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Conserved domains on  [gi|1147376792|ref|XP_020037644|]
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ankyrin repeat domain-containing protein 27 isoform X1 [Castor canadensis]

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];
734-894 1.02e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.02e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTP 813
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  814 LIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCAER--NSKIME 891
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVK 236

                   ...
gi 1147376792  892 LLQ 894
Cdd:COG0666    237 LLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 2.72e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.72e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACA 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  539 RGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCALNPKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
429-468 1.33e-19

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: 82.69  E-value: 1.33e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1147376792  429 KMCHPLCFCDDCERLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
706-747 3.43e-18

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: 78.91  E-value: 3.43e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1147376792  706 ADLEFCHPLCQCPKCAPAQKKLAKVPVSGLGVNVTNQDGSSP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
264-363 8.40e-16

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: 74.17  E-value: 8.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  264 IPRAKRELAQLNRCTSPQQKLVCLRRVVQLIMQTPSQRVSLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80
                           90       100
                   ....*....|....*....|
gi 1147376792  344 AKDELGYCLTSMEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
734-894 1.02e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.02e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTP 813
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  814 LIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCAER--NSKIME 891
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVK 236

                   ...
gi 1147376792  892 LLQ 894
Cdd:COG0666    237 LLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 2.72e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.72e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACA 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  539 RGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCALNPKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-840 3.20e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  748 LHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKpdNKDLRGNTPLIYACSGGHHEVAA 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1147376792  828 LLLQHGVSIDTRN 840
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 2.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  500 LHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYYDVQSCRLDignekGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75
                           90
                   ....*....|
gi 1147376792  580 IIETLVQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
429-468 1.33e-19

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: 82.69  E-value: 1.33e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1147376792  429 KMCHPLCFCDDCERLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
703-874 1.13e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 1.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  703 VSAADLEFCHPLCQCPKCAPAQKKLAKVPVS-GLGVNVTNQDGSSPLHLAALHGRADL--IPLLLKHGANPQAQDAdqai 779
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKSNSYSIVEYLLDnGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNR---- 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  780 plhlacqkghfqaVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVV 859
Cdd:PHA03100   175 -------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
                          170
                   ....*....|....*
gi 1147376792  860 ELLLLHGASVHILNE 874
Cdd:PHA03100   242 KLLLNNGPSIKTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
706-747 3.43e-18

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: 78.91  E-value: 3.43e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1147376792  706 ADLEFCHPLCQCPKCAPAQKKLAKVPVSGLGVNVTNQDGSSP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
264-363 8.40e-16

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: 74.17  E-value: 8.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  264 IPRAKRELAQLNRCTSPQQKLVCLRRVVQLIMQTPSQRVSLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80
                           90       100
                   ....*....|....*....|
gi 1147376792  344 AKDELGYCLTSMEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
460-596 2.13e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  460 DDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLL------------------LLHHK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  520 ASTDVQDNDGSTPLHLACARGHEDCVKALVYYdvqSCRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNR 596
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
375-586 9.53e-09

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: 59.42  E-value: 9.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  375 EGFGDRLCLRQRVSLLSQM--ASTPTDCLFKHIA--AGNQKEVEKLLSQEDHDRDAIqkmchplcfcddcerlvsgrlnD 450
Cdd:cd22193      5 LGFLQDLCRRRKDLTDSEFteSSTGKTCLMKALLnlNPGTNDTIRILLDIAEKTDNL----------------------K 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  451 PSVVTPFsRDD--RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGSTPLHL-ACQKGYQSVTL 513
Cdd:cd22193     63 RFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQY 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  514 LL--LHHKASTDVQDNDGSTPLHLACA-----RGHEDCVKALvyYD---VQSCRL-------DIGNEKGDTPLHIAARWG 576
Cdd:cd22193    142 LLenEHQPADIEAQDSRGNTVLHALVTvadntKENTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
                          250
                   ....*....|
gi 1147376792  577 YQGIIETLVQ 586
Cdd:cd22193    220 KIEILKYILQ 229
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
264-379 5.38e-08

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 52.07  E-value: 5.38e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792   264 IPRAKRELAQLNRCTSPQQKLVCLRRVVQLIMqTPSQRVSLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIY-TLLETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1147376792   344 AKDELGYCLTSMEAAIEYIRQ-GSLSVKPLDSEGFGD 379
Cdd:smart00167   81 LTGEGGYYLTSLSAALALIKGlTEAHALPLSPEQELE 117
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
449-586 4.79e-07

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: 53.93  E-value: 4.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  449 NDPSvvtpFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNA------------TD--YHGSTPLHLACQKGYQSVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  515 LLHHKASTDVQDNDGSTPLHLA------CARGHE---DCVKALVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGII 581
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLvmenefKAEYEElscQMYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVLF 273

                   ....*
gi 1147376792  582 ETLVQ 586
Cdd:TIGR00870  274 RLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
744-893 4.42e-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: 50.78  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  744 GSSPLHLAALHGRADLIPLLLKHGA----NPQAQDADQA-IPLHLACQKGHFQAVKCLLDSNA--------------KPD 804
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPelvnEPMTSDLYQGeTALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPK 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  805 NKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALH------EAVAGKHVFvvELLL-----LHGASV-HIL 872
Cdd:cd22192    131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlqpNKTFACQMY--DLILsydkeDDLQPLdLVP 208
                          170       180
                   ....*....|....*....|...
gi 1147376792  873 NERQRTALDCA--ERNSKIMELL 893
Cdd:cd22192    209 NNQGLTPFKLAakEGNIVMFQHL 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
809-837 3.67e-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: 41.42  E-value: 3.67e-05
                            10        20
                    ....*....|....*....|....*....
gi 1147376792   809 RGNTPLIYACSGGHHEVAALLLQHGVSID 837
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
673-889 4.38e-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: 47.38  E-value: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  673 LLRAVADGDLEMVRYLLEWIEEDVDEGDEIVSAADLEF--------CHPLCQCPKCAPAQkkLAKVPVSGlgvnvTNQDG 744
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYvdaveailLHLLAAFRKSGPLE--LANDQYTS-----EFTPG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  745 SSPLHLAALHGRADLIPLLLKHGANpqaqdadqaipLHLACQKGHFQAvkclldsnaKPDNKDLR-GNTPL-IYACSGgH 822
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGAS-----------VPARACGDFFVK---------SQGVDSFYhGESPLnAAACLG-S 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  823 HEVAALLLQHGVSIDTRNNRGNTALH-------------EAVAGKHVFVVELLLLHGASV---HILNERQRTALDCAERN 886
Cdd:TIGR00870  188 PSIVALLSEDPADILTADSLGNTLLHllvmenefkaeyeELSCQMYNFALSLLDKLRDSKeleVILNHQGLTPLKLAAKE 267

