|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
71-315 |
4.38e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 161.28 E-value: 4.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 71 ENVLLFEGLDGATTVSLDDIFDIIKNGEVSEVENLVDKFGMECLSARDRHGYTPAHWIALNGNVQLMRYLIERTAPIDLP 150
Cdd:COG0666 37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 151 clGTQGPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAA 230
Cdd:COG0666 117 --DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 231 YKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLcEKSQLDLEPRDKNGKTPIMLAQAHQHQDVVRLLYG 310
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL-LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
....*
gi 1624699096 311 EVKKK 315
Cdd:COG0666 274 ALLLL 278
|
|
| DHHC |
pfam01529 |
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
425-539 |
3.07e-28 |
|
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.
Pssm-ID: 396215 Cd Length: 132 Bit Score: 109.76 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 425 RLCHSCRCLRPLRAKHCRVCNRCVSYFDHHCPFIYNCVGLRNRMWFFLFVLSVAVNCSFTIYFACYCV------------ 492
Cdd:pfam01529 6 KYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLvkliesstlfff 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1624699096 493 MIEGFTMLYVLGLIEAVVFCGLGWILTCTSILHACMNLTTNEMFNYK 539
Cdd:pfam01529 86 LILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
|
|
| COG5273 |
COG5273 |
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
352-565 |
4.04e-28 |
|
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 114.85 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 352 YPMYMIRAIPITWNILRRSHYCFIYWNAVMWISWAIANRRDPGYIPLSSDA--YYRAIKQIPYFDKLKKRNVmltrlCHS 429
Cdd:COG5273 40 IVVYTLLVIVKSLSLVVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLsgYRETISRLLDDGKFGTENF-----CST 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 430 CRCLRPLRAKHCRVCNRCVSYFDHHCPFIYNCVGLRNRMWFFLFVLS-VAVNCSFTIYFACYCVMIEG---FTMLYVLGL 505
Cdd:COG5273 115 CNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYtILVALVVLLSTAYYIAGIFSirhDTSLAICFL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624699096 506 IE-----AVVFCGLGWILTCTSILHACMNLTTNEMFNYKRY-------PYLRDKRGRYQNPFSRGPILNLLE 565
Cdd:COG5273 195 IFgcsllGVVFFIITTLLLLFLIYLILNNLTTIEFIQISRGgstleffPLCRESNLPFTNIFDSSEGALPLD 266
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
160-252 |
3.97e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.86 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 160 IHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTdiNGDTALHWAAYKGHADLMR 239
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1624699096 240 LLMYSGVELQKTD 252
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
114-308 |
4.06e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.22 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 114 LSARDRHGYTPAHWIALNGNV-QLMRYLIERTAPIDLPClgTQGPRPIHwACRKG---HASVVQVLLQAGVAVNAADFKG 189
Cdd:PHA03095 76 VNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKD--KVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 190 LTPLHlACMYGRTATAA---YLLGMGALNNLTDINGDTALHWAA--YKGHADLMRLLMYSGVELQKTDNFGSTPLHLACL 264
Cdd:PHA03095 153 MTPLA-VLLKSRNANVEllrLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1624699096 265 SGnmTCVRLLCEK---SQLDLEPRDKNGKTPIMLAQAHQHQDVVRLL 308
Cdd:PHA03095 232 GS--SCKRSLVLPlliAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
116-298 |
4.07e-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: 49.63 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 116 ARDRHGYTPAHWIALNGNVQLMRYLIErTAP--IDLPCLGT--QGPRPIHWACRKGHASVVQVLLQAGVAVNAAdfkglt 191
Cdd:cd22192 46 QRGALGETALHVAALYDNLEAAVVLME-AAPelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSP------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 192 plhlacmygRTATAAYLLGMGALNNLtdinGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCV 271
Cdd:cd22192 119 ---------RATGTFFRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFA 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1624699096 272 R-----LLCEKSQLDLEP----RDKNGKTPIMLAQA 298
Cdd:cd22192 186 CqmydlILSYDKEDDLQPldlvPNNQGLTPFKLAAK 221
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
221-248 |
3.85e-04 |
|
