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Conserved domains on  [gi|2257803366|ref|XP_048588401|]
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transient receptor potential cation channel subfamily A member 1-like [Nematostella vectensis]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-267 3.33e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 3.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 145 TLVSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAKmenl 224
Cdd:COG0666   171 LLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL---- 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2257803366 225 dsllYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREPKDK 267
Cdd:COG0666   246 ----NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
216-531 3.19e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 216 IAKAKMENLDSLLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREPKDKHSPSAFHLACAQGSVKMVKLMVEKDPVI 295
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 296 criTLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTsknvamesvl 375
Cdd:COG0666    81 ---NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN---------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 376 haavghmrtteallngsgaaylipEQDRDGYAPIHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIV 455
Cdd:COG0666   148 ------------------------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 456 DdLLVGRNVRmINLKNNHGKTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLAAITGSKRCVECILIKHPD 531
Cdd:COG0666   203 K-LLLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-267 3.33e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 3.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 145 TLVSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAKmenl 224
Cdd:COG0666   171 LLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL---- 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2257803366 225 dsllYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREPKDK 267
Cdd:COG0666   246 ----NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
216-531 3.19e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 216 IAKAKMENLDSLLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREPKDKHSPSAFHLACAQGSVKMVKLMVEKDPVI 295
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 296 criTLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTsknvamesvl 375
Cdd:COG0666    81 ---NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN---------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 376 haavghmrtteallngsgaaylipEQDRDGYAPIHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIV 455
Cdd:COG0666   148 ------------------------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 456 DdLLVGRNVRmINLKNNHGKTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLAAITGSKRCVECILIKHPD 531
Cdd:COG0666   203 K-LLLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
PHA03095 PHA03095
ankyrin-like protein; Provisional
79-360 6.65e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 6.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  79 KLLDKGVDINCADEYGKTPLH---HATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEA-IVKTLVSNeKCNV 154
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA-GADV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 155 NAKGRGLCTPLHI-ACGMD-KLKICKLLIEHEARIDLKDEDKMTPLgHAVEKGAKNTAEYIFSIAKAkmenlDSLLYQAD 232
Cdd:PHA03095  111 NAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRNANVELLRLLIDA-----GADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 233 IDGSTLLHMAVESG------VTEIVALCLNHGARvrepkDKHSPSAFHLACAQGSVKMVKLmvekDPVICRITLID---R 303
Cdd:PHA03095  185 DRFRSLLHHHLQSFkprariVRELIRAGCDPAAT-----DMLGNTPLHSMATGSSCKRSLV----LPLLIAGISINarnR 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 304 DGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSR 360
Cdd:PHA03095  256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
212-531 2.60e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.02  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 212 YIFSIAKAKMENLDSLL------YQADIDGSTLLHMAVESG---VTEIVALCLNHGARVrEPKDKHSPSAFHL-ACAQGS 281
Cdd:PHA03095   18 YLLNASNVTVEEVRRLLaagadvNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADV-NAPERCGFTPLHLyLYNATT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 282 VKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTN--IVEFLLDQGAQVDLTDKTHCTPL--FMAASNGATETVKLL 357
Cdd:PHA03095   97 LDVIKLLIKAG---ADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 358 MSRGANVTSKNVAMESVLHAAVGHMRTTEALLNGSGAAYLIPE-QDRDGYAPIHRAARGGYLQNIHLFitkNKAAAGITa 436
Cdd:PHA03095  174 IDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAaTDMLGNTPLHSMATGSSCKRSLVL---PLLIAGIS- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 437 dsldtplhvackfgwleivddllvgrnvrmINLKNNHGKTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLAAI 515
Cdd:PHA03095  250 ------------------------------INARNRYGQTPLHYAAVFNNPRACRRLIALGADINaVSSDGNTPLSLMVR 299
                         330
                  ....*....|....*.
gi 2257803366 516 TGSKRCVECILIKHPD 531
Cdd:PHA03095  300 NNNGRAVRAALAKNPS 315
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-191 2.48e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  98 LHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTLVSNEKCNVNAKGRglcTPLHIACGMDKLKIC 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2257803366 178 KLLIEHEARIDLKD 191
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-368 3.07e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 273 FHLACAQGSVKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTNIVEFLLDQgAQVDLTDKTHcTPLFMAASNGATE 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG---ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 2257803366 353 TVKLLMSRGANVTSKN 368
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
227-424 3.70e-07

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: 53.09  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 227 LLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREpKDKHSPSAFHLACAQGSVKMVKLMVEKDPVICR--ITLIDRD 304
Cdd:cd22192    10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQ-RGALGETALHVAALYDNLEAAVVLMEAAPELVNepMTSDLYQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 305 GMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKT--------HCT------PLFMAASNGATETVKLLMSRGANVTSKNVA 370
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 371 MESVLHAAVGHMRTTEA------LLN-----GSGAAYLIPeqDRDGYAPIHRAARGGylqNIHLF 424
Cdd:cd22192   169 GNTVLHILVLQPNKTFAcqmydlILSydkedDLQPLDLVP--NNQGLTPFKLAAKEG---NIVMF 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
123-360 1.27e-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: 51.17  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 123 QDQRG-DTPLHAAVRTGDEAIVKTLVSNEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEhEARiDLKDEdKMTplgha 201
Cdd:cd22192    12 QQKRIsESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAP-ELVNE-PMT----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 202 vekgakntaeyifsiakakmenldSLLYQadidGSTLLHMAVESGVTEIVALCLNHGARVREP--------KDKHS---- 269
Cdd:cd22192    84 ------------------------SDLYQ----GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyy 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 270 ---PSAFhlACAQGSVKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTNIV----EFLLDQGAQVD------LTDK 336
Cdd:cd22192   136 gehPLSF--AACVGNEEIVRLLIEHG---ADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNN 210
                         250       260
                  ....*....|....*....|....
gi 2257803366 337 THCTPLFMAASNGATETVKLLMSR 360
Cdd:cd22192   211 QGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
473-501 6.80e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 6.80e-05
                           10        20
                   ....*....|....*....|....*....
gi 2257803366  473 HGKTPLHFAAGEGHDKVVELLLDRGATID 501
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
51-290 8.50e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  51 QPLKTTVEGTKQEQLCAAAYMGDKETAIKLLD--KGVDINCADEYGKTPLHHATTGKR----IEFVEFLLSRGAEltkqd 124
Cdd:TIGR00870   7 VPAEESPLSDEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENEnlelTELLLNLSCRGAV----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 125 qrGDTPLHAAVRT---GDEAIVKTLVSNEKCNVN---AKGRGLC------TPLHIACGMDKLKICKLLIEHEARIDLK-- 190
Cdd:TIGR00870  82 --GDTLLHAISLEyvdAVEAILLHLLAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARac 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 191 -DEDKMTP----LGHavekgakntAEYIFSIAKA-KMENLDSLLYQ-------ADIDGSTLLHMAVE-----SGVTEIVA 252
Cdd:TIGR00870 160 gDFFVKSQgvdsFYH---------GESPLNAAAClGSPSIVALLSEdpadiltADSLGNTLLHLLVMenefkAEYEELSC 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2257803366 253 LC----LNHGARVREPKD-KHSP-----SAFHLACAQGSVKMVKLMVE 290
Cdd:TIGR00870 231 QMynfaLSLLDKLRDSKElEVILnhqglTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
213-379 1.70e-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: 41.22  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 213 IFSIAKAKmENLD--SLL--YQADID-GSTLLHMAVEsGVTEIVALCLNHgarvREPKDKHSPSAFHLacaqgsvkmvkl 287
Cdd:TIGR00870  56 LFVAAIEN-ENLEltELLlnLSCRGAvGDTLLHAISL-EYVDAVEAILLH----LLAAFRKSGPLELA------------ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 288 mveKDPVICRITLidrdGMSPLHRAAANNQTNIVEFLLDQGAQVDLtdKTHC----------------TPLFMAASNGAT 351
Cdd:TIGR00870 118 ---NDQYTSEFTP----GITALHLAAHRQNYEIVKLLLERGASVPA--RACGdffvksqgvdsfyhgeSPLNAAACLGSP 188
                         170       180
                  ....*....|....*....|....*...
