NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|565472768|ref|XP_006294186|]
View 

putative E3 ubiquitin-protein ligase XBAT31 [Capsella rubella]

Protein Classification

ankyrin repeat domain-containing RING finger protein( domain architecture ID 18454366)

ankyrin (ANK) repeat domain-containing RING finger protein may be involved in mediating protein-protein interactions, and may function as an E3 ubiquitin-protein ligase that mediates through its RING domain the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin; similar to Arabidopsis thaliana E3 ubiquitin-protein ligase XBAT31

CATH:  3.30.40.10|1.25.40.20
EC:  2.3.2.27
Gene Ontology:  GO:0008270|GO:0016567|GO:0004842|GO:0005515
PubMed:  19489725|11007473|14731966|8108379
SCOP:  3000160|4000366

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RING-HC_XBAT31-like cd23144
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and ...
 313-377 4.49e-36

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and similar proteins; XBAT31, also called ankyrin repeat domain and RING finger-containing protein XBAT31, or RING-type E3 ubiquitin transferase XB31, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. XBAT31 contains a typical C3HC4-type RING-HC finger.


:

Pssm-ID: 438506  Cd Length: 65  Bit Score: 127.36  E-value: 4.49e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565472768 313 SEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIARLV 377
Cdd:cd23144    1 SSISDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPNPSSSPPRPPACPFCRQDIASLV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-292 1.94e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 1.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  37 LLNQTTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANILMFDSvNRRTC 116
Cdd:COG0666   45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 117 LHYAAYYGHANCVQAILSA-AQsspvavhwgyarfVNIRDDKGATPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPG 195
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAgAD-------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAG----ADVNARDNDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 196 STPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALLNPSSAEPLVWPSPLKFISELDDEAKLLL 275
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                        250
                 ....*....|....*..
gi 565472768 276 EQALMEANREREKTILK 292
Cdd:COG0666  267 IVKLLLLALLLLAAALL 283
 
Name Accession Description Interval E-value
RING-HC_XBAT31-like cd23144
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and ...
 313-377 4.49e-36

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and similar proteins; XBAT31, also called ankyrin repeat domain and RING finger-containing protein XBAT31, or RING-type E3 ubiquitin transferase XB31, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. XBAT31 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438506  Cd Length: 65  Bit Score: 127.36  E-value: 4.49e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565472768 313 SEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIARLV 377
Cdd:cd23144    1 SSISDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPNPSSSPPRPPACPFCRQDIASLV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-292 1.94e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 1.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  37 LLNQTTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANILMFDSvNRRTC 116
Cdd:COG0666   45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 117 LHYAAYYGHANCVQAILSA-AQsspvavhwgyarfVNIRDDKGATPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPG 195
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAgAD-------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAG----ADVNARDNDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 196 STPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALLNPSSAEPLVWPSPLKFISELDDEAKLLL 275
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                        250
                 ....*....|....*..
gi 565472768 276 EQALMEANREREKTILK 292
Cdd:COG0666  267 IVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-134 5.66e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 5.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   50 LHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVgANILMFDsvNRRTCLHYAAYYGHANCV 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHLEIV 77


                  ....*
gi 565472768  130 QAILS 134
Cdd:pfam12796  78 KLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-251 3.20e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  22 GDIVTVRRVMTTEPSLLNQTTSyDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEV 101
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVD-ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 102 GAN--ILMFDSVNR--------------------RTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGA 159
Cdd:PHA02874  91 GVDtsILPIPCIEKdmiktildcgidvnikdaelKTFLHYAIKKGDLESIKMLFE------------YGADVNIEDDNGC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 160 TPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHK 239
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKG----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                        250
                 ....*....|..
gi 565472768 240 HGACGALLNPSS 251
Cdd:PHA02874 235 RSAIELLINNAS 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-228 6.10e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  77 RHKQTPLMLAAMYGRISCVKKLtevganiLMFDSVNR-------RTCLHYAAYYGHANCVQAILSAAqssPVAVhwgyar 149
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKKL-------LKCPSCDLfqrgalgETALHVAALYDNLEAAVVLMEAA---PELV------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 150 FVNIRDD--KGATPLHLASRQRRPECVNVLLDSGSLVCA--ATSVYGSPGST--------PLHLAARSGSIDCVRKLLAW 217
Cdd:cd22192   79 NEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSprATGTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEH 158