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: 37.95 E-value: 3.85e-04
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-242 |
3.01e-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: 40.45 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 67 VEDHENVLLFEGLDGATTvslDDIFDIIKNGEVSEVENL------VDKFGMECLSARDR------HGYTPAHWIALNGNV 134
Cdd:TIGR00870 65 NLELTELLLNLSCRGAVG---DTLLHAISLEYVDAVEAIllhllaAFRKSGPLELANDQytseftPGITALHLAAHRQNY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 135 QLMRYLIERTAPIDLPCLG-----TQ-------GPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACM---- 198
Cdd:TIGR00870 142 EIVKLLLERGASVPARACGdffvkSQgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMenef 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1624699096 199 ---YGRTATAAY--LLGMGA----LNNLTDI---NGDTALHWAAYKGHADLMRLLM 242
Cdd:TIGR00870 222 kaeYEELSCQMYnfALSLLDklrdSKELEVIlnhQGLTPLKLAAKEGRIVLFRLKL 277
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
71-315 |
4.38e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 161.28 E-value: 4.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 71 ENVLLFEGLDGATTVSLDDIFDIIKNGEVSEVENLVDKFGMECLSARDRHGYTPAHWIALNGNVQLMRYLIERTAPIDLP 150
Cdd:COG0666 37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 151 clGTQGPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAA 230
Cdd:COG0666 117 --DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 231 YKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLcEKSQLDLEPRDKNGKTPIMLAQAHQHQDVVRLLYG 310
Cdd:COG0666 195 ENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL-LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
....*
gi 1624699096 311 EVKKK 315
Cdd:COG0666 274 ALLLL 278
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
90-291 |
2.07e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 143.17 E-value: 2.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 90 IFDIIKNGEVSEVENLVDKfGMEcLSARDRHGYTPAHWIALNGNVQLMRYLIERTAPIDLPclGTQGPRPIHWACRKGHA 169
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEA-GAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHLAAANGNL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 170 SVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQ 249
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1624699096 250 KTDNFGSTPLHLACLSGNMTCVRLLCEKSQLDLEPRDKNGKT 291
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
118-308 |
1.72e-35 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 135.08 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 118 DRHGYTPAHWIALNGNVQLMRYLIERTAPIDLPCLGTQGPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLAC 197
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 198 MYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEK 277
Cdd:COG0666 96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
|
170 180 190
....*....|....*....|....*....|.
gi 1624699096 278 SqLDLEPRDKNGKTPIMLAQAHQHQDVVRLL 308
Cdd:COG0666 176 G-ADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
|
| DHHC |
pfam01529 |
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which ... |
425-539 |
3.07e-28 |
|
DHHC palmitoyltransferase; This entry refers to the DHHC domain, found in DHHC proteins which are palmitoyltransferases. Palmitoylation or, more specifically S-acylation, plays important roles in the regulation of protein localization, stability, and activity. It is a post-translational protein modification that involves the attachment of palmitic acid to Cys residues through a thioester linkage. Protein acyltransferases (PATs), also known as palmitoyltransferases, catalyze this reaction by transferring the palmitoyl group from palmitoyl-CoA to the thiol group of Cys residues. They are characterized by the presence of a 50-residue-long domain called the DHHC domain, which in most but not all cases is also cysteine-rich and gets its name from a highly conserved DHHC signature tetrapeptide (Asp-His-His-Cys). The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. Some proteins containing a DHHC domain include Drosophila DNZ1 protein, Mouse Abl-philin 2 (Aph2) protein, Mammalian ZDHHC9, Yeast ankyrin repeat-containing protein AKR1, Yeast Erf2 protein, and Arabidopsis thaliana tip growth defective 1.