                   ...
gi 1147376792  887 SKI 889
Cdd:TIGR00870  268 GRI 270
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
528-553 6.80e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 6.80e-05
                            10        20
                    ....*....|....*....|....*.
gi 1147376792   528 DGSTPLHLACARGHEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
734-894 1.02e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.02e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTP 813
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  814 LIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCAER--NSKIME 891
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVK 236

                   ...
gi 1147376792  892 LLQ 894
Cdd:COG0666    237 LLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
663-889 1.16e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.16e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  663 ARKDYREVEKLLRAVADGDLEMVRYLLEwieedvdegdeivsaadlefchplcqcpkcapaqkklakvpvSGLGVNVTNQ 742
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE------------------------------------------AGADVNARDK 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  743 DGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGH 822
Cdd:COG0666    119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  823 HEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCAERNSKI 889
Cdd:COG0666    199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-880 1.22e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 1.22e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  476 ASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYYDVqs 555
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  556 cRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPqqcalnpkilsimeahrlsfekrpkpseapvpsp 635
Cdd:COG0666     79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP---------------------------------- 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  636 qrsvdsvsqgsssssfsstvvsvrqeearkdyrevekLLRAVADGDLEMVRYLLEwieedvdegdeivSAADlefchplc 715
Cdd:COG0666    124 -------------------------------------LHLAAYNGNLEIVKLLLE-------------AGAD-------- 145
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  716 qcpkcapaqkklakvpvsglgVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKC 795
Cdd:COG0666    146 ---------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  796 LLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNER 875
Cdd:COG0666    205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284

                   ....*
gi 1147376792  876 QRTAL 880
Cdd:COG0666    285 LLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-893 9.88e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 9.88e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  725 KKLAKVPVSGLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPD 804
Cdd:COG0666     35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  805 NKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA- 883
Cdd:COG0666    115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAa 194
                          170
                   ....*....|.
gi 1147376792  884 -ERNSKIMELL 893
Cdd:COG0666    195 eNGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 2.72e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.72e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACA 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  539 RGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCALNPKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-619 3.34e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACA 538
Cdd:COG0666    116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  539 RGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCALNPKILSIMEAHR 618
Cdd:COG0666    196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                   .
gi 1147376792  619 L 619
Cdd:COG0666    273 L 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-893 1.26e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 1.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  725 KKLAKVPVSGLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPD 804
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  805 NKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA- 883
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAa 161
                          170
                   ....*....|.
gi 1147376792  884 -ERNSKIMELL 893
Cdd:COG0666    162 aNGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-840 3.20e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 3.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  748 LHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKpdNKDLRGNTPLIYACSGGHHEVAA 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1147376792  828 LLLQHGVSIDTRN 840
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-873 1.70e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  781 LHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHgVSIDTRNNrGNTALHEAVAGKHVFVVE 860
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1147376792  861 LLLLHGASVHILN 873
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 2.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  500 LHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYYDVQSCRLDignekGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75
                           90
                   ....*....|
gi 1147376792  580 IIETLVQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
429-468 1.33e-19

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: 82.69  E-value: 1.33e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1147376792  429 KMCHPLCFCDDCERLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
703-874 1.13e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 1.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  703 VSAADLEFCHPLCQCPKCAPAQKKLAKVPVS-GLGVNVTNQDGSSPLHLAALHGRADL--IPLLLKHGANPQAQDAdqai 779
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKSNSYSIVEYLLDnGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNR---- 174
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  780 plhlacqkghfqaVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVV 859
Cdd:PHA03100   175 -------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
                          170
                   ....*....|....*
gi 1147376792  860 ELLLLHGASVHILNE 874
Cdd:PHA03100   242 KLLLNNGPSIKTIIE 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
738-872 1.82e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 1.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  738 NVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYA 817
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147376792  818 CSGGHHEVAALLLQHGVSIDTRNNRGN-TALHEAVAGKHVFVVELLLLHGASVHIL 872
Cdd:PHA02875   176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
706-747 3.43e-18

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: 78.91  E-value: 3.43e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1147376792  706 ADLEFCHPLCQCPKCAPAQKKLAKVPVSGLGVNVTNQDGSSP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-553 7.01e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 7.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  467 LHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDvqDNDGSTPLHLACARGHEDCVK 546
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                   ....*..
gi 1147376792  547 ALVYYDV 553
Cdd:pfam12796   79 LLLEKGA 85
PHA02878 PHA02878
ankyrin repeat protein; Provisional
714-883 1.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 1.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  714 LCQCPKCAPAQKKLAKVPVS-GLGVNVTNQD-GSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQ 791
Cdd:PHA02878   136 IDKKSKDDIIEAEITKLLLSyGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  792 AVKCLLDSNAKPDNKDLRGNTPLIYACSG-GHHEVAALLLQHGVSIDTRNN-RGNTALHEAVAGKHvfVVELLLLHGASV 869
Cdd:PHA02878   216 IVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADI 293
                          170
                   ....*....|....
gi 1147376792  870 HILNERQRTALDCA 883
Cdd:PHA02878   294 NSLNSYKLTPLSSA 307
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
264-363 8.40e-16

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: 74.17  E-value: 8.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  264 IPRAKRELAQLNRCTSPQQKLVCLRRVVQLIMQTPSQRVSLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80
                           90       100
                   ....*....|....*....|
gi 1147376792  344 AKDELGYCLTSMEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02875 PHA02875
ankyrin repeat protein; Provisional
733-871 5.20e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.49  E-value: 5.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  733 SGLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDN---KDlr 809
Cdd:PHA02875    24 IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD-- 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147376792  810 GNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHI 871
Cdd:PHA02875   102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
PHA02874 PHA02874
ankyrin repeat protein; Provisional
734-913 1.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTP 813
Cdd:PHA02874   147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  814 LIYACSggHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGK-HVFVVELLLLHGASVHILNERQRTALDCA----ERNSK 888
Cdd:PHA02874   227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAfkyiNKDPV 304
                          170       180
                   ....*....|....*....|....*..
gi 1147376792  889 IMELL--QVVPSCVASLGDTEEADHRE 913
Cdd:PHA02874   305 IKDIIanAVLIKEADKLKDSDFLEHIE 331
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
429-466 3.49e-14