gi 2257803366 352 ETVKLLMSRGANVTSKNVAMESVLHAAV 379
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
93-122 9.72e-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: 33.72  E-value: 9.72e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2257803366   93 YGKTPLHHATTGKRIEFVEFLLSRGAELTK 122
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-267 3.33e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 3.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 145 TLVSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAKmenl 224
Cdd:COG0666   171 LLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL---- 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2257803366 225 dsllYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREPKDK 267
Cdd:COG0666   246 ----NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
67-291 2.55e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 2.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  67 AAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTL 146
Cdd:COG0666    60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 147 VSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSiAKAKMENLDS 226
Cdd:COG0666   140 LEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDN 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 227 llyqadiDGSTLLHMAVESGVTEIVALCLNHGARVrEPKDKHSPSAFHLACAQGSVKMVKLMVEK 291
Cdd:COG0666   218 -------DGKTALDLAAENGNLEIVKLLLEAGADL-NAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
142-441 1.99e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 1.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 142 IVKTLVSNEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNtaeyifsIAKAKM 221
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDL-------LVALLL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 222 ENLDSLLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVrEPKDKHSPSAFHLACAQGSVKMVKLMVEKDPvicRITLI 301
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGA---DVNAQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 302 DRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV-- 379
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAen 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257803366 380 GHMRTTEALLNgsgAAYLIPEQDRDGYAPIHRAARGGYLQNIHLFITKNKAAAGITADSLDT 441
Cdd:COG0666   230 GNLEIVKLLLE---AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-368 6.69e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 6.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 145 TLVSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPlghavekgakntaeyifsiakakmenl 224
Cdd:COG0666   105 LLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP--------------------------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 225 dsllyqadidgstlLHMAVESGVTEIVALCLNHGARVrEPKDKHSPSAFHLACAQGSVKMVKLMVEKDPvicRITLIDRD 304
Cdd:COG0666   157 --------------LHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKLLLEAGA---DVNAKDND 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257803366 305 GMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKN 368
Cdd:COG0666   219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-381 4.90e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 4.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  78 IKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTLVSNEKCNVNAK 157
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 158 GRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAkntaeyifsiakakmenldsllyqadidgst 237
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN------------------------------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 238 llhmavesgvTEIVALCLNHGARVrEPKDKHSPSAFHLACAQGSVKMVKLMVEKDPvicRITLIDRDGMSPLHRAAANNQ 317
Cdd:COG0666   133 ----------LEIVKLLLEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGH 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2257803366 318 TNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAVGH 381
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
216-531 3.19e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 3.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 216 IAKAKMENLDSLLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREPKDKHSPSAFHLACAQGSVKMVKLMVEKDPVI 295
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 296 criTLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTsknvamesvl 375
Cdd:COG0666    81 ---NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN---------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 376 haavghmrtteallngsgaaylipEQDRDGYAPIHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIV 455
Cdd:COG0666   148 ------------------------AQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 456 DdLLVGRNVRmINLKNNHGKTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLAAITGSKRCVECILIKHPD 531
Cdd:COG0666   203 K-LLLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-474 1.01e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 184 EARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAKMENLDSLLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVrE 263
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI-N 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 264 PKDKHSPSAFHLACAQGSVKMVKLMVEKDPvicRITLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLF 343
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGA---DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 344 MAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV--GHMRTTEALLNgSGAAYLIpeQDRDGYAPIHRAARGGYLQNI 421
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAenGHLEIVKLLLE-AGADVNA--KDNDGKTALDLAAENGNLEIV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2257803366 422 HLFITKNKAAAGITADSLDTPLHVACKFGWLEIVDDLLVGRNVRMINLKNNHG 474
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-228 1.28e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 145 TLVSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAKMENL 224
Cdd:COG0666   204 LLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282

                  ....
gi 2257803366 225 DSLL 228
Cdd:COG0666   283 LDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
79-360 6.65e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.56  E-value: 6.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  79 KLLDKGVDINCADEYGKTPLH---HATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEA-IVKTLVSNeKCNV 154
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA-GADV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 155 NAKGRGLCTPLHI-ACGMD-KLKICKLLIEHEARIDLKDEDKMTPLgHAVEKGAKNTAEYIFSIAKAkmenlDSLLYQAD 232
Cdd:PHA03095  111 NAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL-AVLLKSRNANVELLRLLIDA-----GADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 233 IDGSTLLHMAVESG------VTEIVALCLNHGARvrepkDKHSPSAFHLACAQGSVKMVKLmvekDPVICRITLID---R 303
Cdd:PHA03095  185 DRFRSLLHHHLQSFkprariVRELIRAGCDPAAT-----DMLGNTPLHSMATGSSCKRSLV----LPLLIAGISINarnR 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 304 DGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSR 360
Cdd:PHA03095  256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
212-531 2.60e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.02  E-value: 2.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 212 YIFSIAKAKMENLDSLL------YQADIDGSTLLHMAVESG---VTEIVALCLNHGARVrEPKDKHSPSAFHL-ACAQGS 281
Cdd:PHA03095   18 YLLNASNVTVEEVRRLLaagadvNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADV-NAPERCGFTPLHLyLYNATT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 282 VKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTN--IVEFLLDQGAQVDLTDKTHCTPL--FMAASNGATETVKLL 357
Cdd:PHA03095   97 LDVIKLLIKAG---ADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 358 MSRGANVTSKNVAMESVLHAAVGHMRTTEALLNGSGAAYLIPE-QDRDGYAPIHRAARGGYLQNIHLFitkNKAAAGITa 436
Cdd:PHA03095  174 IDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAaTDMLGNTPLHSMATGSSCKRSLVL---PLLIAGIS- 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 437 dsldtplhvackfgwleivddllvgrnvrmINLKNNHGKTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLAAI 515
Cdd:PHA03095  250 ------------------------------INARNRYGQTPLHYAAVFNNPRACRRLIALGADINaVSSDGNTPLSLMVR 299
                         330
                  ....*....|....*.
