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Conserved domains on  [gi|568945777|ref|XP_006540049|]
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ankyrin repeat domain-containing protein 27 isoform X1 [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];
686-856 5.69e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 5.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  686 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 765
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  766 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 845
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 568945777  846 EQ--DSKIMELLQ 856
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
422-579 3.01e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  422 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 501
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  502 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 579
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 392-431 1.39e-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: 1.39e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568945777  392 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 431
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). ...
 227-326 4.43e-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: 71.86  E-value: 4.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   227 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 306
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 568945777   307 AKDELGYCLTSVEAAIEYIR 326
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
686-856 5.69e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 5.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  686 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 765
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  766 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 845
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 568945777  846 EQ--DSKIMELLQ 856
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
422-579 3.01e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  422 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 501
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  502 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 579
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
743-835 8.72e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 8.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   743 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 822
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568945777   823 LLLFYGASVDILN 835
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
463-552 1.26e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   463 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 542
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 568945777   543 IIETLLQNGA 552
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 392-431 1.39e-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: 1.39e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568945777  392 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 431
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 692-836 8.20e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 8.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  692 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 767
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  768 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 831
Cdd:PHA03100  172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 568945777  832 DILNK 836
Cdd:PHA03100  252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 669-709 1.28e-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: 1.28e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568945777  669 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 709
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 227-326 4.43e-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: 71.86  E-value: 4.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   227 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 306
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 568945777   307 AKDELGYCLTSVEAAIEYIR 326
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 423-585 1.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  423 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 482
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  483 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 559
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568945777  560 ---LKETPLKCALNSKIL--SIMEAHHLSSD 585
Cdd:PHA03100  258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 425-549 9.86e-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: 9.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  425 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEV 487
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568945777  488 QDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 549
Cdd:cd22193   155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 400-549 3.70e-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: 3.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   400 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 460
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   461 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 526
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 568945777   527 KGDTALHIAARWGYEGIIETLLQ 549
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 227-325 5.97e-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: 5.97e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777    227 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 306
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 568945777    307 AKDELGYCLTSVEAAIEYI 325
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 772-800 8.59e-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: 8.59e-06
                            10        20
                    ....*....|....*....|....*....
gi 568945777    772 GNTPLICACSAGHHEVAALLLQHGASINA 800
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 491-516 2.69e-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: 2.69e-04
                            10        20
                    ....*....|....*....|....*.
gi 568945777    491 NGNTPLHLACTYGQEDCVKALVYYDV 516
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
686-856 5.69e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 5.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  686 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 765
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  766 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 845
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 568945777  846 EQ--DSKIMELLQ 856
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
636-845 6.57e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 6.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  636 LLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAAL 715
Cdd:COG0666    91 LHAAARNGDLEIVKLLLE-----------------------------------------AGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  716 HGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHG 795
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568945777  796 ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 845
Cdd:COG0666   210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
439-842 1.79e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  439 ASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVqa 518
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  519 cRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLkcalnskilsimeahhlssdrrprpsevpaqsp 598
Cdd:COG0666    79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL--------------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  599 trsvdsisqgsstssfssisvsfrqeevkkdyreveklLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplc 678
Cdd:COG0666   125 --------------------------------------HLAAYNGNLEIVKLLLE------------------------- 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  679 qcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCL 758
Cdd:COG0666   142 ----------------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  759 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQ 838
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 568945777  839 YTAA 842
Cdd:COG0666   286 LTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
688-855 1.27e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 1.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  688 KLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNK 767
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  768 KDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA-- 845
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAae 195

                         170
                  ....*....|
gi 568945777  846 EQDSKIMELL 855
Cdd:COG0666   196 NGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
422-579 3.01e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 3.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  422 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 501
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  502 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 579
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
423-809 2.25e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  423 DDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTY 502
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  503 GQEDCVKALVYYDVQacrLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPlkcalnskilsimeahhl 582
Cdd:COG0666    98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------------------ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  583 ssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekLLRAVADGDLEMVRYLLEwteddlddv 662
Cdd:COG0666   157 -----------------------------------------------------LHLAAANGNLEIVKLLLE--------- 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  663 edaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVP 742
Cdd:COG0666   175 --------------------------------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568945777  743 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTAL 809
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
422-579 3.52e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 3.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  422 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 501
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  502 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 579
Cdd:COG0666   196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-776 7.34e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 7.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  420 FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 499
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  500 CTYGQEDCVKALVYY--DVqacrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLkcalnskilsim 577
Cdd:COG0666   128 AYNGNLEIVKLLLEAgaDV-----NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL------------ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  578 eahHLssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekllrAVADGDLEMVRYLLEwted 657
Cdd:COG0666   191 ---HL--------------------------------------------------------AAENGHLEIVKLLLE---- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  658 dlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNT 737
Cdd:COG0666   208 -------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 568945777  738 SQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPL 776
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
686-855 8.60e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 8.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  686 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 765
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  766 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA---A 842
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlA 160