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: 67.28  E-value: 3.49e-14
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1147376792  429 KMCHPLCFCDDCERLVSGRLNDPSVVTPFSRDDRGHTP 466
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
724-869 1.20e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 75.29  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  724 QKKLAKVPVSGLGVNVTNQDG----SSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDS 799
Cdd:PLN03192   501 HKELHDLNVGDLLGDNGGEHDdpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  800 NAKPDNKDLRGNTPLIYACSGGHHEV-------AAL------------------------LLQHGVSIDTRNNRGNTALH 848
Cdd:PLN03192   581 ACNVHIRDANGNTALWNAISAKHHKIfrilyhfASIsdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQ 660
                          170       180
                   ....*....|....*....|.
gi 1147376792  849 EAVAGKHVFVVELLLLHGASV 869
Cdd:PLN03192   661 VAMAEDHVDMVRLLIMNGADV 681
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
757-893 2.13e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.91  E-value: 2.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  757 ADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSI 836
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1147376792  837 DTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA--ERNSKIMELL 893
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayNGNLEIVKLL 139
PHA03100 PHA03100
ankyrin repeat protein; Provisional
460-596 2.13e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  460 DDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLL------------------LLHHK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  520 ASTDVQDNDGSTPLHLACARGHEDCVKALVYYdvqSCRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNR 596
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
673-807 4.13e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 4.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  673 LLRAVADGDLEMVRYLLEwieedvdegdeivsaadlefchplcqcpkcapaqkklakvpvSGLGVNVTNQDGSSPLHLAA 752
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE------------------------------------------NGADANLQDKNGRTALHLAA 38
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  753 LHGRADLIPLLLKHgANPQAQDADQAiPLHLACQKGHFQAVKCLLDSNAKPDNKD 807
Cdd:pfam12796   39 KNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
737-893 5.80e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 5.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  737 VNVTNQDGSSPLHLAAL------HGRaDLIPLLLKHGANPQAQDADQAIPLHLACQK--GHFQAVKCLLDSNAKPDNKDL 808
Cdd:PHA03100    61 INSSTKNNSTPLHYLSNikynltDVK-EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNS 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  809 RGNTPLIYACSGGHH--EVAALLLQHGV----------------SIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVH 870
Cdd:PHA03100   140 DGENLLHLYLESNKIdlKILKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
                          170       180
                   ....*....|....*....|....*
gi 1147376792  871 ILNERQRTALD--CAERNSKIMELL 893
Cdd:PHA03100   220 LVNKYGDTPLHiaILNNNKEIFKLL 244
PHA02876 PHA02876
ankyrin repeat protein; Provisional
480-869 2.23e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.25  E-value: 2.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  480 DLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVyydvqSCRLD 559
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  560 IgnEKGDTPLHIAARwgyQGIIET---LVQNGAPTEVQNRLRETPQQCALNPKILSimeahRLSfekrPKPSEAPVpspq 636
Cdd:PHA02876   237 I--NKNDLSLLKAIR---NEDLETsllLYDAGFSVNSIDDCKNTPLHHASQAPSLS-----RLV----PKLLERGA---- 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  637 rsvdsvsqgsssssfsstvvsvrQEEARKDYREVEKLLRAVADGDLEMVRYLlewIEEDVDegdeiVSAADLEFCHPLCQ 716
Cdd:PHA02876   299 -----------------------DVNAKNIKGETPLYLMAKNGYDTENIRTL---IMLGAD-----VNAADRLYITPLHQ 347
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  717 CPKCapAQKKLAKVPVSGLGVNVTNQD--GSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLA-CQKGHFQAV 793
Cdd:PHA02876   348 ASTL--DRNKDIVITLLELGANVNARDycDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSV 425
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147376792  794 KCLLD--SNAKPDNKDLrgNTPLIYACSGG-HHEVAALLLQHGVSIDTRNNRGNTALheAVAGKHVFVVELLLLHGASV 869
Cdd:PHA02876   426 KTLIDrgANVNSKNKDL--STPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
725-874 2.47e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 2.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  725 KKLAKVPVSGLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQA-----VKCLLDS 799
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEY 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147376792  800 NAKPDNKDLRGNTPLIYACSG--GHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHV--FVVELLLLHGASVHILNE 874
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 3.56e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.56e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1147376792  456 PFSRDDRGHTPLHVAALCGQASLIDLLVSKgAVVNATDYhGSTPLHLACQKGYQSVTLLLLHHKASTDVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
459-606 4.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 4.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACA 538
Cdd:PHA02874   153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1147376792  539 rgHEDCVKALVyydVQSCRLDIGNEKGDTPLHIAARWG-YQGIIETLVQNGAPTEVQNRLRETPQQCAL 606
Cdd:PHA02874   233 --HNRSAIELL---INNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAF 296
PHA03095 PHA03095
ankyrin-like protein; Provisional
459-800 7.60e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 7.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQ---ASLIDLLVSKGAVVNATDYHGSTPLHL-ACQKGYQSVTLLLLHHKASTDVQDNDGSTPLH 534
Cdd:PHA03095    43 RGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  535 lACARG---HEDCVKALVYYDVQSCRLDignEKGDTPLHIAARWG--YQGIIETLVQNGA-PTEVQNRLRetpqqcalnp 608
Cdd:PHA03095   123 -VYLSGfniNPKVIRLLLRKGADVNALD---LYGMTPLAVLLKSRnaNVELLRLLIDAGAdVYAVDDRFR---------- 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  609 kilSIMEAHRLSFekrpkpseapvpspqrsvdsvsqgsssssfsstvvsvrqeeaRKDYREVEKLLRAVADgdlemvryl 688
Cdd:PHA03095   189 ---SLLHHHLQSF------------------------------------------KPRARIVRELIRAGCD--------- 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  689 lewieedvdegdeiVSAADLEFCHPLCQCPK-CAPAQKKLAKVPVSGLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHG 767
Cdd:PHA03095   215 --------------PAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1147376792  768 ANPQAQDADQAIPLHLACQKGHFQAVKCLLDSN 800
Cdd:PHA03095   281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
PHA02874 PHA02874
ankyrin repeat protein; Provisional
459-608 1.18e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACA 538
Cdd:PHA02874   120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  539 RGHEDCVKALVyydVQSCRLDIGNEKGDTPLHIAARWGyQGIIETLVQNgAPTEVQNRLRETPQQCALNP 608
Cdd:PHA02874   200 YGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINN-ASINDQDIDGSTPLHHAINP 264
PHA03095 PHA03095
ankyrin-like protein; Provisional
756-893 1.53e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  756 RADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQ---AVKCLLDSNAKPDNKDLRGNTPLI-YACSGGHHEVAALLLQ 831
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  832 HGVSIDTRNNRGNTALHEAVAGK--HVFVVELLLLHGASVHILNERQRTALDCAERNSKI-MELL 893
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnVELL 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
478-613 2.67e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  478 LIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTL--LLLHHKASTDVQDNDGSTPLHLACARGHED--CVKALVY--Y 551
Cdd:PHA03100    88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDkgV 167
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147376792  552 DVQS-----------CRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCALNPKILSI 613
Cdd:PHA03100   168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
468-559 3.27e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 3.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  468 HVAAlCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKA 547
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                           90
                   ....*....|..
gi 1147376792  548 LVYYDVQSCRLD 559
Cdd:PTZ00322   167 LSRHSQCHFELG 178
PHA02878 PHA02878
ankyrin repeat protein; Provisional
461-601 3.81e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 3.81e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  461 DRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARg 540
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  541 hedcvkaLVYYDVQSCRLDIG---NEK----GDTPLHIAARwgYQGIIETLVQNGAPTEVQNRLRETP 601
Cdd:PHA02878   245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTP 303
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
709-747 4.52e-11

