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Conserved domains on  [gi|125988393|ref|NP_663608|]
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ankyrin repeat domain-containing protein 27 isoform 1 [Mus musculus]

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];
723-893 1.13e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  723 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 802
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  803 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 882
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 125988393  883 EQ--DSKIMELLQ 893
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 7.65e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 7.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.54e-19

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


:

Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 82.69  E-value: 1.54e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 125988393  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
VPS9 super family cl19569
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.01e-15

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: 72.24  E-value: 4.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 125988393   344 AKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
723-893 1.13e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  723 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 802
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  803 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 882
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 125988393  883 EQ--DSKIMELLQ 893
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 7.65e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 7.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
780-872 6.13e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 6.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   780 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 859
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 125988393   860 LLLFYGASVDILN 872
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 8.93e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 8.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   500 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 125988393   580 IIETLLQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.54e-19

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


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 82.69  E-value: 1.54e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 125988393  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 729-873 8.62e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 8.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  729 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 804
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  805 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 868
Cdd:PHA03100  172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 125988393  869 DILNK 873
Cdd:PHA03100  252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-746 1.51e-17

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


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 76.98  E-value: 1.51e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 125988393  706 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 746
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.01e-15

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: 72.24  E-value: 4.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 125988393   344 AKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-622 1.58e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  460 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 519
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  520 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 596
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 125988393  597 ---LKETPLKCALNSKIL--SIMEAHHLSSD 622
Cdd:PHA03100  258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 462-586 9.31e-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: 55.96  E-value: 9.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEV 524
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125988393  525 QDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22193   155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 437-586 3.87e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.32  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   437 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 497
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   498 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 563
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 125988393   564 KGDTALHIAARWGYEGIIETLLQ 586
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 5.63e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 46.29  E-value: 5.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393    264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 125988393    344 AKDELGYCLTSVEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 809-837 7.32e-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: 43.35  E-value: 7.32e-06
                            10        20
                    ....*....|....*....|....*....
gi 125988393    809 GNTPLICACSAGHHEVAALLLQHGASINA 837
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 2.36e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.36e-04
                            10        20
                    ....*....|....*....|....*.
gi 125988393    528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
723-893 1.13e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  723 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 802
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  803 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 882
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 125988393  883 EQ--DSKIMELLQ 893
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
673-882 1.12e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  673 LLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAAL 752
Cdd:COG0666    91 LHAAARNGDLEIVKLLLE-----------------------------------------AGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  753 HGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHG 832
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 125988393  833 ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 882
Cdd:COG0666   210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-879 2.40e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 2.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  476 ASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVqa 555
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  556 cRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLkcalnskilsimeahhlssdrrprpsevpaqsp 635
Cdd:COG0666    79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL--------------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  636 trsvdsisqgsstssfssisvsfrqeevkkdyreveklLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplc 715
Cdd:COG0666   125 --------------------------------------HLAAYNGNLEIVKLLLE------------------------- 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  716 qcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCL 795
Cdd:COG0666   142 ----------------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  796 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQ 875
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 125988393  876 YTAA 879
Cdd:COG0666   286 LTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-892 3.06e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 3.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  725 KLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNK 804
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  805 KDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA-- 882
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAae 195

                         170
                  ....*....|
gi 125988393  883 EQDSKIMELL 892
Cdd:COG0666   196 NGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 7.65e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 7.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
460-846 3.30e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 3.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  460 DDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTY 539
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  540 GQEDCVKALVYYDVQacrLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPlkcalnskilsimeahhl 619
Cdd:COG0666    98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------------------ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  620 ssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekLLRAVADGDLEMVRYLLEwteddlddv 699
Cdd:COG0666   157 -----------------------------------------------------LHLAAANGNLEIVKLLLE--------- 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  700 edaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVP 779
Cdd:COG0666   175 --------------------------------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125988393  780 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTAL 846
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 8.48e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 8.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666   196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
457-813 1.03e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  457 FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  537 CTYGQEDCVKALVYY--DVqacrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLkcalnskilsim 614
Cdd:COG0666   128 AYNGNLEIVKLLLEAgaDV-----NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL------------ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  615 eahHLssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekllrAVADGDLEMVRYLLEwted 694
Cdd:COG0666   191 ---HL--------------------------------------------------------AAENGHLEIVKLLLE---- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  695 dlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNT 774
Cdd:COG0666   208 -------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 125988393  775 SQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPL 813
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
723-892 3.00e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 3.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  723 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 802
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  803 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA---A 879
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlA 160

