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Conserved domains on  [gi|386771204|ref|NP_001246786|]
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myosin binding subunit, isoform O [Drosophila melanogaster]

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];
50-300 7.90e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 7.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   50 FLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIAR 129
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  130 YLVENGADVAAVNSDGDLALDLAIDVQHMAMIdymekmvqelninvdearkaeelamlndakKWLRSDAAEVDRPHPKtG 209
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIV------------------------------KLLLEAGADVNARDND-G 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  210 ATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKF 289
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                         250
                  ....*....|.
gi 386771204  290 LEELRANKRNK 300
Cdd:COG0666   267 IVKLLLLALLL 277
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 1177-1273 6.02e-34

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


:

Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 125.88  E-value: 6.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  1177 DYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFA-----NATTKNSLSELEKRERRAMERKLSELEEELKQLDAYK 1251
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqqrqeSFSDRSSLLETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 386771204  1252 SDNHRLKEENAALIRVISKLSK 1273
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 606-648 2.12e-16

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


:

Pssm-ID: 412018  Cd Length: 47  Bit Score: 73.92  E-value: 2.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEE 648
Cdd:cd21930     5 RSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-300 7.90e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 7.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   50 FLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIAR 129
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  130 YLVENGADVAAVNSDGDLALDLAIDVQHMAMIdymekmvqelninvdearkaeelamlndakKWLRSDAAEVDRPHPKtG 209
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIV------------------------------KLLLEAGADVNARDND-G 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  210 ATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKF 289
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                         250
                  ....*....|.
gi 386771204  290 LEELRANKRNK 300
Cdd:COG0666   267 IVKLLLLALLL 277
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 1177-1273 6.02e-34

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 125.88  E-value: 6.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  1177 DYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFA-----NATTKNSLSELEKRERRAMERKLSELEEELKQLDAYK 1251
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqqrqeSFSDRSSLLETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 386771204  1252 SDNHRLKEENAALIRVISKLSK 1273
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
PHA03095 PHA03095
ankyrin-like protein; Provisional
 48-282 5.68e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.95  E-value: 5.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   48 CVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALH-QACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFV- 125
Cdd:PHA03095   52 HLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNIn 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  126 -SIARYLVENGADVAAVNSDGDLALD-----------------------LAIDVQHMAMIDYMekmvqeLNINVDEARKA 181
Cdd:PHA03095  132 pKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvellrllidagadvYAVDDRFRSLLHHH------LQSFKPRARIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  182 EELAMLNdakkwlrSDAAEVDRphpkTGATALHVAAAKGYTK---VLGLLLAGRGnVDRQDNDGWTPLHAASHWGQRETA 258
Cdd:PHA03095  206 RELIRAG-------CDPAATDM----LGNTPLHSMATGSSCKrslVLPLLIAGIS-INARNRYGQTPLHYAAVFNNPRAC 273

                         250       260
                  ....*....|....*....|....
gi 386771204  259 EMLVESLADMDIRNYAGQSCIDVA 282
Cdd:PHA03095  274 RRLIALGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-138 6.89e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 6.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204    53 ACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERgADINRQDNeGWTPLHATASCGFVSIARYLV 132
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81


                   ....*.
gi 386771204   133 ENGADV 138
Cdd:pfam12796   82 EKGADI 87
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 606-648 2.12e-16

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 73.92  E-value: 2.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEE 648
Cdd:cd21930     5 RSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 58-224 4.32e-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: 51.17  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQLLDQGAD--IN---TANV-DGLTALHQACIDDNLDMVEFLVERGADIN-----------RQDNE---GWTPLH 117
Cdd:cd22192    62 DNLEAAVVLMEAAPelVNepmTSDLyQGETALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLiyyGEHPLS 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  118 ATASCGFVSIARYLVENGADVAAVNSDGDLALdlaidvqHMAMidymekmvqeLNINVDEARKAEELAMLNDAKKwlrsD 197
Cdd:cd22192   142 FAACVGNEEIVRLLIEHGADIRAQDSLGNTVL-------HILV----------LQPNKTFACQMYDLILSYDKED----D 200

                         170       180
                  ....*....|....*....|....*..
gi 386771204  198 AAEVDRPHPKTGATALHVAAAKGYTKV 224
Cdd:cd22192   201 LQPLDLVPNNQGLTPFKLAAKEGNIVM 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-106 1.06e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 1.06e-05
                            10        20
                    ....*....|....*....|....*....
gi 386771204     78 DGLTALHQACIDDNLDMVEFLVERGADIN 106
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 79-230 1.08e-04

