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Conserved domains on  [gi|330253086|gb|AEC08180|]
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hypothetical protein AT2G28840 [Arabidopsis thaliana]

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

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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 ...
 297-361 2.63e-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: 127.74  E-value: 2.63e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253086 297 SEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIACLV 361
Cdd:cd23144    1 SSISDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPNPSSSPPRPPACPFCRQDIASLV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-233 3.45e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 3.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSA-AQsspvavhwgyar 135
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD------------ 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 136 fVNIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGR 215
Cdd:COG0666  146 -VNAQDNDGNTPLHLAAANGNLEIVKLLLEAG----ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220

                        170
                 ....*....|....*...
gi 330253086 216 IPYVVAMKHKHGACGALL 233
Cdd:COG0666  221 TALDLAAENGNLEIVKLL 238
 
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 ...
 297-361 2.63e-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: 127.74  E-value: 2.63e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253086 297 SEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIACLV 361
Cdd:cd23144    1 SSISDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPNPSSSPPRPPACPFCRQDIASLV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-233 3.45e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 3.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSA-AQsspvavhwgyar 135
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD------------ 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 136 fVNIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGR 215
Cdd:COG0666  146 -VNAQDNDGNTPLHLAAANGNLEIVKLLLEAG----ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220

                        170
                 ....*....|....*...
gi 330253086 216 IPYVVAMKHKHGACGALL 233
Cdd:COG0666  221 TALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-167 1.19e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086   69 LMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSAAQsspvavhwgyarfVNIRDDkGATPL 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD-------------VNLKDN-GRTAL 65

                          90
                  ....*....|....*....
gi 330253086  149 HLAARQRRPECVNVLLDSG 167
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEKG 84
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 81-237 6.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  81 VKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLAARQRRPECV 160
Cdd:PHA02874 107 IKTILDCGIDVNIKDA-ELKTFLHYAIKKGDLESIKMLFE------------YGADVNIEDDNGCYPIHIAIKHNFFDII 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253086 161 NVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKHGACGALLNPSS 237
Cdd:PHA02874 174 KLLLEKG----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-206 3.52e-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: 40.65  E-value: 3.52e-05
                           10        20
                   ....*....|....*....|....*.
gi 330253086   181 GSTPLHLAARSGSIDCVRKLLAWGAD 206
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 100-206 5.22e-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: 45.64  E-value: 5.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 100 RTCLHYAAYYGHANCVQAILSAAQSSPVAVHWGYARFVNIRDD--KGATPLHLAARQRRPECVNVLLDSGSLVCAS---T 174
Cdd:cd21882   27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARatgR 106

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 330253086 175 SVYGSP------GSTPLHLAARSGSIDCVRKLLAWGAD 206
Cdd:cd21882  107 FFRKSPgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ 144
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
301-357 6.69e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 37.35  E-value: 6.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 330253086  301 DTELCCICFEQVCTIEVKDCGHQ-MCAQCTLALCCHNKpnpttstvtppVCPFCRSTI 357
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLRKKK-----------KCPICRQPI 47
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-214 1.79e-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: 40.83  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  101 TCLHYAA--YYGHANCVQAILSAAQSSPVAVHWGYARFVNiRDDKGATPLHLAARQRRPECVNVLLDSGSLV-------- 170
Cdd:TIGR00870  84 TLLHAISleYVDAVEAILLHLLAAFRKSGPLELANDQYTS-EFTPGITALHLAAHRQNYEIVKLLLERGASVparacgdf 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 330253086  171 CASTSVYGS--PGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASG 214
Cdd:TIGR00870 163 FVKSQGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLG 208
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
284-356 2.48e-03

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 40.00  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253086 284 LPSPSFSDTDDnmsevsDTELCCICFEQVCTIEVKDCGHQMCAQCTLAL-CCHNKPNpttstvtppvCPFCRST 356
Cdd:COG5236   49 LTTSSADDTDE------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 ...
 297-361 2.63e-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: 127.74  E-value: 2.63e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253086 297 SEVSDTELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNPTTSTVTPPVCPFCRSTIACLV 361
Cdd:cd23144    1 SSISDEDVCCICFEHLCTIEIKDCGHQMCATCALKLCCHNKPNPSSSPPRPPACPFCRQDIASLV 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-233 3.45e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 3.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSA-AQsspvavhwgyar 135
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD------------ 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 136 fVNIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGR 215
Cdd:COG0666  146 -VNAQDNDGNTPLHLAAANGNLEIVKLLLEAG----ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220

