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Conserved domains on  [gi|2024349109|ref|XP_015147921|]
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ankyrin repeat domain-containing protein 27 isoform X1 [Gallus gallus]

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];
732-897 1.34e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGN 811
Cdd:COG0666     75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  812 TPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCA--EPNSNI 889
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaeNGNLEI 234


                   ....*...
gi 2024349109  890 IKLLETAA 897
Cdd:COG0666    235 VKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
375-619 7.78e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 7.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  375 DRLYDKLLLRQRMNFLSQMATTPIDCLFKHIASGNQEEVERLLSQGDSDKDTVQKMCHPLCYC------DKCEKLVSGKL 448
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAarngdlEIVKLLLEAGA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  449 NdpsiitPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNN 528
Cdd:COG0666    112 D------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  529 GNTPLHLACTYGHEDCVKALVYYDVhscRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNS 608
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262

                          250
                   ....*....|.
gi 2024349109  609 KILSLMELNYL 619
Cdd:COG0666    263 GAALIVKLLLL 273
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 2.05e-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: 79.29  E-value: 2.05e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024349109  706 SKPEFCHPLCQCSKCGPAQKKFARVPANGLGVNVSNQDGFTP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 super family cl19569
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 7.84e-14

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.


The actual alignment was detected with superfamily member pfam02204:

Pssm-ID: 473191  Cd Length: 104  Bit Score: 68.39  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  264 IPRAKRELSQLNKCTSPQQKLLCLRKVVQIIMQSPSQRVNMETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRLCSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 2024349109  344 VKDELGYCLTSIEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
732-897 1.34e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGN 811
Cdd:COG0666     75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  812 TPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCA--EPNSNI 889
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaeNGNLEI 234


                   ....*...
gi 2024349109  890 IKLLETAA 897
Cdd:COG0666    235 VKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
375-619 7.78e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 7.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  375 DRLYDKLLLRQRMNFLSQMATTPIDCLFKHIASGNQEEVERLLSQGDSDKDTVQKMCHPLCYC------DKCEKLVSGKL 448
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAarngdlEIVKLLLEAGA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  449 NdpsiitPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNN 528
Cdd:COG0666    112 D------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  529 GNTPLHLACTYGHEDCVKALVYYDVhscRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNS 608
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262

                          250
                   ....*....|.
gi 2024349109  609 KILSLMELNYL 619
Cdd:COG0666    263 GAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-595 7.47e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  500 LHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYYdvhsCRLDIGNEkGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 2024349109  580 IIEVLLQNGANPNTQN 595
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-840 7.44e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  748 LHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYnAKQNKKDaYGNTPLIYACLNGHYETTA 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2024349109  828 LLLQRGASVNLSN 840
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.11e-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: 83.07  E-value: 1.11e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024349109  429 KMCHPLCYCDKCEKLVSGKLNDPSIITPFSRDDRGYTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 732-867 1.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHMAALHGHSDL--VSLLLKHGASISAKNaehavplhlacqkghsqVVECLMDYNAKQNKKDAY 809
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKN-----------------RVNYLLSYGVPINIKDVY 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349109  810 GNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGA 867
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 2.05e-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: 79.29  E-value: 2.05e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024349109  706 SKPEFCHPLCQCSKCGPAQKKFARVPANGLGVNVSNQDGFTP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 465-604 2.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  465 TPLHIAAICGQTSLVDLLVAKGAIVNATDYH-GSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHED 543
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024349109  544 CVKALVYydvHSCRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQC 604
Cdd:PHA02875   150 GIELLID---HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 7.84e-14

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: 68.39  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  264 IPRAKRELSQLNKCTSPQQKLLCLRKVVQIIMQSPSQRVNMETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRLCSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 2024349109  344 VKDELGYCLTSIEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 449-586 3.56e-09

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: 60.87  E-value: 3.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  449 NDPSiitpFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNA------------TD--YHGSTPLHLACQKGYQNVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  515 LLHYKASTDVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVHSCRL----DIGNEKGDTPLHIAARWGYQGI 580
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 2024349109  581 IEVLLQ 586
Cdd:TIGR00870  273 FRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 744-889 6.98e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 56.63  E-value: 6.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  744 GFTPLHMAALHGHSDLVSLLLKHGASISAK-NAEhavplhlACQKghSQVVECLmdynakqnkkdAYGNTPL-IYACLnG 821
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARaCGD-------FFVK--SQGVDSF-----------YHGESPLnAAACL-G 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  822 HYETTALLLQRGASVNLSNAKGNTALHEAVI-----GKNEALV----DLLLQNGAMT-------HIRNERNCTPADCAEP 885
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLHLLVMenefkAEYEELScqmyNFALSLLDKLrdskeleVILNHQGLTPLKLAAK 266


                   ....
gi 2024349109  886 NSNI 889
Cdd:TIGR00870  267 EGRI 270
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 744-889 1.57e-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: 55.40  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  744 GFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVplhlacqkghsqvveclmdYNAKQNKKDAYGNTPLIYACLNGHY 823
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTF-------------------FRPGPKNLIYYGEHPLSFAACVGNE 149

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  824 ETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALV----DLLL------QNGAMTHIRNERNCTPADCAEPNSNI 889
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILsydkedDLQPLDLVPNNQGLTPFKLAAKEGNI 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 743-772 2.24e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 2.24e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024349109   743 DGFTPLHMAALHGHSDLVSLLLKHGASISA 772
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-372 2.33e-05

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 44.75  E-value: 2.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109   264 IPRAKRELSQLNKCTSPQQKLLCLRKVVQIIMQSPSQRVNmETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRLCSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90       100
                    ....*....|....*....|....*....
gi 2024349109   344 VKDELGYCLTSIEAAIEYIRqgNLSDRST 372
Cdd:smart00167   81 LTGEGGYYLTSLSAALALIK--GLTEAHA 107
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-592 1.46e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.46e-04
                            10        20
                    ....*....|....*....|....*....
gi 2024349109   564 KGDTPLHIAARWGYQGIIEVLLQNGANPN 592
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
732-897 1.34e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGN 811
Cdd:COG0666     75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  812 TPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCA--EPNSNI 889
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaeNGNLEI 234