                         170
                  ....*....|...
gi 568945777  843 dCAEQDSKIMELL 855
Cdd:COG0666   161 -AANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
743-835 8.72e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 8.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   743 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 822
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568945777   823 LLLFYGASVDILN 835
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
710-800 3.51e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 3.51e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   710 LHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDsNAKPNKKDlSGNTPLICACSAGHHEVAA 789
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 568945777   790 LLLQHGASINA 800
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
463-552 1.26e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   463 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 542
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 568945777   543 IIETLLQNGA 552
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 392-431 1.39e-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: 1.39e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568945777  392 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 431
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 692-836 8.20e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 8.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  692 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 767
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  768 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 831
Cdd:PHA03100  172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 568945777  832 DILNK 836
Cdd:PHA03100  252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 669-709 1.28e-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: 1.28e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 568945777  669 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 709
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
430-522 2.27e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   430 LHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEvqDNNGNTPLHLACTYGQEDCVK 509
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568945777   510 ALVYYDVQACRLD 522
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 700-834 6.86e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 6.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  700 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICA 779
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568945777  780 CSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDIL 834
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 227-326 4.43e-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: 71.86  E-value: 4.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   227 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 306
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 568945777   307 AKDELGYCLTSVEAAIEYIR 326
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 694-835 1.20e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.61  E-value: 1.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  694 ANGLSVNVTNQD-GFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSG 772
Cdd:PHA02878  155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568945777  773 NTPL-ICACSAGHHEVAALLLQHGASINACNN-KGNTALHEAVmgRHTLVVELLLFYGASVDILN 835
Cdd:PHA02878  235 NTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLN 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 423-585 1.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  423 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 482
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  483 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 559
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568945777  560 ---LKETPLKCALNSKIL--SIMEAHHLSSD 585
Cdd:PHA03100  258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 350-570 1.57e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  350 MNLLSQMTSTPidcLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSC-----EDCEKLISGRLNDPSV-------- 416
Cdd:PHA02874   28 INISVDETTTP---LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigaHDIIKLLIDNGVDTSIlpipciek 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  417 ----------VTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTE 486
Cdd:PHA02874  105 dmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  487 VQDNNGNTPLHLACTYGQEDCVKALVyydVQACRLDIGNEKGDTALHIAARWGYEGIieTLLQNGAPTAVQNRLKETPLK 566
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLH 259


                  ....
gi 568945777  567 CALN 570
Cdd:PHA02874  260 HAIN 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
636-769 1.17e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   636 LLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAAL 715
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-----------------------------------------NGADANLQDKNGRTALHLAAK 39

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568945777   716 HGRTDLVPLLLKHGAysGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKD 769
Cdd:pfam12796   40 NGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 424-569 1.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.53  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  424 DRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYg 503
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568945777  504 qedcvkaLVYYDVQACRLDIG---NEK----GDTALHIAARwgYEGIIETLLQNGAPTAVQNRLKETPLKCAL 569
Cdd:PHA02878  245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 691-839 2.28e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  691 RISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-----VAKCLLDSNAKP 765
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  766 NKKDLSGNTPLICACSA--GHHEVAALLLQHGASINACNNKGNTALHEAVMGRH--TLVVELLLFYGASVDILNKRQY 839
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY 177
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 392-429 2.55e-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: 64.97  E-value: 2.55e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568945777  392 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTP 429
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 696-850 2.96e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  696 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTP 775
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  776 LICACSAGHHEVAALLLQHGASI-NACNNkGNTALHEAVMGRHTlVVELL--------------------LFYGASVDIL 834
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHImNKCKN-GFTPLHNAIIHNRS-AIELLinnasindqdidgstplhhaINPPCDIDII 271

