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Conserved domains on  [gi|1039745922|ref|XP_017171442|]
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sodium bicarbonate cotransporter 3 isoform X3 [Mus musculus]

Protein Classification

anion exchanger family transporter( domain architecture ID 705853)

anion exchanger family transporter similar to human SLC4 proteins which function as bicarbonate transporters

Gene Ontology:  GO:0005452|GO:0022857|GO:0055085
SCOP:  4003612
TCDB:  2.A.31

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Band_3_cyto super family cl26877
Band 3 cytoplasmic domain; This family contains the cytoplasmic domain of the Band 3 anion ...
118-1159 0e+00

Band 3 cytoplasmic domain; This family contains the cytoplasmic domain of the Band 3 anion exchange proteins that exchange Cl-/HCO3-. Band 3 constitutes the most abundant polypeptide in the red blood cell membrane, comprising 25% of the total membrane protein. The cytoplasmic domain of band 3 functions primarily as an anchoring site for other membrane-associated proteins. Included among the protein ligands of cdb3 are ankyrin, protein 4.2, protein 4.1, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), phosphofructokinase, aldolase, hemoglobin, hemichromes, and the protein tyrosine kinase (p72syk).


The actual alignment was detected with superfamily member TIGR00834:

Pssm-ID: 452680 [Multi-domain]  Cd Length: 900  Bit Score: 1053.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  118 FTEMDELCYRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLD 197
Cdd:TIGR00834    1 FVELNELMLDRNQEPEWRETARWIKFEEDVEEGGGRWGKPHVATLSFHSLLELRRCFAKGAILLDLAATSLPGVANMVVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  198 NMIASGQLDDSIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKKHSdphllerngeglsasrhslrtglsaSNLSl 277
Cdd:TIGR00834   81 HLIYSGQIRPEDRDEVLRALLLKHSHQSDAKKLGGLSRARSQSSIGKTLS-------------------------HDAS- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  278 rgesplslllshllpssragtpagsrcttpvptpqssppsspdlsrlasrsfQQTQPQAPEVLVSPDRDDIPRVvIHPPe 357
Cdd:TIGR00834  135 ----------------------------------------------------EMPNPDNGAPLLPHQPLTEMQL-LSVP- 160
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  358 ediealkgqeqkneentaftpgilaspqsapgnldnsksgemkgnGSGGSRENSTVDFskesaswhcscgtlgvglkkpa 437
Cdd:TIGR00834  161 ---------------------------------------------GDIGSREKSKLKF---------------------- 173