gi 2257803366 516 TGSKRCVECILIKHPD 531
Cdd:PHA03095  300 NNNGRAVRAALAKNPS 315
PHA03100 PHA03100
ankyrin repeat protein; Provisional
129-364 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.65  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 129 TPLHAAVRTGDEAIVKTLVsNEKCNVNAKGRGLCTPLHIACGM-----DKLKICKLLIEHEARIDLKDEDKMTPLGHAVE 203
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILL-DNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 204 K--GAKNTAEYIFSIAkAKMENLDSllyqadiDGSTLLHMAVESGV--TEIVALCLNHGARVREpKDKhspsafhlacaq 279
Cdd:PHA03100  116 KksNSYSIVEYLLDNG-ANVNIKNS-------DGENLLHLYLESNKidLKILKLLIDKGVDINA-KNR------------ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 280 gsvkmVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMS 359
Cdd:PHA03100  175 -----VNYLLSYG---VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                  ....*
gi 2257803366 360 RGANV 364
Cdd:PHA03100  247 NGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-191 2.48e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  98 LHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTLVSNEKCNVNAKGRglcTPLHIACGMDKLKIC 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2257803366 178 KLLIEHEARIDLKD 191
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-198 9.35e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 9.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2257803366 145 TLVSNEKcNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPL 198
Cdd:COG0666   237 LLLEAGA-DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
73-259 1.79e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.80  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  73 DKETAIKLLDKGVDINCADEYGKTPLHHATTGKR--IEFVEFLLSRGAELTKQDQRGDTPLHAAVR--TGDEAIVKTLVS 148
Cdd:PHA03100   85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLID 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 149 NeKCNVNAKGRglctplhiacgmdklkiCKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIfsiakakmenldsLL 228
Cdd:PHA03100  165 K-GVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL-------------LD 213
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2257803366 229 YQADI-----DGSTLLHMAVESGVTEIVALCLNHGA 259
Cdd:PHA03100  214 LGANPnlvnkYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02876 PHA02876
ankyrin repeat protein; Provisional
47-378 3.07e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.20  E-value: 3.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  47 DESEQPLKTTVEGTKQEQLCAAAYmgdketaikLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQR 126
Cdd:PHA02876  140 NESIEYMKLIKERIQQDELLIAEM---------LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 127 GDTPLHAAVRTGDEAIVKTLVSNeKCNVNAKGRGLCTplhiACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGA 206
Cdd:PHA02876  211 DLSVLECAVDSKNIDTIKAIIDN-RSNINKNDLSLLK----AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPS 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 207 kntaeyiFSIAKAKMENLDSLLYQADIDGSTLLHMAVESGV-TEIVALCLNHGARVrEPKDKHSPSAFHLACAqgsvkmv 285
Cdd:PHA02876  286 -------LSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV-NAADRLYITPLHQAST------- 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 286 kLMVEKDPVICRITL------IDRDGMSPLHRAAANNQTNIVEFLLDQGAQVD-LTDKTHCTPLFMAASNGATETVKLLM 358
Cdd:PHA02876  351 -LDRNKDIVITLLELganvnaRDYCDKTPIHYAAVRNNVVIINTLLDYGADIEaLSQKIGTALHFALCGTNPYMSVKTLI 429
                         330       340
                  ....*....|....*....|
gi 2257803366 359 SRGANVTSKNVAMESVLHAA 378
Cdd:PHA02876  430 DRGANVNSKNKDLSTPLHYA 449
PHA03100 PHA03100
ankyrin repeat protein; Provisional
264-501 1.60e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 264 PKDKHSPSAFHLACAQGSVKMVKLMVEKDpviCRITLIDRDGMSPLH-----RAAANNQTNIVEFLLDQGAQVDLTDKTH 338
Cdd:PHA03100   30 YSYKKPVLPLYLAKEARNIDVVKILLDNG---ADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 339 CTPLFMAASN--GATETVKLLMSRGANVTSKNVAMESVLHAAVGHMRTT----EALL-NGSGaaylIPEQDRdgyapihr 411
Cdd:PHA03100  107 ITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkilKLLIdKGVD----INAKNR-------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 412 aarggylqnIHLFITKnkaaaGITADSLD----TPLHVACKFGWLEIVDDLL-VGRNvrmINLKNNHGKTPLHFAAGEGH 486
Cdd:PHA03100  175 ---------VNYLLSY-----GVPINIKDvygfTPLHYAVYNNNPEFVKYLLdLGAN---PNLVNKYGDTPLHIAILNNN 237
                         250
                  ....*....|....*
gi 2257803366 487 DKVVELLLDRGATID 501
Cdd:PHA03100  238 KEIFKLLLNNGPSIK 252
PHA02874 PHA02874
ankyrin repeat protein; Provisional
131-449 2.79e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 2.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 131 LHAAVRTGDEAIVKTLVSNEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNta 210
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 211 eyifsIAKakmenldsLLYQADIDGSTLLHMAVESgvtEIVALCLNHGARVrEPKDKHSPSAFHLACAQGSVKMVKLMVE 290
Cdd:PHA02874   83 -----IIK--------LLIDNGVDTSILPIPCIEK---DMIKTILDCGIDV-NIKDAELKTFLHYAIKKGDLESIKMLFE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 291 KDpviCRITLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVA 370
Cdd:PHA02874  146 YG---ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2257803366 371 MESVLHAAVGHMRTTEALLNGSGAaylIPEQDRDGYAPIHRAARGGYLQNIHLFITKNKAAAGITADSLDTPLHVACKF 449
Cdd:PHA02874  223 GFTPLHNAIIHNRSAIELLINNAS---INDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-368 3.07e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 273 FHLACAQGSVKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTNIVEFLLDQgAQVDLTDKTHcTPLFMAASNGATE 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG---ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 2257803366 353 TVKLLMSRGANVTSKN 368
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
163-363 2.33e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 2.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 163 TPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAkmenLDSLLYQadiDGSTLLHMA 242
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKF----ADDVFYK---DGMTPLHLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 243 VESGVTEIVALCLNHGARVREPK-DKHSPsaFHLACAQGSVKMVKLMVEKDPVIcriTLIDRDGMSPLHRAAANNQTNIV 321
Cdd:PHA02875  110 TILKKLDIMKLLIARGADPDIPNtDKFSP--LHLAVMMGDIKGIELLIDHKACL---DIEDCCGCTPLIIAMAKGDIAIC 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2257803366 322 EFLLDQGAQVDLTDKTHC-TPLFMAASNGATETVKLLMSRGAN 363
Cdd:PHA02875  185 KMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA03100 PHA03100
ankyrin repeat protein; Provisional
173-379 2.70e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 173 KLKICKLLIEHEARIDLKDEDKMTPLGHAVEKgakntaeyifsiakAKMENLDSLLYQ-ADIDG-----STLLH-----M 241
Cdd:PHA03100   14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEA--------------RNIDVVKILLDNgADINSstknnSTPLHylsniK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 242 AVESGVTEIVALCLNHGARVREPKDKHSPSAFHLACAQ-GSVKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQ--T 318
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNG---ANVNIKNSDGENLLHLYLESNKidL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 319 NIVEFLLDQGAQVDLTDKTHC----------------TPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV 379
Cdd:PHA03100  157 KILKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
409-502 1.15e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 409 IHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIVDDLLVGRNVRMinlkNNHGKTPLHFAAGEGHDK 488
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLE 75
                          90
                  ....*....|....