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: 46.61  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204    79 GLTALHQACIDDNLDMVEFLVERGADIN----------RQDNE----GWTPLHATASCGFVSIARYLVENGADVAAvnsd 144
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILT---- 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   145 gdlALDLAIDVQHMAMI------DYME---KMVQELNINVDEARKAEEL-AMLNDAkkwlrsdaaevdrphpktGATALH 214
Cdd:TIGR00870  204 ---ADSLGNTLLHLLVMenefkaEYEElscQMYNFALSLLDKLRDSKELeVILNHQ------------------GLTPLK 262

                          170
                   ....*....|....*.
gi 386771204   215 VAAAKGYTKVLGLLLA 230
Cdd:TIGR00870  263 LAAKEGRIVLFRLKLA 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-300 7.90e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 7.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   50 FLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIAR 129
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  130 YLVENGADVAAVNSDGDLALDLAIDVQHMAMIdymekmvqelninvdearkaeelamlndakKWLRSDAAEVDRPHPKtG 209
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIV------------------------------KLLLEAGADVNARDND-G 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  210 ATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKF 289
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                         250
                  ....*....|.
gi 386771204  290 LEELRANKRNK 300
Cdd:COG0666   267 IVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-339 1.25e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.25e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   50 FLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIAR 129
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  130 YLVENGADVAAVNSDGDLALDLAIDVQHMAMIdymekmvqelninvdearkaeelamlndakKWLRSDAAEVDRPHpKTG 209
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIV------------------------------KLLLEAGADVNAQD-NDG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  210 ATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVA----DRK 285
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaengNLE 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386771204  286 IVKFLEELRANKRNKRRPSSQIRISDAMENHVEKTPTKLVRVEVRTDATKDAEN 339
Cdd:COG0666   234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 1177-1273 6.02e-34

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 125.88  E-value: 6.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  1177 DYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFA-----NATTKNSLSELEKRERRAMERKLSELEEELKQLDAYK 1251
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqqrqeSFSDRSSLLETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 386771204  1252 SDNHRLKEENAALIRVISKLSK 1273
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
PHA03095 PHA03095
ankyrin-like protein; Provisional
 48-282 5.68e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.95  E-value: 5.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   48 CVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALH-QACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFV- 125
Cdd:PHA03095   52 HLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNIn 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  126 -SIARYLVENGADVAAVNSDGDLALD-----------------------LAIDVQHMAMIDYMekmvqeLNINVDEARKA 181
Cdd:PHA03095  132 pKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvellrllidagadvYAVDDRFRSLLHHH------LQSFKPRARIV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  182 EELAMLNdakkwlrSDAAEVDRphpkTGATALHVAAAKGYTK---VLGLLLAGRGnVDRQDNDGWTPLHAASHWGQRETA 258
Cdd:PHA03095  206 RELIRAG-------CDPAATDM----LGNTPLHSMATGSSCKrslVLPLLIAGIS-INARNRYGQTPLHYAAVFNNPRAC 273

                         250       260
                  ....*....|....*....|....
gi 386771204  259 EMLVESLADMDIRNYAGQSCIDVA 282
Cdd:PHA03095  274 RRLIALGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-138 6.89e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 6.89e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204    53 ACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERgADINRQDNeGWTPLHATASCGFVSIARYLV 132
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81


                   ....*.
gi 386771204   133 ENGADV 138
Cdd:pfam12796   82 EKGADI 87
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 606-648 2.12e-16

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 73.92  E-value: 2.12e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEE 648
Cdd:cd21930     5 RSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 58-318 3.91e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 3.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGAD 137
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  138 VAAVNSDGDLALDLAIDVQHMAMIDYMekMVQELNINVDearkaeelamlndakkwlrsdaaevdrphPKTGATALHVAA 217
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLL--IDHGNHIMNK-----------------------------CKNGFTPLHNAI 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  218 AkgYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWG-QRETAEMLVESLADMDIRNYAGQSCIDVADRKIVK--FLEELR 294
Cdd:PHA02874  232 I--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpVIKDII 309

                         250       260
                  ....*....|....*....|....
gi 386771204  295 ANKRNKRRpSSQIRISDAMeNHVE 318
Cdd:PHA02874  310 ANAVLIKE-ADKLKDSDFL-EHIE 331
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-163 4.54e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 4.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204    83 LHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGAdvAAVNSDGDLALDLAIDVQHMAMID 162
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                   .
gi 386771204   163 Y 163
Cdd:pfam12796   79 L 79
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-299 5.23e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 5.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   59 KDEVVQLLDQGADINTANVDGLTALH-----QACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASC--GFVSIARYL 131
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  132 VENGADVAAVNSDGDLALDLAIDVQHmamIDYmeKMVQEL---NINVDEARKAEelamlndakkwlrsdaaevdrphpkt 208
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNK---IDL--KILKLLidkGVDINAKNRVN-------------------------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  209 gatalhvaaakgytkvlgLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVA-DRKIV 287
Cdd:PHA03100  177 ------------------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAiLNNNK 238

