH superfamily member (HflC) 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: 259802 [Multi-domain]  Cd Length: 266  Bit Score: 113.76  E-value: 5.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   9 IALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVAYKV-VTK----DIILDV-QEQEVITRDNA 82
Cdd:cd03404    1 LILLLLLLVWLLSGFYTVDPGERGVVLRFGKYVRTVGPGLHWKLPFPIEVVEKVnVTQvrsvEIGFRVpEESLMLTGDEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  83 VIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIAD--EAIDWGLTVKS 159
Cdd:cd03404   81 IVDVDFVVQYRISDPVAYLFNVRDPEETLRQAAESALREVVGSRTLDDVLTEgRAEIAADVRELLQEilDRYDLGIEIVQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519008854 160 VEIQDINPSDSMQRAME--QQASAERERK---------AMVTRSEGQKQSMILEAEA----RLESAKRDAA 215
Cdd:cd03404  161 VQLQDADPPEEVQDAFDdvNAARQDKERLineaqayanEVIPRARGEAARIIQEAEAykaeVVARAEGDAA 231
SPFH_SLPs cd13434
Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) ...
 67-168 2.98e-29

Stomatin-like proteins (slipins) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes proteins similar to stomatin, podocin, and other members of the stomatin-like protein family (SLPs or slipins). The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. 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. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome. Bacterial and archaebacterial SLPs and many of the eukaryotic family members remain uncharacterized.


Pssm-ID: 259812 [Multi-domain]  Cd Length: 108  Bit Score: 107.28  E-value: 2.98e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  67 IILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESI 146
Cdd:cd13434    6 QSVDVPPQEILTKDNVTVSVDAVVYYRVVDPLKAVLNVEDYKKATELLAQTTLRNVLGTRTLDELLSEREEISQQLQEIL 85

                         90       100
                 ....*....|....*....|..
gi 519008854 147 ADEAIDWGLTVKSVEIQDINPS 168
Cdd:cd13434   86 DEATDPWGIKVERVEIKDIILP 107
SPFH_like_u4 cd03407
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 25-271 2.11e-27

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of 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: 259805 [Multi-domain]  Cd Length: 269  Bit Score: 106.90  E-value: 2.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  25 VVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVAYKVVTKDIILDVQEqEVITRDNAVIRTNAVAFIKVTDP--VKAVY 102
Cdd:cd03407    1 CVSQSTVAIVERFGKFSRIAEPGLHFIIPPIESVAGRVSLRVQQLDVRV-ETKTKDNVFVTLVVSVQYRVVPEkvYDAFY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 103 GVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQASAE 182
Cdd:cd03407   80 KLTNPEQQIQSYVFDVVRASVPKLTLDEVFESKDEIAKAVKEELAKVMSEYGYEIVKTLVTDIEPDASVKAAMNEINAAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 183 RERKAMVTRSEGQKQSMILEAEARLESAK---RDAAAQ----VTLAEASAESIRRVTASLGEQQlPMMYLLGEKYIAALN 255
Cdd:cd03407  160 RLREAAEEKAEAEKILQVKAAEAEAEAKRlqgVGIAEQrkaiVDGLRESIEDFQEAVPGVSSKE-VMDLLLITQYFDTLK 238

                        250
                 ....*....|....*.
gi 519008854 256 KLGESPNAKVVVLPAD 271
Cdd:cd03407  239 EVGKSSKSSTVFLPHG 254
SPFH_stomatin cd03403
Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 46-226 4.40e-27

Stomatin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; Stomatin (or band 7) is widely expressed and, highly expressed in red blood cells. It localizes predominantly to the plasma membrane and to intracellular vesicles of the endocytic pathway, where it is present in higher order homo-oligomeric complexes (of between 9 and 12 monomers). Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and, is implicated in trafficking of Glut1 glucose transporters. This subgroup found in animals, also contains proteins similar to Caenorhabditis elegans MEC-2. MEC-2 interacts with MEC-4, which is part of the degenerin channel complex required for response to gentle body touch.