gi 2257803366 489 VVELLLDRGATIDR 502
Cdd:pfam12796  76 IVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
64-190 1.79e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.77  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  64 QLCAAAYMGDKETAIK--LLDKGVDINCADEY-GKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDE 140
Cdd:PHA02878  135 YIDKKSKDDIIEAEITklLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNK 214
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2257803366 141 AIVKTLVSNeKCNVNAKGRGLCTPLHIACGMDK-LKICKLLIEHEARIDLK 190
Cdd:PHA02878  215 PIVHILLEN-GASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAK 264
PHA02874 PHA02874
ankyrin repeat protein; Provisional
242-481 3.68e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 3.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 242 AVESGVTEIVALCLNHGARVREPKDKhSPSAFHLACAQGSVKMVKLMVEKD------PVIC--------------RITLI 301
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTK-IPHPLLTAIKIGAHDIIKLLIDNGvdtsilPIPCiekdmiktildcgiDVNIK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 302 DRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV-- 379
Cdd:PHA02874  121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAey 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 380 GHMRTTEALL-NGSGaaylIPEQDRDGYAPIHRAarggYLQN---IHLFItkNKAAAGITADSLDTPLHVACKFGW-LEI 454
Cdd:PHA02874  201 GDYACIKLLIdHGNH----IMNKCKNGFTPLHNA----IIHNrsaIELLI--NNASINDQDIDGSTPLHHAINPPCdIDI 270
                         250       260
                  ....*....|....*....|....*..
gi 2257803366 455 VDDLLVgrNVRMINLKNNHGKTPLHFA 481
Cdd:PHA02874  271 IDILLY--HKADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
73-261 3.91e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  73 DKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTLVSNeKC 152
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GA 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 153 NVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVekgakntaeyIFSIAKAKMENLDSLLYQAD 232
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI----------IHNRSAIELLINNASINDQD 251
                         170       180       190
                  ....*....|....*....|....*....|
gi 2257803366 233 IDGSTLLHMAVESGVT-EIVALCLNHGARV 261
Cdd:PHA02874  252 IDGSTPLHHAINPPCDiDIIDILLYHKADI 281
PHA02878 PHA02878
ankyrin repeat protein; Provisional
130-448 4.83e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.61  E-value: 4.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 130 PLHAAVRTGDEAIVKTLVSNEKcNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKmtplghavekgAKNT 209
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGH-NVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLV-----------AIKD 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 210 AEYIFSIAKAKMENLDSLLYQADIDGSTLLHMAVESGV-TEIVALCLNHGARVREpKDKHSpsafhlacaqgsvkmvklm 288
Cdd:PHA02878  108 AFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIeAEITKLLLSYGADINM-KDRHK------------------- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 289 vekdpvicritlidrdGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKN 368
Cdd:PHA02878  168 ----------------GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 369 VAMESVLHAAVGHMRTTEAL--LNGSGAAYLIPEQDRdGYAPIHRAARGGYLQNIHLfitKNKAAAGITADSLDTPLHVA 446
Cdd:PHA02878  232 KCGNTPLHISVGYCKDYDILklLLEHGVDVNAKSYIL-GLTALHSSIKSERKLKLLL---EYGADINSLNSYKLTPLSSA 307

                  ..
gi 2257803366 447 CK 448
Cdd:PHA02878  308 VK 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-157 6.90e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAelTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2257803366 145 TLVSNEkCNVNAK 157
Cdd:pfam12796  79 LLLEKG-ADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
106-365 7.22e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 7.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 106 RIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTG---DEAIVKTLVsNEKCNVNAKGRGLCTPLHI-ACGMDKLKICKLLI 181
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLL-EAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 182 EHEARIDLKDEDKMTPLgHAVEKGaKNTAEYIFSIAKAKMENLDSLlyqaDIDGSTLLHMAVES-GVT-EIVALCLNHGA 259
Cdd:PHA03095  105 KAGADVNAKDKVGRTPL-HVYLSG-FNINPKVIRLLLRKGADVNAL----DLYGMTPLAVLLKSrNANvELLRLLIDAGA 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 260 RVREPKDKHSpSAFHLACaQGSVKMVKLMVEKDPVICRITLIDRDGMSPLHRAAANNQTN--IVEFLLDQGAQVDLTDKT 337
Cdd:PHA03095  179 DVYAVDDRFR-SLLHHHL-QSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY 256
                         250       260
                  ....*....|....*....|....*...
gi 2257803366 338 HCTPLFMAASNGATETVKLLMSRGANVT 365
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGADIN 284
PHA02874 PHA02874
ankyrin repeat protein; Provisional
72-203 7.38e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 7.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  72 GDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTLVSNEK 151
Cdd:PHA02874  135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2257803366 152 CNVNAKGRGLcTPLHIACGMDKLKIcKLLIeHEARIDLKDEDKMTPLGHAVE 203
Cdd:PHA02874  215 HIMNKCKNGF-TPLHNAIIHNRSAI-ELLI-NNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
70-389 7.72e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 7.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  70 YMGDKETAIKLLDKgvdINCADEYGKT-------PLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAI 142
Cdd:PHA02878    9 YTDNYETILKYIEY---IDHTENYSTSaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 143 VKTLVSNE-KCNVNAKGRGLCTplhiACGMDKLKICKLLI----EHEARIDLKDedkmtplghavekgakntaeyifsia 217
Cdd:PHA02878   86 MKEMIRSInKCSVFYTLVAIKD----AFNNRNVEIFKIILtnryKNIQTIDLVY-------------------------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 218 kakmenLDSLLYQADIDgstllhmavesgvTEIVALCLNHGARVREpKDKHS-PSAFHLACAQGSVKMVKLMVEKDpviC 296
Cdd:PHA02878  136 ------IDKKSKDDIIE-------------AEITKLLLSYGADINM-KDRHKgNTALHYATENKDQRLTELLLSYG---A 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 297 RITLIDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGAT-ETVKLLMSRGANVTSKNVAME-SV 374
Cdd:PHA02878  193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYILGlTA 272
                         330
                  ....*....|....*
gi 2257803366 375 LHAAVGHMRTTEALL 389
Cdd:PHA02878  273 LHSSIKSERKLKLLL 287
PHA02876 PHA02876
ankyrin repeat protein; Provisional
172-501 1.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.03  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 172 DKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGakntaeyifsiaKAKMENLdSLLYQADI-----DGSTLLHMAVESG 246
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERG------------NAKMVNL-LLSYGADVniialDDLSVLECAVDSK 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 247 VTEIVALCLNHgarvREPKDKHSPSAFHlACAQGSVKMVKLMVEKDpviCRITLIDRDGMSPLHRAA-ANNQTNIVEFLL 325
Cdd:PHA02876  223 NIDTIKAIIDN----RSNINKNDLSLLK-AIRNEDLETSLLLYDAG---FSVNSIDDCKNTPLHHASqAPSLSRLVPKLL 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 326 DQGAQVDLTDKTHCTPLFMAASNG-ATETVKLLMSRGANVTSKNVAMESVLHAAVGHMRTTEALLNGSGAAYLIPEQDRD 404
Cdd:PHA02876  295 ERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYC 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 405 GYAPIHRAArggYLQNIHLFITKNKAAAGITADS--LDTPLHVA-CKFGWLEIVDDLL-VGRNVrmiNLKNNHGKTPLHF 480
Cdd:PHA02876  375 DKTPIHYAA---VRNNVVIINTLLDYGADIEALSqkIGTALHFAlCGTNPYMSVKTLIdRGANV---NSKNKDLSTPLHY 448
                         330       340
                  ....*....|....*....|..