                         250
                  ....*....|..
gi 386771204  288 KFLEELRANKRN 299
Cdd:PHA03100  239 EIFKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-132 4.74e-14

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 67.68  E-value: 4.74e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386771204    79 GLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLV 132
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 50-157 3.48e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   50 FLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQA--CIDDNLDMVEFLVERGADINRQ----------------DNE 111
Cdd:PHA03100  112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVY 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 386771204  112 GWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQH 157
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN 237
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 606-652 1.28e-11

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412020  Cd Length: 54  Bit Score: 60.87  E-value: 1.28e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKK 652
Cdd:cd21945     8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-117 1.31e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 57.74  E-value: 1.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386771204    65 LLDQG-ADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLH 117
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
213-297 3.11e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 3.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   213 LHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESlADMDIRNYaGQSCIDVA----DRKIVK 288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsgHLEIVK 78


                   ....*....
gi 386771204   289 FLEELRANK 297
Cdd:pfam12796   79 LLLEKGADI 87
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-262 5.68e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 5.68e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386771204   211 TALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLV 262
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-109 6.85e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 6.85e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 386771204    52 AACLSGDKDEVVQLLDQgADINtANVDGLTALHQACIDDNLDMVEFLVERGADINRQD 109
Cdd:pfam12796   36 LAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 73-292 7.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 7.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   73 NTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVE--NGADVA-AVNSDGDLAL 149
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsiNKCSVFyTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  150 DLAIDVQHMAMIDYMEKmvqELNINVDEARKAEELAMLnDAK--KWLRSDAAEVDRPHPKTGATALHVAAAKGYTKVLGL 227
Cdd:PHA02878  111 NRNVEIFKIILTNRYKN---IQTIDLVYIDKKSKDDII-EAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTEL 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  228 LLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVA-----DRKIVKFLEE 292
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgyckDYDILKLLLE 256
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-143 2.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   59 KDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLH-ATASCgFVSIARYLVENGAD 137
Cdd:PHA03100  172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHiAILNN-NKEIFKLLLNNGPS 250


                  ....*.
gi 386771204  138 VAAVNS 143
Cdd:PHA03100  251 IKTIIE 256
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 606-652 5.33e-09

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412019  Cd Length: 57  Bit Score: 53.37  E-value: 5.33e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKK 652
Cdd:cd21944    10 RSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-272 1.09e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   116 LHATASCGFVSIARYLVENGADVAAVNSDGDlaldlaidvqhmamidymekmvqelninvdearkaeelamlndakkwlr 195
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGR------------------------------------------------- 31

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386771204   196 sdaaevdrphpktgaTALHVAAAKGYTKVLGLLLAgRGNVDRQDNdGWTPLHAASHWGQRETAEMLVESLADMDIRN 272
Cdd:pfam12796   32 ---------------TALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-153 1.19e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   65 LLDQGADINTANVDGLTALHQA---CIDDNLDMVEFLvERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAV 141
Cdd:PHA03095  208 LIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLL-IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286

                          90
                  ....*....|..
gi 386771204  142 NSDGDLALDLAI 153
Cdd:PHA03095  287 SSDGNTPLSLMV 298
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-152 2.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 2.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386771204    98 LVERG-ADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLA 152
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 60-175 8.10e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.38  E-value: 8.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   60 DEVVQLLDQGADINTANVDGLTALhqaC------IDDN--LDMVEFLVERGADINRQDNEGWTPLHATASCGFVS---IA 128
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleIL 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 386771204  129 RYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQE-LNINV 175
Cdd:PHA02798  129 LFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEKgVDINT 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-149 2.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   65 LLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSD 144
Cdd:PHA02875  121 LIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200


                  ....*
gi 386771204  145 GDLAL 149
Cdd:PHA02875  201 GCVAA 205
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-153 2.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   49 VFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQAC-IDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSI 127
Cdd:PHA02876  311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90       100
                  ....*....|....*....|....*.
gi 386771204  128 ARYLVENGADVAAVNSDGDLALDLAI 153
Cdd:PHA02876  391 INTLLDYGADIEALSQKIGTALHFAL 416
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-99 3.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 386771204    49 VFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLV 99
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 606-648 3.42e-07

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, also called protein phosphatase 1 regulatory subunit 12B (PPP1R12B), or myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. This model corresponds to the inhibitory phosphorylation domain of MYPT2.


