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Conserved domains on  [gi|1622898470|ref|XP_028695873|]
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ankyrin repeat domain-containing protein 27 isoform X5 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-698 1.15e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 477 LLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 556
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 557 LHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQH 636
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 637 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQ--NSKIMELLQ 698
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-420 1.74e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 342
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 343 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 420
Cdd:COG0666   163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 233-272 2.58e-20

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


:

Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 84.61  E-value: 2.58e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622898470 233 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 272
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 68-167 4.50e-17

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


:

Pssm-ID: 460489  Cd Length: 104  Bit Score: 77.25  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470  68 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 147
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|
gi 1622898470 148 AKDELGYCLTSFEAAIEYIR 167
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-698 1.15e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 477 LLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 556
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 557 LHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQH 636
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 637 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQ--NSKIMELLQ 698
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-420 1.74e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 342
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 343 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 420
Cdd:COG0666   163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
552-644 1.52e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 552 LHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDsNAKPNKKDlSGNTPLIYACSGGHHEVAA 631
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1622898470 632 LLLQHGASINASN 644
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
304-399 4.65e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 4.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 304 LHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALvyydVESCRLDIGNEkGDTPLHIAARWGYQG 383
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL----LEHADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1622898470 384 VIETLLQNGASTEIQN 399
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 538-678 1.68e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 538 GLGVNVTSQDGSSPLHVAALH--GRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQV------------------V 597
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrV 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 598 KYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLN 677
Cdd:PHA03100  176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                  .
gi 1622898470 678 K 678
Cdd:PHA03100  256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 233-272 2.58e-20

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 84.61  E-value: 2.58e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622898470 233 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 272
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 510-551 1.36e-17

second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the second Zn-fingernail of ANKRD27.


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 76.98  E-value: 1.36e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622898470 510 ADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 551
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 68-167 4.50e-17

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 77.25  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470  68 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 147
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|
gi 1622898470 148 AKDELGYCLTSFEAAIEYIR 167
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 264-430 5.10e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 5.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 264 DDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLL------------------LLHYK 323
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 324 ASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdveSCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNR--- 400
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622898470 401 -LKETPLKCALNSKIL--SIMEAHHL--SFERRQK 430
Cdd:PHA03100  260 yFKDKDLNTITKIKMLkkSIMYMFLLdpGFYKNRK 294
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 175-390 9.49e-10

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: 62.12  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 175 PPESEGFGDRLFLKQRMSLLSQMTSSPT--DCLFKHIAS--GNQKEVERLLSQEDHDKDAVqkmchplcfcddceklvsg 250
Cdd:cd22193     1 LEELLGFLQDLCRRRKDLTDSEFTESSTgkTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 251 rlnDPSVVTPFsRDD--RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQ 313
Cdd:cd22193    62 ---KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 314 SVTLLL--LHYKASAEVQDNNGNTPLHLACTYG-----HEDCVKALvyYD---VESCRL-------DIGNEKGDTPLHIA 376
Cdd:cd22193   138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                         250
                  ....*....|....
gi 1622898470 377 ARWGYQGVIETLLQ 390
Cdd:cd22193   216 AKMGKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 253-390 5.48e-08

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: 56.63  E-value: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 253 NDPSvvtpFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNA------------TD--YHGATPLHLACQKGYQSVTLL 318
Cdd:TIGR00870 118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 319 LLHYKASAEVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGV 384
Cdd:TIGR00870 194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                  ....*.
gi 1622898470 385 IETLLQ 390
Cdd:TIGR00870 273 FRLKLA 278
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 68-166 9.73e-07

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 48.22  E-value: 9.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470   68 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 147
Cdd:smart00167   2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90
                   ....*....|....*....
gi 1622898470  148 AKDELGYCLTSFEAAIEYI 166
Cdd:smart00167  81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 614-642 3.27e-06

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: 44.12  E-value: 3.27e-06
                           10        20
                   ....*....|....*....|....*....
gi 1622898470  614 GNTPLIYACSGGHHEVAALLLQHGASINA 642
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 332-358 2.69e-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: 41.80  E-value: 2.69e-05
                           10        20
                   ....*....|....*....|....*..
gi 1622898470  332 NGNTPLHLACTYGHEDCVKALVYYDVE 358
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 548-693 4.67e-05

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: 47.00  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 548 GSSPLHVAALHGRVDLIPLLLKHGANAGARnadqavplhlACqqGHFQVVKYLLDSnakpnkkdLS-GNTPL-IYACSGg 625
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------AC--GDFFVKSQGVDS--------FYhGESPLnAAACLG- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 626 HHEVAALLLQHGASINASNNKGNTALHEAVIEKHvFVVE----------LLLLHGASAQ-------VLNKRQRTAVDCAE 688
Cdd:TIGR00870 187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENE-FKAEyeelscqmynFALSLLDKLRdskelevILNHQGLTPLKLAA 265