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: 58.42  E-value: 4.52e-11
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1147376792  709 EFCHPLCQCPKCAPAQKKLAKVPvSGLGVNVTNQDGSSP 747
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDP-SGVGVNSRDQDGRTP 38
Ank_4 pfam13637
Ankyrin repeats (many copies);
810-863 7.82e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 7.82e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1147376792  810 GNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLL 863
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
673-850 1.00e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 1.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  673 LLRAVADGDLEMVRYLLEWIEEdvdegdeiVSAADLEFCHPLCQCPKCAPAQkkLAKVPV-SGLGVNVTNQDGSSPLHLA 751
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIKHNFFD--IIKLLLeKGAYANVKDNNGESPLHNA 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  752 ALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQkgHFQAVKCLLDSNAKPDNKDLRGNTPLIYA----CSgghHEVAA 827
Cdd:PHA02874   198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIID 272
                          170       180
                   ....*....|....*....|...
gi 1147376792  828 LLLQHGVSIDTRNNRGNTALHEA 850
Cdd:PHA02874   273 ILLYHKADISIKDNKGENPIDTA 295
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
749-832 1.83e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  749 HLAAlHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAAL 828
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ....
gi 1147376792  829 LLQH 832
Cdd:PTZ00322   167 LSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
734-906 2.19e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHL---AALHGRADLIPLLLKHGANPQAQDADQAIPLHL-ACQKGHFQAVKCLLDSNAKPDNKDLR 809
Cdd:PHA03095    37 GADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKV 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  810 GNTPL-IYACSGG-HHEVAALLLQHGVSIDTRNNRGNTALHEAV--AGKHVFVVELLLLHGASVHILNERQRTALD---- 881
Cdd:PHA03095   117 GRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLksRNANVELLRLLIDAGADVYAVDDRFRSLLHhhlq 196
                          170       180
                   ....*....|....*....|....*...
gi 1147376792  882 -CAERNSKIMEL--LQVVPSCVASLGDT 906
Cdd:PHA03095   197 sFKPRARIVRELirAGCDPAATDMLGNT 224
PHA02875 PHA02875
ankyrin repeat protein; Provisional
465-589 2.32e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 2.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  465 TPLHVAALCGQASLIDLLVSKGAVVNATDYH-GSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHED 543
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1147376792  544 CVKALVyyDVQSCrLDIGNEKGDTPLHIAARWGYQGIIETLVQNGA 589
Cdd:PHA02875   150 GIELLI--DHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA02876 PHA02876
ankyrin repeat protein; Provisional
673-896 1.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  673 LLRAVADGDLEMVRYLLewieedvDEGDEIVSAADLEFChPLCQCPKCAPAQKKLAKVPVSGLGVNVTNQDGSSPLHLAA 752
Cdd:PHA02876   244 LLKAIRNEDLETSLLLY-------DAGFSVNSIDDCKNT-PLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  753 LHG-RADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQ-AVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLL 830
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  831 QHGVSIDTRNNRGNTALHEAVAGKHVFV-VELLLLHGASVHILNERQRTALDCAERNSKIMELLQVV 896
Cdd:PHA02876   396 DYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEML 462
PHA02878 PHA02878
ankyrin repeat protein; Provisional
475-598 1.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 1.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  475 QASLIDLLVSKGAVVNATDYH-GSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYYdv 553
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1147376792  554 qSCRLDIGNEKGDTPLHIAArwGY---QGIIETLVQNGAPTEVQNRLR 598
Cdd:PHA02878   224 -GASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYIL 268
PHA02875 PHA02875
ankyrin repeat protein; Provisional
462-549 1.29e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGH 541
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                   ....*...
gi 1147376792  542 EDCVKALV 549
Cdd:PHA02875   181 IAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
744-797 1.58e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.58e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1147376792  744 GSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLL 797
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-549 1.67e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.67e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1147376792  496 GSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALV 549
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
737-880 1.91e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  737 VNVTNQDGSSPLH--LAALHGRADLIPLLLKHGANPQAQDADQAIPLHlACQKGH---FQAVKCLLDSNAKPDNKDLRGN 811
Cdd:PHA03095   110 VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRnanVELLRLLIDAGADVYAVDDRFR 188
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  812 TPLiyacsggHH---------EVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVF--VVELLLLHGASVHILNERQRTAL 880
Cdd:PHA03095   189 SLL-------HHhlqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPL 261
PHA02874 PHA02874
ankyrin repeat protein; Provisional
758-893 1.95e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  758 DLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSID 837
Cdd:PHA02874   105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  838 TRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA-ERNSKIMELL 893
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiIHNRSAIELL 241
PHA02875 PHA02875
ankyrin repeat protein; Provisional
463-613 2.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 2.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  463 GHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKG-YQSVTLLLLHHKASTDVQDNDGSTPLHLACARGH 541
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1147376792  542 EDCVKALVYYDVQScrlDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCALNPKILSI 613
Cdd:PHA02875   115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PHA03095 PHA03095
ankyrin-like protein; Provisional
481-863 7.50e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 7.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  481 LLVSKGAVVNATDYHGSTPLHLACQKGYQSVT---LLLLHHKASTDVQDNDGSTPLHL-ACARGHEDCVKALVYYDVqsc 556
Cdd:PHA03095    32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGA--- 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  557 RLDIGNEKGDTPLHIAAR--WGYQGIIETLVQNGAPTEVQNRLRETPQQCalnpkilsimeahrlsfekrpkpseapvps 634
Cdd:PHA03095   109 DVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAV------------------------------ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  635 pqrsvdsvsqgsssssfsstvvsvrqeearkdyrevekLLRAVaDGDLEMVRYLLEWIEEdvdegdeiVSAADLEF---C 711
Cdd:PHA03095   159 --------------------------------------LLKSR-NANVELLRLLIDAGAD--------VYAVDDRFrslL 191
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  712 HPLCQCPKcaPAQKKLAKVPVSGLGVNVTNQDGSSPLHLAALHG---RADLIPLLLKhganpqaqdadqaiplhlacqkg 788
Cdd:PHA03095   192 HHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA----------------------- 246
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  789 hfqavkclldsNAKPDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLL 863
Cdd:PHA03095   247 -----------GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
780-830 8.74e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 8.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1147376792  780 PLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLL 830
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
375-586 9.53e-09