                         170
                  ....*....|...
gi 125988393  880 dCAEQDSKIMELL 892
Cdd:COG0666   161 -AANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
780-872 6.13e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 6.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   780 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 859
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 125988393   860 LLLFYGASVDILN 872
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
747-837 2.55e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.55e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   747 LHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDsNAKPNKKDlSGNTPLICACSAGHHEVAA 826
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 125988393   827 LLLQHGASINA 837
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 8.93e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 8.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   500 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 125988393   580 IIETLLQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.54e-19

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


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 82.69  E-value: 1.54e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 125988393  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 729-873 8.62e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 8.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  729 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 804
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  805 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 868
Cdd:PHA03100  172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 125988393  869 DILNK 873
Cdd:PHA03100  252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-746 1.51e-17

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


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 76.98  E-value: 1.51e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 125988393  706 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 746
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-559 1.65e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   467 LHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEvqDNNGNTPLHLACTYGQEDCVK 546
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 125988393   547 ALVYYDVQACRLD 559
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 737-871 7.20e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 7.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  737 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICA 816
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 125988393  817 CSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDIL 871
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.01e-15

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: 72.24  E-value: 4.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 125988393   344 AKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 731-872 1.00e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  731 ANGLSVNVTNQD-GFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSG 809
Cdd:PHA02878  155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125988393  810 NTPL-ICACSAGHHEVAALLLQHGASINACNN-KGNTALHEAVmgRHTLVVELLLFYGASVDILN 872
Cdd:PHA02878  235 NTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLN 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-622 1.58e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  460 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 519
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  520 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 596
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 125988393  597 ---LKETPLKCALNSKIL--SIMEAHHLSSD 622
Cdd:PHA03100  258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 387-607 1.65e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  387 MNLLSQMTSTPidcLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSC-----EDCEKLISGRLNDPSV-------- 453
Cdd:PHA02874   28 INISVDETTTP---LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigaHDIIKLLIDNGVDTSIlpipciek 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  454 ----------VTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTE 523
Cdd:PHA02874  105 dmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  524 VQDNNGNTPLHLACTYGQEDCVKALVyydVQACRLDIGNEKGDTALHIAARWGYEGIieTLLQNGAPTAVQNRLKETPLK 603
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLH 259


                  ....
gi 125988393  604 CALN 607
Cdd:PHA02874  260 HAIN 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
673-806 8.10e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 8.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   673 LLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAAL 752
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-----------------------------------------NGADANLQDKNGRTALHLAAK 39

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 125988393   753 HGRTDLVPLLLKHGAysGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKD 806
Cdd:pfam12796   40 NGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 461-606 1.12e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  461 DRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYg 540
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125988393  541 qedcvkaLVYYDVQACRLDIG---NEK----GDTALHIAARwgYEGIIETLLQNGAPTAVQNRLKETPLKCAL 606
Cdd:PHA02878  245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 728-876 2.39e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  728 RISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-----VAKCLLDSNAKP 802
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  803 NKKDLSGNTPLICACSA--GHHEVAALLLQHGASINACNNKGNTALHEAVMGRH--TLVVELLLFYGASVDILNKRQY 876
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY 177
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 733-887 3.11e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  733 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTP 812
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  813 LICACSAGHHEVAALLLQHGASI-NACNNkGNTALHEAVMGRHTlVVELL--------------------LFYGASVDIL 871
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHImNKCKN-GFTPLHNAIIHNRS-AIELLinnasindqdidgstplhhaINPPCDIDII 271