Pssm-ID: 396215 Cd Length: 132 Bit Score: 109.76 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 425 RLCHSCRCLRPLRAKHCRVCNRCVSYFDHHCPFIYNCVGLRNRMWFFLFVLSVAVNCSFTIYFACYCV------------ 492
Cdd:pfam01529 6 KYCSTCNIYKPPRSKHCRVCNRCVLRFDHHCPWLNNCIGKRNHKYFILFLLYLTLYLILYLVLSLYYLvkliesstlfff 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1624699096 493 MIEGFTMLYVLGLIEAVVFCGLGWILTCTSILHACMNLTTNEMFNYK 539
Cdd:pfam01529 86 LILFLFSISIILLILSLFFLLFLGILLFFHLYLISRNLTTYEFMKKK 132
|
|
| COG5273 |
COG5273 |
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only]; |
352-565 |
4.04e-28 |
|
Uncharacterized protein containing DHHC-type Zn finger [General function prediction only];
Pssm-ID: 227598 [Multi-domain] Cd Length: 309 Bit Score: 114.85 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 352 YPMYMIRAIPITWNILRRSHYCFIYWNAVMWISWAIANRRDPGYIPLSSDA--YYRAIKQIPYFDKLKKRNVmltrlCHS 429
Cdd:COG5273 40 IVVYTLLVIVKSLSLVVLFIILFIVILVLASFSYLLLLVSDPGYLGENITLsgYRETISRLLDDGKFGTENF-----CST 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 430 CRCLRPLRAKHCRVCNRCVSYFDHHCPFIYNCVGLRNRMWFFLFVLS-VAVNCSFTIYFACYCVMIEG---FTMLYVLGL 505
Cdd:COG5273 115 CNIYKPPRSHHCSICNRCVLKFDHHCPWINNCVGFRNYRFFYQFLLYtILVALVVLLSTAYYIAGIFSirhDTSLAICFL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624699096 506 IE-----AVVFCGLGWILTCTSILHACMNLTTNEMFNYKRY-------PYLRDKRGRYQNPFSRGPILNLLE 565
Cdd:COG5273 195 IFgcsllGVVFFIITTLLLLFLIYLILNNLTTIEFIQISRGgstleffPLCRESNLPFTNIFDSSEGALPLD 266
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
94-259 |
1.01e-26 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 110.04 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 94 IKNGEVSEVENLVDKfGMEcLSARDRHGYTPAHWIALNGNVQLMRYLIERTAPIDLPclGTQGPRPIHWACRKGHASVVQ 173
Cdd:COG0666 128 AYNGNLEIVKLLLEA-GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHLAAENGHLEIVK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 174 VLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDN 253
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
....*.
gi 1624699096 254 FGSTPL 259
Cdd:COG0666 284 DLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
136-308 |
4.46e-24 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.72 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 136 LMRYLIERTAPIDLPCLGTQGPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALN 215
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 216 NLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEKsQLDLEPRDKNGKTPIML 295
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHL 159
|
170
....*....|...
gi 1624699096 296 AQAHQHQDVVRLL 308
Cdd:COG0666 160 AAANGNLEIVKLL 172
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
160-252 |
3.97e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.86 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 160 IHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTdiNGDTALHWAAYKGHADLMR 239
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1624699096 240 LLMYSGVELQKTD 252
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
226-308 |
4.49e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.17 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 226 LHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEKSQLDLeprDKNGKTPIMLAQAHQHQDVV 305
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
|
...
gi 1624699096 306 RLL 308
Cdd:pfam12796 78 KLL 80
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
193-277 |
1.89e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 193 LHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMySGVELQKTDNfGSTPLHLACLSGNMTCVR 272
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78
|
....*
gi 1624699096 273 LLCEK 277
Cdd:pfam12796 79 LLLEK 83
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
114-308 |
4.06e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.22 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 114 LSARDRHGYTPAHWIALNGNV-QLMRYLIERTAPIDLPClgTQGPRPIHwACRKG---HASVVQVLLQAGVAVNAADFKG 189
Cdd:PHA03095 76 VNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKD--KVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 190 LTPLHlACMYGRTATAA---YLLGMGALNNLTDINGDTALHWAA--YKGHADLMRLLMYSGVELQKTDNFGSTPLHLACL 264
Cdd:PHA03095 153 MTPLA-VLLKSRNANVEllrLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1624699096 265 SGnmTCVRLLCEK---SQLDLEPRDKNGKTPIMLAQAHQHQDVVRLL 308
Cdd:PHA03095 232 GS--SCKRSLVLPlliAGISINARNRYGQTPLHYAAVFNNPRACRRL 276
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
126-219 |
1.70e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.99 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 126 HWIALNGNVQLMRYLIErtAPIDLPCLGTQGPRPIHWACRKGHASVVQVLLQaGVAVNAADfKGLTPLHLACMYGRTATA 205
Cdd:pfam12796 2 HLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1624699096 206 AYLLGMGALNNLTD 219
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
94-308 |
3.97e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.61 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 94 IKNGEVSEVENLVDKFGmECLSARDRHGYTPAHWIALNGNVQLMRYLIERTAPIDLpcLGTQGPRPIHWACRKGHASVVQ 173
Cdd:PHA02874 9 IYSGDIEAIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINH--INTKIPHPLLTAIKIGAHDIIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 174 VL-----------------------LQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAA 230
Cdd:PHA02874 86 LLidngvdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624699096 231 YKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEKSQlDLEPRDKNGKTPIMLAQAHqHQDVVRLL 308
Cdd:PHA02874 166 KHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAIIH-NRSAIELL 241
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
99-305 |
2.35e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 72.30 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 99 VSEVENLVDKFGMEC---LSARDRHGYTPAHWIALNGNVQLMRYLIERTAPIDLPclGTQGPRPIHWACRKGHASVVQVL 175
Cdd:PHA02874 99 IPCIEKDMIKTILDCgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE--DDNGCYPIHIAIKHNFFDIIKLL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 176 LQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGalNNLTDI--NGDTALHWAAYKGHADLMRLLMYSGVELQKTDn 253
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG--NHIMNKckNGFTPLHNAIIHNRSAIELLINNASINDQDID- 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1624699096 254 fGSTPLHLAClsgNMTCVR-----LLCEKSqlDLEPRDKNGKTPIMLAQAHQHQDVV 305
Cdd:PHA02874 254 -GSTPLHHAI---NPPCDIdiidiLLYHKA--DISIKDNKGENPIDTAFKYINKDPV 304
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
94-262 |
1.47e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 69.99 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 94 IKNGEVsEVENLVDKFGMEcLSARDRHGYTPAHwIALNGN-VQLMRYLIERTAPIDLPclGTQGPRPIHWACRKGHASVV 172
Cdd:PHA02874 132 IKKGDL-ESIKMLFEYGAD-VNIEDDNGCYPIH-IAIKHNfFDIIKLLLEKGAYANVK--DNNGESPLHNAAEYGDYACI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 173 QVLLQAGVAVNAADFKGLTPLHLACMYGRTATAayLLGMGALNNLTDINGDTALHWA-AYKGHADLMRLLMYSGVELQKT 251
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIK 284
|
170
....*....|.
gi 1624699096 252 DNFGSTPLHLA 262
Cdd:PHA02874 285 DNKGENPIDTA 295
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
167-308 |
1.96e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 70.28 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 167 GHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLmYSGV 246
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFA 614
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624699096 247 ELQKTDNFGSTpLHLACLSGNMTCVRLLCeKSQLDLEPRDKNGKTPIMLAQAHQHQDVVRLL 308
Cdd:PLN03192 615 SISDPHAAGDL-LCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
171-308 |
4.99e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 68.15 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 171 VVQVLLQAGVAVNAADFKGLTPLHLACMY--GRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADL--MRLLMYSGV 246
Cdd:PHA03100 88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGV 167
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624699096 247 ELQK----------------TDNFGSTPLHLACLSGNMTCVRLLCEKSQlDLEPRDKNGKTPIMLAQAHQHQDVVRLL 308
Cdd:PHA03100 168 DINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGA-NPNLVNKYGDTPLHIAILNNNKEIFKLL 244
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
137-306 |
5.79e-12 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 68.13 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 137 MRYLIERTApiDLPCLGTQGPRPIHWACRKGH---ASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTA-TAAYLLGMG 212
Cdd:PHA03095 30 VRRLLAAGA--DVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 213 ALNNLTDINGDTALHwaAYKG----HADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMT--CVRLLCEKSQlDLEPRD 286
Cdd:PHA03095 108 ADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGA-DVYAVD 184
|
170 180
....*....|....*....|
gi 1624699096 287 KNGKTPImlaqaHQHQDVVR 306
Cdd:PHA03095 185 DRFRSLL-----HHHLQSFK 199
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
73-264 |
1.03e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.21 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 73 VLLFEGLDGATTVSLDDIFDIIKNGEV-SEVENLVDKFGMEcLSARDRH-GYTPAHWIALNGNVQLMRYLIERTAPIDLP 150
Cdd:PHA02878 119 IILTNRYKNIQTIDLVYIDKKSKDDIIeAEITKLLLSYGAD-INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIP 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 151 CLGTQGPrpIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRT-ATAAYLLGMGA-LNNLTDINGDTALHW 228
Cdd:PHA02878 198 DKTNNSP--LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVdVNAKSYILGLTALHS 275
|
170 180 190
....*....|....*....|....*....|....*.
gi 1624699096 229 AAYKghADLMRLLMYSGVELQKTDNFGSTPLHLACL 264
Cdd:PHA02878 276 SIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
92-247 |
1.76e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.17 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 92 DIIKNGEVSEVENLVD--KFGMECLSardRHGYTPAHWIALNGNVQLMRYLIERTAPIDLPclGTQGPRPIHWACRKGHA 169
Cdd:PHA02875 74 DAVEEGDVKAVEELLDlgKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIP--NTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1624699096 170 SVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGD-TALHWAAYKGHADLMRLLMYSGVE 247
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
222-274 |
1.09e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 1.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1624699096 222 GDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLL 274
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
113-274 |
1.68e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 60.06 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 113 CLSARDRHGYTPAHWIALN--GNVQLMRYLIERTAPIDLpcLGTQGPRPIHWACRKGHA--SVVQVLLQAGVAVNAADfk 188
Cdd:PHA03100 98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNI--KNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 189 gltplhlacmygrtaTAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNM 268
Cdd:PHA03100 174 ---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
....*.
gi 1624699096 269 TCVRLL 274
Cdd:PHA03100 239 EIFKLL 244
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
230-310 |
3.27e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.91 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 230 AYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEKSQlDLEPRDKNGKTPIMLAQAHQHQDVVRLLY 309
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA-DPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
.
gi 1624699096 310 G 310
Cdd:PTZ00322 169 R 169
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
167-242 |
3.95e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 3.95e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1624699096 167 GHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLM 242
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
94-186 |
5.37e-09 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 53.58 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 94 IKNGEVSEVENLVdKFGMEClSARDRHGYTPAHWIALNGNVQLMRYLIERtAPIDLPCLGTqgpRPIHWACRKGHASVVQ 173
Cdd:pfam12796 5 AKNGNLELVKLLL-ENGADA-NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR---TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1624699096 174 VLLQAGVAVNAAD 186
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
189-241 |
5.86e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 5.86e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1624699096 189 GLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLL 241
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
121-308 |
7.01e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 121 GYTPAHWIALNGNVQLMRYLIERTAPIDLPCLGTQGPrpIHWACRKGHASVVQVLLQAGVAVNAADFK-GLTPLHLACMY 199
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESE--LHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATIL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 200 GRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEkSQ 279
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLD-SG 191
|
170 180 190
....*....|....*....|....*....|
gi 1624699096 280 LDLEPRDKNGKTPIM-LAQAHQHQDVVRLL 308
Cdd:PHA02875 192 ANIDYFGKNGCVAALcYAIENNKIDIVRLF 221
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
140-196 |
1.01e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.58 E-value: 1.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1624699096 140 LIERTaPIDLPCLGTQGPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLA 196
Cdd:pfam13857 1 LLEHG-PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
114-317 |
2.34e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.00 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 114 LSARDRHGYTPAHWIALNG-NVQLMRYLIERTApiDLPCLGTQGPRPIHWACR-KGHASVVQVLLQAGVAVNAADFKGLT 191
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGA--DVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKT 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 192 PLHLACMYGRTATAAYLLGMGA-LNNLTDINGdTALHWAAYKGHADL-MRLLMYSGVELQKTDNFGSTPLHLACLSG-NM 268
Cdd:PHA02876 378 PIHYAAVRNNVVIINTLLDYGAdIEALSQKIG-TALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1624699096 269 TCVRLLCEKSQlDLEPRDKNGKTPIMLAQAHQHQDVVRLLYGEVKKKSR 317
Cdd:PHA02876 457 DVIEMLLDNGA-DVNAINIQNQYPLLIALEYHGIVNILLHYGAELRDSR 504
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
114-272 |
3.25e-08 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 56.19 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 114 LSARDRHGYTPAHwiAL----NGNVQLMRYLIERTAPI---DLPClgtQGPRPIHWACRKGHASVVQVLLQAGVAVNAAD 186
Cdd:PHA03095 145 VNALDLYGMTPLA--VLlksrNANVELLRLLIDAGADVyavDDRF---RSLLHHHLQSFKPRARIVRELIRAGCDPAATD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 187 FKGLTPLHLACMYGRTATA--AYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACL 264
Cdd:PHA03095 220 MLGNTPLHSMATGSSCKRSlvLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
|
....*...