                         170
                  ....*....|....*.
gi 568945777  835 NKRQYTAADCAEQDSK 850
Cdd:PHA02874  272 DILLYHKADISIKDNK 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
 689-836 4.65e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 4.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  689 LARISANGLSVNVTNQDGFSPLHM---AALHGRTDLVPLLLKHGAYSGARNTSQAVPLHL-ACQQGHFQVAKCLLDSNAK 764
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568945777  765 PNKKDLSGNTPL-ICACS-AGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVELL-LFYGASVDILNK 836
Cdd:PHA03095  110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELLrLLIDAGADVYAV 183
PHA03095 PHA03095
ankyrin-like protein; Provisional
 445-832 4.70e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  445 LVSKGAVVNATDYHGSTPLHLACQKGFQSVT---LLLLHYKASTEVQDNNGNTPLHLACTYGQ-EDCVKALVYY--DVQA 518
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVNA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  519 CrldigNEKGDTALHIAAR--WGYEGIIETLLQNGA-PTAVQNRLKeTPLKCALNSKilsimeahhlssdrrprpsevpa 595
Cdd:PHA03095  113 K-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGAdVNALDLYGM-TPLAVLLKSR----------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  596 qsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekllravaDGDLEMVRYLLEWTEDdlddvedaISTVDLEF-- 673
Cdd:PHA03095  164 ----------------------------------------------NANVELLRLLIDAGAD--------VYAVDDRFrs 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  674 -CHPLCQCPKcAPAQKLARISANGLSVNVTNQDGFSPLHMAALHG---RTDLVPLLLKhGAYSGARNTSQAVPLHLACQQ 749
Cdd:PHA03095  190 lLHHHLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVF 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  750 GHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHE-VAALLLQH------GASINACNNKGNTALHEAvmgRHTLVVE 822
Cdd:PHA03095  268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNpsaetvAATLNTASVAGGDIPSDA---TRLCVAK 344

                         410
                  ....*....|
gi 568945777  823 LLLFYGASVD 832
Cdd:PHA03095  345 VVLRGAFSLL 354
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 441-576 5.06e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 5.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  441 LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL--LLLHYKASTEVQDNNGNTPLHLA--CTYGQEDCVKALVY--Y 514
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDkgV 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568945777  515 DVQA-----------CRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 576
Cdd:PHA03100  168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 443-831 9.83e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 9.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  443 DFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVyydvqACRLD 522
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  523 IgnEKGDTALHIAARwgYEGIIETLLQNGAPTAVQ--NRLKETPLkcalnskilsimeaHHLSsdRRPRPSEVPAQSPTR 600
Cdd:PHA02876  237 I--NKNDLSLLKAIR--NEDLETSLLLYDAGFSVNsiDDCKNTPL--------------HHAS--QAPSLSRLVPKLLER 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  601 SVDSisqgsstssfssisvsfrqeEVKKDYREVEKLLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQc 680
Cdd:PHA02876  297 GADV--------------------NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQ- 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  681 pkcapAQKLAR-----ISANGLSVNVTNQDGF--SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA-CQQGHF 752
Cdd:PHA02876  348 -----ASTLDRnkdivITLLELGANVNARDYCdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPY 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  753 QVAKCLLDSNAKPNKKDLSGNTPLICACSAG-HHEVAALLLQHGASINACNNKGNTALHEAvMGRHTlVVELLLFYGASV 831
Cdd:PHA02876  423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 720-844 1.44e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  720 DLVPLLLKHGA---YSGARNTSqavPLHLACQQGHFQVAK---CLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 792
Cdd:PHA03095   28 EEVRRLLAAGAdvnFRGEYGKT---PLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568945777  793 QHGASINACNNKGNTALHE--AVMGRHTLVVELLLFYGASVDILNKRQYTAADC 844
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 636-824 9.60e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 9.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  636 LLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAAL 715
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  716 HGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQqgHFQVAKCLLDSNAKPNKKDLSGNTPLICA----CSAghhEVAALL 791
Cdd:PHA02874  200 YGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCDI---DIIDIL 274

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 568945777  792 LQHGASINACNNKGNTALHEAV--MGRHTLVVELL 824
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFkyINKDPVIKDII 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
772-825 2.07e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 2.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568945777   772 GNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLL 825
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 741-855 3.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 3.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  741 VPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHH-----EVAALLLQHGASINACNNKGNTALHEAVMG 815
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568945777  816 R--HTLVVELLLFYGASVDILNKRQYT----AADCAEQDSKIMELL 855
Cdd:PHA03100  117 KsnSYSIVEYLLDNGANVNIKNSDGENllhlYLESNKIDLKILKLL 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 423-514 4.06e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.85  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  423 DDRGQTPLHVAA--LC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTP 495
Cdd:PTZ00322   72 EVIDPVVAHMLTveLCqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151