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  438 vdmnfMRKIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLSGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMT 517
Cdd:TIGR00834  174 -----LKKIPEDAEATNVLVGEVDFLEQPALAFVRLKEAVPLEALLEVPVPVRFLFVLLGPSGPGKDYHEIGRAIATLMS 248
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  518 DEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKSVPSQEKRK----IPVFPNGSAaMSVDPPKEDDH 593
Cdd:TIGR00834  249 DEVFHDAAYLADDRDDLLAGIDEFLDCSIVLPPGEWDPEIRLEPPAPLQRELLRKryepSTVRPENPT-MGGDTEPEDGG 327
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  594 HAGP-----ELQRTGRLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESL 668
Cdd:TIGR00834  328 SEGPhgdddPLQRTGRPFGGLIRDIKRRYPHYLSDFTDALNPQCLAAVIFIYFAALSPAITFGGLLGEKTRNMMGVSELL 407
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  669 FGASLTGIAYSLFAGQPLTILGSTGPVLVFEKILFKFCRDYHLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTE 748
Cdd:TIGR00834  408 ISTAVQGVLFALLAAQPLLVVGFSGPLLVFEEAFFSFCESNGLEYLVGRVWIGLWLVLLVLLLVATEGSFLVRYISRFTQ 487
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  749 EAFAALICIIFIYEALEKLfhlgeIYAFNMHNNLDELTSYTCVCAEPSNPSnetlelwkrknitaysVSWGNLTvsECKT 828
Cdd:TIGR00834  488 EIFSFLISLIFIYETFSKL-----IKIFQEHPLQVFYNTLFCVPPKPQGPS----------------VSALLEK--DCSK 544
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  829 FHGMFVGSACGPhgpyVPDVLFWCVVLFFTTFFLSSFLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVAIDYLVG-IPSP 907
Cdd:TIGR00834  545 LGGTLGGNNCRF----QPNTALLSLVLMLGTFFLAMFLRKFKNSRYFPGKARRLIGDFGVPISILIMVLVDIFIGdTYTQ 620
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  908 KLHVPEKFEPTDPS-RGWIISPLGDN---PWWTLLIAAVPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVG 983
Cdd:TIGR00834  621 KLSVPSGLKVTNPSaRGWFIPPLGENrpfPWWMMFAAALPALLVFILIFMEQQITTLIVSKKERKLKKGSGFHLDLLLVV 700
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  984 VMLGVCSIMGLPWFVAATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKFIPMPVLYG 1063
Cdd:TIGR00834  701 GMGGVAALFGLPWLSAATVRSVTHANALTVMSKASAPGEKAQIQEVREQRVTGLLVAVLVGLSILMEPILKRIPLAVLFG 780
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922 1064 VFLYMGVSSLKGIQFFDRIKLFGMPAKHQPDLIYLRYVPLWKVHVFTVVQLTCLVLLWVIKASAAAVVFPMMVLALVFVR 1143
Cdd:TIGR00834  781 IFLYMGVTSLSGIQLFDRLLLLLMPPKYHPDVPYVRRVKTWRMHLFTAIQILCLALLWVVKSTPASLAFPFVLILTVPLR 860
                         1050
                   ....*....|....*..
gi 1039745922 1144 KLMD-LCFTKRELSWLD 1159
Cdd:TIGR00834  861 RLLLpRLFTERELKCLD 877
 