                        170
                 ....*....|.
gi 565472768 218 GADRLQRDSSG 228
Cdd:cd22192  159 GADIRAQDSLG 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 195-220 5.07e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 5.07e-05
                           10        20
                   ....*....|....*....|....*.
gi 565472768   195 GSTPLHLAARSGSIDCVRKLLAWGAD 220
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-228 1.16e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768    1 MGQSLSCGtrpEHGIFASVQCGDIVTVRRvMTTEPSLLNQ--TTSYDRHSVLHVAAANGQIEILSLLLERftnpdllnrh 78
Cdd:TIGR00870  10 EESPLSDE---EKAFLPAAERGDLASVYR-DLEEPKKLNIncPDRLGRSALFVAAIENENLELTELLLNL---------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   79 kqtplmlaamygriscvKKLTEVGanilmfdsvnrRTCLHYAA--YYGHANCVQAILSAAQSSPVAVHWGYARFVNiRDD 156
Cdd:TIGR00870  76 -----------------SCRGAVG-----------DTLLHAISleYVDAVEAILLHLLAAFRKSGPLELANDQYTS-EFT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  157 KGATPLHLASRQRRPECVNVLLDSGSLV--------CAATSVYGS--PGSTPLHLAARSGSIDCVRKLLAWGADRLQRDS 226
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVparacgdfFVKSQGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206


                  ..
gi 565472768  227 SG 228
Cdd:TIGR00870 207 LG 208
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
317-373 4.06e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 38.13  E-value: 4.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768  317 DTELCCICFEQVCTIEVKDCGHQ-MCAQCTLALCCHNKpnpttstvtppVCPFCRSTI 373
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLRKKK-----------KCPICRQPI 47
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
306-372 5.10e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 42.32  E-value: 5.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768 306 TASDDNMSEvsDTELCCICFEQVCTIEVKDCGHQMCAQCTLAL-CCHNKPNpttstvtppvCPFCRST 372
Cdd:COG5236   51 TSSADDTDE--ENMNCQICAGSTTYSARYPCGHQICHACAVRLrALYMQKG----------CPLCRTE 106
 
Name Accession Description Interval E-value
RING-HC_XBAT31-like cd23144
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and ...
 313-377 4.49e-36

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 1 (XBAT31) and similar proteins; XBAT31, also called ankyrin repeat domain and RING finger-containing protein XBAT31, or RING-type E3 ubiquitin transferase XB31, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. XBAT31 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438506  Cd Length: 65  Bit Score: 127.36  E-value: 4.49e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 565472768 313 SEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIARLV 377
Cdd:cd23144    1 SSISDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPNPSSSPPRPPACPFCRQDIASLV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-292 1.94e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 1.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  37 LLNQTTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANILMFDSvNRRTC 116
Cdd:COG0666   45 LALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETP 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 117 LHYAAYYGHANCVQAILSA-AQsspvavhwgyarfVNIRDDKGATPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPG 195
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAgAD-------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAG----ADVNARDNDG 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 196 STPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALLNPSSAEPLVWPSPLKFISELDDEAKLLL 275
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                        250
                 ....*....|....*..
gi 565472768 276 EQALMEANREREKTILK 292
Cdd:COG0666  267 IVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-225 2.74e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 2.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  15 IFASVQCGDIVTVRRvmttepsLLNQ-----TTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMY 89
Cdd:COG0666   91 LHAAARNGDLEIVKL-------LLEAgadvnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  90 GRISCVKKLTEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSA-AQsspvavhwgyarfVNIRDDKGATPLHLASRQ 168
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAgAD-------------VNAKDNDGKTALDLAAEN 229

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 565472768 169 RRPECVNVLLDSGSLVCAATsvygSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRD 225
Cdd:COG0666  230 GNLEIVKLLLEAGADLNAKD----KDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-134 5.66e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 5.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   50 LHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVgANILMFDsvNRRTCLHYAAYYGHANCV 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHLEIV 77