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: 59.42  E-value: 9.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  375 EGFGDRLCLRQRVSLLSQM--ASTPTDCLFKHIA--AGNQKEVEKLLSQEDHDRDAIqkmchplcfcddcerlvsgrlnD 450
Cdd:cd22193      5 LGFLQDLCRRRKDLTDSEFteSSTGKTCLMKALLnlNPGTNDTIRILLDIAEKTDNL----------------------K 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  451 PSVVTPFsRDD--RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGSTPLHL-ACQKGYQSVTL 513
Cdd:cd22193     63 RFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQY 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  514 LL--LHHKASTDVQDNDGSTPLHLACA-----RGHEDCVKALvyYD---VQSCRL-------DIGNEKGDTPLHIAARWG 576
Cdd:cd22193    142 LLenEHQPADIEAQDSRGNTVLHALVTvadntKENTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
                          250
                   ....*....|
gi 1147376792  577 YQGIIETLVQ 586
Cdd:cd22193    220 KIEILKYILQ 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
473-606 9.79e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 9.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  473 CGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYyd 552
Cdd:PHA02874   101 CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-- 178
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1147376792  553 vQSCRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCAL 606
Cdd:PHA02874   179 -KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
456-547 1.03e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  456 PFSRDDRGHTPLHVAALCG--QASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPL 533
Cdd:PHA03095   215 PAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
                           90
                   ....*....|....
gi 1147376792  534 HLACARGHEDCVKA 547
Cdd:PHA03095   295 SLMVRNNNGRAVRA 308
Ank_5 pfam13857
Ankyrin repeats (many copies);
482-536 2.29e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 2.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147376792  482 LVSKGAV-VNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLA 536
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
264-379 5.38e-08

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 52.07  E-value: 5.38e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792   264 IPRAKRELAQLNRCTSPQQKLVCLRRVVQLIMqTPSQRVSLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIY-TLLETQSGEVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80
                            90       100       110
                    ....*....|....*....|....*....|....*..
gi 1147376792   344 AKDELGYCLTSMEAAIEYIRQ-GSLSVKPLDSEGFGD 379
Cdd:smart00167   81 LTGEGGYYLTSLSAALALIKGlTEAHALPLSPEQELE 117
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
470-589 5.58e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  470 AALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALV 549
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  550 YY--------------------DVQSCR------LDIGNE--KGDTPLHIAARWGYQGIIETLVQNGA 589
Cdd:PLN03192   612 HFasisdphaagdllctaakrnDLTAMKellkqgLNVDSEdhQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02798 PHA02798
ankyrin-like protein; Provisional
758-882 6.90e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.38  E-value: 6.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  758 DLIPLLLKHGANPQAQDADQAIPL-----HLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGH---HEVAALL 829
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFM 131
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  830 LQHGVSIDTRNNRGNTALHEAVAGKH---VFVVELLLLHGASVHIL-NERQRTALDC 882
Cdd:PHA02798   132 IENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHnNKEKYDTLHC 188
PHA02876 PHA02876
ankyrin repeat protein; Provisional
734-916 7.76e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 7.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRgntp 813
Cdd:PHA02876   168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  814 LIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVF-VVELLLLHGASVHILNERQRTALDCAERNSKIMEL 892
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEN 323
                          170       180
                   ....*....|....*....|....
gi 1147376792  893 LQVvpscVASLGDTEEADHREYVT 916
Cdd:PHA02876   324 IRT----LIMLGADVNAADRLYIT 343
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
462-604 1.09e-07

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: 56.04  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD-------------YHGSTPLHL-ACQKGYQSVTLLLLH--HKASTDVQ 525
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQ 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  526 DNDGSTPLH--------------LACARGHEdcvkaLVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGIIETLVQN 587
Cdd:cd21882    152 DSLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
                          170
                   ....*....|....*..
gi 1147376792  588 GAPTEVQNRLRETPQQC 604
Cdd:cd21882    227 EFSGPYQPLSRKFTEWT 243
PHA02875 PHA02875
ankyrin repeat protein; Provisional
467-606 1.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  467 LHVAALC-----GQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLACARGh 541
Cdd:PHA02875     1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  542 eDCVKALVYYDVQSCRLDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETPQQCAL 606
Cdd:PHA02875    80 -DVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-850 3.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.25e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1147376792  803 PDNKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEA 850
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
458-592 4.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 4.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  458 SRDDRGHTPLHVAALCGQAS-LIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTL-LLLHHKASTDVQDNDGSTPLHL 535
Cdd:PHA02876   268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  536 ACARG-HEDCVKALVYYDVQSCRLDIGNEkgdTPLHIAARWGYQGIIETLVQNGAPTE 592
Cdd:PHA02876   348 ASTLDrNKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIE 402
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
749-870 4.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 4.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  749 HLAALHG--RADLIPlllKHGANPQaQDADQAIPLHLACQKGHFQA------VKCLLDSNAKPDNKDLRGNTPLIYACSG 820
Cdd:PTZ00322    50 HLEALEAteNKDATP---DHNLTTE-EVIDPVVAHMLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACAN 125
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1147376792  821 GHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVH 870
Cdd:PTZ00322   126 GHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
449-586 4.79e-07