Pssm-ID: 259801 [Multi-domain]  Cd Length: 202  Bit Score: 104.55  E-value: 4.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  46 PGLNIIIPYLDDVAyKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGE 125
Cdd:cd03403    7 PGLFFILPCIDSYR-KVDLRTVSFDVPPQEILTKDSVTVAVDAVVYYRVQNATIAVTNVENADRSTRLLAQTTLRNVLGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 126 MDLDQALSSRDKIKVRLRESIaDEAID-WGLTVKSVEIQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQSMILEAE 204
Cdd:cd03403   86 KNLSEILSDRETISHQMQSTL-DEATDpWGVKVERVEIKDVRLPVQLQRAMAAEAEAAREARAKVIAAEGEQNASRALKE 164

                        170       180
                 ....*....|....*....|....*.
gi 519008854 205 ARLESAKRDAAAQV----TLAEASAE 226
Cdd:cd03403  165 AADVISESPAALQLrylqTLNTISAE 190
SPFH_eoslipins_u3 cd13775
Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of ...
 74-203 2.43e-26

Uncharacterized prokaryotic subfamily of the stomatin-like proteins (slipins), a subgroup of the SPFH family (stomatin, prohibitin, flotillin, and HflK/C); This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria and archaebacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial and archaebacterial SLPs remain uncharacterized.


Pssm-ID: 259817 [Multi-domain]  Cd Length: 177  Bit Score: 101.55  E-value: 2.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  74 QEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDW 153
Cdd:cd13775   13 EQTLTKDLVPVDVDAVLFWMVWDAEKAALEVEDYRAAVSLAAQTALRDAIGRSELAELLSRREQIDEELQDIIDEKTTPW 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 519008854 154 GLTVKSVEIQDINPSDSMQRAMEQQASAERERKAMVTRSEGQKQ--SMILEA 203
Cdd:cd13775   93 GITVQSVEIRDIIIPKELQDAMSREAQAEREKNARVILAEAEKEiaEMFVEA 144
SPFH_HflC cd03405
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ...
 25-230 1.43e-23

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: 96.40  E-value: 1.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  25 VVPQGEEWVVQRMGKYLRTLL-PGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVK---A 100
Cdd:cd03405    4 IVDETEQAVVLQFGKPVRVITePGLHFKLPFIQNV-RKFDKRILTLDGPPEEVLTKDKKRLIVDSYARWRITDPLRfyqS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 101 VYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-RDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQA 179
Cdd:cd03405   83 VGGEEGAESRLDDIVDSALRNEIGKRTLAEVVSGgRDELMEEILEQANEEAKEYGIEVVDVRIKRIDLPEEVSESVYERM 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 519008854 180 SAERERKAMVTRSEGQKQSMILEAEArlesakrDAAAQVTLAEA--SAESIRR 230
Cdd:cd03405  163 RAERERIAAEYRAEGEEEAEKIRAEA-------DRERTVILAEAyrEAEEIRG 208
SPFH_eoslipins_u2 cd13438
Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging ...
 26-224 6.21e-23

Uncharacterized prokaryotic subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in bacteria. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Bacterial SLPs remain uncharacterized.


Pssm-ID: 259816 [Multi-domain]  Cd Length: 215  Bit Score: 93.75  E-value: 6.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  26 VPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVAYKVV-TKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGV 104
Cdd:cd13438    1 VPPGERGLLYRDGKLVRTLEPGRYAFWKFGRKVQVELVdLREQLLEVSGQEILTADKVALRVNLVATYRVVDPVKAVETV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 105 TDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQASAERe 184
Cdd:cd13438   81 DDPEEQLYLALQLALREAVAARTLDELLEDREDLSEFLLAAVKEAAAELGVEVLSVGVKDIILPGEIREILNQVLEAEK- 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 519008854 185 rkamvtrsegqkqsmilEAEARLESAKRDAAAQVTLAEAS 224
Cdd:cd13438  160 -----------------RAQANLIRAREETAATRSLLNAA 182
SPFH_SLP-3 cd08828
Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; ...
 46-195 1.57e-21

Slipin-3 (SLP-3), an uncharacterized subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Members of this slipin subgroup remain uncharacterized, except for Caenorhabditis elegans UNC-1. Mutations in the unc-1 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259810 [Multi-domain]  Cd Length: 154  Bit Score: 88.55  E-value: 1.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  46 PGLNIIIPYLDdVAYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGE 125
Cdd:cd08828    3 PGLILVLPCTD-TFIKVDLRTVTCNIPPQEILTKDSVTTQVDGVVYYRIQSAVKAVANVNNVHIATFLLAQTTLRNVLGT 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 126 MDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQASAERERKAMVTRSEGQ 195
Cdd:cd08828   82 QTLAQILAGREEIAHSIQSILDHATEKWGIKVARVEIKDVRIPVQMQRAMAAEAEATREARAKVVAAEGE 151
hflK TIGR01933
HflK protein; HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, ...
 24-229 1.92e-21