                  ....*
gi 1622898470 689 QNSKI 693
Cdd:TIGR00870 266 KEGRI 270
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-698 1.15e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 1.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 477 LLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 556
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 557 LHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQH 636
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 637 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQ--NSKIMELLQ 698
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-693 3.16e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 3.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 477 LLRAVADGDLEMVRYLLEwteedledaedtvsaadlefchplcqcpkcapaqkrlakvpaSGLGVNVTSQDGSSPLHVAA 556
Cdd:COG0666    91 LHAAARNGDLEIVKLLLE------------------------------------------AGADVNARDKDGETPLHLAA 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 557 LHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQH 636
Cdd:COG0666   129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898470 637 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQNSKI 693
Cdd:COG0666   209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-683 1.61e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 1.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 280 ASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVEs 359
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 360 crLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLkcalnskilsimeahhlsferrqkaseapvqsp 439
Cdd:COG0666    80 --INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL--------------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 440 qrsvdsisqesstssfssmsagsrqeetkkdyreveklLRAVADGDLEMVRYLLEwteedledaedtvSAADlefchplc 519
Cdd:COG0666   125 --------------------------------------HLAAYNGNLEIVKLLLE-------------AGAD-------- 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 520 qcpkcapaqkrlakvpasglgVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKY 599
Cdd:COG0666   146 ---------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 600 LLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKR 679
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                  ....
gi 1622898470 680 QRTA 683
Cdd:COG0666   285 LLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-420 1.74e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 1.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 342
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 343 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 420
Cdd:COG0666   163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
264-651 5.08e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 5.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 264 DDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTY 343
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 344 GHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLkcalnskilsimeahhl 423
Cdd:COG0666    98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL----------------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 424 sferrqkaseapvqspqrsvdsisqesstssfssmsagsrqeetkkdyreveklLRAVADGDLEMVRYLLEwteedleda 503
Cdd:COG0666   158 ------------------------------------------------------HLAAANGNLEIVKLLLE--------- 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 504 edtvSAADlefchplcqcpkcapaqkrlakvpasglgVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAV 583
Cdd:COG0666   175 ----AGAD-----------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 584 PLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTAL 651
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-420 1.11e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 342
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 343 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 420
Cdd:COG0666   196 NGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
Ank_2 pfam12796
Ankyrin repeats (3 copies);
552-644 1.52e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 1.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 552 LHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDsNAKPNKKDlSGNTPLIYACSGGHHEVAA 631
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1622898470 632 LLLQHGASINASN 644
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
585-672 7.12e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 585 LHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHgASINASNNkGNTALHEAVIEKHVFVVE 664
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*...
gi 1622898470 665 LLLLHGAS 672
Cdd:pfam12796  79 LLLEKGAD 86
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
529-697 8.24e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 8.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 529 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPN 608
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 609 KKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA- 687
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAa 161

                         170
                  ....*....|.
gi 1622898470 688 -EQNSKIMELL 697
Cdd:COG0666   162 aNGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
304-399 4.65e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 4.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 304 LHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALvyydVESCRLDIGNEkGDTPLHIAARWGYQG 383
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL----LEHADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1622898470 384 VIETLLQNGASTEIQN 399
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 538-678 1.68e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 538 GLGVNVTSQDGSSPLHVAALH--GRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQV------------------V 597
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrV 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 598 KYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLN 677
Cdd:PHA03100  176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                  .
gi 1622898470 678 K 678
Cdd:PHA03100  256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 233-272 2.58e-20

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 84.61  E-value: 2.58e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622898470 233 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 272
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 542-676 2.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 542 NVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYA 621
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 622 CSGGHHEVAALLLQHGASINASNNKGN-TALHEAVIEKHVFVVELLLLHGASAQVL 676
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-358 4.58e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 4.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 271 LHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEvqDNNGNTPLHLACTYGHEDCVK 350
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 1622898470 351 ALVYYDVE 358
Cdd:pfam12796  79 LLLEKGAD 86
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 510-551 1.36e-17

second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the second Zn-fingernail of ANKRD27.


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 76.98  E-value: 1.36e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622898470 510 ADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 551
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 68-167 4.50e-17

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 77.25  E-value: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470  68 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 147
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|
gi 1622898470 148 AKDELGYCLTSFEAAIEYIR 167
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIE 100
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 284-678 8.25e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 85.12  E-value: 8.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 284 DLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVyydveSCRLD 363
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 364 IgnEKGDTPLHIAARwgyQGVIET---LLQNGASTEIQNRLKETPLkcalnskilsimeaHHlsferrqkASEAPVQSpq 440
Cdd:PHA02876  237 I--NKNDLSLLKAIR---NEDLETsllLYDAGFSVNSIDDCKNTPL--------------HH--------ASQAPSLS-- 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 441 rsvdsisqesstssfssmsagsrqeetkkdyREVEKLLRAVADGDLEMVR-----YLLEWTEEDLEDAEDTVS------A 509
Cdd:PHA02876  288 -------------------------------RLVPKLLERGADVNAKNIKgetplYLMAKNGYDTENIRTLIMlgadvnA 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 510 ADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLA- 588
Cdd:PHA02876  337 ADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 589 CQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGG-HHEVAALLLQHGASINASNNKGNTALHEAvIEKHVfVVELLL 667
Cdd:PHA02876  417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILL 494

                         410
                  ....*....|....
gi 1622898470 668 LHGAS---AQVLNK 678
Cdd:PHA02876  495 HYGAElrdSRVLHK 508
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 264-430 5.10e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 5.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 264 DDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLL------------------LLHYK 323
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 324 ASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdveSCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNR--- 400
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622898470 401 -LKETPLKCALNSKIL--SIMEAHHL--SFERRQK 430
Cdd:PHA03100  260 yFKDKDLNTITKIKMLkkSIMYMFLLdpGFYKNRK 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-352 6.93e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 6.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 342
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                          90
                  ....*....|
gi 1622898470 343 YGHEDCVKAL 352
Cdd:COG0666   262 AGAALIVKLL 271
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 537-667 1.26e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.01  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 537 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNT 616
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 617 PLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVfVVELLL 667
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 233-270 2.42e-15

Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails.