                         170
                  ....*....|....*.
gi 125988393  872 NKRQYTAADCAEQDSK 887
Cdd:PHA02874  272 DILLYHKADISIKDNK 287
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-466 3.25e-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: 64.58  E-value: 3.25e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 125988393  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTP 466
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
 482-869 3.47e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  482 LVSKGAVVNATDYHGSTPLHLACQKGFQSVT---LLLLHYKASTEVQDNNGNTPLHLACTYGQ-EDCVKALVYY--DVQA 555
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVNA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  556 CrldigNEKGDTALHIAAR--WGYEGIIETLLQNGA-PTAVQNRLKeTPLKCALNSKilsimeahhlssdrrprpsevpa 632
Cdd:PHA03095  113 K-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGAdVNALDLYGM-TPLAVLLKSR----------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  633 qsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekllravaDGDLEMVRYLLEWTEDdlddvedaISTVDLEF-- 710
Cdd:PHA03095  164 ----------------------------------------------NANVELLRLLIDAGAD--------VYAVDDRFrs 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  711 -CHPLCQCPKcAPAQKLARISANGLSVNVTNQDGFSPLHMAALHG---RTDLVPLLLKhGAYSGARNTSQAVPLHLACQQ 786
Cdd:PHA03095  190 lLHHHLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVF 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  787 GHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHE-VAALLLQH------GASINACNNKGNTALHEAvmgRHTLVVE 859
Cdd:PHA03095  268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNpsaetvAATLNTASVAGGDIPSDA---TRLCVAK 344

                         410
                  ....*....|
gi 125988393  860 LLLFYGASVD 869
Cdd:PHA03095  345 VVLRGAFSLL 354
PHA03095 PHA03095
ankyrin-like protein; Provisional
 726-873 4.29e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  726 LARISANGLSVNVTNQDGFSPLHM---AALHGRTDLVPLLLKHGAYSGARNTSQAVPLHL-ACQQGHFQVAKCLLDSNAK 801
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125988393  802 PNKKDLSGNTPL-ICACS-AGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVELL-LFYGASVDILNK 873
Cdd:PHA03095  110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELLrLLIDAGADVYAV 183
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 478-613 5.31e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  478 LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL--LLLHYKASTEVQDNNGNTPLHLA--CTYGQEDCVKALVY--Y 551
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDkgV 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125988393  552 DVQA-----------CRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 613
Cdd:PHA03100  168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 480-868 6.62e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.79  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  480 DFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVyydvqACRLD 559
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  560 IgnEKGDTALHIAARwgYEGIIETLLQNGAPTAVQ--NRLKETPLkcalnskilsimeaHHLSsdRRPRPSEVPAQSPTR 637
Cdd:PHA02876  237 I--NKNDLSLLKAIR--NEDLETSLLLYDAGFSVNsiDDCKNTPL--------------HHAS--QAPSLSRLVPKLLER 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  638 SVDSisqgsstssfssisvsfrqeEVKKDYREVEKLLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQc 717
Cdd:PHA02876  297 GADV--------------------NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQ- 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  718 pkcapAQKLAR-----ISANGLSVNVTNQDGF--SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA-CQQGHF 789
Cdd:PHA02876  348 -----ASTLDRnkdivITLLELGANVNARDYCdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPY 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  790 QVAKCLLDSNAKPNKKDLSGNTPLICACSAG-HHEVAALLLQHGASINACNNKGNTALHEAvMGRHTlVVELLLFYGASV 868
Cdd:PHA02876  423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 757-881 1.25e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  757 DLVPLLLKHGA---YSGARNTSqavPLHLACQQGHFQVAK---CLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 829
Cdd:PHA03095   28 EEVRRLLAAGAdvnFRGEYGKT---PLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 125988393  830 QHGASINACNNKGNTALHE--AVMGRHTLVVELLLFYGASVDILNKRQYTAADC 881
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 673-861 1.01e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  673 LLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAAL 752
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  753 HGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQqgHFQVAKCLLDSNAKPNKKDLSGNTPLICA----CSAghhEVAALL 828
Cdd:PHA02874  200 YGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCDI---DIIDIL 274

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 125988393  829 LQHGASINACNNKGNTALHEAV--MGRHTLVVELL 861
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFkyINKDPVIKDII 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
809-862 1.89e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.89e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 125988393   809 GNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLL 862
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 778-892 3.76e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  778 VPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHH-----EVAALLLQHGASINACNNKGNTALHEAVMG 852
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 125988393  853 R--HTLVVELLLFYGASVDILNKRQYT----AADCAEQDSKIMELL 892
Cdd:PHA03100  117 KsnSYSIVEYLLDNGANVNIKNSDGENllhlYLESNKIDLKILKLL 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 460-551 4.16e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  460 DDRGQTPLHVAA--LC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTP 532
Cdd:PTZ00322   72 EVIDPVVAHMLTveLCqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151