                  ....*
gi 565472768  130 QAILS 134
Cdd:pfam12796  78 KLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-181 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   83 LMLAAMYGRISCVKKLTEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSAAQsspvavhwgyarfVNIRDDkGATPL 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD-------------VNLKDN-GRTAL 65

                          90
                  ....*....|....*....
gi 565472768  163 HLASRQRRPECVNVLLDSG 181
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-220 9.38e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 9.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  117 LHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLHLASRQRRPECVNVLLDSGSLVCAatsvygSPGS 196
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------------ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK------DNGR 62

                          90       100
                  ....*....|....*....|....
gi 565472768  197 TPLHLAARSGSIDCVRKLLAWGAD 220
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-109 1.37e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   15 IFASVQCGDIVTVRRVMT--TEPSLLNQttsyDRHSVLHVAAANGQIEILSLLLERFtNPDLLNrHKQTPLMLAAMYGRI 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEngADANLQDK----NGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 565472768   93 SCVKKLTEVGANILMFD 109
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-251 3.20e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  22 GDIVTVRRVMTTEPSLLNQTTSyDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEV 101
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVD-ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 102 GAN--ILMFDSVNR--------------------RTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGA 159
Cdd:PHA02874  91 GVDtsILPIPCIEKdmiktildcgidvnikdaelKTFLHYAIKKGDLESIKMLFE------------YGADVNIEDDNGC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 160 TPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHK 239
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKG----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                        250
                 ....*....|..
gi 565472768 240 HGACGALLNPSS 251
Cdd:PHA02874 235 RSAIELLINNAS 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-254 8.22e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 8.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  53 AAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGAnILMFDSVNRRTCLHYAAYYGHANCVQAI 132
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 133 LSAAQsspvavhwgYARFVNIRDdkGATPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPGSTPLHLAARSGSIDCVR 212
Cdd:PHA02875  88 LDLGK---------FADDVFYKD--GMTPLHLATILKKLDIMKLLIARG----ADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 565472768 213 KLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALLNPSSAEP 254
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-220 1.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  59 IEILSLLLERFTNPDLLNRHKQTPLMLAAMY--GRISCVKKLTEVGANILMFDSVNRrTCLHYAAYYGH----------- 125
Cdd:PHA03100  86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKidlkilkllid 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 126 -------ANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLASRQRRPECVNVLLDSGSLVcAATSVYgspGSTP 198
Cdd:PHA03100 165 kgvdinaKNRVNYLLS------------YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP-NLVNKY---GDTP 228