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: 53.93  E-value: 4.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  449 NDPSvvtpFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNA------------TD--YHGSTPLHLACQKGYQSVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  515 LLHHKASTDVQDNDGSTPLHLA------CARGHE---DCVKALVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGII 581
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLvmenefKAEYEElscQMYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVLF 273

                   ....*
gi 1147376792  582 ETLVQ 586
Cdd:TIGR00870  274 RLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 5.10e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 5.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  529 GSTPLHLACARGHEDCVKALVYYDVQSCRLDIGnekGDTPLHIAARWGYQGIIETLV 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
459-562 6.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 6.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  459 RDDRGHTPLHVA-ALCGQASLIDLLVSKGAVVNATDY-HGSTPLHLACQKgyQSVTLLLLHHKASTDVQDNDGSTPLHLA 536
Cdd:PHA02878   230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
                           90       100
                   ....*....|....*....|....*.
gi 1147376792  537 carghedcvkALVYYDVQSCRLDIGN 562
Cdd:PHA02878   308 ----------VKQYLCINIGRILISN 323
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
463-587 6.78e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 6.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  463 GHTPLHVAALCGQASLIDLLVSKGAVVN---ATD-----------YHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDND 528
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  529 GSTPLH---------LACARghEDCVKALVYYDVQSCRLDIGNEKGDTPLHIAARWGYQGIIETLVQN 587
Cdd:cd22192    169 GNTVLHilvlqpnktFACQM--YDLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
737-784 7.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 7.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1147376792  737 VNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLA 784
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
456-518 7.08e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.08e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147376792  456 PFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHH 518
Cdd:PTZ00322   108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 9.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 9.95e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1147376792  514 LLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYYDVQscrLDIGNEKGDTPLHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
733-804 1.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  733 SGLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLL---------DSNAKP 803
Cdd:PTZ00322   104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKP 183

                   .
gi 1147376792  804 D 804
Cdd:PTZ00322   184 D 184
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
514-627 1.66e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  514 LLLHHKASTDVQDNDGSTPLHLACARGHEDCVKALVYYDVQSCRLDignEKGDTPLHIAARWGYQGIIETLVQNgAPTEV 593
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLSRH-SQCHF 175
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1147376792  594 QNRLRETPQQCALNPKIL--SIMEAHRLSFEKRPKP 627
Cdd:PTZ00322   176 ELGANAKPDSFTGKPPSLedSPISSHHPDFSAVPQP 211
PHA02876 PHA02876
ankyrin repeat protein; Provisional
458-589 1.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  458 SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLAC--QKGYQSVTlLLLHHKASTDVQDNDGSTPLHL 535
Cdd:PHA02876   370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcgTNPYMSVK-TLIDRGANVNSKNKDLSTPLHY 448
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  536 ACARGHE-DCVKALVYYDVQSCRLDIGNEkgdTPLHIAArwGYQGIIETLVQNGA 589
Cdd:PHA02876   449 ACKKNCKlDVIEMLLDNGADVNAINIQNQ---YPLLIAL--EYHGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
458-527 4.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 4.27e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  458 SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDN 527
Cdd:PHA03100   187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
744-893 4.42e-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: 50.78  E-value: 4.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  744 GSSPLHLAALHGRADLIPLLLKHGA----NPQAQDADQA-IPLHLACQKGHFQAVKCLLDSNA--------------KPD 804
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPelvnEPMTSDLYQGeTALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPK 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  805 NKDLRGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALH------EAVAGKHVFvvELLL-----LHGASV-HIL 872
Cdd:cd22192    131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlqpNKTFACQMY--DLILsydkeDDLQPLdLVP 208
                          170       180
                   ....*....|....*....|...
gi 1147376792  873 NERQRTALDCA--ERNSKIMELL 893
Cdd:cd22192    209 NNQGLTPFKLAakEGNIVMFQHL 231
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 6.55e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.55e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1147376792  456 PFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
463-516 6.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 6.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1147376792  463 GHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLL 516
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
465-606 6.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 6.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  465 TPLHvaalcgQASLID-------LLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPLHLA- 536
Cdd:PHA02876   343 TPLH------QASTLDrnkdiviTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1147376792  537 CARGHEDCVKALVYydvQSCRLDIGNEKGDTPLHIAARWGYQ-GIIETLVQNGAPTEVQNRLRETPQQCAL 606
Cdd:PHA02876   417 CGTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
462-576 1.00e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.76  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGSTPLHL-ACQKGYQSVTLLLlhHKASTDV-- 524
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLM--EKESTDIts 217
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147376792  525 QDNDGSTPLHLAC-----ARGHEDCVKALvyYD--VQSCR---LD-IGNEKGDTPLHIAARWG 576
Cdd:cd22194    218 QDSRGNTVLHALVtvaedSKTQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMG 278
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
462-586 1.33e-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: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGSTPLHL-ACQKGYQSVTLLLL--HHKASTDV 524
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  525 QDNDGSTPLH--LACARGHEDCVKALV-YYD---VQSCRL-------DIGNEKGDTPLHIAARWGYQGIIETLVQ 586
Cdd:cd22196    173 RDSMGNTVLHalVEVADNTPENTKFVTkMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
Ank_5 pfam13857
Ankyrin repeats (many copies);
763-817 1.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147376792  763 LLKHG-ANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYA 817
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
465-601 1.94e-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: 48.47  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  465 TPLHVAALCGQ-ASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLhhKASTDVQDN-------DGSTPLHLA 536
Cdd:cd22192     19 SPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--EAAPELVNEpmtsdlyQGETALHIA 96
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1147376792  537 CARGHEDCVKALVYY--DVQSCR-------LDIGN--EKGDTPLHIAARWGYQGIIETLVQNGAPTEVQNRLRETP 601
Cdd:cd22192     97 VVNQNLNLVRELIARgaDVVSPRatgtffrPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
PHA02875 PHA02875
ankyrin repeat protein; Provisional
751-893 2.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  751 AALHGRADLIPLLLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYACSGGHHEVAALLL 830
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1147376792  831 QHGVSI-DTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA--ERNSKIMELL 893
Cdd:PHA02875    89 DLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAvmMGDIKGIELL 154
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
809-841 2.16e-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: 42.28  E-value: 2.16e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1147376792  809 RGNTPLIYAC-SGGHHEVAALLLQHGVSIDTRNN 841
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
462-586 3.19e-05