gi 2257803366 481 AAGEG-HDKVVELLLDRGATID 501
Cdd:PHA02876  449 ACKKNcKLDVIEMLLDNGADVN 470
Ank_2 pfam12796
Ankyrin repeats (3 copies);
239-335 1.74e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 239 LHMAVESGVTEIVALCLNHGARVREpKDKHSPSAFHLACAQGSVKMVKLMVEKDPVicritLIDRDGMSPLHRAAANNQT 318
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLEHADV-----NLKDNGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 2257803366 319 NIVEFLLDQGAQVDLTD 335
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
74-203 7.42e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 7.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  74 KETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAV-RTGDEAIVKTLVsNEKC 152
Cdd:PHA02876  355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcGTNPYMSVKTLI-DRGA 433
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2257803366 153 NVNAKGRGLCTPLHIACGMD-KLKICKLLIEHEARIDLKDEDKMTPLGHAVE 203
Cdd:PHA02876  434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485
Ank_2 pfam12796
Ankyrin repeats (3 copies);
443-537 8.86e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 8.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 443 LHVACKFGWLEIVDDLLVGRNVrmINLKNNHGKTPLHFAAGEGHDKVVELLLDRgATIDRDHTERTPLHLAAITGSKRCV 522
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD--ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....*
gi 2257803366 523 EcILIKHPDCLNSVD 537
Cdd:pfam12796  78 K-LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
250-513 1.87e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 250 IVALCLNHGARVrEPKDKHSPSAFHLACAQGSVKMVKLMVEKDPVICRITLidrDGMSPLHRAAANNQTNIVEFLLDQGA 329
Cdd:PHA02876  160 IAEMLLEGGADV-NAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL---DDLSVLECAVDSKNIDTIKAIIDNRS 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 330 QVDLTDKThctpLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV---GHMRTTEALLNgSGAAylIPEQDRDGY 406
Cdd:PHA02876  236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqapSLSRLVPKLLE-RGAD--VNAKNIKGE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 407 APIHRAARGGY-LQNIHLFITKnkAAAGITADSL-DTPLHVACKFG-WLEIVDDLL-VGRNVrmiNLKNNHGKTPLHFAA 482
Cdd:PHA02876  309 TPLYLMAKNGYdTENIRTLIML--GADVNAADRLyITPLHQASTLDrNKDIVITLLeLGANV---NARDYCDKTPIHYAA 383
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2257803366 483 GEGHDKVVELLLDRGATIDR-DHTERTPLHLA 513
Cdd:PHA02876  384 VRNNVVIINTLLDYGADIEAlSQKIGTALHFA 415
PHA02874 PHA02874
ankyrin repeat protein; Provisional
307-515 2.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 307 SPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVtsknvameSVLHAAVGHMRTTE 386
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT--------SILPIPCIEKDMIK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 387 ALLNgSGAAYLIpeQDRDGYAPIHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIVDDLLvgRNVRM 466
Cdd:PHA02874  109 TILD-CGIDVNI--KDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL--EKGAY 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257803366 467 INLKNNHGKTPLHFAAGEGHDKVVELLLDRGATI-DRDHTERTPLHLAAI 515
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHImNKCKNGFTPLHNAII 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
312-501 7.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 312 AAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV--GHMRTTEALL 389
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeeGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 390 NGSgaAYLIPEQDRDGYAPIHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIVDDLLVGRNVrmINL 469
Cdd:PHA02875   89 DLG--KFADDVFYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC--LDI 163
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2257803366 470 KNNHGKTPLHFAAGEGHDKVVELLLDRGATID 501
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
64-160 4.49e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 68.77  E-value: 4.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  64 QLCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIV 143
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164
                          90
                  ....*....|....*..
gi 2257803366 144 KTLVSNEKCNVNAKGRG 160
Cdd:PTZ00322  165 QLLSRHSQCHFELGANA 181
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-390 1.02e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 309 LHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRG-ANVTSKNvamESVLHAAV--GHMRTT 385
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAdVNLKDNG---RTALHYAArsGHLEIV 77

                  ....*
gi 2257803366 386 EALLN 390
Cdd:pfam12796  78 KLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
165-261 3.25e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 165 LHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIFSIAKAKMENldsllyqadiDGSTLLHMAVE 244
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----------NGRTALHYAAR 70
                          90
                  ....*....|....*..
gi 2257803366 245 SGVTEIVALCLNHGARV 261
Cdd:pfam12796  71 SGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
30-192 3.26e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  30 VELVMVNGKAKEADldDDESEQPLkttvegtkqeQLCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEF 109
Cdd:PHA03100   89 VKLLLEYGANVNAP--DNNGITPL----------LYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 110 --VEFLLSRGAELTKQ----------------DQRGDTPLHAAVRTGDEAIVKTLVsNEKCNVNAKGRGLCTPLHIACGM 171
Cdd:PHA03100  157 kiLKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILN 235
                         170       180
                  ....*....|....*....|.
gi 2257803366 172 DKLKICKLLIEHEARIDLKDE 192
Cdd:PHA03100  236 NNKEIFKLLLNNGPSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
306-514 2.25e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 306 MSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAVG--HMR 383
Cdd:PHA02876  146 MKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDskNID 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 384 TTEALLNGSGAaylIPEQDrdgyAPIHRAARGGYLQNIHLFITknkaaAGITADSLD----TPLHVACKFGWLEIVDDLL 459
Cdd:PHA02876  226 TIKAIIDNRSN---INKND----LSLLKAIRNEDLETSLLLYD-----AGFSVNSIDdcknTPLHHASQAPSLSRLVPKL 293
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 460 VGRNVRmINLKNNHGKTPLHFAAGEGHD-KVVELLLDRGATID-RDHTERTPLHLAA 514
Cdd:PHA02876  294 LERGAD-VNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNaADRLYITPLHQAS 349
PHA02875 PHA02875
ankyrin repeat protein; Provisional
62-259 2.56e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  62 QEQLCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGA-----------ELTKQDQRGD-- 128
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipdvkypdiesELHDAVEEGDvk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 129 ---------------------TPLHAAVRTGDEAIVKTLVSnEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARI 187
Cdd:PHA02875   83 aveelldlgkfaddvfykdgmTPLHLATILKKLDIMKLLIA-RGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2257803366 188 DLKDEDKMTPLGHAVEKGakNTAeyifsIAKAKMENLDSLLYQADIDGSTLLHMAVESGVTEIVALCLNHGA 259
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKG--DIA-----ICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
404-537 1.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 404 DGYAPIHRAARGGYLQNIHLFITKNkAAAGITADSLDTPLHVACKFGWLEIVDDLL-VGRNVRMINLKNnhGKTPLHFAA 482
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHG-AIPDVKYPDIESELHDAVEEGDVKAVEELLdLGKFADDVFYKD--GMTPLHLAT 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2257803366 483 GEGHDKVVELLLDRGATIDRDHTER-TPLHLAAITGSKRCVEcILIKHPDCLNSVD 537
Cdd:PHA02875  111 ILKKLDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDIKGIE-LLIDHKACLDIED 165
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
264-359 1.84e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 264 PKDKHSPSAFHLAcaqgSVKMVKLMVEKDPVICRITL--------IDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTD 335
Cdd:PTZ00322   70 TEEVIDPVVAHML----TVELCQLAASGDAVGARILLtggadpncRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
                          90       100
                  ....*....|....*....|....