                          90
                  ....*....|....*....
gi 125988393  533 LHLACTYGQEDCVKALVYY 551
Cdd:PTZ00322  152 LELAEENGFREVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 5.89e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.89e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125988393   456 PFSRDDRGQTPLHVAALCGQASLIDFLVSKgAVVNATDYhGSTPLHLACQKGFQSVTLLLLHYKASTEVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-608 3.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  475 QASLIDFLVSKGAVVNATDYH-GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdv 553
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  554 qACRLDIGNEKGDTALHIAARW--GYEgIIETLLQNGAPTAVQNRLKE-TPLKCALNS 608
Cdd:PHA02878  224 -GASTDARDKCGNTPLHISVGYckDYD-ILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 756-907 3.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  756 TDLVPLLLKHGAYSGARNTSQ-AVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGAS 834
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 125988393  835 INACNNKGNTALHEAVmGR--HTLVVELLLFYGASVDILNK-RQYTAADCAEQDSKIMELLQVVPGCVASLDSVEE 907
Cdd:PHA02878  227 TDARDKCGNTPLHISV-GYckDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNSYKL 301
PHA02798 PHA02798
ankyrin-like protein; Provisional
 756-881 5.07e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.32  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  756 TDLVPLLLKHGAYSGARNTSQAVPL-----HLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGH---HEVAAL 827
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  828 LLQHGASINACNNKGNTALHEAVMGRHTL---VVELLLFYGASVDIL-NKRQYTAADC 881
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHnNKEKYDTLHC 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 722-853 6.09e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 6.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  722 PAQKLAR-ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQ-GHFQVAKCLLDSN 799
Cdd:PHA02878  179 KDQRLTElLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 125988393  800 AKPNKKD-LSGNTPLicACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGR 853
Cdd:PHA02878  259 VDVNAKSyILGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 670-877 1.89e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  670 VEKLLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVtnqdgfspLHM 749
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGAD--------INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  750 AALHgrTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 829
Cdd:PHA02874  100 PCIE--KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 125988393  830 QHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYT 877
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 733-878 2.44e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 2.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  733 GLSVNVTNQDGFSPLHMAA-LHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH-FQVAKCLLDSNAKPNKKDLSGN 810
Cdd:PHA02876  263 GFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI 342

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125988393  811 TPLICACSAGHH-EVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA 878
Cdd:PHA02876  343 TPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 673-888 2.77e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  673 LLRAVADGDLEMVRYLLEWTEDDLDDVEDAIStvdlefchPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAAL 752
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGIS--------PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  753 HGRTDLVPLLLKHGAYSGARNTSQA-VPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQH 831
Cdd:PHA02875   78 EGDVKAVEELLDLGKFADDVFYKDGmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  832 GASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADC-AEQDSKI 888
Cdd:PHA02875  158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKI 215
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 673-836 3.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  673 LLRAVADGDLEMVRYLLEwTEDDLDDV--EDAIStvdlefchPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMA 750
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLD-LGKFADDVfyKDGMT--------PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  751 ALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 829
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFI 222


                  ....*..
gi 125988393  830 QHGASIN 836
Cdd:PHA02875  223 KRGADCN 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 737-831 3.45e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  737 NVTNQDGFSP--LHMAALH-------GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDL 807
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                          90       100
                  ....*....|....*....|....
gi 125988393  808 SGNTPLICACSAGHHEVAALLLQH 831
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 733-872 5.90e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  733 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKdlSGNTP 812
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDL 625

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  813 LICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILN 872
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
779-829 7.75e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 125988393   779 PLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 829
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 567-873 1.58e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  567 TALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEAhhlssdrrprpsevpaqsptrSVDSisqgs 646
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA---------------------IIDN----- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  647 stssfssisvsfRQEEVKKDYreveKLLRAVADGDLEmvryllewTEDDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKL 726
Cdd:PHA02876  234 ------------RSNINKNDL----SLLKAIRNEDLE--------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  727 A-RISANGLSVNVTNQDGFSPLHMAALHG-RTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-VAKCLLDSNAKPN 803
Cdd:PHA02876  290 VpKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVN 369