Pssm-ID: 439264 [Multi-domain]  Cd Length: 38  Bit Score: 70.36  E-value: 2.42e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622898470 233 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTP 270
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 536-687 4.69e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.77  E-value: 4.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 536 ASGLGVNVTSQD-GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSG 614
Cdd:PHA02878  155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622898470 615 NTPLIYACSG-GHHEVAALLLQHGASINA-SNNKGNTALHEAVIEKHvfVVELLLLHGASAQVLNKRQRTAVDCA 687
Cdd:PHA02878  235 NTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 263-411 8.09e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 8.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 342
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898470 343 YGHEDCVKALVyydVESCRLDIGNEKGDTPLHIAARWGyQGVIEtLLQNGASTEIQNRLKETPLKCALN 411
Cdd:PHA02874  200 YGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHN-RSAIE-LLINNASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 538-737 1.10e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 538 GLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTP 617
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 618 LIYACSggHHEVAALLLQHGASINASNNKGNTALHEAVIEK-HVFVVELLLLHGASAQVLNKRQRTAVDCAEQNSKIMEL 696
Cdd:PHA02874  227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV 304

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622898470 697 LQ-VVPSCV--ASLDDVAETDRREYVTVKIRKKWNSKLYDLPDE 737
Cdd:PHA02874  305 IKdIIANAVliKEADKLKDSDFLEHIEIKDNKEFSDFIKECNEE 348
Ank_2 pfam12796
Ankyrin repeats (3 copies);
477-611 1.14e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 477 LLRAVADGDLEMVRYLLEwteedledaedtvsaadlefchplcqcpkcapaqkrlakvpaSGLGVNVTSQDGSSPLHVAA 556
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE------------------------------------------NGADANLQDKNGRTALHLAA 38

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622898470 557 LHGRVDLIPLLLKHgANAGARNADQAvPLHLACQQGHFQVVKYLLDSNAKPNKKD 611
Cdd:pfam12796  39 KNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 537-675 5.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.03  E-value: 5.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 537 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNK---KDls 613
Cdd:PHA02875   24 IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD-- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898470 614 GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQV 675
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 282-417 8.06e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 8.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 282 LIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTL--LLLHYKASAEVQDNNGNTPLHLACTYGHED--CVKALVYYDV 357
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGV 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 358 E-------------SCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSI 417
Cdd:PHA03100  168 DinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 265-410 1.81e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 265 DRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYg 344
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 345 hedcvkaLVYYDVESCRLDIG---NEK----GDTPLHIAARwgYQGVIETLLQNGASTEIQNRLKETPLKCAL 410
Cdd:PHA02878  245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 285-671 2.41e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 285 LLVSKGAVVNATDYHGATPLHLACQKGYQSVT---LLLLHYKASAEVQDNNGNTPLHLACTYGH-EDCVKALVYY--DVE 358
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 359 SCrldigNEKGDTPLHIAAR--WGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKilsimeahhlsferrqkaseapv 436
Cdd:PHA03095  112 AK-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR----------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 437 qspqrsvdsisqesstssfssmsagsrqeetkkdyrevekllravaDGDLEMVRYLLewteedleDAEDTVSAADLEF-- 514
Cdd:PHA03095  164 ----------------------------------------------NANVELLRLLI--------DAGADVYAVDDRFrs 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 515 -CHPLCQCPKcaPAQKRLAKVPASGLGVNVTSQDGSSPLHVAALHG---RVDLIPLLLKhGANAGARNADQAVPLHLACQ 590
Cdd:PHA03095  190 lLHHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAV 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 591 QGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHE-VAALLLQHGAS--INASNNKGNTALHEAVIEKHVFVVELLL 667
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSAetVAATLNTASVAGGDIPSDATRLCVAKVV 346


                  ....
gi 1622898470 668 LHGA 671
Cdd:PHA03095  347 LRGA 350
PHA03095 PHA03095
ankyrin-like protein; Provisional
 560-686 4.26e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 4.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 560 RVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ---VVKYLLDSNAKPNKKDLSGNTPLI-YACSGGHHEVAALLLQ 635
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 636 HGASINASNNKGNTALHE--AVIEKHVFVVELLLLHGASAQVLNKRQRTAVDC 686
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA03095 PHA03095
ankyrin-like protein; Provisional
 536-715 6.85e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 6.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 536 ASGLGVNVTSQDGSSPLHV---AALHGRVDLIPLLLKHGANAGARNADQAVPLHL-ACQQGHFQVVKYLLDSNAKPNKKD 611
Cdd:PHA03095   35 AAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKD 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 612 LSGNTPL-IYACSGG-HHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFV--VELLLLHGASAQVLNKRQRTAVDCA 687
Cdd:PHA03095  115 KVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHH 194

                         170       180
                  ....*....|....*....|....*...
gi 1622898470 688 EQNSKIMEllQVVPSCVASLDDVAETDR 715
Cdd:PHA03095  195 LQSFKPRA--RIVRELIRAGCDPAATDM 220
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 371-700 1.10e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.63  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 371 TPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEAhhlsferrqkaseapvqspqrSVDSisqes 450
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA---------------------IIDN----- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 451 stssfssmsagsRQEETKKDYreveKLLRAVADGDLEmvryllewTEEDLEDAEDTVSAADLEFCHPLCQCPKcAPAQKR 530
Cdd:PHA02876  234 ------------RSNINKNDL----SLLKAIRNEDLE--------TSLLLYDAGFSVNSIDDCKNTPLHHASQ-APSLSR 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 531 LA-KVPASGLGVNVTSQDGSSPLHVAALHG-RVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ-VVKYLLDSNAKP 607
Cdd:PHA02876  289 LVpKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANV 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 608 NKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFV-VELLLLHGASAQVLNKRQRTAVDC 686
Cdd:PHA02876  369 NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHY 448

                         330
                  ....*....|....
gi 1622898470 687 AEQNSKIMELLQVV 700
Cdd:PHA02876  449 ACKKNCKLDVIEML 462
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 580-697 1.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 580 DQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHH-----EVAALLLQHGASINASNNKGNTALHEA 654
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1622898470 655 VIEK--HVFVVELLLLHGASAQVLNKRQRT----AVDCAEQNSKIMELL 697
Cdd:PHA03100  114 ISKKsnSYSIVEYLLDNGANVNIKNSDGENllhlYLESNKIDLKILKLL 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 529-678 1.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 529 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ-----VVKYLLDS 603
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898470 604 NAKPNKKDLSGNTPLIYACSG--GHHEVAALLLQHGASINASNNKGNTALHEAVIEKHV--FVVELLLLHGASAQVLNK 678
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR 174
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 513-551 1.81e-12

Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails.