gi 2257803366 336 KTHCTPLFMAASNGATETVKLLMS 359
Cdd:PTZ00322  146 KDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
305-357 1.94e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2257803366 305 GMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLL 357
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
65-114 4.24e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.24e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLL 114
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
65-124 1.56e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKgVDINCADeYGKTPLHHATTGKRIEFVEFLLSRGAELTKQD 124
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
308-534 2.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 308 PLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSrgaNVTSKNVAMESVLHAAVGHMRTTEA 387
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR---SINKCSVFYTLVAIKDAFNNRNVEI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 388 ----LLNgsgaaYLIPEQDRDgyapIHRAARGGYLQNIHLFITKNKAAAG-----ITADSLDTPLHVACKFGWLEIVDDL 458
Cdd:PHA02878  117 fkiiLTN-----RYKNIQTID----LVYIDKKSKDDIIEAEITKLLLSYGadinmKDRHKGNTALHYATENKDQRLTELL 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257803366 459 LV-GRNVRMINLKNNhgkTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLAAITGSKRCVECILIKHPDCLN 534
Cdd:PHA02878  188 LSyGANVNIPDKTNN---SPLHHAVKHYNKPIVHILLENGASTDaRDKCGNTPLHISVGYCKDYDILKLLLEHGVDVN 262
PHA02874 PHA02874
ankyrin repeat protein; Provisional
340-526 3.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 340 TPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV---GHMRTTEALLNGSGAAYL-IPEQDRDgyaPIHRAARG 415
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIkigAHDIIKLLIDNGVDTSILpIPCIEKD---MIKTILDC 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 416 GYLQNihlfiTKNKaaagitadSLDTPLHVACKFGWLEIVDDLLVGRnvRMINLKNNHGKTPLHFAAGEGHDKVVELLLD 495
Cdd:PHA02874  114 GIDVN-----IKDA--------ELKTFLHYAIKKGDLESIKMLFEYG--ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2257803366 496 RGATID-RDHTERTPLHLAAITGSKRCVECIL 526
Cdd:PHA02874  179 KGAYANvKDNNGESPLHNAAEYGDYACIKLLI 210
Ank_4 pfam13637
Ankyrin repeats (many copies);
96-147 3.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 3.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2257803366  96 TPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKTLV 147
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
227-424 3.70e-07

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: 53.09  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 227 LLYQADIDGSTLLHMAVESGVTEIVALCLNHGARVREpKDKHSPSAFHLACAQGSVKMVKLMVEKDPVICR--ITLIDRD 304
Cdd:cd22192    10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQ-RGALGETALHVAALYDNLEAAVVLMEAAPELVNepMTSDLYQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 305 GMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKT--------HCT------PLFMAASNGATETVKLLMSRGANVTSKNVA 370
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 371 MESVLHAAVGHMRTTEA------LLN-----GSGAAYLIPeqDRDGYAPIHRAARGGylqNIHLF 424
Cdd:cd22192   169 GNTVLHILVLQPNKTFAcqmydlILSydkedDLQPLDLVP--NNQGLTPFKLAAKEG---NIVMF 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
312-544 8.50e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 8.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 312 AAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV--GHMRTTEALL 389
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIsaKHHKIFRILY 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 390 NGSGAAylipeqdrdgyapihraarggylqnihlfitkNKAAAGitaDSLDTplhvACKFGWLEIVDDLL-VGRNVrmiN 468
Cdd:PLN03192  612 HFASIS--------------------------------DPHAAG---DLLCT----AAKRNDLTAMKELLkQGLNV---D 649
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257803366 469 LKNNHGKTPLHFAAGEGHDKVVELLLDRGATIDRDHT--ERTPLHLAAITGSKRCVECILIkhPDCLNSVDEDQVRKG 544
Cdd:PLN03192  650 SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTddDFSPTELRELLQKRELGHSITI--VDSVPADEPDLGRDG 725
Ank_4 pfam13637
Ankyrin repeats (many copies);
271-325 1.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 271 SAFHLACAQGSVKMVKLMVEKDPVICRItliDRDGMSPLHRAAANNQTNIVEFLL 325
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV---DGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
340-519 1.10e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 340 TPLFMAASNGATETVK-LLMSRGANVTSKNVAMESVLHAAV--GHMRTTEALLNGsgAAYLIPEQdrdgyapihraargg 416
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAVVLMEA--APELVNEP--------------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 417 ylqnihlfitknkaaagITADSL--DTPLHVACKFGWLEIVDDLLvGRNVRMIN--------LKNNH-----GKTPLHFA 481
Cdd:cd22192    82 -----------------MTSDLYqgETALHIAVVNQNLNLVRELI-ARGADVVSpratgtffRPGPKnliyyGEHPLSFA 143
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2257803366 482 AGEGHDKVVELLLDRGATI-DRDHTERTPLHLAAITGSK 519
Cdd:cd22192   144 ACVGNEEIVRLLIEHGADIrAQDSLGNTVLHILVLQPNK 182
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
123-360 1.27e-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: 51.17  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 123 QDQRG-DTPLHAAVRTGDEAIVKTLVSNEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEhEARiDLKDEdKMTplgha 201
Cdd:cd22192    12 QQKRIsESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAP-ELVNE-PMT----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 202 vekgakntaeyifsiakakmenldSLLYQadidGSTLLHMAVESGVTEIVALCLNHGARVREP--------KDKHS---- 269
Cdd:cd22192    84 ------------------------SDLYQ----GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyy 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 270 ---PSAFhlACAQGSVKMVKLMVEKDpviCRITLIDRDGMSPLHRAAANNQTNIV----EFLLDQGAQVD------LTDK 336
Cdd:cd22192   136 gehPLSF--AACVGNEEIVRLLIEHG---ADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNN 210
                         250       260
                  ....*....|....*....|....
gi 2257803366 337 THCTPLFMAASNGATETVKLLMSR 360
Cdd:cd22192   211 QGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
476-526 1.45e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2257803366 476 TPLHFAAGEGHDKVVELLLDRGATIDR-DHTERTPLHLAAITGSKRCVECIL 526
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAvDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
68-250 3.85e-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: 3.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  68 AAYMGDKETAIKLLD-KGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAEL-----TKQDQRGDTPLHAAVRTGDEA 141
Cdd:cd22192    24 AAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVVNQNLN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 142 IVKTLVSNEKCNVNAKGRGLC-------------TPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKN 208
Cdd:cd22192   104 LVRELIARGADVVSPRATGTFfrpgpknliyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKT 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2257803366 209 TAEYIFSI--AKAKMENLDSLLYQADIDGSTLLHMAVESGVTEI 250
Cdd:cd22192   184 FACQMYDLilSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVM 227
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
80-195 5.62e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.37  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  80 LLDKGVDIN-CA----------DE---YGKTPLHHATTGKRIEFVEFLLSRGAE-LTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:cd22194   160 LIAKGADVNaHAkgvffnpkykHEgfyFGETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVTVAEDSKTQ 239
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 145 T----------LVSNEKCNV----NAKGrglCTPLHIACGMDKLKICKLLIEHEaridLKDEDKM 195
Cdd:cd22194   240 NdfvkrmydmiLLKSENKNLetirNNEG---LTPLQLAAKMGKAEILKYILSRE----IKEKPNR 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
163-212 6.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2257803366 163 TPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEY 212
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
172-368 8.09e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 8.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 172 DKLKICKLLIEHEARI-DLKDEDKMtplghaVEKGAKNTAEYIFS--IAKAKMEN---LDSLL---YQADI---DGSTLL 239
Cdd:PLN03192  489 DNVVILKNFLQHHKELhDLNVGDLL------GDNGGEHDDPNMASnlLTVASTGNaalLEELLkakLDPDIgdsKGRTPL 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 240 HMAVESGVTEIVALCLNHGARVrepkdkhspsafHLACAQGSVKMVKLMVEKDPVICRITLIDRDGMSP------LHRAA 313
Cdd:PLN03192  563 HIAASKGYEDCVLVLLKHACNV------------HIRDANGNTALWNAISAKHHKIFRILYHFASISDPhaagdlLCTAA 630
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 314 ANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMAASNGATETVKLLMSRGANVTSKN 368
Cdd:PLN03192  631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02736 PHA02736
Viral ankyrin protein; Provisional
107-188 1.33e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 45.25  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 107 IEFVEFLLSRGAELTKQDQR-GDTPLHAAVRTGDEAIVKTLVSNEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEA 185
Cdd:PHA02736   71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150

                  ...