                        170
                 ....*....|....*...
gi 330253086 216 IPYVVAMKHKHGACGALL 233
Cdd:COG0666  221 TALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-233 8.51e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 8.51e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSA-AQsspvavhwgyar 135
Cdd:COG0666  112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAgAD------------ 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 136 fVNIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGR 215
Cdd:COG0666  179 -VNARDNDGETPLHLAAENGHLEIVKLLLEAG----ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                        170
                 ....*....|....*...
gi 330253086 216 IPYVVAMKHKHGACGALL 233
Cdd:COG0666  254 TALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-167 1.19e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086   69 LMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSAAQsspvavhwgyarfVNIRDDkGATPL 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD-------------VNLKDN-GRTAL 65

                          90
                  ....*....|....*....
gi 330253086  149 HLAARQRRPECVNVLLDSG 167
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-206 5.96e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 5.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  103 LHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLHLAARQRRPECVNVLLDSGSLVCASTsvygspGS 182
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD------------ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN------GR 62

                          90       100
                  ....*....|....*....|....
gi 330253086  183 TPLHLAARSGSIDCVRKLLAWGAD 206
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-170 2.75e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 2.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSAaqsspvavhwgyARF 136
Cdd:COG0666  178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEA------------GAD 244

                         90       100       110
                 ....*....|....*....|....*....|....
gi 330253086 137 VNIRDDKGATPLHLAARQRRPECVNVLLDSGSLV 170
Cdd:COG0666  245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-120 8.67e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 8.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253086   53 ERFTNPDLLNRHKQTPLMLAAMYGRISCVKKLAEVgANILMFDsvNRRTCLHYAAYYGHANCVQAILS 120
Cdd:pfam12796  18 ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHLEIVKLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 81-237 6.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  81 VKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLAARQRRPECV 160
Cdd:PHA02874 107 IKTILDCGIDVNIKDA-ELKTFLHYAIKKGDLESIKMLFE------------YGADVNIEDDNGCYPIHIAIKHNFFDII 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253086 161 NVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKHGACGALLNPSS 237
Cdd:PHA02874 174 KLLLEKG----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS 246
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 81-206 2.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  81 VKKLAEVGANILMFDSVNRRTCLHYAAYYGHANCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLAARQRRPECV 160
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLS------------YGANVNIPDKTNNSPLHHAVKHYNKPIV 217

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 330253086 161 NVLLDSGslvcASTSVYGSPGSTPLHLA-ARSGSIDCVRKLLAWGAD 206
Cdd:PHA02878 218 HILLENG----ASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVD 260
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-240 4.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 4.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGAnILMFDSVNRRTCLHYAAYYGHANCVQAILSAAQsspvavhwgYARF 136
Cdd:PHA02875  27 NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIESELHDAVEEGDVKAVEELLDLGK---------FADD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 137 VNIRDdkGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRI 216
Cdd:PHA02875  97 VFYKD--GMTPLHLATILKKLDIMKLLIARG----ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                        170       180
                 ....*....|....*....|....
gi 330253086 217 PYVVAMKHKHGACGALLNPSSAEP 240
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANI 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
67-116 6.81e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 6.81e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 330253086   67 TPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYAAYYGHANCVQ 116
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLK 51
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-206 5.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  53 ERFTNPDLLNRHKQTPLMLAAMY--GRISCVKKLAEVGANILMFDSVNRrTCLHYAAYYGH------------------A 112
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKidlkilkllidkgvdinaK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 113 NCVQAILSaaqsspvavhwgYARFVNIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSG 192
Cdd:PHA03100 173 NRVNYLLS------------YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG----ANPNLVNKYGDTPLHIAILNN 236