                          90
                  ....*....|....*....
gi 568945777  496 LHLACTYGQEDCVKALVYY 514
Cdd:PTZ00322  152 LELAEENGFREVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
419-489 7.24e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 7.24e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568945777   419 PFSRDDRGQTPLHVAALCGQASLIDFLVSKgAVVNATDYhGSTPLHLACQKGFQSVTLLLLHYKASTEVQD 489
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 438-571 4.44e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  438 QASLIDFLVSKGAVVNATDYH-GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdv 516
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  517 qACRLDIGNEKGDTALHIAARW--GYEgIIETLLQNGAPTAVQNRLKE-TPLKCALNS 571
Cdd:PHA02878  224 -GASTDARDKCGNTPLHISVGYckDYD-ILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 719-870 4.76e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  719 TDLVPLLLKHGAYSGARNTSQ-AVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGAS 797
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568945777  798 INACNNKGNTALHEAVmGR--HTLVVELLLFYGASVDILNK-RQYTAADCAEQDSKIMELLQVVPGCVASLDSVEE 870
Cdd:PHA02878  227 TDARDKCGNTPLHISV-GYckDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNSYKL 301
PHA02798 PHA02798
ankyrin-like protein; Provisional
 719-844 4.84e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.32  E-value: 4.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  719 TDLVPLLLKHGAYSGARNTSQAVPL-----HLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGH---HEVAAL 790
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  791 LLQHGASINACNNKGNTALHEAVMGRHTL---VVELLLFYGASVDIL-NKRQYTAADC 844
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHnNKEKYDTLHC 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 685-816 6.85e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  685 PAQKLAR-ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQ-GHFQVAKCLLDSN 762
Cdd:PHA02878  179 KDQRLTElLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568945777  763 AKPNKKD-LSGNTPLicACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGR 816
Cdd:PHA02878  259 VDVNAKSyILGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 633-840 1.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  633 VEKLLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVtnqdgfspLHM 712
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGAD--------INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  713 AALHgrTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 792
Cdd:PHA02874  100 PCIE--KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 568945777  793 QHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYT 840
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 636-851 2.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  636 LLRAVADGDLEMVRYLLEWTEDDLDDVEDAIStvdlefchPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAAL 715
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGIS--------PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  716 HGRTDLVPLLLKHGAYSGARNTSQA-VPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQH 794
Cdd:PHA02875   78 EGDVKAVEELLDLGKFADDVFYKDGmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  795 GASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADC-AEQDSKI 851
Cdd:PHA02875  158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKI 215
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 696-841 2.78e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  696 GLSVNVTNQDGFSPLHMAA-LHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH-FQVAKCLLDSNAKPNKKDLSGN 773
Cdd:PHA02876  263 GFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI 342

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568945777  774 TPLICACSAGHH-EVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA 841
Cdd:PHA02876  343 TPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 636-799 2.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  636 LLRAVADGDLEMVRYLLEwTEDDLDDV--EDAIStvdlefchPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMA 713
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLD-LGKFADDVfyKDGMT--------PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  714 ALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 792
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFI 222


                  ....*..
gi 568945777  793 QHGASIN 799
Cdd:PHA02875  223 KRGADCN 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 700-794 3.40e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  700 NVTNQDGFSP--LHMAALH-------GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDL 770
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                          90       100
                  ....*....|....*....|....
gi 568945777  771 SGNTPLICACSAGHHEVAALLLQH 794
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 696-835 5.63e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  696 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKdlSGNTP 775
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDL 625

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  776 LICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILN 835
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
742-792 9.09e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568945777   742 PLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 792
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 672-709 2.04e-08

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


Pssm-ID: 439264 [Multi-domain]  Cd Length: 38  Bit Score: 51.10  E-value: 2.04e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568945777  672 EFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSP 709
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 530-836 2.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  530 TALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEAhhlssdrrprpsevpaqsptrSVDSisqgs 609
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA---------------------IIDN----- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  610 stssfssisvsfRQEEVKKDYreveKLLRAVADGDLEmvryllewTEDDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKL 689
Cdd:PHA02876  234 ------------RSNINKNDL----SLLKAIRNEDLE--------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  690 A-RISANGLSVNVTNQDGFSPLHMAALHG-RTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-VAKCLLDSNAKPN 766
Cdd:PHA02876  290 VpKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVN 369