                        170       180
                 ....*....|....*....|..
gi 565472768 199 LHLAARSGSIDCVRKLLAWGAD 220
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-247 5.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 5.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  37 LLNQTTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYG-RISCVKK----LTEVGANILMFDSv 111
Cdd:PHA03100  26 DLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKyNLTDVKEivklLLEYGANVNAPDN- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 112 NRRTCLHYAAYY--GHANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLASRQRRP--ECVNVLLDSGSLVCAA 187
Cdd:PHA03100 105 NGITPLLYAISKksNSYSIVEYLLD------------NGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAK 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 565472768 188 TSV-----YGSP-------GSTPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALL 247
Cdd:PHA03100 173 NRVnyllsYGVPinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 18-220 1.30e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  18 SVQCGDIVTVRRVMTTEpSLLNQTTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKK 97
Cdd:PHA02875  75 AVEEGDVKAVEELLDLG-KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIEL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  98 LtevganilmfdsVNRRTCLhyaayyghancvqailsaaqsspvavhwgyarfvNIRDDKGATPLHLASRQRRPECVNVL 177
Cdd:PHA02875 154 L------------IDHKACL----------------------------------DIEDCCGCTPLIIAMAKGDIAICKML 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 565472768 178 LDSGslvcAATSVYG-SPGSTPLHLAARSGSIDCVRKLLAWGAD 220
Cdd:PHA02875 188 LDSG----ANIDYFGkNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 23-247 1.41e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  23 DIVTVRRVMTTEPSLlNQTTSYDR---HSVLHVAAANGQiEILSLLLERFTNPDLLNRHKQTPLMLAAMYG-RISCVKKL 98
Cdd:PHA03095  26 TVEEVRRLLAAGADV-NFRGEYGKtplHLYLHYSSEKVK-DIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  99 TEVGANILMFDsVNRRTCLHyaAYYG----HANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLH--LASRQRRPE 172
Cdd:PHA03095 104 IKAGADVNAKD-KVGRTPLH--VYLSgfniNPKVIRLLLRKGAD------------VNALDLYGMTPLAvlLKSRNANVE 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768 173 CVNVLLDSGSLVCAATSVygspGSTPLHLAARS--GSIDCVRKLLAWGADRLQRDSSGRIP-YVVAMkhkHGACGALL 247
Cdd:PHA03095 169 LLRLLIDAGADVYAVDDR----FRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPlHSMAT---GSSCKRSL 239
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-98 1.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 565472768   46 RHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKL 98
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-243 4.38e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  49 VLHVAAANGQI--EILSLLLERFTNPDLLNRHKQTPLmlaAMYGR-----ISCVKKLTEVGANILMFDsVNRRTCLHYAA 121
Cdd:PHA03095 120 PLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPL---AVLLKsrnanVELLRLLIDAGADVYAVD-DRFRSLLHHHL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 122 YYGHAN-CVQAILSAAQSSPVAvhwgyarfvniRDDKGATPLHLA---SRQRRPECVNVLLDSGSLvcAATSVYGSpgsT 197
Cdd:PHA03095 196 QSFKPRaRIVRELIRAGCDPAA-----------TDMLGNTPLHSMatgSSCKRSLVLPLLIAGISI--NARNRYGQ---T 259

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 565472768 198 PLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGAC 243
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-238 4.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 4.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  50 LHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANILmfdsvnrrtclhyaayyghancv 129
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM----------------------- 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 130 qailsaaqsspvavhwgyarfvnIRDDKGATPLHLASRQRRpECVNVLLDSGSLvcaatSVYGSPGSTPLHLAAR-SGSI 208
Cdd:PHA02874 218 -----------------------NKCKNGFTPLHNAIIHNR-SAIELLINNASI-----NDQDIDGSTPLHHAINpPCDI 268

                        170       180       190
                 ....*....|....*....|....*....|
gi 565472768 209 DCVRKLLAWGADRLQRDSSGRIPYVVAMKH 238
Cdd:PHA02874 269 DIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-181 4.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 4.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  23 DIVTVRRVMTTEPSLLNQTTSYDRHSvLHVAAAN--GQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRI--SCVKKL 98
Cdd:PHA03100  84 DVKEIVKLLLEYGANVNAPDNNGITP-LLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLL 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  99 TEVGANILMFDSVNR---------------RTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLH 163
Cdd:PHA03100 163 IDKGVDINAKNRVNYllsygvpinikdvygFTPLHYAVYNNNPEFVKYLLD------------LGANPNLVNKYGDTPLH 230

                        170
                 ....*....|....*...
gi 565472768 164 LASRQRRPECVNVLLDSG 181
Cdd:PHA03100 231 IAILNNNKEIFKLLLNNG 248
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 45-247 6.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 6.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  45 DRH---SVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANIlmfdsvnrrtclhyaa 121
Cdd:PHA02878 164 DRHkgnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST---------------- 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 122 yyghancvqailsaaqsspvavhwgyarfvNIRDDKGATPLHLA-SRQRRPECVNVLLDSGSLVCAATSVYgspGSTPLH 200
Cdd:PHA02878 228 ------------------------------DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIL---GLTALH 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 565472768 201 LAARSGsiDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHG-ACGALL 247
Cdd:PHA02878 275 SSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRIL 320
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-220 1.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  95 VKKLTEVGANILMFDSVNRRTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLASRQRRPECV 174
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLS------------YGANVNIPDKTNNSPLHHAVKHYNKPIV 217