                   ....*...
gi 2024349109  890 IKLLETAA 897
Cdd:COG0666    235 VKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
673-894 2.90e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 2.90e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  673 LLRAVADGDLEMVRYLLEwteedlededdtvstskpefchplcqcskcgpaqkkfarvpaNGLGVNVSNQDGFTPLHMAA 752
Cdd:COG0666     91 LHAAARNGDLEIVKLLLE------------------------------------------AGADVNARDKDGETPLHLAA 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  753 LHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQR 832
Cdd:COG0666    129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349109  833 GASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCAEPNSNIIKLLE 894
Cdd:COG0666    209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
448-847 1.11e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 1.11e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  448 LNDPSIITPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDN 527
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  528 NGNTPLHLACTYGHEDCVKALVYYDVHscrLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSlqcaln 607
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  608 skilslmelnyltfergqsasesplrspqhstetfsrgssvsslssasidtrqdeaknsykevekLLRAVADGDLEMVRY 687
Cdd:COG0666    157 -----------------------------------------------------------------LHLAAANGNLEIVKL 171

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  688 LLEwteedlededdtvstskpefchplcqcskcgpaqkkfarvpaNGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHG 767
Cdd:COG0666    172 LLE------------------------------------------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  768 ASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTAL 847
Cdd:COG0666    210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-880 2.39e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 2.39e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  477 SLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYYDVHsc 556
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  557 rLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLqcalnskilslmelnyltfergqsasesplrspq 636
Cdd:COG0666     80 -INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL---------------------------------- 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  637 hstetfsrgssvsslssasidtrqdeaknsykeveklLRAVADGDLEMVRYLLEwteedlededdtvstskpefchplcq 716
Cdd:COG0666    125 -------------------------------------HLAAYNGNLEIVKLLLE-------------------------- 141

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  717 cskcgpaqkkfarvpaNGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECL 796
Cdd:COG0666    142 ----------------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  797 MDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERN 876
Cdd:COG0666    206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                   ....
gi 2024349109  877 CTPA 880
Cdd:COG0666    286 LTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
375-619 7.78e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 7.78e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  375 DRLYDKLLLRQRMNFLSQMATTPIDCLFKHIASGNQEEVERLLSQGDSDKDTVQKMCHPLCYC------DKCEKLVSGKL 448
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAarngdlEIVKLLLEAGA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  449 NdpsiitPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNN 528
Cdd:COG0666    112 D------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  529 GNTPLHLACTYGHEDCVKALVYYDVhscRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNS 608
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262

                          250
                   ....*....|.
gi 2024349109  609 KILSLMELNYL 619
Cdd:COG0666    263 GAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
732-893 2.12e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.12e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGN 811
Cdd:COG0666     42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  812 TPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCA--EPNSNI 889
Cdd:COG0666    122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaeNGHLEI 201


                   ....
gi 2024349109  890 IKLL 893
Cdd:COG0666    202 VKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-595 7.47e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  500 LHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYYdvhsCRLDIGNEkGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 2024349109  580 IIEVLLQNGANPNTQN 595
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-840 7.44e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.44e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  748 LHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYnAKQNKKDaYGNTPLIYACLNGHYETTA 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 2024349109  828 LLLQRGASVNLSN 840
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
741-893 1.45e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  741 NQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLN 820
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  821 GHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTP---AdCAEPNSNIIKLL 893
Cdd:COG0666     98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlA-AANGNLEIVKLL 172
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.11e-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: 83.07  E-value: 1.11e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024349109  429 KMCHPLCYCDKCEKLVSGKLNDPSIITPFSRDDRGYTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 732-867 1.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.72  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHMAALHGHSDL--VSLLLKHGASISAKNaehavplhlacqkghsqVVECLMDYNAKQNKKDAY 809
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKN-----------------RVNYLLSYGVPINIKDVY 191

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349109  810 GNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGA 867
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-554 2.02e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  467 LHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDvqDNNGNTPLHLACTYGHEDCVK 546
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 2024349109  547 ALVYYDVH 554
Cdd:pfam12796   79 LLLEKGAD 86
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 2.05e-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: 79.29  E-value: 2.05e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024349109  706 SKPEFCHPLCQCSKCGPAQKKFARVPANGLGVNVSNQDGFTP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-867 9.59e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 9.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  781 LHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRgASVNLSNaKGNTALHEAVIGKNEALVD 860
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 2024349109  861 LLLQNGA 867
Cdd:pfam12796   79 LLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 738-893 5.49e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 5.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  738 NVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYA 817
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  818 CLNGHYETTALLLQRGASVNLSNAKGN-TALHEAVIGKNEALVDLLLQNGA----MTHIRNERnCTPAD-----CAEPNS 887
Cdd:PHA02875   176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAdcniMFMIEGEE-CTILDmicnmCTNLES 254


                   ....*.
gi 2024349109  888 NIIKLL 893
Cdd:PHA02875   255 EAIDAL 260
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 732-879 5.13e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.24  E-value: 5.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQD-GFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYG 810
Cdd:PHA02878   155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349109  811 NTPLIYA---CLNghYETTALLLQRGASVNL-SNAKGNTALHEAVigKNEALVDLLLQNGAMTHIRNERNCTP 879
Cdd:PHA02878   235 NTPLHISvgyCKD--YDILKLLLEHGVDVNAkSYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTP 303
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 478-875 5.67e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.80  E-value: 5.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  478 LVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVyydvhSCR 557
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNR 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  558 LDIgnEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNSKILSLMELNYLtfERGQSASesplrspqh 637
Cdd:PHA02876   235 SNI--NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLL--ERGADVN--------- 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  638 stetfsrgssvsslssasidtrqdeAKNSYKEVEKLLRAVADGDLEMVRYLLewteedleDEDDTVSTSKPEFCHPLCQC 717
Cdd:PHA02876   302 -------------------------AKNIKGETPLYLMAKNGYDTENIRTLI--------MLGADVNAADRLYITPLHQA 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  718 SKCGpaQKKFARVPANGLGVNVSNQDGF--TPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLA-CQKGHSQVVE 794
Cdd:PHA02876   349 STLD--RNKDIVITLLELGANVNARDYCdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  795 CLMDYNAKQNKKDAYGNTPLIYACLNG-HYETTALLLQRGASVNLSNAKGNTALHEAVigKNEALVDLLLQNGAmtHIRN 873
Cdd:PHA02876   427 TLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGA--ELRD 502


                   ..
gi 2024349109  874 ER 875
Cdd:PHA02876   503 SR 504
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 729-893 8.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 8.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  729 RVPANGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQ-----VVECLMDYNAKQ 803
Cdd:PHA03100    20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  804 NKKDAYGNTPLIYACLN--GHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEAL------------------VDLLL 863
Cdd:PHA03100   100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLL 179