HflK 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.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03]


Pssm-ID: 130988 [Multi-domain]  Cd Length: 261  Bit Score: 90.92  E-value: 1.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   24 RVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVaYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYG 103
Cdd:TIGR01933   2 YTIGEAERGVVLRFGKYHRTVDPGLNWKPPFIEEV-YPVNVTAVRNLRKQGLMLTGDENIVNVEMNVQYRITDPYKYLFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  104 VTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-----RDKIKVRLRESIadEAIDWGLTVKSVEIQDINPSDSMQRAMEQQ 178
Cdd:TIGR01933  81 VENPEDSLRQATDSALRGVIGDSTMDDILTEgrsqiREDTKERLNEII--DNYDLGITVTDVNFQSARPPEEVKEAFDDV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 519008854  179 ASAERERKAMVTRSEGQKQSMILEAEARLESAKRDAAA--QVTLAEASAESIR 229
Cdd:TIGR01933 159 IIAREDEERYINEAEAYANEVVPKARGDAQRIIEEARGykERRINRAKGDVAR 211
SPFH_prohibitin cd03401
Prohibitin family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 23-227 2.15e-17

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: 78.32  E-value: 2.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  23 LRVVPQGEEWVVQRMGKY--LRTLLPGLNIIIPYLDDVaykvvtkdIILDVQEQ------EVITRDNAVIRTN-AVAFIK 93
Cdd:cd03401    1 FYTVDAGEVGVVFRRGKGvkDEVLGEGLHFKIPWIQVV--------IIYDVRTQpreitlTVLSKDGQTVNIDlSVLYRP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  94 VTDPVKAVY---GVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDS 170
Cdd:cd03401   73 DPEKLPELYqnlGPDYEERVLPPIVREVLKAVVAQYTAEELYTKREEVSAEIREALTERLAPFGIIVDDVLITNIDFPDE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519008854 171 MQRAMEQQASAERErkamvtrsegqkqsmILEAEARLESAKRDAAAQVTLAEASAES 227
Cdd:cd03401  153 YEKAIEAKQVAEQE---------------AERAKFELEKAEQEAERKVIEAEGEAEA 194
SPFH_podocin cd08827
Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH ...
 23-196 6.56e-14

Podocin, a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in vertebrates. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Podocin is expressed in the kidney and mutations in the gene have been linked to familial idiopathic nephrotic syndrome. Podocin interacts with the TRP ion channel TRPV-6 and may function as a scaffolding protein in the organization of lipid-protein domains.


Pssm-ID: 259809 [Multi-domain]  Cd Length: 223  Bit Score: 69.15  E-value: 6.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  23 LRVVPQGEEWVVQRMGKYL--RTLLPGLNIIIPYLDdVAYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKA 100
Cdd:cd08827    4 VKVVREYERAVIFRLGHLLqgRARGPGLFFYLPCLD-VCHKVDIRLQTLEIPFHMIVTKDLVCTEIDAICYYRIENASVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 101 VYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQAS 180
Cdd:cd08827   83 LSSFASISDAMQALVQTTVKRLLAHRAFTDILLERKSIAQEIKVALDSGTCRWGIKVERAEIKDVNLPPELQHSFAVEAE 162

                        170
                 ....*....|....*.
gi 519008854 181 AERERKAMVTRSEGQK 196
Cdd:cd08827  163 AQRQAKVKVIAAEGEK 178
SPFH_SLP-1 cd13436
Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; ...
 46-164 1.15e-13

Stomatin-like protein 1 (SLP-1), a subgroup of the stomatin-like proteins (slipins) family; belonging to the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes a subgroup of the stomatin-like protein family (SLPs or slipins) that is found in animals. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. The family contains human SLP-1, which has been found to be expressed in the brain, and Caenorhabditis elegans UNC-24, which is a lipid raft-associated protein required for normal locomotion. It may mediate the correct localization of UNC-1. Mutations in the unc-24 gene result in abnormal motion and altered patterns of sensitivity to volatile anesthetics.