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568945777  767 KKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLV-VELLLFYGASVDILNK 836
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNK 440
PHA03095 PHA03095
ankyrin-like protein; Provisional
 694-833 4.90e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 4.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  694 ANGLSVNVTNQDGFSPLHmaALHGRTD----LVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 767
Cdd:PHA03095  140 RKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAA 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568945777  768 KDLSGNTPL-----ICACSAGHheVAALLLqHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDI 833
Cdd:PHA03095  218 TDMLGNTPLhsmatGSSCKRSL--VLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 429-580 5.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  429 PLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQ---------------------------------------- 468
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  469 ------KGFQS------------------VTLLLLHYKASTEVQD-NNGNTPLHLACTYGQEDCVKALVYYDVQACRLDI 523
Cdd:PHA02878  120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568945777  524 GNekgDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCA----LNSKILSIMEAH 580
Cdd:PHA02878  200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLLEH 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 424-508 6.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  424 DRGQTPLHVAALCGQaSLIDFLVSKgAVVNATDYHGSTPLHLA----CQKgfqSVTLLLLHYKASTEVQDNNGNTPLHLA 499
Cdd:PHA02874  221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                  ....*....
gi 568945777  500 CTYGQEDCV 508
Cdd:PHA02874  296 FKYINKDPV 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 426-576 6.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  426 GQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKG-FQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 504
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568945777  505 EDCVKALVYYDVQAcrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 576
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 425-512 6.53e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  425 RGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 504
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                  ....*...
gi 568945777  505 EDCVKALV 512
Cdd:PHA02875  181 IAICKMLL 188
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 425-549 9.86e-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: 9.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  425 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEV 487
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568945777  488 QDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 549
Cdd:cd22193   155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
492-548 1.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568945777   492 GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGnekGDTALHIAARWGYEGIIETLL 548
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 359-510 1.78e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  359 TPIDCLFKhiaSGN-QKEVERLL---SQDDQDKDA-MQKMCHPLC-SCEDCEKLIsgRLNDPSVVTPFSRDDRGQTPLHV 432
Cdd:PHA03095  154 TPLAVLLK---SRNaNVELLRLLidaGADVYAVDDrFRSLLHHHLqSFKPRARIV--RELIRAGCDPAATDMLGNTPLHS 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  433 AALCG--QASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKA 510
Cdd:PHA03095  229 MATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 755-827 2.25e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.25e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568945777  755 AKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFY 827
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
708-759 2.26e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.26e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568945777   708 SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL 759
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 421-798 2.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  421 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQK----------------GFQSVTLL------- 477
Cdd:PHA02876  173 AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidtikaiidnrsniNKNDLSLLkairned 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  478 ----LLHYKASTEVQ--DNNGNTPLHLACtygQEDCVKALVYYDVQ-ACRLDIGNEKGDTALHIAARWGYEGI-IETLLQ 549
Cdd:PHA02876  253 letsLLLYDAGFSVNsiDDCKNTPLHHAS---QAPSLSRLVPKLLErGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIM 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  550 NGAPTAVQNRLKETPLkcalnskilsimeaHHLSSDRRPRPSEVPAQSPTRSVDSisqgsstssfssisvsfrqeevkKD 629
Cdd:PHA02876  330 LGADVNAADRLYITPL--------------HQASTLDRNKDIVITLLELGANVNA-----------------------RD 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  630 YREVEKLLRAVADGDLEMVRYLLEWTEDdLDDVEDAISTVdLEFChpLCqcpkcapaqklarisanglsvnvtnqdGFSP 709
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVIINTLLDYGAD-IEALSQKIGTA-LHFA--LC---------------------------GTNP 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  710 lHMAalhgrtdlVPLLLKHGAYSGARNTSQAVPLHLACQQG-HFQVAKCLLDSNAKPNKKDLSGNTPLICACsaGHHEVA 788
Cdd:PHA02876  422 -YMS--------VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIV 490

                         410
                  ....*....|
gi 568945777  789 ALLLQHGASI 798
Cdd:PHA02876  491 NILLHYGAEL 500
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 379-481 2.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  379 LLSQDDQDKDAMQKMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYH 458
Cdd:PTZ00322   68 LTTEEVIDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147