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: 47.93  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD-------------YHGSTPLHL-ACQKGYQSVTLLL--LHHKASTDVQ 525
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1147376792  526 DNDGSTPLH-LACARGHEDCVKALV--YYD---VQSCRLD-------IGNEKGDTPLHIAARWGYQGIIETLVQ 586
Cdd:cd22197    173 DSLGNTVLHaLVMIADNSPENSALVikMYDgllQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
809-837 3.67e-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: 41.42  E-value: 3.67e-05
                            10        20
                    ....*....|....*....|....*....
gi 1147376792   809 RGNTPLIYACSGGHHEVAALLLQHGVSID 837
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
426-466 3.75e-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: 41.93  E-value: 3.75e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1147376792  426 AIQKMCHPLCFCDDCERLVSG-RLNDPSVVTPFSRDDRGHTP 466
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
673-889 4.38e-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: 47.38  E-value: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  673 LLRAVADGDLEMVRYLLEWIEEDVDEGDEIVSAADLEF--------CHPLCQCPKCAPAQkkLAKVPVSGlgvnvTNQDG 744
Cdd:TIGR00870   56 LFVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYvdaveailLHLLAAFRKSGPLE--LANDQYTS-----EFTPG 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  745 SSPLHLAALHGRADLIPLLLKHGANpqaqdadqaipLHLACQKGHFQAvkclldsnaKPDNKDLR-GNTPL-IYACSGgH 822
Cdd:TIGR00870  129 ITALHLAAHRQNYEIVKLLLERGAS-----------VPARACGDFFVK---------SQGVDSFYhGESPLnAAACLG-S 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  823 HEVAALLLQHGVSIDTRNNRGNTALH-------------EAVAGKHVFVVELLLLHGASV---HILNERQRTALDCAERN 886
Cdd:TIGR00870  188 PSIVALLSEDPADILTADSLGNTLLHllvmenefkaeyeELSCQMYNFALSLLDKLRDSKeleVILNHQGLTPLKLAAKE 267

                   ...
gi 1147376792  887 SKI 889
Cdd:TIGR00870  268 GRI 270
Ank_5 pfam13857
Ankyrin repeats (many copies);
829-883 4.72e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1147376792  829 LLQHG-VSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA 883
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
826-904 5.46e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  826 AALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCAERNS--KIMELLQVVPSCVASL 903
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQLLSRHSQCHFEL 177

                   .
gi 1147376792  904 G 904
Cdd:PTZ00322   178 G 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
528-553 6.80e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 6.80e-05
                            10        20
                    ....*....|....*....|....*.
gi 1147376792   528 DGSTPLHLACARGHEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA03095 PHA03095
ankyrin-like protein; Provisional
456-569 6.92e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 6.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  456 PFSRDDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGSTPLHLACQKG--YQSVTLLLLHHKASTDVQDNDGST 531
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQT 259
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1147376792  532 PLHLA-CARGHEDCVKALvyydVQSCRLDIGNEKGDTPL 569
Cdd:PHA03095   260 PLHYAaVFNNPRACRRLI----ALGADINAVSSDGNTPL 294
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
743-770 8.52e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 8.52e-05
                            10        20
                    ....*....|....*....|....*...
gi 1147376792   743 DGSSPLHLAALHGRADLIPLLLKHGANP 770
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
842-874 8.55e-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: 40.74  E-value: 8.55e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1147376792  842 RGNTALHEAVA-GKHVFVVELLLLHGASVHILNE 874
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
455-549 9.08e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 9.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  455 TPFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLAC---QKGYQSVTLLLLHHKASTDVQDNDGST 531
Cdd:PHA02946    64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143
                           90
                   ....*....|....*...
gi 1147376792  532 PLhLACARGHEDCVKALV 549
Cdd:PHA02946   144 PL-LACTDPSERVFKKIM 160
PHA02946 PHA02946
ankyin-like protein; Provisional
688-787 1.02e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  688 LLEWIEEDVDEGDEIVSAADLEFCHPLCQCPKcaPAQKKLAKVPVSGLGVNVTNQDGSSPLH--LAALHGRADLIPLLLK 765
Cdd:PHA02946   119 VIERINLLVQYGAKINNSVDEEGCGPLLACTD--PSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMK 196
                           90       100
                   ....*....|....*....|..
gi 1147376792  766 HGANPQAQDADQAIPLHLACQK 787
Cdd:PHA02946   197 LGISPSKPDHDGNTPLHIVCSK 218
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
743-774 1.13e-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: 40.35  E-value: 1.13e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1147376792  743 DGSSPLHLAALH-GRADLIPLLLKHGANPQAQD 774
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
401-560 1.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  401 LFKHIAAGNQKEVEKLLSQEDHDRDAIQKMCH-PLCFCD-----DCERLVSGRLNDPSVvtpfSRDDRgHTPLHVAALCG 474
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMtPLHLATilkklDIMKLLIARGADPDI----PNTDK-FSPLHLAVMMG 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  475 QASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGstplhlacarghedCVKALVyYDVQ 554
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG--------------CVAALC-YAIE 211