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 565472768 175 NVLLDSGslvcAATSVYGSPGSTPLHLA-ARSGSIDCVRKLLAWGAD 220
Cdd:PHA02878 218 HILLENG----ASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVD 260
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-130 1.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 565472768   81 TPLMLAAMYGRISCVKKLTEVGANILMFDSvNRRTCLHYAAYYGHANCVQ 130
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLK 51
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-228 6.10e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  77 RHKQTPLMLAAMYGRISCVKKLtevganiLMFDSVNR-------RTCLHYAAYYGHANCVQAILSAAqssPVAVhwgyar 149
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKKL-------LKCPSCDLfqrgalgETALHVAALYDNLEAAVVLMEAA---PELV------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 150 FVNIRDD--KGATPLHLASRQRRPECVNVLLDSGSLVCA--ATSVYGSPGST--------PLHLAARSGSIDCVRKLLAW 217
Cdd:cd22192   79 NEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSprATGTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEH 158

                        170
                 ....*....|.
gi 565472768 218 GADRLQRDSSG 228
Cdd:cd22192  159 GADIRAQDSLG 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
151-202 2.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 565472768  151 VNIRDDKGATPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPGSTPLHLA 202
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYG----VDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 114-228 2.25e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.80  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 114 RTCLHYAAYYGHANCVQAILSAAQSSPVAVHWGYARFVNIRDD--KGATPLHLASRQRRPECVNVLLDSGSLVCAA---T 188
Cdd:cd21882   27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARatgR 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 565472768 189 SVYGSP------GSTPLHLAARSGSIDCVRKLLAWGAD---RLQRDSSG 228
Cdd:cd21882  107 FFRKSPgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLG 155
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 83-240 3.06e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  83 LMLAAMYGRISCVKKLTEVGANILMFDSVNRrTCLHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPL 162
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACN------------VHIRDANGNTAL 595

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768 163 HLASRQRRPECVNVLLDsgslvCAATSVYGSPGSTpLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKH 240
Cdd:PLN03192 596 WNAISAKHHKIFRILYH-----FASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 195-225 3.13e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 3.13e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 565472768  195 GSTPLHLAA-RSGSIDCVRKLLAWGADRLQRD 225
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-178 4.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 565472768  113 RRTCLHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLHLASRQRRPECVNVLL 178
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD------------INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 195-220 5.07e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 5.07e-05
                           10        20
                   ....*....|....*....|....*.
gi 565472768   195 GSTPLHLAARSGSIDCVRKLLAWGAD 220
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 48-208 5.58e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  48 SVLHVAAANGQIEILSLLLErfTNPDLLNR-------HKQTPLMLAAMYGRISCVKKLTEVGAnilmfDSVNRRTC---- 116
Cdd:cd22192   53 TALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARGA-----DVVSPRATgtff 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 117 --------------LHYAAYYGHANCVQAILSAAqSSPVAvhwgyarfvniRDDKGATPLHL----ASRQRRPECVNVLL 178
Cdd:cd22192  126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHG-ADIRA-----------QDSLGNTVLHIlvlqPNKTFACQMYDLIL 193

                        170       180       190
                 ....*....|....*....|....*....|...
gi 565472768 179 DS---GSLVCAATsVYGSPGSTPLHLAARSGSI 208
Cdd:cd22192  194 SYdkeDDLQPLDL-VPNNQGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-228 1.16e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768    1 MGQSLSCGtrpEHGIFASVQCGDIVTVRRvMTTEPSLLNQ--TTSYDRHSVLHVAAANGQIEILSLLLERftnpdllnrh 78
Cdd:TIGR00870  10 EESPLSDE---EKAFLPAAERGDLASVYR-DLEEPKKLNIncPDRLGRSALFVAAIENENLELTELLLNL---------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   79 kqtplmlaamygriscvKKLTEVGanilmfdsvnrRTCLHYAA--YYGHANCVQAILSAAQSSPVAVHWGYARFVNiRDD 156
Cdd:TIGR00870  76 -----------------SCRGAVG-----------DTLLHAISleYVDAVEAILLHLLAAFRKSGPLELANDQYTS-EFT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  157 KGATPLHLASRQRRPECVNVLLDSGSLV--------CAATSVYGS--PGSTPLHLAARSGSIDCVRKLLAWGADRLQRDS 226
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVparacgdfFVKSQGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206