                        170
                 ....*....|....
gi 330253086 193 SIDCVRKLLAWGAD 206
Cdd:PHA03100 237 NKEIFKLLLNNGPS 250
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-188 6.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 6.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 330253086  137 VNIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLA 188
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYG----VDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 67-233 8.59e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 8.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  67 TPLMLAAMYG-RISCVKKLAEV----GANILMFDSvNRRTCLHYAAYY--GHANCVQAILSaaqsspvavhwgYARFVNI 139
Cdd:PHA03100  70 TPLHYLSNIKyNLTDVKEIVKLlleyGANVNAPDN-NGITPLLYAISKksNSYSIVEYLLD------------NGANVNI 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 140 RDDKGATPLHLAARQRRP--ECVNVLLDSGSLVCASTSV-----YGSP-------GSTPLHLAARSGSIDCVRKLLAWGA 205
Cdd:PHA03100 137 KNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRVnyllsYGVPinikdvyGFTPLHYAVYNNNPEFVKYLLDLGA 216

                        170       180
                 ....*....|....*....|....*...
gi 330253086 206 DRLQRDASGRIPYVVAMKHKHGACGALL 233
Cdd:PHA03100 217 NPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_4 pfam13637
Ankyrin repeats (many copies);
99-164 1.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 1.24e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253086   99 RRTCLHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLHLAARQRRPECVNVLL 164
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD------------INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-211 1.64e-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: 41.51  E-value: 1.64e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 330253086  181 GSTPLHLAA-RSGSIDCVRKLLAWGADRLQRD 211
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-229 1.94e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  78 ISCVKKLAEVGANILMFDsVNRRTCLHYAAYYGHAN-CVQAILSAAQSSPVAvhwgyarfvniRDDKGATPLHLAARQRR 156
Cdd:PHA03095 167 VELLRLLIDAGADVYAVD-DRFRSLLHHHLQSFKPRaRIVRELIRAGCDPAA-----------TDMLGNTPLHSMATGSS 234

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253086 157 PECVNV--LLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKHGAC 229
Cdd:PHA03095 235 CKRSLVlpLLIAG----ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 69-226 2.04e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  69 LMLAAMYGRISCVKKLAEVGANILMFDSVNRrTCLHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPL 148
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACN------------VHIRDANGNTAL 595

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253086 149 HLAARQRRPECVNVLLDsgslvCASTSVYGSPGSTpLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKH 226
Cdd:PLN03192 596 WNAISAKHHKIFRILYH-----FASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-201 2.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253086  146 TPLHLAARQRRPECVNVLLDSGSLVCASTSVygspGSTPLHLAARSGSIDCVRKLL 201
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN----GETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-206 3.52e-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: 40.65  E-value: 3.52e-05
                           10        20
                   ....*....|....*....|....*.
gi 330253086   181 GSTPLHLAARSGSIDCVRKLLAWGAD 206
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 100-206 5.22e-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: 45.64  E-value: 5.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 100 RTCLHYAAYYGHANCVQAILSAAQSSPVAVHWGYARFVNIRDD--KGATPLHLAARQRRPECVNVLLDSGSLVCAS---T 174
Cdd:cd21882   27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARatgR 106

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 330253086 175 SVYGSP------GSTPLHLAARSGSIDCVRKLLAWGAD 206
Cdd:cd21882  107 FFRKSPgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ 144
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 63-214 5.84e-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: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  63 RHKQTPLMLAAMYGRISCVKKLaevganiLMFDSVNR-------RTCLHYAAYYGHANCVQAILSAAqssPVAVhwgyar 135
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKKL-------LKCPSCDLfqrgalgETALHVAALYDNLEAAVVLMEAA---PELV------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 136 FVNIRDD--KGATPLHLAARQRRPECVNVLLDSGSLVCA--STSVYGSPGST--------PLHLAARSGSIDCVRKLLAW 203
Cdd:cd22192   79 NEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSprATGTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEH 158

                        170
                 ....*....|.
gi 330253086 204 GADRLQRDASG 214
Cdd:cd22192  159 GADIRAQDSLG 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
181-221 1.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 330253086  181 GSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVA 221
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 70-234 1.85e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  70 MLAAMYG--------RISCVKKLAEVGANIlMFDSVNRRTCLHYAAYYGHANC---VQAILSAAQsspvavhwgyarFVN 138
Cdd:PHA03095  11 MEAALYDyllnasnvTVEEVRRLLAAGADV-NFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGA------------DVN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 139 IRDDKGATPLHLAAR-QRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSID--CVRKLLAWGADRLQRDASGR 215
Cdd:PHA03095  78 APERCGFTPLHLYLYnATTLDVIKLLIKAG----ADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGM 153