                   ....*.
gi 1147376792  555 SCRLDI 560
Cdd:PHA02875   212 NNKIDI 217
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-533 1.29e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.33  E-value: 1.29e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1147376792  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTDVQDNDGSTPL 533
Cdd:COG0666    215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
793-896 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  793 VKCLLDSNAKPDNKDL-RGNTPLIYACSGGHHEVAALLLQHGVSIDTRNNRGNTALHEAVAGKHVFVVELLLLHGASVHI 871
Cdd:PHA02878   150 TKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                           90       100
                   ....*....|....*....|....*
gi 1147376792  872 LNERQRTALDCAERNSKIMELLQVV 896
Cdd:PHA02878   230 RDKCGNTPLHISVGYCKDYDILKLL 254
PHA02946 PHA02946
ankyin-like protein; Provisional
734-848 2.37e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  734 GLGVNVTNQDGSSPLHLAALHGRADLIPLLLKHGANPQAQDADQAIPLHL--ACQKGHFQAVKCLLDSNAKPDNK-DLRG 810
Cdd:PHA02946    62 GYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSvDEEG 141
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1147376792  811 NTPLIyACSGGHHEVAALLLQHGVSIDTRNNRGNTALH 848
Cdd:PHA02946   142 CGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
Ank_4 pfam13637
Ankyrin repeats (many copies);
843-883 2.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.77e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1147376792  843 GNTALHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCA 883
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
462-493 3.13e-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: 3.13e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1147376792  462 RGHTPLHVAAL-CGQASLIDLLVSKGAVVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
455-586 5.63e-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: 44.07  E-value: 5.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  455 TPFsRD--DRGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGSTPLHLA-CQKGYQSVTLLL-- 515
Cdd:cd22195    128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  516 LHHKASTDVQDNDGSTPLH--LACARGHEDCVKALV-YYDV---------QSCRLD-IGNEKGDTPLHIAARWGYQGIIE 582
Cdd:cd22195    207 AHKKADLRRQDSRGNTVLHalVAIADNTRENTKFVTkMYDLllikcaklyPDCNLEaILNNDGMSPLMMAAKLGKIGIFQ 286

                   ....
gi 1147376792  583 TLVQ 586
Cdd:cd22195    287 HIIR 290
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
743-772 5.74e-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: 5.74e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1147376792  743 DGSSPLHLAALHGRADLIPLLLKHGANPQA 772
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
462-491 6.07e-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: 6.07e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1147376792   462 RGHTPLHVAALCGQASLIDLLVSKGAVVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
809-838 7.33e-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: 7.33e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1147376792  809 RGNTPLIYACSGGHHEVAALLLQHGVSIDT 838
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
564-596 7.96e-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: 7.96e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1147376792  564 KGDTPLHIAA-RWGYQGIIETLVQNGAPTEVQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
842-871 8.57e-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: 37.57  E-value: 8.57e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1147376792   842 RGNTALHEAVAGKHVFVVELLLLHGASVHI 871
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
452-527 9.38e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 9.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  452 SVVTPF--------SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQKGYQSVTLLLLHHKASTD 523
Cdd:PHA03095   238 SLVLPLliagisinARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317

                   ....
gi 1147376792  524 VQDN 527
Cdd:PHA03095   318 TVAA 321
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
495-527 1.44e-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: 37.27  E-value: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1147376792  495 HGSTPLHLAC-QKGYQSVTLLLLHHKASTDVQDN 527
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
528-551 1.65e-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: 36.88  E-value: 1.65e-03
                           10        20
                   ....*....|....*....|....*
gi 1147376792  528 DGSTPLHLACAR-GHEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSK 25
PHA02946 PHA02946
ankyin-like protein; Provisional
763-837 2.02e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.96  E-value: 2.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1147376792  763 LLKHGANPQAQDADQAIPLHLACQKGHFQAVKCLLDSNAKPDNKDLRGNTPLIYaCSGGHHEVAA---LLLQHGVSID 837
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIErinLLVQYGAKIN 134
PHA02946 PHA02946
ankyin-like protein; Provisional
431-535 2.38e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 2.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  431 CHPLCFCDD-CERLVSGRLN---DPSVVTPFSRDdrgHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGSTPLHLACQK 506
Cdd:PHA02946   142 CGPLLACTDpSERVFKKIMSigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218
                           90       100       110
                   ....*....|....*....|....*....|
gi 1147376792  507 GYQSVTLL-LLHHKASTDVQDNDGSTPLHL 535
Cdd:PHA02946   219 TVKNVDIInLLLPSTDVNKQNKFGDSPLTL 248
PHA02741 PHA02741
hypothetical protein; Provisional
454-536 3.54e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.64  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  454 VTPFSR-----------DDRGHTPLHVAALCGQA----SLIDLLVSKGAVVNATD-YHGSTPLHLAC-QKGYQSVTLLLL 516
Cdd:PHA02741    40 FTPFIRgdchaaalnatDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCC 119
                           90       100
                   ....*....|....*....|
gi 1147376792  517 HHKASTDVQDNDGSTPLHLA 536
Cdd:PHA02741   120 QPGIDLHFCNADNKSPFELA 139
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
564-589 4.51e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.51e-03
                            10        20
                    ....*....|....*....|....*.
gi 1147376792   564 KGDTPLHIAARWGYQGIIETLVQNGA 589
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_2 pfam12796
Ankyrin repeats (3 copies);
847-906 6.57e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.02  E-value: 6.57e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1147376792  847 LHEAVAGKHVFVVELLLLHGASVHILNERQRTALDCAERNSK---IMELLQVVPSCVASLGDT 906
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHleiVKLLLEHADVNLKDNGRT 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
780-804 7.38e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 7.38e-03
                            10        20
                    ....*....|....*....|....*
gi 1147376792   780 PLHLACQKGHFQAVKCLLDSNAKPD 804
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
842-871 7.61e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.61e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1147376792  842 RGNTALHEAVAGKHVFVVELLLLHGASVHI 871
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
453-593 8.99e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 8.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1147376792  453 VVTPFSRDDRGHTPLHVaaLCGQASLIDLLVSKGAVVNATDY-------HGSTPLHLACQKGY---QSVTLLLLHHKAST 522
Cdd:PHA02736     7 IIFASEPDIEGENILHY--LCRNGGVTDLLAFKNAISDENRYlvleynrHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1147376792  523 DVQDN-DGSTPLHLACARGHEDCVKALvyydvqsCR-----LDIGNEKGDTPLHIAARWGYQGIIETLVQNGAPTEV 593
Cdd:PHA02736    85 NGKERvFGNTPLHIAVYTQNYELATWL-------CNqpgvnMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
 
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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