Name Accession Description Interval E-value
ae TIGR00834
anion exchange protein; The Anion Exchanger (AE) Family (TC 2.A.31)Characterized protein ...
118-1159 0e+00

anion exchange protein; The Anion Exchanger (AE) Family (TC 2.A.31)Characterized protein members of the AE family are found only in animals.They preferentially catalyze anion exchange (antiport) reactions, typically acting as HCO3-:Cl- antiporters, but also transporting a range of other inorganic and organic anions. Additionally, renal Na+:HCO3- cotransporters have been found to be members of the AE family. They catalyze the reabsorption of HCO3- in the renal proximal tubule. [Transport and binding proteins, Anions]


Pssm-ID: 273290 [Multi-domain]  Cd Length: 900  Bit Score: 1053.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  118 FTEMDELCYRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLD 197
Cdd:TIGR00834    1 FVELNELMLDRNQEPEWRETARWIKFEEDVEEGGGRWGKPHVATLSFHSLLELRRCFAKGAILLDLAATSLPGVANMVVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  198 NMIASGQLDDSIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKKHSdphllerngeglsasrhslrtglsaSNLSl 277
Cdd:TIGR00834   81 HLIYSGQIRPEDRDEVLRALLLKHSHQSDAKKLGGLSRARSQSSIGKTLS-------------------------HDAS- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  278 rgesplslllshllpssragtpagsrcttpvptpqssppsspdlsrlasrsfQQTQPQAPEVLVSPDRDDIPRVvIHPPe 357
Cdd:TIGR00834  135 ----------------------------------------------------EMPNPDNGAPLLPHQPLTEMQL-LSVP- 160
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  358 ediealkgqeqkneentaftpgilaspqsapgnldnsksgemkgnGSGGSRENSTVDFskesaswhcscgtlgvglkkpa 437
Cdd:TIGR00834  161 ---------------------------------------------GDIGSREKSKLKF---------------------- 173
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  438 vdmnfMRKIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLSGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMT 517
Cdd:TIGR00834  174 -----LKKIPEDAEATNVLVGEVDFLEQPALAFVRLKEAVPLEALLEVPVPVRFLFVLLGPSGPGKDYHEIGRAIATLMS 248
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  518 DEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKSVPSQEKRK----IPVFPNGSAaMSVDPPKEDDH 593
Cdd:TIGR00834  249 DEVFHDAAYLADDRDDLLAGIDEFLDCSIVLPPGEWDPEIRLEPPAPLQRELLRKryepSTVRPENPT-MGGDTEPEDGG 327
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  594 HAGP-----ELQRTGRLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESL 668
Cdd:TIGR00834  328 SEGPhgdddPLQRTGRPFGGLIRDIKRRYPHYLSDFTDALNPQCLAAVIFIYFAALSPAITFGGLLGEKTRNMMGVSELL 407
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  669 FGASLTGIAYSLFAGQPLTILGSTGPVLVFEKILFKFCRDYHLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTE 748
Cdd:TIGR00834  408 ISTAVQGVLFALLAAQPLLVVGFSGPLLVFEEAFFSFCESNGLEYLVGRVWIGLWLVLLVLLLVATEGSFLVRYISRFTQ 487
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  749 EAFAALICIIFIYEALEKLfhlgeIYAFNMHNNLDELTSYTCVCAEPSNPSnetlelwkrknitaysVSWGNLTvsECKT 828
Cdd:TIGR00834  488 EIFSFLISLIFIYETFSKL-----IKIFQEHPLQVFYNTLFCVPPKPQGPS----------------VSALLEK--DCSK 544
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  829 FHGMFVGSACGPhgpyVPDVLFWCVVLFFTTFFLSSFLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVAIDYLVG-IPSP 907
Cdd:TIGR00834  545 LGGTLGGNNCRF----QPNTALLSLVLMLGTFFLAMFLRKFKNSRYFPGKARRLIGDFGVPISILIMVLVDIFIGdTYTQ 620
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  908 KLHVPEKFEPTDPS-RGWIISPLGDN---PWWTLLIAAVPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVG 983
Cdd:TIGR00834  621 KLSVPSGLKVTNPSaRGWFIPPLGENrpfPWWMMFAAALPALLVFILIFMEQQITTLIVSKKERKLKKGSGFHLDLLLVV 700
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  984 VMLGVCSIMGLPWFVAATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKFIPMPVLYG 1063
Cdd:TIGR00834  701 GMGGVAALFGLPWLSAATVRSVTHANALTVMSKASAPGEKAQIQEVREQRVTGLLVAVLVGLSILMEPILKRIPLAVLFG 780
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922 1064 VFLYMGVSSLKGIQFFDRIKLFGMPAKHQPDLIYLRYVPLWKVHVFTVVQLTCLVLLWVIKASAAAVVFPMMVLALVFVR 1143
Cdd:TIGR00834  781 IFLYMGVTSLSGIQLFDRLLLLLMPPKYHPDVPYVRRVKTWRMHLFTAIQILCLALLWVVKSTPASLAFPFVLILTVPLR 860
                         1050
                   ....*....|....*..
gi 1039745922 1144 KLMD-LCFTKRELSWLD 1159
Cdd:TIGR00834  861 RLLLpRLFTERELKCLD 877
HCO3_cotransp pfam00955
HCO3- transporter family; This family contains Band 3 anion exchange proteins that exchange ...
604-1112 0e+00

HCO3- transporter family; This family contains Band 3 anion exchange proteins that exchange CL-/HCO3-. This family also includes cotransporters of Na+/HCO3-.