Pssm-ID: 439264 [Multi-domain]  Cd Length: 38  Bit Score: 62.27  E-value: 1.81e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622898470 513 EFCHPLCQCPKCAPAQKRLAKVPaSGLGVNVTSQDGSSP 551
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDP-SGVGVNSRDQDGRTP 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 279-412 2.07e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 279 QASLIDLLVSKGAVVNATDYH-GATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdv 357
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898470 358 eSCRLDIGNEKGDTPLHIAArwGY---QGVIETLLQNGASTEIQNRLKE-TPLKCALNS 412
Cdd:PHA02878  224 -GASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 562-697 3.52e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 562 DLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASIN 641
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898470 642 ASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA-EQNSKIMELL 697
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiIHNRSAIELL 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 562-713 3.68e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.52  E-value: 3.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 562 DLIPLLLKHGA--NAGARNADQAvPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGAS 639
Cdd:PHA02878  148 EITKLLLSYGAdiNMKDRHKGNT-ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 640 INASNNKGNTALHEAVIE-KHVFVVELLLLHGASAQVLNK-RQRTAVDCAEQNSKIMELLQVVPSCVASLDDVAET 713
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNSYKLT 302
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 272-363 4.97e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.54  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 272 HVAAlCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKA 351
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|..
gi 1622898470 352 LVYYDVESCRLD 363
Cdd:PTZ00322  167 LSRHSQCHFELG 178
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 277-410 7.25e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 7.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 277 CGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYyd 356
Cdd:PHA02874  101 CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-- 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 357 vESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 410
Cdd:PHA02874  179 -KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
260-330 2.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 260 PFSRDDRGHTPLHVAALCGQASLIDLLVSKgAVVNATDYhGATPLHLACQKGYQSVTLLLLHYKASAEVQD 330
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 477-654 2.88e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 2.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 477 LLRAVADGDLEMVRYLLEWTEEdledaedtVSAADLEFCHPLCQCPKcAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 556
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIK-HNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 557 LHGRVDLIPLLLKHGANAGARNADQAVPLHLACQqgHFQVVKYLLDSNAKPNKKDLSGNTPLIYA----CSgghHEVAAL 632
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDI 273

                         170       180
                  ....*....|....*....|..
gi 1622898470 633 LLQHGASINASNNKGNTALHEA 654
Cdd:PHA02874  274 LLYHKADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
584-634 2.98e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.98e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 584 PLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLL 634
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
548-601 3.95e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 3.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 548 GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLL 601
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
561-697 4.82e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 561 VDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASI 640
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898470 641 NASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA--EQNSKIMELL 697
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
614-667 9.43e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 9.43e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 614 GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 667
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 267-417 1.24e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 267 GHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKG-YQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGH 345
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898470 346 EDCVKALVYYDVEScrlDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSI 417
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 564-636 3.32e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 3.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 564 IPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQH 636
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 528-672 3.46e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 528 QKRLAKVPASGLGVNVTSQDG----SSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDS 603
Cdd:PLN03192  501 HKELHDLNVGDLLGDNGGEHDdpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 604 NAKPNKKDLSGNTPLIYACSGGHHEV-------AAL------------------------LLQHGASINASNNKGNTALH 652
Cdd:PLN03192  581 ACNVHIRDANGNTALWNAISAKHHKIfrilyhfASIsdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQ 660

                         170       180
                  ....*....|....*....|
gi 1622898470 653 EAVIEKHVFVVELLLLHGAS 672
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGAD 680
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 270-421 3.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 270 PLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQ---------------------------------------- 309
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 310 ------KGYQS------------------VTLLLLHYKASAEVQD-NNGNTPLHLACTYGHEDCVKALVYYDVESCRLDI 364
Cdd:PHA02878  120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 365 GNekgDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCA----LNSKILSIMEAH 421
Cdd:PHA02878  200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLLEH 257
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 175-390 9.49e-10

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: 62.12  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 175 PPESEGFGDRLFLKQRMSLLSQMTSSPT--DCLFKHIAS--GNQKEVERLLSQEDHDKDAVqkmchplcfcddceklvsg 250
Cdd:cd22193     1 LEELLGFLQDLCRRRKDLTDSEFTESSTgkTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 251 rlnDPSVVTPFsRDD--RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQ 313
Cdd:cd22193    62 ---KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 314 SVTLLL--LHYKASAEVQDNNGNTPLHLACTYG-----HEDCVKALvyYD---VESCRL-------DIGNEKGDTPLHIA 376
Cdd:cd22193   138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                         250
                  ....*....|....
gi 1622898470 377 ARWGYQGVIETLLQ 390
Cdd:cd22193   216 AKMGKIEILKYILQ 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 269-408 1.21e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 269 TPLHVAALCGQASLIDLLVSKGAVVNATDYH-GATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHED 347
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 348 CVKALVyyDVESCrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKC 408
Cdd:PHA02875  150 GIELLI--DHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 541-677 2.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 541 VNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYL-------------------- 600
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmi 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 601 ---LDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLN 677
Cdd:PHA02874  108 ktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 274-410 2.45e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 274 AALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALV 353
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898470 354 YYdvesCRLDIGNEKGDTpLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 410
Cdd:PLN03192  612 HF----ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 542-693 3.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 542 NVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAG-ARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIY 620
Cdd:PHA02875   62 DVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 621 ACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDC-AEQNSKI 693
Cdd:PHA02875  142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKI 215
PHA02798 PHA02798
ankyrin-like protein; Provisional
 561-686 3.44e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 561 VDLIPLLLKHGANAGARNADQAVPL-----HLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGH---HEVAAL 632
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 633 LLQHGASINASNNKGNTALHEAVIEKH---VFVVELLLLHGASA-QVLNKRQRTAVDC 686
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDInTHNNKEKYDTLHC 188
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 540-715 5.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.08  E-value: 5.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 540 GVNVTSQD--GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSgntp 617
Cdd:PHA02876  168 GADVNAKDiyCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 618 LIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVF-VVELLLLHGASAQVLNKRQRTAVDCAEQNSKIMEL 696
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEN 323