Pssm-ID: 412021  Cd Length: 53  Bit Score: 48.12  E-value: 3.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEE 648
Cdd:cd21946     5 RSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAER 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-110 5.23e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 5.23e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 386771204    78 DGLTALHQACID-DNLDMVEFLVERGADINRQDN 110
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 90-282 5.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 5.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   90 DNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHmamIDYMEKMV- 168
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN---IDTIKAIId 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  169 QELNINVDE-----ARKAEELA---MLNDAKKWLRS-------------DAAEVDRPHPK-------------TGATALH 214
Cdd:PHA02876  233 NRSNINKNDlsllkAIRNEDLEtslLLYDAGFSVNSiddckntplhhasQAPSLSRLVPKllergadvnakniKGETPLY 312

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  215 VAAAKGY-TKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQ-RETAEMLVESLADMDIRNYAGQSCIDVA 282
Cdd:PHA02876  313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYA 382
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 606-649 6.61e-07

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and similar proteins; Protein phosphatase 1 regulatory subunit 12A-like (PPP1R12A-like) is a homolog of MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit. MYPT1 is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of PPP1R12A-like protein.


Pssm-ID: 412022  Cd Length: 50  Bit Score: 47.18  E-value: 6.61e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 386771204  606 KSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEEL 649
Cdd:cd22527     7 RSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 51-131 6.72e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 6.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   51 LAAclSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARY 130
Cdd:PTZ00322   89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 386771204  131 L 131
Cdd:PTZ00322  167 L 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 62-301 6.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 6.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   62 VVQLLDQGADINTANVDGLTALHQACIDD-NLDMVEFLVERGADINRQDNEGWTPLHATASCG-FVSIARYLVENGADVA 139
Cdd:PHA02876  290 VPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  140 AVnsdgdlaldlaidvqhmamiDYMEKMvqelniNVDEARKAEELAMLNDakkwLRSDAAEVDRPHPKTGaTALHVA--A 217
Cdd:PHA02876  370 AR--------------------DYCDKT------PIHYAAVRNNVVIINT----LLDYGADIEALSQKIG-TALHFAlcG 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  218 AKGYTKVLGLLLAGrGNVDRQDNDGWTPLH-AASHWGQRETAEMLVESLADMDIRNYAGQS--CIDVADRKIVKFLEELR 294
Cdd:PHA02876  419 TNPYMSVKTLIDRG-ANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYplLIALEYHGIVNILLHYG 497


                  ....*..
gi 386771204  295 ANKRNKR 301
Cdd:PHA02876  498 AELRDSR 504
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 91-300 8.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 8.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   91 NLDMVEFLVE-RGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQhmamidyMEKMVQ 169
Cdd:PHA02874   13 DIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG-------AHDIIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  170 ELNINVDEARKAEELAMLNDAKKWLRSDAAEVDRPHPKTgATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAA 249
Cdd:PHA02874   86 LLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386771204  250 SHWGQRETAEMLVESLADMDIRNYAGQS----CIDVADRKIVKFLEELRANKRNK 300
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESplhnAAEYGDYACIKLLIDHGNHIMNK 219
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-106 1.33e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 45.71  E-value: 1.33e-06
                           10        20
                   ....*....|....*....|....*....
gi 386771204    78 DGLTALHQACIDDNLDMVEFLVERGADIN 106
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-153 1.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   65 LLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLH-ATASCGFVSIARYLVENGADVAAVNS 143
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGVDVNAKSY 266

                          90
                  ....*....|.
gi 386771204  144 DGDL-ALDLAI 153
Cdd:PHA02878  267 ILGLtALHSSI 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-249 1.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQ------LLDQGADINTANVDGL-TALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARY 130
Cdd:PHA02878  140 SKDDIIEaeitklLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  131 LVENGADVAAVNSDGDLALDLAIDvqhmAMIDY-MEKMVQELNINVdearkaeelamlnDAKKWLRsdaaevdrphpktG 209
Cdd:PHA02878  220 LLENGASTDARDKCGNTPLHISVG----YCKDYdILKLLLEHGVDV-------------NAKSYIL-------------G 269