Pssm-ID: 259814 [Multi-domain]  Cd Length: 131  Bit Score: 66.65  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  46 PGLNIIIPYLDDVAyKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGE 125
Cdd:cd13436    9 PGIVLILPCIDNFT-RVDMRTRAFNVPPQKIITKDGGLVSVGADVQFRIWDPVLSVMAVQDLNTSTRTTAQTSLTNSLSK 87

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 519008854 126 MDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQD 164
Cdd:cd13436   88 KTVREIQSDRRKINEELKDELNKMTTAWGLEVTRVELSD 126
SPFH_like cd02106
core domain of the SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model ...
 69-169 7.07e-13

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: 63.54  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  69 LDVQEQEVITRDNAVIRTNAVAFIKVTDPVKA-----VYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSSRDKIKVRLR 143
Cdd:cd02106    5 DDVRVEPVGTADGVPVAVDLVVQFRITDYNALpafylVDFVKDIKADIRRKIADVLRAAIGRMTLDQIISGRDEIAKAVK 84

                         90       100
                 ....*....|....*....|....*.
gi 519008854 144 ESIADEAIDWGLTVKSVEIQDINPSD 169
Cdd:cd02106   85 EDLEEDLENFGVVISDVDITSIEPPD 110
PRK10930 PRK10930
FtsH protease activity modulator HflK;
3-237 9.06e-13

FtsH protease activity modulator HflK;


Pssm-ID: 236799 [Multi-domain]  Cd Length: 419  Bit Score: 67.93  E-value: 9.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   3 SGLIVVIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVayKVVTKDIILDVQEQEV-ITRDN 81
Cdd:PRK10930  77 GGRVVGIAAAAVVIIWAASGFYTIKEAERGVVTRFGKFSHLVEPGLNWKPTFIDEV--KPVNVEAVRELAASGVmLTSDE 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  82 AVIRTNAVAFIKVTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQALSS-----RDKIKVRLRESIadEAIDWGLT 156
Cdd:PRK10930 155 NVVRVEMNVQYRVTDPEKYLFSVTSPDDSLRQATDSALRGVIGKYTMDRILTEgrtviRSDTQRELEETI--RPYDMGIT 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 157 VKSVEIQDINPSDSMQRAMEqQASAERErkamvtrsegQKQSMILEAEARLESAKRDA--AAQVTLAEASAESIRRVTAS 234
Cdd:PRK10930 233 LLDVNFQAARPPEEVKAAFD-DAIAARE----------NEQQYIREAEAYTNEVQPRAngQAQRILEEARAYKAQTILEA 301


                 ...
gi 519008854 235 LGE 237
Cdd:PRK10930 302 QGE 304
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
5-226 1.31e-12

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 67.21  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   5 LIVVIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLRTLLPGLNIIIPYLDDVAYkVVTKDIILDVQ-EQEVITRDNAV 83
Cdd:COG2268   10 IGVIVVVLLLLLIILARFYRKVPPNEALVITGRGGGYKVVTGGGAFVLPVLHRAER-MSLSTMTIEVErTEGLITKDGIR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  84 IRTNAVAFIKVTDPVKAVYGV-----TDFSEAIRNLIMTT----LRSIVGEMDLDQALSSRDKIKVRLRESIADEAIDWG 154
Cdd:COG2268   89 VDVDAVFYVKVNSDPEDIANAaerflGRDPEEIEELAEEKlegaLRAVAAQMTVEELNEDREKFAEKVQEVAGTDLAKNG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 155 LTVKSVEIQDI----NPSDSM-------QRAMEQQASAERERKAMVTRSEGQKQSMILEAEARLESA-KRDAAAQVTLAE 222
Cdd:COG2268  169 LELESVAITDLedenNYLDALgrrkiaeIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIEtARIAEAEAELAK 248


                 ....
gi 519008854 223 ASAE 226
Cdd:COG2268  249 KKAE 252
SPFH_like_u2 cd03402
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 15-211 3.49e-09