Pssm-ID: 460009  Cd Length: 497  Bit Score: 885.72  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  604 RLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESLFGASLTGIAYSLFAG 683
Cdd:pfam00955    1 RLFGGLINDIKRRYPHYLSDFTDALNLQCLASIIFLYFACLSPAITFGGLLGDATDGYIGVSESILSQAIGGIIFALFAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  684 QPLTILGSTGPVLVFEKILFKFCRDYHLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTEEAFAALICIIFIYEA 763
Cdd:pfam00955   81 QPLTILGSTGPLLVFEKILFKFCKDNGLDYLSFRAWIGLWLAFFLLLLVAFDASFLVRYITRFTEEIFALLISLIFIYEA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  764 LEKLFHLGEIYAFNMHnnldeltsYTCVCAEPS--NPSNETLELWKRKNITAYSvswGNLTVSECKT-FHGMFVGSACGp 840
Cdd:pfam00955  161 FKKLIKIFKKYPLYLN--------YDCTCVPPSsnNTTNSTLSLSTESSSINWS---SLLTNSECTEsYGGTLVGSGCG- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  841 hgpYVPDVLFWCVVLFFTTFFLSSFLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVAIDYLVGIPSPKLHVPEKFEPTDP 920
Cdd:pfam00955  229 ---YVPDTALLSLILFLGTFWLAYFLKQFKNSPFFPTKVRRLISDFAVPIAILIMVLVDYFLGVYTPKLQVPSGFKPTRP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  921 SRGWIISPLGDNPWWTLLIAAVPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVGVMLGVCSIMGLPWFVAA 1000
Cdd:pfam00955  306 DRGWIINPFGKNPWWLILAAILPALLVTILIFMDQQITAVIVNRKENKLKKGSGYHLDLFVVAILNGICSLFGLPWMVAA 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922 1001 TVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKFIPMPVLYGVFLYMGVSSLKGIQFFD 1080
Cdd:pfam00955  386 TVRSITHVNSLKVESECVAPGEKPKILGVREQRVTGLLVFILIGLSVFMTPVLKLIPMPVLYGVFLYMGVTSLSGIQFFD 465
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1039745922 1081 RIKLFGMPAKHQPDLIYLRYVPLWKVHVFTVV 1112
Cdd:pfam00955  466 RILLLFMPQKHQPDTHYLRHVPLRKVHLFTLI 497
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
458-542 8.55e-04

Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 441368 [Multi-domain]  Cd Length: 150  Bit Score: 40.99  E-value: 8.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  458 GEVDFLERPIIAFVRLAPAVLLSGLTEVPVptRFLFLLLGPAGKAPQYHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSG 537
Cdd:COG1762     68 ARPEGVKKPGIAVARLKEPVDFGAMDGEPV--DLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILEL 145

                   ....*
gi 1039745922  538 IDEFL 542
Cdd:COG1762    146 LKEAE 150
PH_Phafin2-like cd01218
Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; ...
656-707 8.13e-03

Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; Phafin2 is differentially expressed in the liver cancer cell and regulates the structure and function of the endosomes through Rab5-dependent processes. Phafin2 modulates the cell's response to extracellular stimulation by modulating the receptor density on the cell surface. Phafin2 contains a PH domain and a FYVE domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269927 [Multi-domain]  Cd Length: 123  Bit Score: 37.62  E-value: 8.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039745922  656 EATEGRISAIESLFGASltgiayslfaGQPLTIlgsTGPVLVFEKILFKFCR 707
Cdd:cd01218      3 EANRRRIAAVESCFGGS----------GQPLVK---PGRVLVGEGVLTKVCR 41
 
Name Accession Description Interval E-value
ae TIGR00834
anion exchange protein; The Anion Exchanger (AE) Family (TC 2.A.31)Characterized protein ...
118-1159 0e+00

anion exchange protein; The Anion Exchanger (AE) Family (TC 2.A.31)Characterized protein members of the AE family are found only in animals.They preferentially catalyze anion exchange (antiport) reactions, typically acting as HCO3-:Cl- antiporters, but also transporting a range of other inorganic and organic anions. Additionally, renal Na+:HCO3- cotransporters have been found to be members of the AE family. They catalyze the reabsorption of HCO3- in the renal proximal tubule. [Transport and binding proteins, Anions]