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125988393  804 KKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLV-VELLLFYGASVDILNK 873
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNK 440
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 709-746 2.58e-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: 50.72  E-value: 2.58e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 125988393  709 EFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSP 746
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
 731-870 4.39e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  731 ANGLSVNVTNQDGFSPLHmaALHGRTD----LVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 804
Cdd:PHA03095  140 RKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAA 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125988393  805 KDLSGNTPL-----ICACSAGHheVAALLLqHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDI 870
Cdd:PHA03095  218 TDMLGNTPLhsmatGSSCKRSL--VLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 466-617 4.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  466 PLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQ---------------------------------------- 505
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  506 ------KGFQS------------------VTLLLLHYKASTEVQD-NNGNTPLHLACTYGQEDCVKALVYYDVQACRLDI 560
Cdd:PHA02878  120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125988393  561 GNekgDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCA----LNSKILSIMEAH 617
Cdd:PHA02878  200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLLEH 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-545 6.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 6.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  461 DRGQTPLHVAALCGQaSLIDFLVSKgAVVNATDYHGSTPLHLA----CQKgfqSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:PHA02874  221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                  ....*....
gi 125988393  537 CTYGQEDCV 545
Cdd:PHA02874  296 FKYINKDPV 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 463-613 6.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  463 GQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKG-FQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125988393  542 EDCVKALVYYDVQAcrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 613
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-549 6.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                  ....*...
gi 125988393  542 EDCVKALV 549
Cdd:PHA02875  181 IAICKMLL 188
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 462-586 9.31e-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: 55.96  E-value: 9.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEV 524
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125988393  525 QDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22193   155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 9.33e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 9.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 125988393   529 GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGnekGDTALHIAARWGYEGIIETLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 396-547 1.61e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  396 TPIDCLFKhiaSGN-QKEVERLL---SQDDQDKDA-MQKMCHPLC-SCEDCEKLIsgRLNDPSVVTPFSRDDRGQTPLHV 469
Cdd:PHA03095  154 TPLAVLLK---SRNaNVELLRLLidaGADVYAVDDrFRSLLHHHLqSFKPRARIV--RELIRAGCDPAATDMLGNTPLHS 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  470 AALCG--QASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKA 547
Cdd:PHA03095  229 MATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-835 1.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  458 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQK----------------GFQSVTLL------- 514
Cdd:PHA02876  173 AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidtikaiidnrsniNKNDLSLLkairned 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  515 ----LLHYKASTEVQ--DNNGNTPLHLACtygQEDCVKALVYYDVQ-ACRLDIGNEKGDTALHIAARWGYEGI-IETLLQ 586
Cdd:PHA02876  253 letsLLLYDAGFSVNsiDDCKNTPLHHAS---QAPSLSRLVPKLLErGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIM 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  587 NGAPTAVQNRLKETPLkcalnskilsimeaHHLSSDRRPRPSEVPAQSPTRSVDSisqgsstssfssisvsfrqeevkKD 666
Cdd:PHA02876  330 LGADVNAADRLYITPL--------------HQASTLDRNKDIVITLLELGANVNA-----------------------RD 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  667 YREVEKLLRAVADGDLEMVRYLLEWTEDdLDDVEDAISTVdLEFChpLCqcpkcapaqklarisanglsvnvtnqdGFSP 746
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVIINTLLDYGAD-IEALSQKIGTA-LHFA--LC---------------------------GTNP 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  747 lHMAalhgrtdlVPLLLKHGAYSGARNTSQAVPLHLACQQG-HFQVAKCLLDSNAKPNKKDLSGNTPLICACsaGHHEVA 825
Cdd:PHA02876  422 -YMS--------VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIV 490

                         410
                  ....*....|
gi 125988393  826 ALLLQHGASI 835
Cdd:PHA02876  491 NILLHYGAEL 500
Ank_4 pfam13637
Ankyrin repeats (many copies);
745-796 2.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.00e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 125988393   745 SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL 796
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 792-864 2.35e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.35e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 125988393  792 AKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFY 864
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 416-518 2.81e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  416 LLSQDDQDKDAMQKMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYH 495
Cdd:PTZ00322   68 LTTEEVIDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147