                  ..
gi 565472768  227 SG 228
Cdd:TIGR00870 207 LG 208
Ank_5 pfam13857
Ankyrin repeats (many copies);
195-235 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 565472768  195 GSTPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVA 235
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-226 1.29e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  58 QIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGA--NILMFDSVnrrTCLHYAAYYGHANCVQAIL-- 133
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDL---SVLECAVDSKNIDTIKAIIdn 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 134 -----------------SAAQSSPVAVHWGYArfVNIRDDKGATPLHLASRQRR-PECVNVLLDSGSLVCAATsvygSPG 195
Cdd:PHA02876 234 rsninkndlsllkairnEDLETSLLLYDAGFS--VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKN----IKG 307

                        170       180       190
                 ....*....|....*....|....*....|..
gi 565472768 196 STPLHLAARSG-SIDCVRKLLAWGADRLQRDS 226
Cdd:PHA02876 308 ETPLYLMAKNGyDTENIRTLIMLGADVNAADR 339
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 22-98 1.69e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 1.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 565472768  22 GDIVTVRRVMTTEPSllNQTTSYDRHSVLHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKL 98
Cdd:PTZ00322  93 GDAVGARILLTGGAD--PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
160-215 2.68e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 565472768  160 TPLHLASRQRRPECVNVLLDSGSLVCAATSVygspGSTPLHLAARSGSIDCVRKLL 215
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN----GETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-120 3.42e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 3.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 565472768   65 LLERFT-NPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANILMFDSvNRRTCLHYA 120
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
317-373 4.06e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 38.13  E-value: 4.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768  317 DTELCCICFEQVCTIEVKDCGHQ-MCAQCTLALCCHNKpnpttstvtppVCPFCRSTI 373
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLRKKK-----------KCPICRQPI 47
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 195-220 4.53e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 4.53e-04
                          10        20
                  ....*....|....*....|....*.
gi 565472768  195 GSTPLHLAARSGSIDCVRKLLAWGAD 220
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
306-372 5.10e-04

Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 42.32  E-value: 5.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768 306 TASDDNMSEvsDTELCCICFEQVCTIEVKDCGHQMCAQCTLAL-CCHNKPNpttstvtppvCPFCRST 372
Cdd:COG5236   51 TSSADDTDE--ENMNCQICAGSTTYSARYPCGHQICHACAVRLrALYMQKG----------CPLCRTE 106
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 152-215 5.92e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 5.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565472768 152 NIRDDKGATPLHLASRQRRPECVNVLLDSGslvcAATSVYGSPGSTPLHLAARSGSIDCVRKLL 215
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFG----ADPTLLDKDGKTPLELAEENGFREVVQLLS 168
RING-HC_Cbl-like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
 319-370 7.95e-04

RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor protein family contains a small class of RING-type E3 ubiquitin ligases with oncogenic activity, which is represented by three mammalian members, c-Cbl, Cbl-b and Cbl-c, as well as two invertebrate Cbl-family proteins, D-Cbl in Drosophila and Sli-1 in C. elegans. Cbl proteins function as potent negative regulators of various signaling cascades in a wide range of cell types. They play roles in ubiquitinating activated tyrosine kinases and targeting them for degradation. D-Cbl associates with the Drosophila epidermal growth factor receptor (EGFR) and overexpression of D-Cbl in the eye of Drosophila embryos inhibits EGFR-dependent photoreceptor cell development. Sli-1 is a negative regulator of the Let-23 receptor tyrosine kinase, an EGFR homolog, in vulva development. Cbl proteins in this subfamily consist of a highly conserved N-terminal half that includes a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain) and a C3HC4-type RING-HC finger, both of which are required for Cbl-mediated downregulation of RTKs, and a divergent C-terminal region.