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2024349109  864 QNGAMTHIRNERNCTPADCA--EPNSNIIKLL 893
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAvyNNNPEFVKYL 211
PHA03095 PHA03095
ankyrin-like protein; Provisional
 479-863 2.56e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 2.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  479 VDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVT---LLLLHYKASTDVQDNNGNTPLHLACTYGH-EDCVKALVYYDVh 554
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA- 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  555 scRLDIGNEKGDTPLHIAAR--WGYQGIIEVLLQNGANPNTQNRMKETSLQCALNSKilslmelnyltfergqsasespl 632
Cdd:PHA03095   109 --DVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR----------------------- 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  633 rspqhstetfsrgssvsslssasidtrqdeaknsykevekllravaDGDLEMVRYLLEwteedledEDDTVSTSKPEF-- 710
Cdd:PHA03095   164 ----------------------------------------------NANVELLRLLID--------AGADVYAVDDRFrs 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  711 -CHPLCQCSKcgPAQKKFARVPANGLGVNVSNQDGFTPLHMAALHG---HSDLVSLLLKhGASISAKNAEHAVPLHLACq 786
Cdd:PHA03095   190 lLHHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAA- 265

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  787 kghsqvveclmdynakqnkkdAYGNTPliyAClnghyettALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLL 863
Cdd:PHA03095   266 ---------------------VFNNPR---AC--------RRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 465-604 2.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  465 TPLHIAAICGQTSLVDLLVAKGAIVNATDYH-GSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHED 543
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024349109  544 CVKALVYydvHSCRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQC 604
Cdd:PHA02875   150 GIELLID---HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 734-879 2.86e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.18  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  734 GLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNK---KDayG 810
Cdd:PHA02875    25 GINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD--G 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349109  811 NTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTP 879
Cdd:PHA02875   103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 734-868 4.45e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.77  E-value: 4.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  734 GLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTP 813
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024349109  814 LIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIgKNEALVDLLLQNGAM 868
Cdd:PHA02874   194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLINNASI 247
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 567-893 4.73e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 4.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  567 TPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNSKILSLMElnyltfergqsasesplrspqhstetfsrgs 646
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK------------------------------- 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  647 svsslssASIDTRQDEAKNSYkeveKLLRAVADGDLEMVRYLLEwteedlededDTVSTSKPEFCH--PLCQCSKCGPAQ 724
Cdd:PHA02876   229 -------AIIDNRSNINKNDL----SLLKAIRNEDLETSLLLYD----------AGFSVNSIDDCKntPLHHASQAPSLS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  725 KKFARVPANGLGVNVSNQDGFTPLHMAALHGH-SDLVSLLLKHGASISAKNAEHAVPLHLACQ-KGHSQVVECLMDYNAK 802
Cdd:PHA02876   288 RLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGAN 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  803 QNKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEAL-VDLLLQNGAMTHIRNERNCTPAD 881
Cdd:PHA02876   368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLH 447

                          330
                   ....*....|....*
gi 2024349109  882 CAEPNS---NIIKLL 893
Cdd:PHA02876   448 YACKKNcklDVIEML 462
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 382-607 6.02e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.39  E-value: 6.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  382 LLRQRMNFLSQMATTPIDCLFKHIASGNQEEVERLLSQGDSDKDTVQKMCHPLCYCDKCE-----KLVSGKLNDPSI--- 453
Cdd:PHA02874    20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGahdiiKLLIDNGVDTSIlpi 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  454 ---------------ITPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHY 518
Cdd:PHA02874   100 pciekdmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  519 KASTDVQDNNGNTPLHLACTYGHEDCVKALVyydVHSCRLDIGNEKGDTPLHIAARWGyQGIIEVLLQNgANPNTQNRMK 598
Cdd:PHA02874   180 GAYANVKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINN-ASINDQDIDG 254


                   ....*....
gi 2024349109  599 ETSLQCALN 607
Cdd:PHA02874   255 STPLHHAIN 263
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 7.84e-14

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: 68.39  E-value: 7.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  264 IPRAKRELSQLNKCTSPQQKLLCLRKVVQIIMQSPSQRVNMETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRLCSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 2024349109  344 VKDELGYCLTSIEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 461-606 1.96e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.15  E-value: 1.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  461 DRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYg 540
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349109  541 hedcvkaLVYYDVHSCRLDIG---NEK----GDTPLHIAARwgYQGIIEVLLQNGANPNTQNRMKETSLQCAL 606
Cdd:PHA02878   245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 380-551 2.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 2.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  380 KLLLRQRMNFLSQMAT----TPIDCLFKHIASGNQEEVERLLSQGDSDKDTVQKMCHPLCYCdkceklVSGKLNDPSIIT 455
Cdd:PHA03100    52 KILLDNGADINSSTKNnstpLHYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYA------ISKKSNSYSIVE 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  456 PF--------SRDDRGYTPLHIAAICGQTSL------------------VDLLVAKGAIVNATDYHGSTPLHLACQKGYQ 509
Cdd:PHA03100   126 YLldnganvnIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNP 205

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2024349109  510 NVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYY 551
Cdd:PHA03100   206 EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-466 5.92e-13

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: 63.81  E-value: 5.92e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2024349109  429 KMCHPLCYCDKCEKLVSGKLNDPSIITPFSRDDRGYTP 466
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 733-893 6.93e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 6.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  733 NGLGVNVSNQDGFTPLHMAALHGHS-----DLVSLLLKHGASISAKNAEHAVPLHLACQK--GHSQVVECLMDYNAKQNK 805
Cdd:PHA03100    57 NGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNI 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  806 KDAYGNTPLIYACLNGHYET--TALLLQRGASVN----------------LSNAKGNTALHEAVIGKNEALVDLLLQNGA 867
Cdd:PHA03100   137 KNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216