                          90       100
                  ....*....|....*....|...
gi 568945777  459 GSTPLHLACQKGFQSVTLLLLHY 481
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 657-836 3.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  657 DDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARN 736
Cdd:PHA02878   21 EYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  737 TSQAVplHLACQQGHFQVAKCLLDSNAKPNKkdlSGNTPLICACSAG---HHEVAALLLQHGASINACN-NKGNTALHEA 812
Cdd:PHA02878  101 TLVAI--KDAFNNRNVEIFKIILTNRYKNIQ---TIDLVYIDKKSKDdiiEAEITKLLLSYGADINMKDrHKGNTALHYA 175

                         170       180
                  ....*....|....*....|....
gi 568945777  813 VMGRHTLVVELLLFYGASVDILNK 836
Cdd:PHA02878  176 TENKDQRLTELLLSYGANVNIPDK 199
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 433-552 3.56e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  433 AALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPL---------------- 496
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  497 HLA------------CTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGA 552
Cdd:PLN03192  612 HFAsisdphaagdllCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 400-549 3.70e-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: 3.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   400 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 460
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777   461 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 526
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 568945777   527 KGDTALHIAARWGYEGIIETLLQ 549
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 772-803 9.02e-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: 9.02e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568945777   772 GNTPLICAC-SAGHHEVAALLLQHGASINACNN 803
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
445-499 9.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 9.95e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568945777   445 LVSKGAV-VNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 499
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
459-512 1.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.53e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568945777   459 GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALV 512
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 426-550 1.80e-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: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  426 GQTPLHVAALCGQASLIDFLVSKGAVVN---ATD-----------YHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 491
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  492 GNTPLHLACTygQEDCVKALVYYDV---------QACRLDIGNEKGDTALHIAARWGYEGIIETLLQN 550
Cdd:cd22192   169 GNTVLHILVL--QPNKTFACQMYDLilsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
419-466 1.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.94e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568945777   419 PFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLA 466
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 422-525 2.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  422 RDDRGQTPLHVA-ALCGQASLIDFLVSKGAVVNATDY-HGSTPLHLACQKgfQSVTLLLLHYKASTEVQDNNGNTPLHLA 499
Cdd:PHA02878  230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                          90       100
                  ....*....|....*....|....*.
gi 568945777  500 ctygqedcvkALVYYDVQACRLDIGN 525
Cdd:PHA02878  308 ----------VKQYLCINIGRILISN 323
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 425-548 3.28e-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: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  425 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLlhYKASTEV-- 487
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLM--EKESTDIts 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568945777  488 QDNNGNTPLHLACTYG-----QEDCVKALvyYD--VQACR---LD-IGNEKGDTALHIAARWGYEGIIETLL 548
Cdd:cd22194   218 QDSRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 665-814 4.84e-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: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  665 AISTVDLEFCHPLCQCPKCAPAQKLARisanglsvnvtnqdGFSPLHMAALHGRTDLVPLLLKhgaysGARN------TS 738
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGAL--------------GETALHVAALYDNLEAAVVLME-----AAPElvnepmTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  739 Q----AVPLHLACQQGHFQVAKCLLDSNA------------KPNKKDLS--GNTPLICACSAGHHEVAALLLQHGASINA 800
Cdd:cd22192    85 DlyqgETALHIAVVNQNLNLVRELIARGAdvvspratgtffRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                         170
                  ....*....|....
gi 568945777  801 CNNKGNTALHEAVM 814
Cdd:cd22192   165 QDSLGNTVLHILVL 178
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 227-325 5.97e-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: 5.97e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777    227 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 306
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 568945777    307 AKDELGYCLTSVEAAIEYI 325
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
Ank_5 pfam13857
Ankyrin repeats (many copies);
477-535 6.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568945777   477 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQacrLDIGNEKGDTALHIA 535
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
428-479 6.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 6.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568945777   428 TPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLL 479
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 772-800 8.59e-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: 8.59e-06
                            10        20
                    ....*....|....*....|....*....
gi 568945777    772 GNTPLICACSAGHHEVAALLLQHGASINA 800
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 391-429 1.01e-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: 1.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 568945777  391 QKMCHPLCSCEDCEKLISG-RLNDPSVVTPFSRDDRGQTP 429
Cdd:cd22886     3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
692-746 1.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568945777   692 ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA 746
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
765-812 1.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.22e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568945777   765 PNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEA 812
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 758-832 1.22e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568945777  758 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVD 832
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 430-578 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  430 LHVAALC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 504
Cdd:PHA02875    1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568945777  505 EDCVKALVyyDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIME 578
Cdd:PHA02875   81 VKAVEELL--DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 421-491 3.75e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568945777  421 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 491
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 425-549 4.20e-05