                          90       100
                  ....*....|....*....|...
gi 125988393  496 GSTPLHLACQKGFQSVTLLLLHY 518
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 694-873 3.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  694 DDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARN 773
Cdd:PHA02878   21 EYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  774 TSQAVplHLACQQGHFQVAKCLLDSNAKPNKkdlSGNTPLICACSAG---HHEVAALLLQHGASINACN-NKGNTALHEA 849
Cdd:PHA02878  101 TLVAI--KDAFNNRNVEIFKIILTNRYKNIQ---TIDLVYIDKKSKDdiiEAEITKLLLSYGADINMKDrHKGNTALHYA 175

                         170       180
                  ....*....|....*....|....
gi 125988393  850 VMGRHTLVVELLLFYGASVDILNK 873
Cdd:PHA02878  176 TENKDQRLTELLLSYGANVNIPDK 199
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 470-589 3.73e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  470 AALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPL---------------- 533
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  534 HLA------------CTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:PLN03192  612 HFAsisdphaagdllCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 437-586 3.87e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.32  E-value: 3.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   437 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 497
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393   498 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 563
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 125988393   564 KGDTALHIAARWGYEGIIETLLQ 586
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 809-840 7.91e-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: 46.13  E-value: 7.91e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 125988393   809 GNTPLICAC-SAGHHEVAALLLQHGASINACNN 840
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
482-536 8.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 8.73e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 125988393   482 LVSKGAV-VNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-549 1.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 125988393   496 GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALV 549
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 1.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.69e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 125988393   456 PFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 463-587 1.88e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  463 GQTPLHVAALCGQASLIDFLVSKGAVVN---ATD-----------YHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 528
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  529 GNTPLHLACTygQEDCVKALVYYDV---------QACRLDIGNEKGDTALHIAARWGYEGIIETLLQN 587
Cdd:cd22192   169 GNTVLHILVL--QPNKTFACQMYDLilsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-562 1.94e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  459 RDDRGQTPLHVA-ALCGQASLIDFLVSKGAVVNATDY-HGSTPLHLACQKgfQSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:PHA02878  230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                          90       100
                  ....*....|....*....|....*.
gi 125988393  537 ctygqedcvkALVYYDVQACRLDIGN 562
Cdd:PHA02878  308 ----------VKQYLCINIGRILISN 323
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 462-585 3.14e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 51.30  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLlhYKASTEV-- 524
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLM--EKESTDIts 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125988393  525 QDNNGNTPLHLACTYG-----QEDCVKALvyYD--VQACR---LD-IGNEKGDTALHIAARWGYEGIIETLL 585
Cdd:cd22194   218 QDSRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 5.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 125988393   514 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQacrLDIGNEKGDTALHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 702-851 5.06e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  702 AISTVDLEFCHPLCQCPKCAPAQKLARisanglsvnvtnqdGFSPLHMAALHGRTDLVPLLLKhgaysGARN------TS 775
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGAL--------------GETALHVAALYDNLEAAVVLME-----AAPElvnepmTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  776 Q----AVPLHLACQQGHFQVAKCLLDSNA------------KPNKKDLS--GNTPLICACSAGHHEVAALLLQHGASINA 837
Cdd:cd22192    85 DlyqgETALHIAVVNQNLNLVRELIARGAdvvspratgtffRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                         170
                  ....*....|....
gi 125988393  838 CNNKGNTALHEAVM 851
Cdd:cd22192   165 QDSLGNTVLHILVL 178
Ank_4 pfam13637
Ankyrin repeats (many copies);
465-516 5.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 125988393   465 TPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLL 516
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 5.63e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 46.29  E-value: 5.63e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393    264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 125988393    344 AKDELGYCLTSVEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 809-837 7.32e-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: 43.35  E-value: 7.32e-06
                            10        20
                    ....*....|....*....|....*....
gi 125988393    809 GNTPLICACSAGHHEVAALLLQHGASINA 837
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
729-783 9.76e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 9.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 125988393   729 ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA 783
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
802-849 1.08e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.08e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 125988393   802 PNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEA 849
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 428-466 1.09e-05