                          170       180
                   ....*....|....*....|....*...
gi 2024349109  868 MTHIRNERNCTPAD--CAEPNSNIIKLL 893
Cdd:PHA03100   217 NPNLVNKYGDTPLHiaILNNNKEIFKLL 244
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 758-898 8.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.92  E-value: 8.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  758 DLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVN 837
Cdd:PHA02874   105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349109  838 LSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCA-EPNSNIIKLLETAAS 898
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiIHNRSAIELLINNAS 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 9.12e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 9.12e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024349109  456 PFSRDDRGYTPLHIAAICGQTSLVDLLVAKgAIVNATDYhGSTPLHLACQKGYQNVTLLLLHYKASTDVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 558-883 2.74e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.99  E-value: 2.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  558 LDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALN---SKILSLMELNyltferGQSASESPLrs 634
Cdd:PHA02874    28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigaHDIIKLLIDN------GVDTSILPI-- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  635 PQHSTETFSRGSSVSSLssasIDTRQDEAKNSykevekLLRAVADGDLEMVRYLLEWteedlededdtvstskpefchpl 714
Cdd:PHA02874   100 PCIEKDMIKTILDCGID----VNIKDAELKTF------LHYAIKKGDLESIKMLFEY----------------------- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  715 cqcskcgpaqkkfarvpanGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVE 794
Cdd:PHA02874   147 -------------------GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  795 CLMDYNAKQNKKDAYGNTPLIYACLngHYETTALLLQRGASVNLSNAKGNTALHEAVIGK-NEALVDLLLQNGAMTHIRN 873
Cdd:PHA02874   208 LLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285

                          330
                   ....*....|
gi 2024349109  874 ERNCTPADCA 883
Cdd:PHA02874   286 NKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 758-936 3.62e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.05  E-value: 3.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  758 DLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQ---VVECLMDYNAKQNKKDAYGNTPLI-YACLNGHYETTALLLQRG 833
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  834 ASVNLSNAKGNTALHEAVIGKN--EALVDLLLQNGAMTHIRNERNCTPADCAEPNSN----IIKLLETAASYVPPA-AEG 906
Cdd:PHA03095   108 ADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanveLLRLLIDAGADVYAVdDRF 187

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024349109  907 EKECEQHA-TIKIRKKVNSEPCEKADDPISR 936
Cdd:PHA03095   188 RSLLHHHLqSFKPRARIVRELIRAGCDPAAT 218
PHA03095 PHA03095
ankyrin-like protein; Provisional
 732-905 5.91e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 5.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  732 ANGLGVNVSNQDGFTPLHmAALHGHS---DLVSLLLKHGASISAKNAEHAVPLHLACQ--KGHSQVVECLMDYNAKQNKK 806
Cdd:PHA03095   140 RKGADVNALDLYGMTPLA-VLLKSRNanvELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAAT 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  807 DAYGNTPLIYACLNGHYETTAL--LLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCAE 884
Cdd:PHA03095   219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                          170       180
                   ....*....|....*....|.
gi 2024349109  885 PNSNIIkLLETAASYVPPAAE 905
Cdd:PHA03095   299 RNNNGR-AVRAALAKNPSAET 318
PHA03095 PHA03095
ankyrin-like protein; Provisional
 681-898 1.52e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  681 DLEMVRYLLEwteedledEDDTVSTSKPEFCHPLCQC--SKCGPAQKKFARVPANGLGVNVSNQDGFTPLHMAALHGHS- 757
Cdd:PHA03095    26 TVEEVRRLLA--------AGADVNFRGEYGKTPLHLYlhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTl 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  758 DLVSLLLKHGASISAKNAEHAVPLHlACQKG---HSQVVECLMDYNAKQNKKDAYGNTPLiyACL----NGHYETTALLL 830
Cdd:PHA03095    98 DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrNANVELLRLLI 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349109  831 QRGASVNLSNAKGNTALHE--AVIGKNEALVDLLLQNGAMTHIRNERNCTP-----ADCAEPNSNIIKLLETAAS 898
Cdd:PHA03095   175 DAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPlhsmaTGSSCKRSLVLPLLIAGIS 249
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-619 1.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 1.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  475 QTSLVDLLVAKGAIVNATDYH-GSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYYDV 553
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  554 HScrlDIGNEKGDTPLHIA-ARWGYQGIIEVLLQNGANPNTQNRMKETSlqcALNSKILSLMELNYL 619
Cdd:PHA02878   226 ST---DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLT---ALHSSIKSERKLKLL 286
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 734-893 2.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  734 GLGVNVSNQDGFTPLHMAALH----GHSDLVSLLLKHGAS----------------------ISAKNAEHAVPLHLACQK 787
Cdd:PHA02878    60 GHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFytlvaikdafnnrnveifkiilTNRYKNIQTIDLVYIDKK 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  788 GHSQVVEC-----LMDYNAKQNKKDAY-GNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDL 861
Cdd:PHA02878   140 SKDDIIEAeitklLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI 219

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2024349109  862 LLQNGAMTHIRNERNCTPADCAEP---NSNIIKLL 893
Cdd:PHA02878   220 LLENGASTDARDKCGNTPLHISVGyckDYDILKLL 254
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 468-551 5.16e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.85  E-value: 5.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  468 HIAAiCGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKA 547
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 2024349109  548 LVYY 551
Cdd:PTZ00322   167 LSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 470-606 1.09e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  470 AAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALv 549
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL- 610

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  550 yydVHSCRLDIGNEKGDTpLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCAL 606
Cdd:PLN03192   611 ---YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
Ank_4 pfam13637
Ankyrin repeats (many copies);
746-796 7.50e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 7.50e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024349109  746 TPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECL 796
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 734-867 9.23e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 9.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  734 GLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKdaYGNTP 813
Cdd:PLN03192   548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDL 625

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024349109  814 LIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGA 867
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
758-893 1.11e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  758 DLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVN 837
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349109  838 LSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCAEPNSN--IIKLL 893
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNleIVKLL 139
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 462-586 3.27e-09

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: 60.66  E-value: 3.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNATD-------------YHGSTPLHL-ACQKGYQNVTLLLLH--YKASTDVQ 525
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQ 151

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349109  526 DNNGNTPLH--------------LACTYGHEdcvkaLVYYDVHSCRL----DIGNEKGDTPLHIAARWGYQGIIEVLLQ 586
Cdd:cd21882    152 DSLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 449-586 3.56e-09

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: 60.87  E-value: 3.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  449 NDPSiitpFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNA------------TD--YHGSTPLHLACQKGYQNVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  515 LLHYKASTDVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVHSCRL----DIGNEKGDTPLHIAARWGYQGI 580
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 2024349109  581 IEVLLQ 586
Cdd:TIGR00870  273 FRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
481-536 4.59e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 4.59e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  481 LLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLA 536
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 734-879 5.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 5.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  734 GLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDaygnTP 813
Cdd:PHA02876   168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LS 243

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  814 LIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKN-EALVDLLLQNGAMTHIRNERNCTP 879
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETP 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
810-863 6.65e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 6.65e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024349109  810 GNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLL 863
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 462-586 1.11e-08