Pssm-ID: 273290 [Multi-domain]  Cd Length: 900  Bit Score: 1053.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  118 FTEMDELCYRDGEEYEWKETARWLKFEEDVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLD 197
Cdd:TIGR00834    1 FVELNELMLDRNQEPEWRETARWIKFEEDVEEGGGRWGKPHVATLSFHSLLELRRCFAKGAILLDLAATSLPGVANMVVD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  198 NMIASGQLDDSIRENVREALLKRHHHQNEKRFTSRIPLVRSFADIGKKHSdphllerngeglsasrhslrtglsaSNLSl 277
Cdd:TIGR00834   81 HLIYSGQIRPEDRDEVLRALLLKHSHQSDAKKLGGLSRARSQSSIGKTLS-------------------------HDAS- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  278 rgesplslllshllpssragtpagsrcttpvptpqssppsspdlsrlasrsfQQTQPQAPEVLVSPDRDDIPRVvIHPPe 357
Cdd:TIGR00834  135 ----------------------------------------------------EMPNPDNGAPLLPHQPLTEMQL-LSVP- 160
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  358 ediealkgqeqkneentaftpgilaspqsapgnldnsksgemkgnGSGGSRENSTVDFskesaswhcscgtlgvglkkpa 437
Cdd:TIGR00834  161 ---------------------------------------------GDIGSREKSKLKF---------------------- 173
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  438 vdmnfMRKIPTGAEASNVLVGEVDFLERPIIAFVRLAPAVLLSGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMT 517
Cdd:TIGR00834  174 -----LKKIPEDAEATNVLVGEVDFLEQPALAFVRLKEAVPLEALLEVPVPVRFLFVLLGPSGPGKDYHEIGRAIATLMS 248
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  518 DEIFHDVAYKAKDRNDLLSGIDEFLDQVTVLPPGEWDPSIRIEPPKSVPSQEKRK----IPVFPNGSAaMSVDPPKEDDH 593
Cdd:TIGR00834  249 DEVFHDAAYLADDRDDLLAGIDEFLDCSIVLPPGEWDPEIRLEPPAPLQRELLRKryepSTVRPENPT-MGGDTEPEDGG 327
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  594 HAGP-----ELQRTGRLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESL 668
Cdd:TIGR00834  328 SEGPhgdddPLQRTGRPFGGLIRDIKRRYPHYLSDFTDALNPQCLAAVIFIYFAALSPAITFGGLLGEKTRNMMGVSELL 407
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  669 FGASLTGIAYSLFAGQPLTILGSTGPVLVFEKILFKFCRDYHLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTE 748
Cdd:TIGR00834  408 ISTAVQGVLFALLAAQPLLVVGFSGPLLVFEEAFFSFCESNGLEYLVGRVWIGLWLVLLVLLLVATEGSFLVRYISRFTQ 487
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  749 EAFAALICIIFIYEALEKLfhlgeIYAFNMHNNLDELTSYTCVCAEPSNPSnetlelwkrknitaysVSWGNLTvsECKT 828
Cdd:TIGR00834  488 EIFSFLISLIFIYETFSKL-----IKIFQEHPLQVFYNTLFCVPPKPQGPS----------------VSALLEK--DCSK 544
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  829 FHGMFVGSACGPhgpyVPDVLFWCVVLFFTTFFLSSFLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVAIDYLVG-IPSP 907
Cdd:TIGR00834  545 LGGTLGGNNCRF----QPNTALLSLVLMLGTFFLAMFLRKFKNSRYFPGKARRLIGDFGVPISILIMVLVDIFIGdTYTQ 620
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  908 KLHVPEKFEPTDPS-RGWIISPLGDN---PWWTLLIAAVPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVG 983
Cdd:TIGR00834  621 KLSVPSGLKVTNPSaRGWFIPPLGENrpfPWWMMFAAALPALLVFILIFMEQQITTLIVSKKERKLKKGSGFHLDLLLVV 700
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  984 VMLGVCSIMGLPWFVAATVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKFIPMPVLYG 1063
Cdd:TIGR00834  701 GMGGVAALFGLPWLSAATVRSVTHANALTVMSKASAPGEKAQIQEVREQRVTGLLVAVLVGLSILMEPILKRIPLAVLFG 780
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922 1064 VFLYMGVSSLKGIQFFDRIKLFGMPAKHQPDLIYLRYVPLWKVHVFTVVQLTCLVLLWVIKASAAAVVFPMMVLALVFVR 1143
Cdd:TIGR00834  781 IFLYMGVTSLSGIQLFDRLLLLLMPPKYHPDVPYVRRVKTWRMHLFTAIQILCLALLWVVKSTPASLAFPFVLILTVPLR 860
                         1050
                   ....*....|....*..
gi 1039745922 1144 KLMD-LCFTKRELSWLD 1159
Cdd:TIGR00834  861 RLLLpRLFTERELKCLD 877
HCO3_cotransp pfam00955
HCO3- transporter family; This family contains Band 3 anion exchange proteins that exchange ...
604-1112 0e+00