                         170
                  ....*....|....*....
gi 1622898470 697 LQVVPSCVAsldDVAETDR 715
Cdd:PHA02876  324 IRTLIMLGA---DVNAADR 339
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 262-410 5.89e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 262 SRDDRGHTPLHVAALCGQAS-LIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTL-LLLHYKASAEVQDNNGNTPLHL 339
Cdd:PHA02876  268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898470 340 ACTYG-HEDCVKALVYYDVESCRLDIGNEkgdTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 410
Cdd:PHA02876  348 ASTLDrNKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 548-652 8.56e-09

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: 59.26  E-value: 8.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 548 GSSPLHVAALHGRVDLIPLLLkhgaNAGARNADQAV---------PLHLACQQGHFQVVKYLLDSNA------------K 606
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLM----EAAPELVNEPMtsdlyqgetALHIAVVNQNLNLVRELIARGAdvvspratgtffR 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898470 607 PNKKDLS--GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALH 652
Cdd:cd22192   127 PGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
302-353 1.21e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622898470 302 TPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALV 353
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 263-406 1.31e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVAaLCGQ---ASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEV--QDNNGNTPL 337
Cdd:PHA03095  113 KDKVGRTPLHVY-LSGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyaVDDRFRSLL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 338 HLACTYGH--EDCVKALVYYDVE-------------------SCR-------------LDIGNEKGDTPLHIAARWGYQG 383
Cdd:PHA03095  192 HHHLQSFKprARIVRELIRAGCDpaatdmlgntplhsmatgsSCKrslvlplliagisINARNRYGQTPLHYAAVFNNPR 271

                         170       180
                  ....*....|....*....|...
gi 1622898470 384 VIETLLQNGASTEIQNRLKETPL 406
Cdd:PHA03095  272 ACRRLIALGADINAVSSDGNTPL 294
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 187-398 1.33e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 58.35  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 187 LKQRMSLLSQMTSSPTDCLFKHIASGNQKEVERLLSQEDHDKDAVQKMCHPLCFCDDCEKLVsgrlNDPSVVTPFsrddR 266
Cdd:cd21882     1 LEELLGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELV----NAPCTDEFY----Q 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 267 GHTPLHVAALCGQASLIDLLVSKGAVVNATD-------------YHGATPLHL-ACQKGYQSVTLLLLH--YKASAEVQD 330
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 331 NNGNTPLH--------------LACTYGHEdcvkaLVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGVIETLLQNG 392
Cdd:cd21882   153 SLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227


                  ....*.
gi 1622898470 393 ASTEIQ 398
Cdd:cd21882   228 FSGPYQ 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 536-641 1.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 536 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGN 615
Cdd:PHA02875  123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202

                          90       100
                  ....*....|....*....|....*..
gi 1622898470 616 -TPLIYACSGGHHEVAALLLQHGASIN 641
Cdd:PHA02875  203 vAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
286-340 2.33e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 2.33e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 286 LVSKGAV-VNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA 340
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 551-697 3.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 551 PLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAK------------------------ 606
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 607 --PNKKDLSGNTPLIYACSGGHH-----EVAALLLQHGASIN-ASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNK 678
Cdd:PHA02878  120 ilTNRYKNIQTIDLVYIDKKSKDdiieaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180
                  ....*....|....*....|.
gi 1622898470 679 RQRTAVDCA--EQNSKIMELL 697
Cdd:PHA02878  200 TNNSPLHHAvkHYNKPIVHIL 220
PHA03095 PHA03095
ankyrin-like protein; Provisional
 260-351 3.12e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 260 PFSRDDRGHTPLHVAALCG--QASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPL 337
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                          90
                  ....*....|....
gi 1622898470 338 HLACTYGHEDCVKA 351
Cdd:PHA03095  295 SLMVRNNNGRAVRA 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 265-349 3.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 265 DRGHTPLHVAALCGQaSLIDLLVSKgAVVNATDYHGATPLHLA----CQKgyqSVTLLLLHYKASAEVQDNNGNTPLHLA 340
Cdd:PHA02874  221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                  ....*....
gi 1622898470 341 CTYGHEDCV 349
Cdd:PHA02874  296 FKYINKDPV 304
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 538-655 3.85e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 538 GLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQ-GHFQVVKYLLDSNAKPNKKD-LSGN 615
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGL 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622898470 616 TPLIYACSGghHEVAALLLQHGASINASNNKGNTALHEAV 655
Cdd:PHA02878  271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 269-410 4.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 4.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 269 TPLHvaalcgQASLID-------LLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA- 340
Cdd:PHA02876  343 TPLH------QASTLDrnkdiviTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 341 CTYGHEDCVKALVYydvESCRLDIGNEKGDTPLHIAARWGYQ-GVIETLLQNGASTEIQNRLKETPLKCAL 410
Cdd:PHA02876  417 CGTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 253-390 5.48e-08