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 47.49  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  425 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLL--HYKASTEV 487
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568945777  488 QDNNGNTPLHLACTYG---QEDCVKALVYYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 549
Cdd:cd22196   173 RDSMGNTVLHALVEVAdntPENTKFVTKMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 425-549 4.40e-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: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  425 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD-------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEVQ 488
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568945777  489 DNNGNTPLHlACTYGQEDCVK--ALV--YYD--VQA-CRLD-------IGNEKGDTALHIAARWGYEGIIETLLQ 549
Cdd:cd22197   173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDglLQAgARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 804-836 7.46e-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: 7.46e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568945777   804 KGNTALHEAV-MGRHTLVVELLLFYGASVDILNK 836
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 758-832 8.70e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 8.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568945777  758 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVE---LLLFYGASVD 832
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKIN 134
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 379-565 1.97e-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: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  379 LLSQDDQDKDAMQKmchpLCSCEDCEklisgrlndpsvvtPFSRDDRGQTPLHVAALCGQASLIDFLVSKG-AVVN--AT 455
Cdd:cd22192    22 LLAAKENDVQAIKK----LLKCPSCD--------------LFQRGALGETALHVAALYDNLEAAVVLMEAApELVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  456 D--YHGSTPLHLACQKgfQSVTL--LLLHYKASTevqdnngNTPlhLACTYGQEDCVKALVYYdvqacrldignekGDTA 531
Cdd:cd22192    84 SdlYQGETALHIAVVN--QNLNLvrELIARGADV-------VSP--RATGTFFRPGPKNLIYY-------------GEHP 139

                         170       180       190
                  ....*....|....*....|....*....|....
gi 568945777  532 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPL 565
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 772-800 2.56e-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: 2.56e-04
                           10        20
                   ....*....|....*....|....*....
gi 568945777   772 GNTPLICACSAGHHEVAALLLQHGASINA 800
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 418-522 2.58e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  418 TPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLAC---QKGFQSVTLLLLHYKASTEVQDNNGNT 494
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143

                          90       100
                  ....*....|....*....|....*...
gi 568945777  495 PLhLACTYGQEDCVKALVYYDVQACRLD 522
Cdd:PHA02946  144 PL-LACTDPSERVFKKIMSIGFEARIVD 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 491-516 2.69e-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: 2.69e-04
                            10        20
                    ....*....|....*....|....*.
gi 568945777    491 NGNTPLHLACTYGQEDCVKALVYYDV 516
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 623-790 2.88e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  623 QEEVKKDYREVEKLL---RAVADGDLEMVryllewTEDDLDDVEDAISTVDLefchplCQCPKCAPAQKLARISANGLSV 699
Cdd:PTZ00322   41 QEEIARIDTHLEALEateNKDATPDHNLT------TEEVIDPVVAHMLTVEL------CQLAASGDAVGARILLTGGADP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  700 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL---------DSNAKPNKKDL 770
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKPDSFTG 188

                         170       180
                  ....*....|....*....|
gi 568945777  771 SGNTPLICACSAGHHEVAAL 790
Cdd:PTZ00322  189 KPPSLEDSPISSHHPDFSAV 208
Ank_4 pfam13637
Ankyrin repeats (many copies);
689-726 3.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 3.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568945777   689 LARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLL 726
Cdd:pfam13637   17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 425-456 3.88e-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: 3.88e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568945777   425 RGQTPLHVAAL-CGQASLIDFLVSKGAVVNATD 456
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 777-867 3.92e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  777 ICACSAGHHEVAA-LLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCAEQDS--KIME 853
Cdd:PTZ00322   86 LCQLAASGDAVGArILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQ 165