HCO3- transporter family; This family contains Band 3 anion exchange proteins that exchange CL-/HCO3-. This family also includes cotransporters of Na+/HCO3-.


Pssm-ID: 460009  Cd Length: 497  Bit Score: 885.72  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  604 RLFGGLILDIKRKAPFFLSDFKDALSLQCLASILFLYCACMSPVITFGGLLGEATEGRISAIESLFGASLTGIAYSLFAG 683
Cdd:pfam00955    1 RLFGGLINDIKRRYPHYLSDFTDALNLQCLASIIFLYFACLSPAITFGGLLGDATDGYIGVSESILSQAIGGIIFALFAG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  684 QPLTILGSTGPVLVFEKILFKFCRDYHLSYLSLRTSIGLWTSFLCIVLVATDASSLVCYITRFTEEAFAALICIIFIYEA 763
Cdd:pfam00955   81 QPLTILGSTGPLLVFEKILFKFCKDNGLDYLSFRAWIGLWLAFFLLLLVAFDASFLVRYITRFTEEIFALLISLIFIYEA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  764 LEKLFHLGEIYAFNMHnnldeltsYTCVCAEPS--NPSNETLELWKRKNITAYSvswGNLTVSECKT-FHGMFVGSACGp 840
Cdd:pfam00955  161 FKKLIKIFKKYPLYLN--------YDCTCVPPSsnNTTNSTLSLSTESSSINWS---SLLTNSECTEsYGGTLVGSGCG- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  841 hgpYVPDVLFWCVVLFFTTFFLSSFLKQFKTKRYFPTKVRSTISDFAVFLTIVIMVAIDYLVGIPSPKLHVPEKFEPTDP 920
Cdd:pfam00955  229 ---YVPDTALLSLILFLGTFWLAYFLKQFKNSPFFPTKVRRLISDFAVPIAILIMVLVDYFLGVYTPKLQVPSGFKPTRP 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  921 SRGWIISPLGDNPWWTLLIAAVPALLCTILIFMDQQITAVIINRKEHKLKKGAGYHLDLLMVGVMLGVCSIMGLPWFVAA 1000
Cdd:pfam00955  306 DRGWIINPFGKNPWWLILAAILPALLVTILIFMDQQITAVIVNRKENKLKKGSGYHLDLFVVAILNGICSLFGLPWMVAA 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922 1001 TVLSISHVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSVFMTSVLKFIPMPVLYGVFLYMGVSSLKGIQFFD 1080
Cdd:pfam00955  386 TVRSITHVNSLKVESECVAPGEKPKILGVREQRVTGLLVFILIGLSVFMTPVLKLIPMPVLYGVFLYMGVTSLSGIQFFD 465
                          490       500       510
                   ....*....|....*....|....*....|..
gi 1039745922 1081 RIKLFGMPAKHQPDLIYLRYVPLWKVHVFTVV 1112
Cdd:pfam00955  466 RILLLFMPQKHQPDTHYLRHVPLRKVHLFTLI 497
Band_3_cyto pfam07565
Band 3 cytoplasmic domain; This family contains the cytoplasmic domain of the Band 3 anion ...
146-549 1.92e-109

Band 3 cytoplasmic domain; This family contains the cytoplasmic domain of the Band 3 anion exchange proteins that exchange Cl-/HCO3-. Band 3 constitutes the most abundant polypeptide in the red blood cell membrane, comprising 25% of the total membrane protein. The cytoplasmic domain of band 3 functions primarily as an anchoring site for other membrane-associated proteins. Included among the protein ligands of cdb3 are ankyrin, protein 4.2, protein 4.1, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), phosphofructokinase, aldolase, hemoglobin, hemichromes, and the protein tyrosine kinase (p72syk).