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


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 43.47  E-value: 1.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 125988393  428 QKMCHPLCSCEDCEKLISG-RLNDPSVVTPFSRDDRGQTP 466
Cdd:cd22886     3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 795-869 1.27e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125988393  795 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVD 869
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 467-615 1.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  467 LHVAALC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875    1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125988393  542 EDCVKALVyyDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIME 615
Cdd:PHA02875   81 VKAVEELL--DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 458-528 3.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 125988393  458 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 528
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 462-586 4.39e-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: 47.49  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLL--HYKASTEV 524
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125988393  525 QDNNGNTPLHLACTYG---QEDCVKALVYYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22196   173 RDSMGNTVLHALVEVAdntPENTKFVTKMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 462-586 4.56e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 47.54  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD-------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEVQ 525
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125988393  526 DNNGNTPLHlACTYGQEDCVK--ALV--YYD--VQA-CRLD-------IGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22197   173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDglLQAgARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 841-873 6.67e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 6.67e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 125988393   841 KGNTALHEAV-MGRHTLVVELLLFYGASVDILNK 873
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 795-869 8.19e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 8.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 125988393  795 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVE---LLLFYGASVD 869
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKIN 134
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 416-602 2.05e-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: 45.39  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  416 LLSQDDQDKDAMQKmchpLCSCEDCEklisgrlndpsvvtPFSRDDRGQTPLHVAALCGQASLIDFLVSKG-AVVN--AT 492
Cdd:cd22192    22 LLAAKENDVQAIKK----LLKCPSCD--------------LFQRGALGETALHVAALYDNLEAAVVLMEAApELVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  493 D--YHGSTPLHLACQKgfQSVTL--LLLHYKASTevqdnngNTPlhLACTYGQEDCVKALVYYdvqacrldignekGDTA 568
Cdd:cd22192    84 SdlYQGETALHIAVVN--QNLNLvrELIARGADV-------VSP--RATGTFFRPGPKNLIYY-------------GEHP 139

                         170       180       190
                  ....*....|....*....|....*....|....
gi 125988393  569 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPL 602
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 809-837 2.34e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 2.34e-04
                           10        20
                   ....*....|....*....|....*....
gi 125988393   809 GNTPLICACSAGHHEVAALLLQHGASINA 837
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 2.36e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.36e-04
                            10        20
                    ....*....|....*....|....*.
gi 125988393    528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02946 PHA02946
ankyin-like protein; Provisional
 455-559 2.41e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  455 TPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLAC---QKGFQSVTLLLLHYKASTEVQDNNGNT 531
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143

                          90       100
                  ....*....|....*....|....*...
gi 125988393  532 PLhLACTYGQEDCVKALVYYDVQACRLD 559
Cdd:PHA02946  144 PL-LACTDPSERVFKKIMSIGFEARIVD 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 660-827 2.98e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  660 QEEVKKDYREVEKLL---RAVADGDLEMVryllewTEDDLDDVEDAISTVDLefchplCQCPKCAPAQKLARISANGLSV 736
Cdd:PTZ00322   41 QEEIARIDTHLEALEateNKDATPDHNLT------TEEVIDPVVAHMLTVEL------CQLAASGDAVGARILLTGGADP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  737 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL---------DSNAKPNKKDL 807
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKPDSFTG 188

                         170       180
                  ....*....|....*....|
gi 125988393  808 SGNTPLICACSAGHHEVAAL 827
Cdd:PTZ00322  189 KPPSLEDSPISSHHPDFSAV 208
Ank_4 pfam13637
Ankyrin repeats (many copies);
726-763 3.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 3.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 125988393   726 LARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLL 763
Cdd:pfam13637   17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-493 3.54e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.54e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 125988393   462 RGQTPLHVAAL-CGQASLIDFLVSKGAVVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 814-904 4.02e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  814 ICACSAGHHEVAA-LLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCAEQDS--KIME 890
Cdd:PTZ00322   86 LCQLAASGDAVGArILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQ 165