                          90
                  ....*....|....
gi 568945777  854 LLQVVPGCVASLDS 867
Cdd:PTZ00322  166 LLSRHSQCHFELGA 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 705-730 6.14e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 6.14e-04
                            10        20
                    ....*....|....*....|....*.
gi 568945777    705 DGFSPLHMAALHGRTDLVPLLLKHGA 730
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 705-730 9.20e-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: 9.20e-04
                           10        20
                   ....*....|....*....|....*.
gi 568945777   705 DGFSPLHMAALHGRTDLVPLLLKHGA 730
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
528-569 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 568945777   528 GDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCAL 569
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 477-565 1.06e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  477 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDignEKGDTALHIAARWGYEGIIETLLQ------- 549
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLSRhsqchfe 176

                          90       100
                  ....*....|....*....|..
gi 568945777  550 ---NGAP---TAVQNRLKETPL 565
Cdd:PTZ00322  177 lgaNAKPdsfTGKPPSLEDSPI 198
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 527-559 1.22e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.22e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 568945777   527 KGDTALHIAA-RWGYEGIIETLLQNGAPTAVQNR 559
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
791-845 1.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568945777   791 LLQHG-ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 845
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 425-454 1.74e-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: 1.74e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 568945777    425 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 454
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 527-552 1.77e-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: 36.80  E-value: 1.77e-03
                            10        20
                    ....*....|....*....|....*.
gi 568945777    527 KGDTALHIAARWGYEGIIETLLQNGA 552
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 420-534 1.99e-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: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  420 FSRDDRGQTPLHVAAL---CGQASLIDFLV-------SKGAVVNA--TD--YHGSTPLHLACQKgfQSVTL--LLLHYKA 483
Cdd:cd21882    20 YQRGATGKTCLHKAALnlnDGVNEAIMLLLeaapdsgNPKELVNApcTDefYQGQTALHIAIEN--RNLNLvrLLVENGA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568945777  484 STEVQDNN-------------GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHI 534
Cdd:cd21882    98 DVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHA 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 705-736 2.35e-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: 2.35e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568945777   705 DGFSPLHMAALH-GRTDLVPLLLKHGAYSGARN 736
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 742-767 2.58e-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: 2.58e-03
                            10        20
                    ....*....|....*....|....*.
gi 568945777    742 PLHLACQQGHFQVAKCLLDSNAKPNK 767
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 674-711 2.74e-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: 2.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568945777  674 CHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLH 711
Cdd:cd22885     3 CHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 425-454 3.43e-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: 3.43e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568945777   425 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 454
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 522-588 3.57e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  522 DIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSK---ILSIMeaHHLSSDRRP 588
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkIFRIL--YHFASISDP 619
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 491-514 3.81e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.81e-03
                           10        20
                   ....*....|....*....|....*
gi 568945777   491 NGNTPLHLACT-YGQEDCVKALVYY 514
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
Ank_2 pfam12796
Ankyrin repeats (3 copies);
532-579 3.91e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 3.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 568945777   532 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 804-833 4.22e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.22e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 568945777    804 KGNTALHEAVMGRHTLVVELLLFYGASVDI 833
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 804-833 4.43e-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: 4.43e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568945777   804 KGNTALHEAVMGRHTLVVELLLFYGASVDI 833
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 402-523 4.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  402 DCEKLISGRLNDPSVvtpfSRDDRgQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLhy 481
Cdd:PHA02875  116 DIMKLLIARGADPDI----PNTDK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL-- 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568945777  482 kastevqdNNGNTPLHlactYGQEDCVKALVyYDVQACRLDI 523
Cdd:PHA02875  189 --------DSGANIDY----FGKNGCVAALC-YAIENNKIDI 217
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 418-497 6.10e-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: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  418 TPFsRD--DRGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHLA-CQKGFQSVTLLL-- 478
Cdd:cd22195   128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                          90
                  ....*....|....*....
gi 568945777  479 LHYKASTEVQDNNGNTPLH 497
Cdd:cd22195   207 AHKKADLRRQDSRGNTVLH 225
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 491-516 7.32e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.32e-03
                           10        20
                   ....*....|....*....|....*.
gi 568945777   491 NGNTPLHLACTYGQEDCVKALVYYDV 516
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 759-845 8.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568945777  759 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDILNKR 837
Cdd:PHA02884   57 ADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTND 136


                  ....*...
gi 568945777  838 QYTAADCA 845
Cdd:PHA02884  137 MVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 417-469 9.78e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 9.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568945777  417 VTPFSR-----------DDRGQTPLHVAALCGQA----SLIDFLVSKGAVVNATD-YHGSTPLHLACQK 469
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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