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: 59.04  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNATD--------------YHGSTPLHL-ACQKGYQNVTLLL--LHYKASTDV 524
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  525 QDNNGNTPLHLACTYG-----HEDCVKALvyYD---VHSCRL-------DIGNEKGDTPLHIAARWGYQGIIEVLLQ 586
Cdd:cd22193    155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-549 1.44e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.44e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024349109  496 GSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALV 549
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 709-747 1.87e-08

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: 51.10  E-value: 1.87e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024349109  709 EFCHPLCQCSKCGPAQKKFARVPAnGLGVNVSNQDGFTP 747
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPS-GVGVNSRDQDGRTP 38
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 463-587 3.69e-08

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: 57.33  E-value: 3.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  463 GYTPLHIAAICGQTSLVDLLVAKGAIVN---ATD-----------YHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNN 528
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349109  529 GNTPLHLACTYGHEDCVKALvyYDV--------HSCRLD-IGNEKGDTPLHIAARWGYQGIIEVLLQN 587
Cdd:cd22192    169 GNTVLHILVLQPNKTFACQM--YDLilsydkedDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-545 3.90e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  461 DRGYTPLHiAAICGQTSLVDLLVaKGAIVNATDYHGSTPLHLACQKG-YQNVTLLLLHYKASTDVQDNNGNTPLHLACTY 539
Cdd:PHA02874   221 KNGFTPLH-NAIIHNRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298


                   ....*.
gi 2024349109  540 GHEDCV 545
Cdd:PHA02874   299 INKDPV 304
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 744-889 6.98e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 56.63  E-value: 6.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  744 GFTPLHMAALHGHSDLVSLLLKHGASISAK-NAEhavplhlACQKghSQVVECLmdynakqnkkdAYGNTPL-IYACLnG 821
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARaCGD-------FFVK--SQGVDSF-----------YHGESPLnAAACL-G 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  822 HYETTALLLQRGASVNLSNAKGNTALHEAVI-----GKNEALV----DLLLQNGAMT-------HIRNERNCTPADCAEP 885
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLHLLVMenefkAEYEELScqmyNFALSLLDKLrdskeleVILNHQGLTPLKLAAK 266


                   ....
gi 2024349109  886 NSNI 889
Cdd:TIGR00870  267 EGRI 270
Ank_2 pfam12796
Ankyrin repeats (3 copies);
673-774 7.84e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 7.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  673 LLRAVADGDLEMVRYLLEWTEEDLEDEDDTVStskpefchPLCQCSKCGpaQKKFARVPANGLGVNVSNqDGFTPLHMAA 752
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--------ALHLAAKNG--HLEIVKLLLEHADVNLKD-NGRTALHYAA 69

                           90       100
                   ....*....|....*....|..
gi 2024349109  753 LHGHSDLVSLLLKHGASISAKN 774
Cdd:pfam12796   70 RSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 441-602 7.93e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 7.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  441 EKLVSGKLnDPSIitpfsRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKA 520
Cdd:PLN03192   542 EELLKAKL-DPDI-----GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  521 STDVQdnNGNTPLHLACTYGHEDCVKALVYydvHSCRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGAN---PNTQNRM 597
Cdd:PLN03192   616 ISDPH--AAGDLLCTAAKRNDLTAMKELLK---QGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDF 690


                   ....*
gi 2024349109  598 KETSL 602
Cdd:PLN03192   691 SPTEL 695
PHA03095 PHA03095
ankyrin-like protein; Provisional
 456-547 9.40e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 9.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  456 PFSRDDRGYTPLHIAAICG--QTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPL 533
Cdd:PHA03095   215 PAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                           90
                   ....*....|....
gi 2024349109  534 HLACTYGHEDCVKA 547
Cdd:PHA03095   295 SLMVRNNNGRAVRA 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 466-636 1.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  466 PLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQK-----------------------------GYQNV----- 511
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafNNRNVeifki 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  512 ------------------------------TLLLLHYKASTDVQD-NNGNTPLHLACTYGHEDCVKALVYYDVHSCRLDI 560
Cdd:PHA02878   120 iltnrykniqtidlvyidkkskddiieaeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  561 GNekgDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCA----LNSKILSLM-----ELNYLTFERGQSASESP 631
Cdd:PHA02878   200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLlehgvDVNAKSYILGLTALHSS 276


                   ....*
gi 2024349109  632 LRSPQ 636
Cdd:PHA02878   277 IKSER 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
463-516 1.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024349109  463 GYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLL 516
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 744-889 1.57e-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: 55.40  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  744 GFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVplhlacqkghsqvveclmdYNAKQNKKDAYGNTPLIYACLNGHY 823
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTF-------------------FRPGPKNLIYYGEHPLSFAACVGNE 149

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  824 ETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALV----DLLL------QNGAMTHIRNERNCTPADCAEPNSNI 889
Cdd:cd22192    150 EIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILsydkedDLQPLDLVPNNQGLTPFKLAAKEGNI 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 459-592 1.75e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  459 RDDRGYTPLHIAAiCGQ---TSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDV--QDNNGNTPL 533
Cdd:PHA03095   113 KDKVGRTPLHVYL-SGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyaVDDRFRSLL 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  534 HLACTYGH--EDCVKALVYYDVH-------------------SCR-------------LDIGNEKGDTPLHIAARWGYQG 579
Cdd:PHA03095   192 HHHLQSFKprARIVRELIRAGCDpaatdmlgntplhsmatgsSCKrslvlplliagisINARNRYGQTPLHYAAVFNNPR 271

                          170
                   ....*....|...
gi 2024349109  580 IIEVLLQNGANPN 592
Cdd:PHA03095   272 ACRRLIALGADIN 284
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 2.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.02e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349109  514 LLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYYDVHscrLDIGNEKGDTPLHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-606 2.22e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  458 SRDDRGYTPLHIAAICGQTS-LVDLLVAKGAIVNATDYHGSTPLHLACQKGY--QNVTLLLLHyKASTDVQDNNGNTPLH 534
Cdd:PHA02876   268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIML-GADVNAADRLYITPLH 346