                          90
                  ....*....|....
gi 125988393  891 LLQVVPGCVASLDS 904
Cdd:PTZ00322  166 LLSRHSQCHFELGA 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 742-767 5.28e-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: 38.34  E-value: 5.28e-04
                            10        20
                    ....*....|....*....|....*.
gi 125988393    742 DGFSPLHMAALHGRTDLVPLLLKHGA 767
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 742-767 8.31e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 8.31e-04
                           10        20
                   ....*....|....*....|....*.
gi 125988393   742 DGFSPLHMAALHGRTDLVPLLLKHGA 767
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
565-606 9.72e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 9.72e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 125988393   565 GDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCAL 606
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 1.07e-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: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 125988393   564 KGDTALHIAA-RWGYEGIIETLLQNGAPTAVQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 514-627 1.08e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  514 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDignEKGDTALHIAARWGYEGIIETLLQ------- 586
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLSRhsqchfe 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 125988393  587 ---NGAP---TAVQNRLKETPLKcalnskilsimeAHHLSSDRRPRP 627
Cdd:PTZ00322  177 lgaNAKPdsfTGKPPSLEDSPIS------------SHHPDFSAVPQP 211
Ank_5 pfam13857
Ankyrin repeats (many copies);
828-882 1.15e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.15e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 125988393   828 LLQHG-ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 882
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 462-491 1.51e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.51e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 125988393    462 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-589 1.51e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.51e-03
                            10        20
                    ....*....|....*....|....*.
gi 125988393    564 KGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 457-571 2.07e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  457 FSRDDRGQTPLHVAAL---CGQASLIDFLV-------SKGAVVNA--TD--YHGSTPLHLACQKgfQSVTL--LLLHYKA 520
Cdd:cd21882    20 YQRGATGKTCLHKAALnlnDGVNEAIMLLLeaapdsgNPKELVNApcTDefYQGQTALHIAIEN--RNLNLvrLLVENGA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125988393  521 STEVQDNN-------------GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHI 571
Cdd:cd21882    98 DVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHA 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 742-773 2.10e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.10e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 125988393   742 DGFSPLHMAALH-GRTDLVPLLLKHGAYSGARN 773
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 779-804 2.37e-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: 36.41  E-value: 2.37e-03
                            10        20
                    ....*....|....*....|....*.
gi 125988393    779 PLHLACQQGHFQVAKCLLDSNAKPNK 804
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 711-748 3.01e-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: 36.46  E-value: 3.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 125988393  711 CHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLH 748
Cdd:cd22885     3 CHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-491 3.19e-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: 3.19e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 125988393   462 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 491
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-551 3.47e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.47e-03
                           10        20
                   ....*....|....*....|....*
gi 125988393   528 NGNTPLHLACT-YGQEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
Ank_2 pfam12796
Ankyrin repeats (3 copies);
569-616 3.65e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.65e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 125988393   569 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-625 3.72e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  559 DIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSK---ILSIMeaHHLSSDRRP 625
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkIFRIL--YHFASISDP 619
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 841-870 3.77e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.77e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 125988393    841 KGNTALHEAVMGRHTLVVELLLFYGASVDI 870
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 841-870 4.16e-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: 35.70  E-value: 4.16e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 125988393   841 KGNTALHEAVMGRHTLVVELLLFYGASVDI 870
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 439-560 5.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  439 DCEKLISGRLNDPSVvtpfSRDDRgQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLhy 518
Cdd:PHA02875  116 DIMKLLIARGADPDI----PNTDK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL-- 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 125988393  519 kastevqdNNGNTPLHlactYGQEDCVKALVyYDVQACRLDI 560
Cdd:PHA02875  189 --------DSGANIDY----FGKNGCVAALC-YAIENNKIDI 217
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 455-534 6.36e-03

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


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 40.61  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  455 TPFsRD--DRGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHLA-CQKGFQSVTLLL-- 515
Cdd:cd22195   128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                          90
                  ....*....|....*....
gi 125988393  516 LHYKASTEVQDNNGNTPLH 534
Cdd:cd22195   207 AHKKADLRRQDSRGNTVLH 225
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-553 6.81e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 6.81e-03
                           10        20
                   ....*....|....*....|....*.
gi 125988393   528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 796-882 8.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 8.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125988393  796 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDILNKR 874
Cdd:PHA02884   57 ADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTND 136


                  ....*...
gi 125988393  875 QYTAADCA 882
Cdd:PHA02884  137 MVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 454-506 8.52e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.49  E-value: 8.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125988393  454 VTPFSR-----------DDRGQTPLHVAALCGQA----SLIDFLVSKGAVVNATD-YHGSTPLHLACQK 506
Cdd:PHA02741   40 FTPFIRgdchaaalnatDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEmLEGDTALHLAAHR 108
 
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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