Pssm-ID: 438165 [Multi-domain]  Cd Length: 43  Bit Score: 36.94  E-value: 7.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 565472768 319 ELCCICFEQVCTIEVKDCGHQMCAQCTLALccHNKPNPTtstvtppvCPFCR 370
Cdd:cd16502    2 QLCKICAENDKDVRIEPCGHLLCTPCLTSW--QDSDGQT--------CPFCR 43
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 54-137 1.05e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  54 AANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANILMFDSvNRRTCLHYAAYYGHANCVQAIL 133
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVVQLLS 168


                 ....
gi 565472768 134 SAAQ 137
Cdd:PTZ00322 169 RHSQ 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 84-248 1.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  84 MLAAMYG--------RISCVKKLTEVGANIlMFDSVNRRTCLHYAAYYGHANC---VQAILSAAQsspvavhwgyarFVN 152
Cdd:PHA03095  11 MEAALYDyllnasnvTVEEVRRLLAAGADV-NFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGA------------DVN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 153 IRDDKGATPLHL-ASRQRRPECVNVLLDSGslvcAATSVYGSPGSTPLHLAARSGSID--CVRKLLAWGADRLQRDSSGR 229
Cdd:PHA03095  78 APERCGFTPLHLyLYNATTLDVIKLLIKAG----ADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGM 153

                        170
                 ....*....|....*....
gi 565472768 230 IPYVVAMKhKHGACGALLN 248
Cdd:PHA03095 154 TPLAVLLK-SRNANVELLR 171
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
 316-373 1.50e-03

RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; Cbl-c, also known as RING finger protein 57 (RNF57), SH3-binding protein Cbl-3, SH3-binding protein Cbl-c, or signal transduction protein Cbl-c, is an E3 ubiquitin-protein ligase expressed exclusively in epithelial cells. It contains a tyrosine-kinase-binding domain (TKB, also known as the phosphotyrosine binding PTB domain, composed of a four helix-bundle, a Ca2+ binding EF-hand and a highly variant SH2 domain), a C3HC4-type RING-HC finger, and a short proline-rich region, but lacks the ubiquitin-associated (UBA) leucine zipper motif that are present in Cbl and Cbl-b. Cbl-c acts as a regulator of epidermal growth factor receptor (EGFR)-mediated signal transduction. It also suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Moreover, Cbl-c ubiquitinates and downregulates RETMEN2A and implicates Enigma (PDLIM7) as a positive regulator of RETMEN2A by blocking Cbl-mediated ubiquitination and degradation. The ubiquitin ligase activity of Cbl-c is increased via the interaction of its RING-HC finger domain with a LIM domain of the paxillin homolog, hydrogen peroxide induced construct 5 (Hic-5).


Pssm-ID: 438370 [Multi-domain]  Cd Length: 65  Bit Score: 36.99  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 565472768 316 SDTELCCICFEQVCTIEVKDCGHQMCAqCTLALCCHNKPNpttstvtppVCPFCRSTI 373
Cdd:cd16710   11 STFELCKICAERDKDVRIEPCGHLLCS-CCLAAWQHSDSQ---------TCPFCRCEI 58
Ank_5 pfam13857
Ankyrin repeats (many copies);
113-165 1.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 565472768  113 RRTCLHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLHLA 165
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVD------------LNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 174-247 1.98e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 1.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 565472768 174 VNVLLDSGslvcAATSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALL 247
Cdd:PTZ00322  98 ARILLTGG----ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-105 2.23e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.23e-03
                           10        20
                   ....*....|....*....|....*...
gi 565472768    78 HKQTPLMLAAMYGRISCVKKLTEVGANI 105
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
199-247 2.32e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.02  E-value: 2.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 565472768  199 LHLAARSGSIDCVRKLLAWGADRLQRDSSGRIPYVVAMKHKHGACGALL 247
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 112-135 2.60e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 2.60e-03
                           10        20
                   ....*....|....*....|....
gi 565472768   112 NRRTCLHYAAYYGHANCVQAILSA 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
 319-373 2.73e-03

RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) and similar proteins; RSPRY1 is a hypothetical RING and SPRY domain-containing protein of unknown physiological function. Mutations in its corresponding gene RSPRY1 may associate with a distinct skeletal dysplasia syndrome. RSPRY1 contains a B30.2/SPRY domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438228 [Multi-domain]  Cd Length: 43  Bit Score: 35.41  E-value: 2.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 565472768 319 ELCCICFEQVCTIEVKDCGHQ-MCAQCTLALCChnkpnpttstvtppvCPFCRSTI 373
Cdd:cd16566    3 DSCTLCFDKVADTELRPCGHSgFCMECALQLET---------------CPLCRQPI 43
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 50-231 3.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  50 LHVAAANGQIEILSLLLERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLTEVGANI--------------------LMFD 109
Cdd:PHA02876 182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNInkndlsllkairnedletslLLYD 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768 110 ---SVN-----RRTCLHYAayyghancVQAIlSAAQSSPVAVHWGYArfVNIRDDKGATPLHLASRQ-RRPECVNVLLDS 180
Cdd:PHA02876 262 agfSVNsiddcKNTPLHHA--------SQAP-SLSRLVPKLLERGAD--VNAKNIKGETPLYLMAKNgYDTENIRTLIML 330

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 565472768 181 GSLVCAATSVYgspgSTPLHLAAR-SGSIDCVRKLLAWGADRLQRDSSGRIP 231
Cdd:PHA02876 331 GADVNAADRLY----ITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378
zf-RING_2 pfam13639
Ring finger domain;
321-370 3.53e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 35.46  E-value: 3.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 565472768  321 CCICFEQVCT---IEVKDCGHQMCAQCTLALCCHNkpnpttstvtpPVCPFCR 370
Cdd:pfam13639   3 CPICLEEFEEgdkVVVLPCGHHFHRECLDKWLRSS-----------NTCPLCR 44
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 319-369 4.15e-03

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 35.15  E-value: 4.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 565472768 319 ELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNpttstvtppvCPFC 369
Cdd:cd16449    1 LECPICLERLKDPVLLPCGHVFCRECIRRLLESGSIK----------CPIC 41
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-216 5.11e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768   50 LHVAAAN---GQIEILSLLLERF---TNPDLLN-------RHKQTPLMLAAMYGRISCVKKLTEVGANILMFDSVN--RR 114
Cdd:TIGR00870  86 LHAISLEyvdAVEAILLHLLAAFrksGPLELANdqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffVK 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 565472768  115 TCLHYAAYYGhancvQAILSAA----QSSPVAVHWGYARFVNIRDDKGATPLHLASRQR--RPE-------CVNVLLDSG 181
Cdd:TIGR00870 166 SQGVDSFYHG-----ESPLNAAaclgSPSIVALLSEDPADILTADSLGNTLLHLLVMENefKAEyeelscqMYNFALSLL 240

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 565472768  182 SLVCAATSVYGSP---GSTPLHLAARSGSIDCVRKLLA 216
Cdd:TIGR00870 241 DKLRDSKELEVILnhqGLTPLKLAAKEGRIVLFRLKLA 278
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
 319-378 5.35e-03

RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ZNF598 associates with eukaryotic initiation factor 4E (eIF4E) homologous protein from mammals (m4EHP) by binding to Grb10-interacting GYF protein 2 (GIGYF2). The m4EHP-GIGYF2 complex functions as a translational repressor and is essential for normal embryonic development of mammalian. ZNF598 harbors a C3HC4-type RING-HC finger at its N-terminus.


Pssm-ID: 438277 [Multi-domain]  Cd Length: 51  Bit Score: 34.90  E-value: 5.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 565472768 319 ELCCICFEQVCTIEVKDCGHQMCAQCTL---ALCCHNKpnpttstvtppvCPFCRSTIARLVV 378
Cdd:cd16615    1 ETCVICCEEIEYFAVGPCNHPVCYKCSLrmrVLYKDKY------------CPICRTELDKVIF 51
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-107 5.90e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 5.90e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 565472768   78 HKQTPLMLAAMYGRISCVKKLTEVGANILM 107
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH