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Conserved domains on  [gi|1624699096|ref|NP_001356894|]
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patsas, isoform D [Drosophila melanogaster]

Protein Classification

ankyrin repeat domain-containing DHHC palmitoyltransferase family protein( domain architecture ID 12790884)

DHHC family palmitoyltransferase may catalyze the addition of palmitate onto various protein substrates and be involved in a variety of cellular processes; contains N-terminal ankyrin repeats;

EC:  2.3.1.-
Gene Ontology:  GO:0043543|GO:0016747
PubMed:  21388813

Graphical summary

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List of domain hits

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
 
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
                           10        20
                   ....*....|....*....|....*...
gi 1624699096  221 NGDTALHWAAYKGHADLMRLLMYSGVEL 248
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
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
                           10        20
                   ....*....|....*....|....*...
gi 1624699096  221 NGDTALHWAAYKGHADLMRLLMYSGVEL 248
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
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
                           10        20
                   ....*....|....*....|....*.
gi 1624699096  159 PIHWACRKGHASVVQVLLQAGVAVNA 184
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
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
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
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
                           10        20
                   ....*....|....*....|...
gi 1624699096  255 GSTPLHLACLSGNMTCVRLLCEK 277
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDK 24
 
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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