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349109  535 LACTYG-HEDCVKALVYYDVHSCRLDIGNEkgdTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCAL 606
Cdd:PHA02876   347 QASTLDrNKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
Ank_5 pfam13857
Ankyrin repeats (many copies);
737-784 2.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.58e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2024349109  737 VNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLA 784
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 714-810 3.09e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 3.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  714 LCQCSKCGPAQKkfARVP-ANGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQV 792
Cdd:PTZ00322    86 LCQLAASGDAVG--ARILlTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                           90
                   ....*....|....*...
gi 2024349109  793 VECLMDYNAKQNKKDAYG 810
Cdd:PTZ00322   164 VQLLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 4.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  529 GNTPLHLACTYGHEDCVKALVYydvHSCRLDIGNEKGDTPLHIAARWGYQGIIEVLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-774 5.42e-07

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: 46.90  E-value: 5.42e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024349109  743 DGFTPLHMAALH-GHSDLVSLLLKHGASISAKN 774
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-774 5.52e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 5.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  559 DIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNSKILSLMELNYltfergQSASESplrspqhs 638
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY------HFASIS-------- 617

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  639 tetfsrgssvsslssasidtrqdeakNSYKEVEKLLRAVADGDLEMVRYLLEwteedlededdtvstskpefchplcqcs 718
Cdd:PLN03192   618 --------------------------DPHAAGDLLCTAAKRNDLTAMKELLK---------------------------- 643

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  719 kcgpaqkkfarvpaNGLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKN 774
Cdd:PLN03192   644 --------------QGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 462-585 6.01e-07

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: 53.61  E-value: 6.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNATD--------------YHGSTPLHL-ACQKGYQNVTLLLlhYKASTDV-- 524
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLM--EKESTDIts 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349109  525 QDNNGNTPLHLACTYG-----HEDCVKALvyYD--VHSCR---LD-IGNEKGDTPLHIAARWGYQGIIEVLL 585
Cdd:cd22194    218 QDSRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 428-466 6.26e-07

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: 46.93  E-value: 6.26e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024349109  428 QKMCHPLCYCDKCEKLVSG-KLNDPSIITPFSRDDRGYTP 466
Cdd:cd22886      3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 456-518 6.56e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 6.56e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349109  456 PFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHY 518
Cdd:PTZ00322   108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 461-606 7.65e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 7.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  461 DRGY-TPLHIAAICGQTS-LVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLA-C 537
Cdd:PHA02876   338 DRLYiTPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlC 417

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  538 TYGHEDCVKALVYydvHSCRLDIGNEKGDTPLHIAARWGYQ-GIIEVLLQNGANPNTQNRMKETSLQCAL 606
Cdd:PHA02876   418 GTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 438-775 1.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  438 DKCEKLVSGKLNDPSIITPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGY-----QNVT 512
Cdd:PHA03100    10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  513 LLLLHYKASTDVQDNNGNTPLHLACTY--GHEDCVKALVyydVHSCRLDIGNEKGDTPLHIAARWGYQ--GIIEVLLQNG 588
Cdd:PHA03100    90 KLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL---DNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  589 ANPNTQNRMKetslqcalnskilSLMELNYltfergqsasesplrspqhstetfsrgssvsslssaSIDTRqDEAKNSyk 668
Cdd:PHA03100   167 VDINAKNRVN-------------YLLSYGV------------------------------------PINIK-DVYGFT-- 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  669 eveKLLRAVADGDLEMVRYLLEwteedlededdtvstskpefchplcqcskCGpaqkkfarvpANglgVNVSNQDGFTPL 748
Cdd:PHA03100   195 ---PLHYAVYNNNPEFVKYLLD-----------------------------LG----------AN---PNLVNKYGDTPL 229

                          330       340
                   ....*....|....*....|....*..
gi 2024349109  749 HMAALHGHSDLVSLLLKHGASISAKNA 775
Cdd:PHA03100   230 HIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 1.56e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.56e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2024349109  456 PFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 743-772 2.24e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 2.24e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024349109   743 DGFTPLHMAALHGHSDLVSLLLKHGASISA 772
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 749-830 2.44e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  749 HMAAlHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTAL 828
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ..
gi 2024349109  829 LL 830
Cdd:PTZ00322   167 LS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 490-616 2.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  490 NATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPLHLACTYGheDCVKALVYYDVHSCRLDIGNEKGDTPL 569
Cdd:PHA02875    29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG--DVKAVEELLDLGKFADDVFYKDGMTPL 106

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2024349109  570 HIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCALNSKILSLMEL 616
Cdd:PHA02875   107 HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIEL 153
PHA02798 PHA02798
ankyrin-like protein; Provisional
 758-893 4.32e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.60  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  758 DLVSLLLKHGASISAKNAEHAVPL-----HLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLiYACLNGHY----ETTAL 828
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLLSNGYinnlEILLF 130

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349109  829 LLQRGASVNLSNAKGNTALHEAVIGKNEA---LVDLLLQNGA-MTHIRNERNCTPADC------AEPNSNIIKLL 893
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVdINTHNNKEKYDTLHCyfkyniDRIDADILKLF 205
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 4.42e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 4.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024349109  564 KGDTPLHIAA-RWGYQGIIEVLLQNGANPNTQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
380-533 8.28e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.80  E-value: 8.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  380 KLLLRQ--RMNFLSQMATTPidcLFKHIASGNQEEVERLLSQGDSDKDTVQKMCHPLCYC------DKCEKLVSGKlNDP 451
Cdd:COG0666    137 KLLLEAgaDVNAQDNDGNTP---LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenghlEIVKLLLEAG-ADV 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  452 SIitpfsRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNT 531
Cdd:COG0666    213 NA-----KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                   ..
gi 2024349109  532 PL 533
Cdd:COG0666    288 LL 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 788-880 8.76e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 8.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  788 GHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGA 867
Cdd:PLN03192   536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615

                           90
                   ....*....|....*
gi 2024349109  868 MT--HIRNERNCTPA 880
Cdd:PLN03192   616 ISdpHAAGDLLCTAA 630
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 514-585 9.10e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 9.10e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349109  514 LLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVYYDVHSCRLDignEKGDTPLHIAARWGYQGIIEVLL 585
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLS 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 454-602 9.54e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 9.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  454 ITPFSRDDRGYTPLHIAAICGQTSL-VDLLVAKGAIVN--ATD--YHGSTPLHLACQKgyQNVTL--LLLHYKAstDVQd 526
Cdd:cd22192     42 CDLFQRGALGETALHVAALYDNLEAaVVLMEAAPELVNepMTSdlYQGETALHIAVVN--QNLNLvrELIARGA--DVV- 116