gi 2257803366 186 RID 188
Cdd:PHA02736  151 QCK 153
PHA03095 PHA03095
ankyrin-like protein; Provisional
78-145 1.54e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 1.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2257803366  78 IKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVKT 145
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA02946 PHA02946
ankyin-like protein; Provisional
69-358 2.20e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  69 AYMG----DKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAI-- 142
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 143 VKTLVS-NEKCNVNAKGRGlCTPLhIACGMDKLKICK--LLIEHEARIdlkdedkmtplghaVEKGAKNTAEYIFSIAKA 219
Cdd:PHA02946  123 INLLVQyGAKINNSVDEEG-CGPL-LACTDPSERVFKkiMSIGFEARI--------------VDKFGKNHIHRHLMSDNP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 220 KMENLDSLL------YQADIDGSTLLHMAVESGV--TEIVALCLNHGARVREPKDKHSPSAFHLACAQGSVKMVKLM--- 288
Cdd:PHA02946  187 KASTISWMMklgispSKPDHDGNTPLHIVCSKTVknVDIINLLLPSTDVNKQNKFGDSPLTLLIKTLSPAHLINKLLsts 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2257803366 289 -VEKDPVICRITLIDRDgmsplhraaannqtNIVEFLLDQGAQVDLTDkthctpLFMAASNGATETVKLLM 358
Cdd:PHA02946  267 nVITDQTVNICIFYDRD--------------DVLEIINDKGKQYDSTD------FKMAVEVGSIRCVKYLL 317
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
65-213 2.25e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAAVRTGDEAIVK 144
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 145 TLVS-NEKCNVNAKGRGLCTplhiACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYI 213
Cdd:PLN03192  609 ILYHfASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
441-494 2.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2257803366 441 TPLHVACKFGWLEIVDdLLVGRNVRmINLKNNHGKTPLHFAAGEGHDKVVELLL 494
Cdd:pfam13637   3 TALHAAAASGHLELLR-LLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
468-537 4.00e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 4.00e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2257803366 468 NLKNNHGKTPLHFAAGEGHDKVVELLLDRGA---TIDRDhtERTPLHLAAITGSKRCVEcILIKHPDCLNSVD 537
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGAdptLLDKD--GKTPLELAEENGFREVVQ-LLSRHSQCHFELG 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
68-151 4.21e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 4.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  68 AAYMGDKETAIKLLDKGVDINCADEYGKTPLHH----ATTGKRIEFVEFLLSRGAELTKQ------DQRGDTPLHAAVRT 137
Cdd:cd22192   143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKE 222
                          90
                  ....*....|....
gi 2257803366 138 GDEAIVKTLVSNEK 151
Cdd:cd22192   223 GNIVMFQHLVQKRR 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
80-134 4.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 4.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2257803366  80 LLDKG-VDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGDTPLHAA 134
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
127-181 4.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 4.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 127 GDTPLHAAVRTGDEAIVKTLVSNeKCNVNAKGRGLCTPLHIACGMDKLKICKLLI 181
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
288-345 4.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 4.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2257803366 288 MVEKDPVICRITliDRDGMSPLHRAAANNQTNIVEFLLDQGAQVDLTDKTHCTPLFMA 345
Cdd:pfam13857   1 LLEHGPIDLNRL--DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
473-501 6.80e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 6.80e-05
                           10        20
                   ....*....|....*....|....*....
gi 2257803366  473 HGKTPLHFAAGEGHDKVVELLLDRGATID 501
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
473-501 8.28e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 8.28e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2257803366 473 HGKTPLHFAAGE-GHDKVVELLLDRGATID 501
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
235-289 1.51e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 235 GSTLLHMAVESGVTEIVALCLNHGARVREpKDKHSPSAFHLACAQGSVKMVKLMV 289
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
339-526 1.62e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 339 CTPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAVGHMrtteallNGSGAAYLIPEQDRDGYAPIHRAARGG-Y 417
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEP-------NKLGMKEMIRSINKCSVFYTLVAIKDAfN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 418 LQNIHLF--ITKNKAAAGITADsldtpLHVACKFGWLEIVDDLLV------GRNVRMINlkNNHGKTPLHFAAGEGHDKV 489
Cdd:PHA02878  111 NRNVEIFkiILTNRYKNIQTID-----LVYIDKKSKDDIIEAEITklllsyGADINMKD--RHKGNTALHYATENKDQRL 183
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2257803366 490 VELLLDRGATIDR-DHTERTPLHLAAITGSKRCVECIL 526
Cdd:PHA02878  184 TELLLSYGANVNIpDKTNNSPLHHAVKHYNKPIVHILL 221
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
137-215 2.02e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 137 TGDEAIVKTLVSN-EKCN-VNAKGRglcTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEYIF 214
Cdd:PTZ00322   92 SGDAVGARILLTGgADPNcRDYDGR---TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168

                  .
gi 2257803366 215 S 215
Cdd:PTZ00322  169 R 169
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
473-501 2.04e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.04e-04
                          10        20
                  ....*....|....*....|....*....
gi 2257803366 473 HGKTPLHFAAGEGHDKVVELLLDRGATID 501
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
304-336 2.06e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 38.81  E-value: 2.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2257803366 304 DGMSPLHRAAA-NNQTNIVEFLLDQGAQVDLTDK 336
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
305-427 3.60e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 305 GMSPLHRAAANNQTNIVEFLLDQGAQVDL---------TDKTHC-----TPLFMAASNGATETVKLLMSRGA-NVTSKNV 369
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeTPLALAACTNQPEIVQLLMEKEStDITSQDS 220
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2257803366 370 AMESVLHAAVGH-----------MRTTEALLNGSGAAYLIPEQDRDGYAPIHRAARGGYLQNIHLFITK 427
Cdd:cd22194   221 RGNTVLHALVTVaedsktqndfvKRMYDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
235-360 4.54e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 235 GSTLLHMAVESGVTEIVALCLNHGARVR--------EPKDKHS-----PSAFHLACAQGSVKMVKLMVEKDPVIcrITLI 301
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTD--ITSQ 218
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2257803366 302 DRDGMSPLH---RAAAN--NQTNIVEFLLDQ------GAQVD-LTDKTHCTPLFMAASNGATETVKLLMSR 360
Cdd:cd22194   219 DSRGNTVLHalvTVAEDskTQNDFVKRMYDMillkseNKNLEtIRNNEGLTPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
51-290 8.50e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  51 QPLKTTVEGTKQEQLCAAAYMGDKETAIKLLD--KGVDINCADEYGKTPLHHATTGKR----IEFVEFLLSRGAEltkqd 124
Cdd:TIGR00870   7 VPAEESPLSDEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENEnlelTELLLNLSCRGAV----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 125 qrGDTPLHAAVRT---GDEAIVKTLVSNEKCNVN---AKGRGLC------TPLHIACGMDKLKICKLLIEHEARIDLK-- 190
Cdd:TIGR00870  82 --GDTLLHAISLEyvdAVEAILLHLLAAFRKSGPlelANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARac 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 191 -DEDKMTP----LGHavekgakntAEYIFSIAKA-KMENLDSLLYQ-------ADIDGSTLLHMAVE-----SGVTEIVA 252
Cdd:TIGR00870 160 gDFFVKSQgvdsFYH---------GESPLNAAAClGSPSIVALLSEdpadiltADSLGNTLLHLLVMenefkAEYEELSC 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2257803366 253 LC----LNHGARVREPKD-KHSP-----SAFHLACAQGSVKMVKLMVE 290
Cdd:TIGR00870 231 QMynfaLSLLDKLRDSKElEVILnhqglTPLKLAAKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
441-481 9.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 9.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2257803366 441 TPLHVACKFGWLEIVDDLLVGRnvRMINLKNNHGKTPLHFA 481
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYG--VDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
68-172 1.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  68 AAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTKQDQRGD-TPLHAAVRTGDEAIVKTL 146
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLF 221
                          90       100
                  ....*....|....*....|....*...