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: 56.63  E-value: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 253 NDPSvvtpFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNA------------TD--YHGATPLHLACQKGYQSVTLL 318
Cdd:TIGR00870 118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 319 LLHYKASAEVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGV 384
Cdd:TIGR00870 194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                  ....*.
gi 1622898470 385 IETLLQ 390
Cdd:TIGR00870 273 FRLKLA 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 266-353 8.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 8.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 266 RGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGH 345
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                  ....*...
gi 1622898470 346 EDCVKALV 353
Cdd:PHA02875  181 IAICKMLL 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 597-669 1.47e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 597 VKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLH 669
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 263-366 1.56e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 263 RDDRGHTPLHVA-ALCGQASLIDLLVSKGAVVNATDY-HGATPLHLACQKgyQSVTLLLLHYKASAEVQDNNGNTPLHLA 340
Cdd:PHA02878  230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                          90       100
                  ....*....|....*....|....*.
gi 1622898470 341 ctyghedcvkALVYYDVESCRLDIGN 366
Cdd:PHA02878  308 ----------VKQYLCINIGRILISN 323
Ank_4 pfam13637
Ankyrin repeats (many copies);
333-389 2.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 2.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898470 333 GNTPLHLACTYGHEDCVKALVYYDVESCRLDIGnekGDTPLHIAARWGYQGVIETLL 389
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
318-376 3.63e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 3.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898470 318 LLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIA 376
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
607-654 4.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898470 607 PNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEA 654
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 271-419 4.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 271 LHVAALC-----GQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGh 345
Cdd:PHA02875    1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 346 eDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIME 419
Cdd:PHA02875   80 -DVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 68-166 9.73e-07

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 48.22  E-value: 9.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470   68 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 147
Cdd:smart00167   2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90
                   ....*....|....*....
gi 1622898470  148 AKDELGYCLTSFEAAIEYI 166
Cdd:smart00167  81 LTGEGGYYLTSLSAALALI 99
Ank_5 pfam13857
Ankyrin repeats (many copies);
567-621 1.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 567 LLKHG-ANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYA 621
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 267-391 1.37e-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: 51.94  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 267 GHTPLHVAALCGQASLIDLLVSKGAVVN---ATD-----------YHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNN 332
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898470 333 GNTPLH---------LAC-TYgheDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQN 391
Cdd:cd22192   169 GNTVLHilvlqpnktFACqMY---DLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 614-645 1.52e-06

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: 45.36  E-value: 1.52e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622898470 614 GNTPLIYAC-SGGHHEVAALLLQHGASINASNN 645
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 266-390 1.64e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 51.78  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 266 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD-------------YHGATPLHL-ACQKGYQSVTLLL--LHYKASAEVQ 329
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622898470 330 DNNGNTPLHlACTYGHEDCVK--ALV--YYD---VESCRLD-------IGNEKGDTPLHIAARWGYQGVIETLLQ 390
Cdd:cd22197   173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDgllQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 260-322 1.71e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.71e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 260 PFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHY 322
Cdd:PTZ00322  108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 266-380 1.80e-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: 51.68  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 266 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQSVTLLLLHYKASAEVQD 330
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLMEKESTDITSQD 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 331 NNGNTPLHLACTYG-----HEDCVKALvyYDV-----ESCRLD-IGNEKGDTPLHIAARWG 380
Cdd:cd22194   220 SRGNTVLHALVTVAedsktQNDFVKRM--YDMillksENKNLEtIRNNEGLTPLQLAAKMG 278
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 600-673 1.81e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 1.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 600 LLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVElLLLHGASA 673
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASI 616
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 592-715 2.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 592 GHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGA 671
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622898470 672 SAQ-VLNKRQRTAVDCAE--QNSKIMELLQVvpscVASLDDVAETDR 715
Cdd:PHA02875   93 FADdVFYKDGMTPLHLATilKKLDIMKLLIA----RGADPDIPNTDK 135
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 614-642 3.27e-06

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: 44.12  E-value: 3.27e-06
                           10        20
                   ....*....|....*....|....*....
gi 1622898470  614 GNTPLIYACSGGHHEVAALLLQHGASINA 642
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-320 4.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622898470 267 GHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLL 320
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
541-588 4.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898470 541 VNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLA 588
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 537-608 7.12e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 537 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLL---------DSNAKP 607
Cdd:PTZ00322  104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKP 183


                  .
gi 1622898470 608 N 608
Cdd:PTZ00322  184 D 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 262-332 7.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 7.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898470 262 SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNN 332
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 264-399 8.39e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 8.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 264 DDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQdnNGNTPLHLACTY 343
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKR 632

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 344 GHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQN 399
Cdd:PLN03192  633 NDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 266-399 1.20e-05

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: 49.03  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 266 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQSVTLLLL--HYKASAEV 328
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 329 QDNNGNTPLHLACTYG--------------HEDCVKALVYYDVESCRlDIGNEKGDTPLHIAARWGYQGVIETLLQNgas 394
Cdd:cd22196   173 RDSMGNTVLHALVEVAdntpentkfvtkmyNEILILGAKIRPLLKLE-EITNKKGLTPLKLAAKTGKIGIFAYILGR--- 248


                  ....*
gi 1622898470 395 tEIQN 399
Cdd:cd22196   249 -EIKE 252
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 260-406 1.28e-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: 48.86  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 260 PFSRDDRGHTPLHVAALCG--QASLIdLLVSKGAVVN--ATD--YHGATPLHLACQKgyQSVTLLLLHYKASAEVQdnng 333
Cdd:cd22192    44 LFQRGALGETALHVAALYDnlEAAVV-LMEAAPELVNepMTSdlYQGETALHIAVVN--QNLNLVRELIARGADVV---- 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 334 nTPLhlACTYGHEDCVKALVYYdvescrldignekGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 406
Cdd:cd22192   117 -SPR--ATGTFFRPGPKNLIYY-------------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 232-270 1.31e-05

second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the second Zn-fingernail of ANKRD27.