gi 1624699096 265 SGNMTCVR 272
Cdd:PHA03095 300 NNNGRAVR 307
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
158-209 |
9.38e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 9.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1624699096 158 RPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLL 209
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
171-295 |
1.37e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 54.68 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 171 VVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMR----------- 239
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsnink 239
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1624699096 240 -----------------LLMY-SGVELQKTDNFGSTPLHLACLSGNMT-CVRLLCEKSqLDLEPRDKNGKTPIML 295
Cdd:PHA02876 240 ndlsllkairnedletsLLLYdAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERG-ADVNAKNIKGETPLYL 313
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
167-308 |
4.73e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 52.30 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 167 GHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNN------------------------LTDIN- 221
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDvkypdieselhdaveegdvkaveeLLDLGk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 222 ---------GDTALHWAAYKGHADLMRLLMYSGV--ELQKTDNFgsTPLHLACLSGNMTCVRLLCE-KSQLDLEprDKNG 289
Cdd:PHA02875 93 faddvfykdGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDhKACLDIE--DCCG 168
|
170
....*....|....*....
gi 1624699096 290 KTPIMLAQAHQHQDVVRLL 308
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKML 187
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
213-262 |
5.64e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 5.64e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1624699096 213 ALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLA 262
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
159-308 |
9.93e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 51.42 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 159 PIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAYLLGM--------------GALNNlTDINGDT 224
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaikDAFNN-RNVEIFK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 225 ALHWAAYKG------------------HADLMRLLMYSGVELQKTD-NFGSTPLHLACLSGNMTCVRLLCEKSQlDLEPR 285
Cdd:PHA02878 119 IILTNRYKNiqtidlvyidkkskddiiEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGA-NVNIP 197
|
170 180
....*....|....*....|...
gi 1624699096 286 DKNGKTPIMLAQAHQHQDVVRLL 308
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHIL 220
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
159-274 |
1.49e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 51.22 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 159 PIHWACRKGHAS-VVQVLLQAGVAVNAADFKGLTPLHLACMYG-RTATAAYLLGMGALNNLTDINGDTALHWAA-YKGHA 235
Cdd:PHA02876 276 PLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNK 355
|
90 100 110
....*....|....*....|....*....|....*....
gi 1624699096 236 DLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLL 274
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
175-229 |
3.30e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 3.30e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1624699096 175 LLQAG-VAVNAADFKGLTPLHLACMYGRTATAAYLLGMGALNNLTDINGDTALHWA 229
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
116-298 |
4.07e-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: 49.63 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 116 ARDRHGYTPAHWIALNGNVQLMRYLIErTAP--IDLPCLGT--QGPRPIHWACRKGHASVVQVLLQAGVAVNAAdfkglt 191
Cdd:cd22192 46 QRGALGETALHVAALYDNLEAAVVLME-AAPelVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSP------ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 192 plhlacmygRTATAAYLLGMGALNNLtdinGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCV 271
Cdd:cd22192 119 ---------RATGTFFRPGPKNLIYY----GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFA 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1624699096 272 R-----LLCEKSQLDLEP----RDKNGKTPIMLAQA 298
Cdd:cd22192 186 CqmydlILSYDKEDDLQPldlvPNNQGLTPFKLAAK 221
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
185-278 |
5.09e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 48.50 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 185 ADFKGLTPLHLACMYGRTATAAYLLGMGALNNLtdINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACL 264
Cdd:PHA02791 26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103
|
90
....*....|....
gi 1624699096 265 SGNMTCVRLLCEKS 278
Cdd:PHA02791 104 SGNMQTVKLFVKKN 117
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
121-176 |
6.75e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 6.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1624699096 121 GYTPAHWIALNGNVQLMRYLIERTAPIDlpCLGTQGPRPIHWACRKGHASVVQVLL 176
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
218-309 |
9.65e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 48.71 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 218 TDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCeKSQLDLEPRDKNGKTPIMLAQ 297
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAI 599
|
90
....*....|..
gi 1624699096 298 AHQHQDVVRLLY 309
Cdd:PLN03192 600 SAKHHKIFRILY 611
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
200-297 |
1.16e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 200 GRTATAAYLLGMGALNNLTDINGDTALHWAAYKGHADLMRLLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEKSQ 279
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
|
90 100 110
....*....|....*....|....*....|
gi 1624699096 280 LDLE------PRDKNGK------TPIMLAQ 297
Cdd:PTZ00322 173 CHFElganakPDSFTGKppsledSPISSHH 202
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
128-210 |
3.28e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 128 IALNGNVQLMRYLIERTApiDLPCLGTQGPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACMYGRTATAAY 207
Cdd:PTZ00322 89 LAASGDAVGARILLTGGA--DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
...