gi 2257803366 147 VS-NEKCNVNAKGRG-LCTPLHIACGMD 172
Cdd:PHA02875  222 IKrGADCNIMFMIEGeECTILDMICNMC 249
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
304-332 1.15e-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: 36.47  E-value: 1.15e-03
                          10        20
                  ....*....|....*....|....*....
gi 2257803366 304 DGMSPLHRAAANNQTNIVEFLLDQGAQVD 332
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
146-201 1.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2257803366 146 LVSNEKCNVNAKGRGLCTPLHIACGMDKLKICKLLIEHEARIDLKDEDKMTPLGHA 201
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
213-379 1.70e-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: 41.22  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 213 IFSIAKAKmENLD--SLL--YQADID-GSTLLHMAVEsGVTEIVALCLNHgarvREPKDKHSPSAFHLacaqgsvkmvkl 287
Cdd:TIGR00870  56 LFVAAIEN-ENLEltELLlnLSCRGAvGDTLLHAISL-EYVDAVEAILLH----LLAAFRKSGPLELA------------ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 288 mveKDPVICRITLidrdGMSPLHRAAANNQTNIVEFLLDQGAQVDLtdKTHC----------------TPLFMAASNGAT 351
Cdd:TIGR00870 118 ---NDQYTSEFTP----GITALHLAAHRQNYEIVKLLLERGASVPA--RACGdffvksqgvdsfyhgeSPLNAAACLGSP 188
                         170       180
                  ....*....|....*....|....*...
gi 2257803366 352 ETVKLLMSRGANVTSKNVAMESVLHAAV 379
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
162-192 1.71e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 1.71e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2257803366 162 CTPLHIACGM-DKLKICKLLIEHEARIDLKDE 192
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
142-381 2.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 142 IVKTLVSNeKCNVNAKG---RGLCTPL---HIACGMDKlKICKLLIEHEARIDLKDEDKMTPLGHAVEKGAKNTAEyIFS 215
Cdd:PHA02989   52 IVKLLIDN-GADVNYKGyieTPLCAVLrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCD-MLR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 216 IAKAKMENLDSLlyqADIDGSTLLHMAVESGVT--EIVALCLNHGARVREPKdkhspSAFHLA---------CAQGSVKM 284
Cdd:PHA02989  129 FLLSKGINVNDV---KNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFEKT-----SLYGLTpmniylrndIDVISIKV 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 285 VKLMVEKDpviCRITLIDRDGMSPL------HRAAANNQTNIVEFLLDQgAQVDLTDKTHCTPLFMAASNGATETVKLLM 358
Cdd:PHA02989  201 IKYLIKKG---VNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL 276
                         250       260
                  ....*....|....*....|...
gi 2257803366 359 SRGANVTSKNVAMESVLHAAVGH 381
Cdd:PHA02989  277 KLGDDIYNVSKDGDTVLTYAIKH 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
467-513 2.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2257803366 467 INLKNNHGKTPLHFAAGEGHDKVVELLLDRGATID-RDHTERTPLHLA 513
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNlKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
304-333 2.22e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.22e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2257803366  304 DGMSPLHRAAANNQTNIVEFLLDQGAQVDL 333
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
202-360 2.59e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.56  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 202 VEKGAKNTAEYIFSIAKaKMENLDSLLYQADID----GSTLLHMAVESGVTEIVALCLNHGARVREP------KDKHSPS 271
Cdd:cd22196    58 LHNGQNDTISLLLDIAE-KTGNLKEFVNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHARasgeffKKKKGGP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366 272 AFH-------LACAQGSVKMVKLMVEKDPVICRITLIDRDGMSPLHR--AAANNQTNIVEF-------LLDQGAQV---- 331
Cdd:cd22196   137 GFYfgelplsLAACTNQLDIVKFLLENPHSPADISARDSMGNTVLHAlvEVADNTPENTKFvtkmyneILILGAKIrpll 216
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2257803366 332 ---DLTDKTHCTPLFMAASNGATETVKLLMSR 360
Cdd:cd22196   217 kleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
340-389 2.83e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2257803366 340 TPLFMAASNGATETVKLLMSRGANVTSKNVAMESVLHAAV--GHMRTTEALL 389
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAsnGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
65-122 3.65e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 3.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2257803366  65 LCAAAYMGDKETAIKLLDKGVDINCADEYGKTPLHHATTGKRIEFVEFLLSRGAELTK 122
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
80-193 7.34e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 39.06  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  80 LLDKGVDINCA---------DE-----YGKTPLHHATTGKRIEFVEFLLSRG---AELTKQDQRGDTPLHAAVRTGDEA- 141
Cdd:cd22195   156 LVEKGADVHAQargrffqpkDEggyfyFGELPLSLAACTNQPDIVHYLTENAhkkADLRRQDSRGNTVLHALVAIADNTr 235
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2257803366 142 -------------IVKTLVSNEKCNVNA--KGRGLcTPLHIACGMDKLKIckllIEHEARIDLKDED 193
Cdd:cd22195   236 entkfvtkmydllLIKCAKLYPDCNLEAilNNDGM-SPLMMAAKLGKIGI----FQHIIRREIKDEE 297
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
339-365 7.38e-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: 7.38e-03
                           10        20
                   ....*....|....*....|....*..
gi 2257803366  339 CTPLFMAASNGATETVKLLMSRGANVT 365
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
93-184 8.12e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.01  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2257803366  93 YGKTPLHHATTGKRIEFVEFLLS---RGAELTKQDQRGDTPLHAAVRTGDEAIVKT-LVSNEKCNVNAKGRGLC------ 162
Cdd:cd22193   122 FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVTVADNTKENTkFVTRMYDMILIRGAKLCptvele 201
                          90       100       110
                  ....*....|....*....|....*....|
gi 2257803366 163 --------TPLHIACGMDKLKICKLLIEHE 184
Cdd:cd22193   202 eirnndglTPLQLAAKMGKIEILKYILQRE 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-459 9.63e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 9.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2257803366 405 GYAPIHRAARGGYLQNIHLFItKNKAAAGITADSLDTPLHVACKFGWLEIVDDLL 459
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
93-122 9.72e-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: 33.72  E-value: 9.72e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2257803366   93 YGKTPLHHATTGKRIEFVEFLLSRGAELTK 122
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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