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 42.70  E-value: 1.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622898470 232 QKMCHPLCFCDDCEKLVSG-RLNDPSVVTPFSRDDRGHTP 270
Cdd:cd22886     3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
260-307 1.62e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898470 260 PFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLA 307
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 332-358 2.69e-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: 41.80  E-value: 2.69e-05
                           10        20
                   ....*....|....*....|....*..
gi 1622898470  332 NGNTPLHLACTYGHEDCVKALVYYDVE 358
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02946 PHA02946
ankyin-like protein; Provisional
 259-406 2.74e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 259 TPFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQ---DNNGNT 335
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGAKINnsvDEEGCG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 336 PLhLACTYGHEDCVKALVYYDVES----------------------------CRLDIGNEK----GDTPLHIAARWGYQG 383
Cdd:PHA02946  144 PL-LACTDPSERVFKKIMSIGFEArivdkfgknhihrhlmsdnpkastiswmMKLGISPSKpdhdGNTPLHIVCSKTVKN 222

                         170       180
                  ....*....|....*....|....
gi 1622898470 384 V-IETLLQNGASTEIQNRLKETPL 406
Cdd:PHA02946  223 VdIINLLLPSTDVNKQNKFGDSPL 246
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 548-693 4.67e-05

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: 47.00  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 548 GSSPLHVAALHGRVDLIPLLLKHGANAGARnadqavplhlACqqGHFQVVKYLLDSnakpnkkdLS-GNTPL-IYACSGg 625
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------AC--GDFFVKSQGVDS--------FYhGESPLnAAACLG- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 626 HHEVAALLLQHGASINASNNKGNTALHEAVIEKHvFVVE----------LLLLHGASAQ-------VLNKRQRTAVDCAE 688
Cdd:TIGR00870 187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENE-FKAEyeelscqmynFALSLLDKLRdskelevILNHQGLTPLKLAA 265


                  ....*
gi 1622898470 689 QNSKI 693
Cdd:TIGR00870 266 KEGRI 270
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 630-714 4.75e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 630 AALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQNS--KIMELLQVVPSCVASL 707
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQLLSRHSQCHFEL 177


                  ....*..
gi 1622898470 708 DDVAETD 714
Cdd:PTZ00322  178 GANAKPD 184
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 555-697 5.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 555 AALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLL 634
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 635 QHGASIN-ASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA--EQNSKIMELL 697
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAvmMGDIKGIELL 154
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
263-337 7.49e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 7.49e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622898470 263 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPL 337
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 368-400 8.94e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 8.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622898470 368 KGDTPLHIAA-RWGYQGVIETLLQNGASTEIQNR 400
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 614-642 1.09e-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: 39.93  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|....*....
gi 1622898470 614 GNTPLIYACSGGHHEVAALLLQHGASINA 642
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 260-344 1.74e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 260 PFSRDDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGATPLHLACQKG--YQSVTLLLLHYKASAEVQDNNGNT 335
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQT 259


                  ....*....
gi 1622898470 336 PLHLACTYG 344
Cdd:PHA03095  260 PLHYAAVFN 268
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 547-573 1.77e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.77e-04
                           10        20
                   ....*....|....*....|....*..
gi 1622898470  547 DGSSPLHVAALHGRVDLIPLLLKHGAN 573
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
633-687 1.83e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898470 633 LLQHG-ASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA 687
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 584-611 1.89e-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: 39.19  E-value: 1.89e-04
                          10        20
                  ....*....|....*....|....*....
gi 1622898470 584 PLHLACQQ-GHFQVVKYLLDSNAKPNKKD 611
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 567-678 2.20e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 567 LLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYaCSGGHHEVAA---LLLQHGASINAS 643
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIErinLLVQYGAKINNS 136

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622898470 644 NNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNK 678
Cdd:PHA02946  137 VDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDK 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 584-609 2.22e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.22e-04
                           10        20
                   ....*....|....*....|....*.
gi 1622898470  584 PLHLACQQGHFQVVKYLLDSNAKPNK 609
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 205-364 2.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 205 LFKHIASGNQKEVERLLSQEDHDKDAVQKMCH-PLCFCD-----DCEKLVSGRLNDPSVvtpfSRDDRgHTPLHVAALCG 278
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMtPLHLATilkklDIMKLLIARGADPDI----PNTDK-FSPLHLAVMMG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 279 QASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGntplhlactyghedCVKALVyYDVE 358
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG--------------CVAALC-YAIE 211


                  ....*.
gi 1622898470 359 SCRLDI 364
Cdd:PHA02875  212 NNKIDI 217
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 266-297 3.11e-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: 3.11e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622898470 266 RGHTPLHVAAL-CGQASLIDLLVSKGAVVNATD 297
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 256-331 4.17e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 256 SVVTPF--------SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAE 327
Cdd:PHA03095  238 SLVLPLliagisinARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317


                  ....
gi 1622898470 328 VQDN 331
Cdd:PHA03095  318 TVAA 321
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 547-573 5.38e-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: 38.01  E-value: 5.38e-04
                          10        20
                  ....*....|....*....|....*..
gi 1622898470 547 DGSSPLHVAALHGRVDLIPLLLKHGAN 573
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 332-355 5.40e-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: 38.04  E-value: 5.40e-04
                          10        20
                  ....*....|....*....|....*
gi 1622898470 332 NGNTPLHLACT-YGHEDCVKALVYY 355
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 266-295 5.76e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 5.76e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622898470  266 RGHTPLHVAALCGQASLIDLLVSKGAVVNA 295
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 515-553 7.20e-04

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 38.01  E-value: 7.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622898470 515 CHPLCQCPKCapaQKRLAKVPASGLGVNVTSQD--GSSPLH 553
Cdd:cd22885     3 CHPLCSCDKC---EKLLSGNRNDPSAVTVYSRDdrGYTALH 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 547-578 7.25e-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: 37.65  E-value: 7.25e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622898470 547 DGSSPLHVAALH-GRVDLIPLLLKHGANAGARN 578
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 332-358 7.90e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 7.90e-04
                          10        20
                  ....*....|....*....|....*..
gi 1622898470 332 NGNTPLHLACTYGHEDCVKALVYYDVE 358
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 259-390 9.81e-04

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: 42.92  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 259 TPFsRD--DRGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHLA-CQKGYQSVTLLL-- 319
Cdd:cd22195   128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 320 LHYKASAEVQDNNGNTPLH--LACTYGHEDCVKALV-YYDV---------ESCRLD-IGNEKGDTPLHIAARWGYQGVIE 386
Cdd:cd22195   207 AHKKADLRRQDSRGNTVLHalVAIADNTRENTKFVTkMYDLllikcaklyPDCNLEaILNNDGMSPLMMAAKLGKIGIFQ 286