                        170
                 ....*....|....*....
gi 330253086 216 IPYVVAMKhKHGACGALLN 234
Cdd:PHA03095 154 TPLAVLLK-SRNANVELLR 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 138-214 3.00e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 3.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253086 138 NIRDDKGATPLHLAARQRRPECVNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASG 214
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFG----ADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-206 3.76e-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: 37.62  E-value: 3.76e-04
                          10        20
                  ....*....|....*....|....*.
gi 330253086  181 GSTPLHLAARSGSIDCVRKLLAWGAD 206
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-106 4.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 4.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 330253086   57 NPDLLNRHKQTPLMLAAMYGRISCVKKLAEVGANILMFDSvNRRTCLHYA 106
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-95 4.69e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 4.69e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 330253086   64 HKQTPLMLAAMYGRISCVKKLAEVGANILMFD 95
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
301-357 6.69e-04

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 37.35  E-value: 6.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 330253086  301 DTELCCICFEQVCTIEVKDCGHQ-MCAQCTLALCCHNKpnpttstvtppVCPFCRSTI 357
Cdd:pfam13920   1 EDLLCVICLDRPRNVVLLPCGHLcLCEECAERLLRKKK-----------KCPICRQPI 47
RING-HC_Cbl-like cd16502
RING finger, HC subclass, found in Casitas B-lineage lymphoma (Cbl) proteins; The Cbl adaptor ...
 303-354 9.48e-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: 9.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 330253086 303 ELCCICFEQVCTIEVKDCGHQMCAQCTLALccHNKPNPTtstvtppvCPFCR 354
Cdd:cd16502    2 QLCKICAENDKDVRIEPCGHLLCTPCLTSW--QDSDGQT--------CPFCR 43
Ank_5 pfam13857
Ankyrin repeats (many copies);
84-151 1.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253086   84 LAEVGANILMFDSVNRRTCLHYAAYYGHANCVQAILSAAQSspvavhwgyarfVNIRDDKGATPLHLA 151
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD------------LNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 160-233 1.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253086 160 VNVLLDSGslvcASTSVYGSPGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKHGACGALL 233
Cdd:PTZ00322  98 ARILLTGG----ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-233 1.50e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 330253086  185 LHLAARSGSIDCVRKLLAWGADRLQRDASGRIPYVVAMKHKHGACGALL 233
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-225 1.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  62 NRHKQTPLMLAAMYGRISCVKKLAEVGANIlMFDSVNRRTCLHyaayyghancvQAILSAAQSSPVAVHwgyARFVNIRD 141
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLH-----------NAIIHNRSAIELLIN---NASINDQD 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 142 DKGATPLHLAArqrRPECVNVLLDSGSLVCASTSVYGSPGSTPLHLAARSGSIDCVRKLLAwgADRLQRDASGRIPYVVA 221
Cdd:PHA02874 252 IDGSTPLHHAI---NPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDII--ANAVLIKEADKLKDSDF 326


                 ....
gi 330253086 222 MKHK 225
Cdd:PHA02874 327 LEHI 330
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 64-91 1.58e-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: 36.03  E-value: 1.58e-03
                           10        20
                   ....*....|....*....|....*...
gi 330253086    64 HKQTPLMLAAMYGRISCVKKLAEVGANI 91
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-214 1.79e-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: 40.83  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  101 TCLHYAA--YYGHANCVQAILSAAQSSPVAVHWGYARFVNiRDDKGATPLHLAARQRRPECVNVLLDSGSLV-------- 170
Cdd:TIGR00870  84 TLLHAISleYVDAVEAILLHLLAAFRKSGPLELANDQYTS-EFTPGITALHLAAHRQNYEIVKLLLERGASVparacgdf 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 330253086  171 CASTSVYGS--PGSTPLHLAARSGSIDCVRKLLAWGADRLQRDASG 214
Cdd:TIGR00870 163 FVKSQGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLG 208
RING-HC_Cbl-c cd16710
RING finger, HC subclass, found in E3 ubiquitin-protein ligase Cbl-c and similar proteins; ...
 300-357 1.83e-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: 36.60  E-value: 1.83e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 330253086 300 SDTELCCICFEQVCTIEVKDCGHQMCAqCTLALCCHNKPNpttstvtppVCPFCRSTI 357
Cdd:cd16710   11 STFELCKICAERDKDVRIEPCGHLLCS-CCLAAWQHSDSQ---------TCPFCRCEI 58
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 98-121 1.94e-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: 1.94e-03
                           10        20
                   ....*....|....*....|....
gi 330253086    98 NRRTCLHYAAYYGHANCVQAILSA 121
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK 24
COG5236 COG5236
Uncharacterized conserved protein, contains RING Zn-finger [General function prediction only];
284-356 2.48e-03