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  527 nngnTPLhlACTYGHEDCVKALVYYdvhscrldignekGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSL 602
Cdd:cd22192    117 ----SPR--ATGTFFRPGPKNLIYY-------------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 462-586 1.02e-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: 49.47  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNATD-------------YHGSTPLHL-ACQKGYQNVTLLL--LHYKASTDVQ 525
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349109  526 DNNGNTPLHlACTYGHEDCVK--ALV--YYD---VHSCRLD-------IGNEKGDTPLHIAARWGYQGIIEVLLQ 586
Cdd:cd22197    173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDgllQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-562 1.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  459 RDDRGYTPLHIA-AICGQTSLVDLLVAKGAIVNATDY-HGSTPLHLACQKgyQNVTLLLLHYKASTDVQDNNGNTPLHLA 536
Cdd:PHA02878   230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                           90       100
                   ....*....|....*....|....*.
gi 2024349109  537 ctyghedcvkALVYYDVHSCRLDIGN 562
Cdd:PHA02878   308 ----------VKQYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
380-493 1.51e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  380 KLLLRQR--MNFLSQMATTPidcLFKHIASGNQEEVERLLSQGDSDkdtvqkmchplcycdkceklvsgklndpsiitpf 457
Cdd:pfam12796   14 KLLLENGadANLQDKNGRTA---LHLAAKNGHLEIVKLLLEHADVN---------------------------------- 56

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024349109  458 sRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATD 493
Cdd:pfam12796   57 -LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
 476-604 1.66e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.68  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  476 TSLVDLLVAKGAIVNATDYHGSTPLH--LACQKGYQ---NVTLLLLHYKASTDVQDNNGNTPLHLACTYGHEDCVKALVY 550
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCtiLSNIKDYKhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLF 130

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349109  551 YDVHSCRLDIGNEKGDTPLHIAARWGYQ---GIIEVLLQNGANPNT-QNRMKETSLQC 604
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHC 188
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-772 1.69e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.63  E-value: 1.69e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024349109  743 DGFTPLHMAALHGHSDLVSLLLKHGASISA 772
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 462-586 2.13e-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: 48.65  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNATD--------------YHGSTPLHLA-CQKGYQNVTLLLL--HYKASTDV 524
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAaCTNQLDIVKFLLEnpHSPADISA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349109  525 QDNNGNTPLHLACTYGH---EDCVKALVYYD---VHSCRL-------DIGNEKGDTPLHIAARWGYQGIIEVLLQ 586
Cdd:cd22196    173 RDSMGNTVLHALVEVADntpENTKFVTKMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
Ank_5 pfam13857
Ankyrin repeats (many copies);
804-850 2.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.19e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2024349109  804 NKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEA 850
Cdd:pfam13857   10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-372 2.33e-05

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 44.75  E-value: 2.33e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109   264 IPRAKRELSQLNKCTSPQQKLLCLRKVVQIIMQSPSQRVNmETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRLCSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90       100
                    ....*....|....*....|....*....
gi 2024349109   344 VKDELGYCLTSIEAAIEYIRqgNLSDRST 372
Cdd:smart00167   81 LTGEGGYYLTSLSAALALIK--GLTEAHA 107
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 782-870 4.80e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  782 HLACQkGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDL 861
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....*....
gi 2024349109  862 LLQNGAMTH 870
Cdd:PTZ00322   167 LSRHSQCHF 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
763-817 6.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.60e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  763 LLKHG-ASISAKNAEHAVPLHLACQKGHSQVVECLMDYNAKQNKKDAYGNTPLIYA 817
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 452-503 7.47e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 7.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  452 SIITPF--------SRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLA 503
Cdd:PHA03095   238 SLVLPLliagisinARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
555-605 7.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 7.57e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024349109  555 SCRLDIGNEKGDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCA 605
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 456-540 8.35e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 8.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  456 PFSRDDRGYTPLHIAA--ICGQTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLL--LLHYKASTDVQDNNGNT 531
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259


                   ....*....
gi 2024349109  532 PLHLACTYG 540
Cdd:PHA03095   260 PLHYAAVFN 268
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-493 1.07e-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: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024349109  462 RGYTPLHIAAI-CGQTSLVDLLVAKGAIVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
565-606 1.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.27e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024349109  565 GDTPLHIAARWGYQGIIEVLLQNGANPNTQNRMKETSLQCAL 606
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 453-589 1.30e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.33  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  453 IITPFSRDDRGYTPLHIaaICGQTSLVDLLVAKGAIVNATDY-------HGSTPLHLACQKGY---QNVTLLLLHYKAST 522
Cdd:PHA02736     7 IIFASEPDIEGENILHY--LCRNGGVTDLLAFKNAISDENRYlvleynrHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349109  523 DVQDN-NGNTPLHLACTYGHEDCVKALvyydvhsCR-----LDIGNEKGDTPLHIAARWGYQGIIEVLLQNGA 589
Cdd:PHA02736    85 NGKERvFGNTPLHIAVYTQNYELATWL-------CNqpgvnMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 809-838 1.33e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.33e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024349109   809 YGNTPLIYACLNGHYETTALLLQRGASVNL 838
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-592 1.46e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.46e-04
                            10        20
                    ....*....|....*....|....*....
gi 2024349109   564 KGDTPLHIAARWGYQGIIEVLLQNGANPN 592
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 1.65e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.65e-04
                            10        20
                    ....*....|....*....|....*.
gi 2024349109   528 NGNTPLHLACTYGHEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 809-840 2.11e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.11e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2024349109  809 YGNTPLIYACL-NGHYETTALLLQRGASVNLSN 840
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
673-764 2.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  673 LLRAVADGDLEMVRYLLEwteedlededdtvstskpefchplcqcskcgpaqkkfarvpaNGLGVNVSNQDGFTPLHMAA 752
Cdd:pfam13637    5 LHAAAASGHLELLRLLLE------------------------------------------KGADINAVDGNGETALHFAA 42

                           90
                   ....*....|..
gi 2024349109  753 LHGHSDLVSLLL 764
Cdd:pfam13637   43 SNGNVEVLKLLL 54
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 453-582 2.70e-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: 44.84  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  453 IITPFsRD--DRGYTPLHIAAICGQTSLVDLLVAKGAIVNATD--------------YHGSTPLHLACQKGYQNVTLLLL 516
Cdd:cd22195    126 INSPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAACTNQPDIVHYLT 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  517 ---HYKASTDVQDNNGNTPLH--LACTYGHEDCVKALV-YYDV---------HSCRLD-IGNEKGDTPLHIAARWGYQGI 580
Cdd:cd22195    205 enaHKKADLRRQDSRGNTVLHalVAIADNTRENTKFVTkMYDLllikcaklyPDCNLEaILNNDGMSPLMMAAKLGKIGI 284