Pssm-ID: 429542  Cd Length: 255  Bit Score: 343.55  E-value: 1.92e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  146 DVEDGGDRWSKPYVATLSLHSLFELRSCILNGTVMLDMRASTLDEIADMVLDNMIASGQLDDSIRENVREALLKRHHHQN 225
Cdd:pfam07565    1 DVEEEGGRWGKPHVATLSFHSLLELRRCLAKGTVLLDLEATSLPGVAHLVLDQMIYSGQIRPEDREEVLRALLLKHSHQN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  226 E-KRFTSRIPLVRSFADIGKKHSDPHllerngeglsasrhslrtglsasnlslrgesplslllshllpssragtpagsrc 304
Cdd:pfam07565   81 ElKELGGVKPAVRSLSSIGSSLSHGH------------------------------------------------------ 106
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  305 ttpvptpqssppsspdlsrlasrsfqqtqpqapevlvspdrddiprvviHPPEEDIealkgqeqkneentaftpgilasP 384
Cdd:pfam07565  107 -------------------------------------------------DDSKPLL-----------------------P 114
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  385 QSAPGNLDNSKSGEMKGNgsggSRENSTVDFSKesaswhcscgtlgvglkkpaVDMNFMRKIPTGAEASNVLVGEVDFLE 464
Cdd:pfam07565  115 QQSSLEGGLLCEQGEGPN----SDEQLTVSESK--------------------SPLHFLKKIPEDAEATNVLVGEVDFLE 170
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  465 RPIIAFVRLAPAVLLSGLTEVPVPTRFLFLLLGPAGKAPQYHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSGIDEFLDQ 544
Cdd:pfam07565  171 RPVLAFVRLKEAVPLEGVTEVPVPVRFLFILLGPSGPGLDYHEIGRAIATLMSDEVFHDVAYKADDREDLLAGIDEFLDC 250

                   ....*
gi 1039745922  545 VTVLP 549
Cdd:pfam07565  251 SIVLP 255
PtsN COG1762
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ...
458-542 8.55e-04

Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 441368 [Multi-domain]  Cd Length: 150  Bit Score: 40.99  E-value: 8.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039745922  458 GEVDFLERPIIAFVRLAPAVLLSGLTEVPVptRFLFLLLGPAGKAPQYHEIGRSIATLMTDEIFHDVAYKAKDRNDLLSG 537
Cdd:COG1762     68 ARPEGVKKPGIAVARLKEPVDFGAMDGEPV--DLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILEL 145

                   ....*
gi 1039745922  538 IDEFL 542
Cdd:COG1762    146 LKEAE 150
PH_Phafin2-like cd01218
Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; ...
656-707 8.13e-03

Phafin2 (also called EAPF, FLJ13187, ZFYVE18 or PLEKHF2) Pleckstrin Homology (PH) domain; Phafin2 is differentially expressed in the liver cancer cell and regulates the structure and function of the endosomes through Rab5-dependent processes. Phafin2 modulates the cell's response to extracellular stimulation by modulating the receptor density on the cell surface. Phafin2 contains a PH domain and a FYVE domain. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269927 [Multi-domain]  Cd Length: 123  Bit Score: 37.62  E-value: 8.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039745922  656 EATEGRISAIESLFGASltgiayslfaGQPLTIlgsTGPVLVFEKILFKFCR 707
Cdd:cd01218      3 EANRRRIAAVESCFGGS----------GQPLVK---PGRVLVGEGVLTKVCR 41
 
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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