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of 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: 259800  Cd Length: 231  Bit Score: 56.02  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  15 VAVTLAKGLRVVPQGEEWVVQRMGKYLRTL-LPGLNIIIPYLddVAYKVVTKDIILDVQEQEVITRDNAVIRTNAVAFIK 93
Cdd:cd03402    2 VGIILLGGFFVVQPNEAAVLTLFGRYRGTVrRPGLRWVNPFY--RKKRVSLRVRNFESEPLKVNDANGNPIEIAAVVVWR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  94 VTDPVKAVYGVTDFSEAIRNLIMTTLRSIVGEMDLDQA-------LSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDIN 166
Cdd:cd03402   80 VVDTAKAVFDVDDYEEFVSIQSEAALRRVASRYPYDSFedgepslRGNSDEVSEELRRELQERLAVAGVEVIEARITHLA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 519008854 167 PSDSMQRAME--QQASAERERKAMVTRSegqKQSMILEAEARLESAK 211
Cdd:cd03402  160 YAPEIAQAMLqrQQASAIIAARQTIVEG---AVGMVEMALARLEERG 203
SPFH_flotillin cd03399
Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; ...
 50-182 1.01e-08

Flotillin or reggie family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; The flotillin (reggie) like proteins are lipid raft-associated. Individual proteins of this SPFH family may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. In addition, microdomains formed from flotillin proteins may be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and interact with a variety of proteins. They may play a role 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.


Pssm-ID: 259798 [Multi-domain]  Cd Length: 145  Bit Score: 52.89  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  50 IIIPYLDDVAYKVVTKdIILDVQEQEVITRDNAVIRTNAVAFIKV-TDPVKAVYGVTDF----SEAIRNLIMTT----LR 120
Cdd:cd03399    1 FVIPFLQRVQRLSLET-MTIDVKVEEVLTKDGIPVDVTAVAQVKVgSDPEEIAAAAERFlgksTEEIRELVKETleghLR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519008854 121 SIVGEMDLDQALSSRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQASAE 182
Cdd:cd03399   80 AIVGTMTVEEIYQDREKFAEQVQEVAEPDLAKMGLEIDSFNIKDISDDNGYLESLGRKQAAE 141
PRK11029 PRK11029
protease modulator HflC;
8-227 7.68e-08

protease modulator HflC;


Pssm-ID: 182913 [Multi-domain]  Cd Length: 334  Bit Score: 52.82  E-value: 7.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854   8 VIALVVFVAVTLAKGLRVVPQGEEWVVQRMGKYLR-------TLLPGLNIIIPYLDDVayKVVTKDI-ILDVQEQEVITR 79
Cdd:PRK11029   5 VIAIIIIVLVVLYMSVFVVKEGERGIVLRFGKVLRdddnkplVYAPGLHFKIPFIETV--KMLDARIqTMDNQADRFVTK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  80 DNAVIRTNAVAFIKVTDpVKAVYGVT---DFSEA---IRNLIMTTLRSIVGEMDLDQALS-SRDKIKVRLRESI------ 146
Cdd:PRK11029  83 EKKDLIVDSYIKWRISD-FSRYYLATgggDISQAevlLKRKFSDRLRSEIGRLDVKDIVTdSRGRLTLDVRDALnsgsag 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854 147 ---------ADEAID------------------------WGLTVKSVEIQDINPSDSMQRAMEQQASAERERKAMVTRSE 193
Cdd:PRK11029 162 tedevatpaADDAIAsaaerveaetkgkvpvinpnsmaaLGIEVVDVRIKQINLPTEVSDAIYNRMRAEREAVARRHRSQ 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 519008854 194 GQKQSMILEAEARLESAKrdaaaqvTLAEASAES 227
Cdd:PRK11029 242 GQEEAEKLRATADYEVTR-------TLAEAERQG 268
SPFH_like_u1 cd03408
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
 67-181 1.06e-05

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of 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: 259806  Cd Length: 217  Bit Score: 45.62  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519008854  67 IILDVQEQEVITRdnavIRTNAVAFIKVTDPVK---------AVYGVTDFSEAIRNLIMTTLRSIVGEM----DLDQALS 133
Cdd:cd03408   89 IPYRDPEYGIPVR----LRAFGTYSFRVTDPALfltevvgtqGTFTTDEIEEQLRSEIVQALKDAIAELsisgLDLALEA 164

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 519008854 134 SRDKIKVRLRESIADEAIDWGLTVKSVEIQDINPSDSMQRAMEQQASA 181
Cdd:cd03408  165 NLDELSAALKEKLAPEFEKYGLELTSFGIESISLPEEVQKRIDKRASM 212
 
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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