                   ..
gi 2024349109  581 IE 582
Cdd:cd22195    285 FQ 286
PHA02946 PHA02946
ankyin-like protein; Provisional
 455-549 4.14e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 4.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  455 TPFSRDDRGYTPLHIAAICGQTSLVDLLVAKGAIVNATDYHGSTPLHLAC---QKGYQNVTLLLLHYKASTDVQDNNGNT 531
Cdd:PHA02946    64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143

                           90
                   ....*....|....*...
gi 2024349109  532 PLhLACTYGHEDCVKALV 549
Cdd:PHA02946   144 PL-LACTDPSERVFKKIM 160
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 794-872 4.65e-04

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: 44.10  E-value: 4.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  794 ECLMDY-NAKQNKKDAYGNTPLIYACLN---GHYETTALLLQ----RGASVNLSNA-------KGNTALHEAVIGKNEAL 858
Cdd:cd21882      9 ECLRWYlTDSAYQRGATGKTCLHKAALNlndGVNEAIMLLLEaapdSGNPKELVNApctdefyQGQTALHIAIENRNLNL 88

                           90
                   ....*....|....
gi 2024349109  859 VDLLLQNGAMTHIR 872
Cdd:cd21882     89 VRLLVENGADVSAR 102
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 780-867 5.25e-04

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: 43.85  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  780 PLHLACQKGHSQVVECLMDYNAKQN-KKDAYGNTPLIYACLNGHYEtTALLLQRGASVNLSNA------KGNTALHEAVI 852
Cdd:cd22192     20 PLLLAAKENDVQAIKKLLKCPSCDLfQRGALGETALHVAALYDNLE-AAVVLMEAAPELVNEPmtsdlyQGETALHIAVV 98

                           90
                   ....*....|....*
gi 2024349109  853 GKNEALVDLLLQNGA 867
Cdd:cd22192     99 NQNLNLVRELIARGA 113
Ank_5 pfam13857
Ankyrin repeats (many copies);
829-883 8.18e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 8.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349109  829 LLQRG-ASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIRNERNCTPADCA 883
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-491 1.01e-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: 37.62  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024349109  462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNA 491
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-551 1.05e-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: 37.65  E-value: 1.05e-03
                           10        20
                   ....*....|....*....|....*
gi 2024349109  528 NGNTPLHLACT-YGHEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 401-533 1.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  401 LFKHIASGNQEEVERLLSQGDSDKDTVQKMCH-PLCYCDKCEKLVSGKL-----NDPSIitpfSRDDRgYTPLHIAAICG 474
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMtPLHLATILKKLDIMKLliargADPDI----PNTDK-FSPLHLAVMMG 146

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349109  475 QTSLVDLLVAKGAIVNATDYHGSTPLHLACQKGYQNVTLLLLHYKASTDVQDNNGNTPL 533
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 809-837 1.50e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.50e-03
                           10        20
                   ....*....|....*....|....*....
gi 2024349109  809 YGNTPLIYACLNGHYETTALLLQRGASVN 837
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 786-865 1.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  786 QKGHSQVVECLMDYNAKQNKKDAYGNTPLIYACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKNEALVDLLLQN 865
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 711-749 1.94e-03

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: 36.85  E-value: 1.94e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2024349109  711 CHPLCQCSKCgpaQKKFARVPANGLGVNVSNQD--GFTPLH 749
Cdd:cd22885      3 CHPLCSCDKC---EKLLSGNRNDPSAVTVYSRDdrGYTALH 40
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 737-882 2.14e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  737 VNVSNQDGFTPLHMAALHG-HSDLVSLLLKHGASISAKNAehavPLHLAcQKGHSQVVECLMDYNAKQNKKDayGNTPLI 815
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDT----LLHAI-SLEYVDAVEAILLHLLAAFRKS--GPLELA 117

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349109  816 YA-CLNGHYettalllqrgasvnlsnaKGNTALHEAVIGKNEALVDLLLQNGAMTHIRnernCTPADC 882
Cdd:TIGR00870  118 NDqYTSEFT------------------PGITALHLAAHRQNYEIVKLLLERGASVPAR----ACGDFF 163
PHA02946 PHA02946
ankyin-like protein; Provisional
 734-855 2.95e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  734 GLGVNVSNQDGFTPLHMAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQKGHSQV--VECLMDYNAK-QNKKDAYG 810
Cdd:PHA02946    62 GYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKiNNSVDEEG 141

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2024349109  811 NTPLIyACLNGHYETTALLLQRGASVNLSNAKGNTALHEAVIGKN 855
Cdd:PHA02946   142 CGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDN 185
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 810-872 3.18e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.33  E-value: 3.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349109  810 GNTPLIYACLN---GHYETTALLLQRG-----------ASVNLSNAKGNTALHEAVIGKNEALVDLLLQNGAMTHIR 872
Cdd:cd22196     47 GKTCLLKAMLNlhnGQNDTISLLLDIAektgnlkefvnAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHAR 123
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-554 3.54e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 3.54e-03
                           10        20
                   ....*....|....*....|....*..
gi 2024349109  528 NGNTPLHLACTYGHEDCVKALVYYDVH 554
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 462-491 3.78e-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: 36.03  E-value: 3.78e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024349109   462 RGYTPLHIAAICGQTSLVDLLVAKGAIVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 495-527 6.55e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 6.55e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024349109  495 HGSTPLHLAC-QKGYQNVTLLLLHYKASTDVQDN 527
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 709-814 8.79e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 8.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  709 EFCHPLCQCSKcgPAQKKFARVPANGLGVNVSNQDGFTPLH--MAALHGHSDLVSLLLKHGASISAKNAEHAVPLHLACQ 786
Cdd:PHA02946   140 EGCGPLLACTD--PSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024349109  787 K--GHSQVVECLMDyNAKQNKKDAYGNTPL 814
Cdd:PHA02946   218 KtvKNVDIINLLLP-STDVNKQNKFGDSPL 246
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 758-864 9.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349109  758 DLVSLLLKHGASISAKNAEHAVPL------HLACQKGHSQVVECLMDYnAKQNKKDAYGNTPLIYACLNGHYETTALLLQ 831
Cdd:PHA02989   199 KVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2024349109  832 RGASVNLSNAKGNTALHEAVIGKNEALVDLLLQ 864
Cdd:PHA02989   278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
 
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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