gi 1624699096 208 LLG 210
Cdd:PTZ00322 167 LSR 169
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
221-248 |
3.85e-04 |
|
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: 37.95 E-value: 3.85e-04
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
221-296 |
4.96e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 41.02 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 221 NGDTALHWAAYKGHAD---LMRLLMYSGVELQKTDN-FGSTPLHLACLSGNMTCVRLLCEKSQLDLEPRDKNGKTPIMLA 296
Cdd:PHA02736 54 HGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVA 133
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
240-296 |
9.59e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 9.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1624699096 240 LLMYSGVELQKTDNFGSTPLHLACLSGNMTCVRLLCEKsQLDLEPRDKNGKTPIMLA 296
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
221-253 |
1.40e-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: 36.50 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|....
gi 1624699096 221 NGDTALHWAAYK-GHADLMRLLMYSGVELQKTDN 253
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
110-176 |
2.39e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 2.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624699096 110 GMEClSARDRHGYTPAHWIALNGNVQLMRYLIERTApiDLPCLGTQGPRPIHWACRKGHASVVQVLL 176
Cdd:PTZ00322 105 GADP-NCRDYDGRTPLHIACANGHVQVVRVLLEFGA--DPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
67-242 |
3.01e-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: 40.45 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 67 VEDHENVLLFEGLDGATTvslDDIFDIIKNGEVSEVENL------VDKFGMECLSARDR------HGYTPAHWIALNGNV 134
Cdd:TIGR00870 65 NLELTELLLNLSCRGAVG---DTLLHAISLEYVDAVEAIllhllaAFRKSGPLELANDQytseftPGITALHLAAHRQNY 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 135 QLMRYLIERTAPIDLPCLG-----TQ-------GPRPIHWACRKGHASVVQVLLQAGVAVNAADFKGLTPLHLACM---- 198
Cdd:TIGR00870 142 EIVKLLLERGASVPARACGdffvkSQgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMenef 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1624699096 199 ---YGRTATAAY--LLGMGA----LNNLTDI---NGDTALHWAAYKGHADLMRLLM 242
Cdd:TIGR00870 222 kaeYEELSCQMYnfALSLLDklrdSKELEVIlnhQGLTPLKLAAKEGRIVLFRLKL 277
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
159-186 |
3.02e-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: 35.34 E-value: 3.02e-03
10 20
....*....|....*....|....*....
gi 1624699096 159 PIHWAC-RKGHASVVQVLLQAGVAVNAAD 186
Cdd:pfam00023 5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
159-184 |
4.50e-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: 4.50e-03
|
| PHA02741 |
PHA02741 |
hypothetical protein; Provisional |
213-308 |
5.02e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 165108 [Multi-domain] Cd Length: 169 Bit Score: 38.10 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 213 ALNNLTDINGDTALHWAAYKGHA----DLMRLLMYSGVELQKTDNF-GSTPLHLACLSGNMTCVRLLCEKSQLDLEPRDK 287
Cdd:PHA02741 51 AALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMLeGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNA 130
|
90 100
....*....|....*....|.
gi 1624699096 288 NGKTPIMLAQAHQHQDVVRLL 308
Cdd:PHA02741 131 DNKSPFELAIDNEDVAMMQIL 151
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
120-148 |
5.49e-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: 34.54 E-value: 5.49e-03
10 20
....*....|....*....|....*....
gi 1624699096 120 HGYTPAHWIALNGNVQLMRYLIERTAPID 148
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
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| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
172-295 |
6.05e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 39.27 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624699096 172 VQVLLQAGVAVN-AADFKGLTPLhLACMYGRTATAAYLLGMGALNNLTDINGDTALH--WAAYKGHADLMRLLMYSGVEL 248
Cdd:PHA02946 123 INLLVQYGAKINnSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISP 201
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1624699096 249 QKTDNFGSTPLHLACLS--GNMTCVRLLCEKSqlDLEPRDKNGKTPIML 295
Cdd:PHA02946 202 SKPDHDGNTPLHIVCSKtvKNVDIINLLLPST--DVNKQNKFGDSPLTL 248
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|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
255-277 |
8.04e-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: 34.10 E-value: 8.04e-03
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