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


Pssm-ID: 227561 [Multi-domain]  Cd Length: 493  Bit Score: 40.00  E-value: 2.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253086 284 LPSPSFSDTDDnmsevsDTELCCICFEQVCTIEVKDCGHQMCAQCTLAL-CCHNKPNpttstvtppvCPFCRST 356
Cdd:COG5236   49 LTTSSADDTDE------ENMNCQICAGSTTYSARYPCGHQICHACAVRLrALYMQKG----------CPLCRTE 106
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 67-206 2.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086  67 TPLMLAAMYGRISCVKKLAEVGA--NILMFDSVnrrTCLHYAAYYGHANCVQAIL-------------------SAAQSS 125
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGAdvNIIALDDL---SVLECAVDSKNIDTIKAIIdnrsninkndlsllkairnEDLETS 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253086 126 PVAVHWGYArfVNIRDDKGATPLHLAARQRR-PECVNVLLDSGSLVCASTsvygSPGSTPLHLAARSG-SIDCVRKLLAW 203
Cdd:PHA02876 257 LLLYDAGFS--VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKN----IKGETPLYLMAKNGyDTENIRTLIML 330


                 ...
gi 330253086 204 GAD 206
Cdd:PHA02876 331 GAD 333
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 143-167 3.10e-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: 34.87  E-value: 3.10e-03
                           10        20
                   ....*....|....*....|....*
gi 330253086   143 KGATPLHLAARQRRPECVNVLLDSG 167
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKG 25
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 64-93 3.36e-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: 34.93  E-value: 3.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 330253086   64 HKQTPLMLAAMYGRISCVKKLAEVGANILM 93
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
RING-HC_RSPRY1 cd16566
RING finger, HC subclass, found in RING finger and SPRY domain-containing protein 1 (RSPRY1) ...
 303-357 3.42e-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: 3.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253086 303 ELCCICFEQVCTIEVKDCGHQ-MCAQCTLALCChnkpnpttstvtppvCPFCRSTI 357
Cdd:cd16566    3 DSCTLCFDKVADTELRPCGHSgFCMECALQLET---------------CPLCRQPI 43
zf-RING_2 pfam13639
Ring finger domain;
305-354 4.64e-03

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 35.08  E-value: 4.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 330253086  305 CCICFEQVCT---IEVKDCGHQMCAQCTLALCCHNkpnpttstvtpPVCPFCR 354
Cdd:pfam13639   3 CPICLEEFEEgdkVVVLPCGHHFHRECLDKWLRSS-----------NTCPLCR 44
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-174 4.71e-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. 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: 34.57  E-value: 4.71e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 330253086  143 KGATPLHLAARQR-RPECVNVLLDSGSLVCAST 174
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
 303-353 6.03e-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: 34.38  E-value: 6.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 330253086 303 ELCCICFEQVCTIEVKDCGHQMCAQCTLALCCHNKPNpttstvtppvCPFC 353
Cdd:cd16449    1 LECPICLERLKDPVLLPCGHVFCRECIRRLLESGSIK----------CPIC 41
RING-HC_ZNF598 cd16615
RING finger, HC subclass, found in zinc finger protein 598 (ZNF598) and similar proteins; ...
 303-362 9.45e-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: 34.13  E-value: 9.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253086 303 ELCCICFEQVCTIEVKDCGHQMCAQCTL---ALCCHNKpnpttstvtppvCPFCRSTIACLVV 362
Cdd:cd16615    1 ETCVICCEEIEYFAVGPCNHPVCYKCSLrmrVLYKDKY------------CPICRTELDKVIF 51
 
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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