                  ....
gi 1622898470 387 TLLQ 390
Cdd:cd22195   287 HIIR 290
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 368-397 1.17e-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: 37.18  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622898470  368 KGDTPLHIAARWGYQGVIETLLQNGASTEI 397
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 363-581 1.18e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 363 DIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSK---ILSIMeaHHLsferrqkaseAPVQSP 439
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkIFRIL--YHF----------ASISDP 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 440 QRSVDSisqesstssfssmsagsrqeetkkdyrevekLLRAVADGDLEMVRYLLEwteedledaedtvsaadlefchplc 519
Cdd:PLN03192  620 HAAGDL-------------------------------LCTAAKRNDLTAMKELLK------------------------- 643

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898470 520 qcpkcapaqkrlakvpaSGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQ 581
Cdd:PLN03192  644 -----------------QGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 595-697 1.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 595 QVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVF-----VVELLLLH 669
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622898470 670 GASAQVLNKRQRTAVDCA----EQNSKIMELL 697
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAiskkSNSYSIVEYL 127
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 590-667 1.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898470 590 QQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 667
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 584-609 1.70e-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: 1.70e-03
                          10        20
                  ....*....|....*....|....*.
gi 1622898470 584 PLHLACQQGHFQVVKYLLDSNAKPNK 609
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
647-687 1.71e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622898470 647 GNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA 687
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-420 1.76e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898470 373 LHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 420
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 646-678 1.90e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622898470 646 KGNTALHEAVIE-KHVFVVELLLLHGASAQVLNK 678
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 257-393 1.94e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 257 VVTPFSRDDRGHTPLHVaaLCGQASLIDLLVSKGAVVNATDY-------HGATPLHLACQKGY---QSVTLLLLHYKASA 326
Cdd:PHA02736    7 IIFASEPDIEGENILHY--LCRNGGVTDLLAFKNAISDENRYlvleynrHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898470 327 EVQDN-NGNTPLHLACTYGHEDCVKALvyydvesCR-----LDIGNEKGDTPLHIAARWGYQGVIETLLQNGA 393
Cdd:PHA02736   85 NGKERvFGNTPLHIAVYTQNYELATWL-------CNqpgvnMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_4 pfam13637
Ankyrin repeats (many copies);
369-410 2.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622898470 369 GDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 410
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PHA02946 PHA02946
ankyin-like protein; Provisional
 595-671 2.51e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 595 QVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALH------EAVIEKhvfvVELLLL 668
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylsgtdDEVIER----INLLVQ 128


                  ...
gi 1622898470 669 HGA 671
Cdd:PHA02946  129 YGA 131
PHA02946 PHA02946
ankyin-like protein; Provisional
 235-391 2.69e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 235 CHPLCFCDDCEKLVSGRLN----DPSVVTPFSRDdrgHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQK 310
Cdd:PHA02946  142 CGPLLACTDPSERVFKKIMsigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 311 GYQSVTLL-LLHYKASAEVQDNNGNTPLHL---ACTYGH-------------EDCVKALVYYDVESCrLDIGNEKG---- 369
Cdd:PHA02946  219 TVKNVDIInLLLPSTDVNKQNKFGDSPLTLlikTLSPAHlinkllstsnvitDQTVNICIFYDRDDV-LEIINDKGkqyd 297

                         170       180
                  ....*....|....*....|..
gi 1622898470 370 DTPLHIAARWGYQGVIETLLQN 391
Cdd:PHA02946  298 STDFKMAVEVGSIRCVKYLLDN 319
Ank_5 pfam13857
Ankyrin repeats (many copies);
359-406 3.00e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622898470 359 SCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 406
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 548-651 3.50e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 548 GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQ-------------AVPLHLACQQGHFQVVKYLLDSNAKP---NKKD 611
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPHQPaslQAQD 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622898470 612 LSGNTPLiyacsgghhevaalllqHGASINASNNKGNTAL 651
Cdd:cd22197   174 SLGNTVL-----------------HALVMIADNSPENSAL 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 646-672 4.41e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 4.41e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622898470  646 KGNTALHEAVIEKHVFVVELLLLHGAS 672
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 512-671 5.68e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 512 LEFCHPLCQCPKCAPAQKRLAKVPAsglgvnvTSQ--DGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHlAC 589
Cdd:cd21882    42 NEAIMLLLEAAPDSGNPKELVNAPC-------TDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFFRKS-PG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 590 QQGHFqvvkylldsnakpnkkdlsGNTPLIYACSGGHHEVAALLLQHG---ASINASNNKGNTALHEAV------IEKHV 660
Cdd:cd21882   114 NLFYF-------------------GELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVlqadntPENSA 174

                         170
                  ....*....|....
gi 1622898470 661 FVVE---LLLLHGA 671
Cdd:cd21882   175 FVCQmynLLLSYGA 188
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 537-647 6.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 537 SGLGVN-VTSQDGSSPLHVAALHGR---VDLIPLLLKHGANAGARNADQAVPLH--LACQQGHFQVVKYLLDSNAKPNKK 610
Cdd:PHA02859   75 NGADVNfKTRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNK 154

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622898470 611 DLSGNTPL-IYACSGGHHEVAALLLQHGASINASNNKG 647
Cdd:PHA02859  155 DFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSG 192
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 596-687 6.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898470 596 VVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINA-SNNKGNTALHEAVIEKHVFVVELLLLHGASAQ 674
Cdd:PHA02884   52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADIN 131

                          90
                  ....*....|...
gi 1622898470 675 VLNKRQRTAVDCA 687
Cdd:PHA02884  132 IQTNDMVTPIELA 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 266-295 9.89e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 9.89e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622898470 266 RGHTPLHVAALCGQASLIDLLVSKGAVVNA 295
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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