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 386771204  210 ATALHVAAAKgyTKVLGLLLAGRGNVDRQDNDGWTPLHAA 249
Cdd:PHA02878  270 LTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-152 2.09e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 386771204   95 VEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLA 152
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 58-224 4.32e-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: 51.17  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQLLDQGAD--IN---TANV-DGLTALHQACIDDNLDMVEFLVERGADIN-----------RQDNE---GWTPLH 117
Cdd:cd22192    62 DNLEAAVVLMEAAPelVNepmTSDLyQGETALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLiyyGEHPLS 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  118 ATASCGFVSIARYLVENGADVAAVNSDGDLALdlaidvqHMAMidymekmvqeLNINVDEARKAEELAMLNDAKKwlrsD 197
Cdd:cd22192   142 FAACVGNEEIVRLLIEHGADIRAQDSLGNTVL-------HILV----------LQPNKTFACQMYDLILSYDKED----D 200

                         170       180
                  ....*....|....*....|....*..
gi 386771204  198 AAEVDRPHPKTGATALHVAAAKGYTKV 224
Cdd:cd22192   201 LQPLDLVPNNQGLTPFKLAAKEGNIVM 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-269 6.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   53 ACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGA--DINRQDNEgwTPLHATASCGFVSIARY 130
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAVEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  131 LVENGADVAAV-NSDGDLALDLAIDVQHmamIDYMEKMVqelninvdeARKAEelamlndakkwlrSDAAEVDRphpktg 209
Cdd:PHA02875   87 LLDLGKFADDVfYKDGMTPLHLATILKK---LDIMKLLI---------ARGAD-------------PDIPNTDK------ 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  210 ATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMD 269
Cdd:PHA02875  136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-106 1.06e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 1.06e-05
                            10        20
                    ....*....|....*....|....*....
gi 386771204     78 DGLTALHQACIDDNLDMVEFLVERGADIN 106
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-142 1.36e-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: 43.05  E-value: 1.36e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 386771204   111 EGWTPLH-ATASCGFVSIARYLVENGADVAAVN 142
Cdd:pfam00023    1 DGNTPLHlAAGRRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-153 1.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQLLDQGADINTANVDGLTALHQA---CIDdnLDMVEFLVERGADINRQDN-EGWTPLHAtaSCGFVSIARYLVE 133
Cdd:PHA02878  213 NKPIVHILLENGASTDARDKCGNTPLHISvgyCKD--YDILKLLLEHGVDVNAKSYiLGLTALHS--SIKSERKLKLLLE 288

                          90       100
                  ....*....|....*....|
gi 386771204  134 NGADVAAVNSDGDLALDLAI 153
Cdd:PHA02878  289 YGADINSLNSYKLTPLSSAV 308
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 72-155 1.61e-05

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.42  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   72 INTANVD----GLTALHQACIDDNLDMVEFLVERGADIN-RQDNE-------------GWTPLHATASCGFVSIARYLVE 133
Cdd:cd22196    83 VNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHaRASGEffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                          90       100
                  ....*....|....*....|....*
gi 386771204  134 N---GADVAAVNSDGDLALDLAIDV 155
Cdd:cd22196   163 NphsPADISARDSMGNTVLHALVEV 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-298 1.61e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   89 DDNLDMVEF--LVERGADINRQDNEGWTPLHATASCGF---VSIARYLVENGADVAAVNSDGDLALDLaidvqhmamidY 163
Cdd:PHA03095   22 ASNVTVEEVrrLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHL-----------Y 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  164 MekmvqelninvdeaRKAEELAMLndakKWLRSDAAEVDRPHpKTGATALHVAAAKGYT--KVLGLLLAGRGNVDRQDND 241
Cdd:PHA03095   91 L--------------YNATTLDVI----KLLIKAGADVNAKD-KVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLY 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386771204  242 GWTPLHA--ASHWGQRETAEMLVESLADMDIRNYAGQSCIDVadrkivkFLEELRANKR 298
Cdd:PHA03095  152 GMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHH-------HLQSFKPRAR 203
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 53-148 1.62e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   53 ACLSGDKDEVVQLLDQGADINTANVDGLTAL----------------HQACIDD---------------NLDMVEFLVER 101
Cdd:PLN03192  565 AASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASISDphaagdllctaakrnDLTAMKELLKQ 644

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 386771204  102 GADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLA 148
Cdd:PLN03192  645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFS 691
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 45-105 4.53e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 4.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771204   45 SSGCVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADI 105
Cdd:PLN03192  621 AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 241-272 4.76e-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: 41.51  E-value: 4.76e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 386771204   241 DGWTPLH-AASHWGQRETAEMLVESLADMDIRN 272
Cdd:pfam00023    1 DGNTPLHlAAGRRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 79-230 1.08e-04

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: 46.61  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204    79 GLTALHQACIDDNLDMVEFLVERGADIN----------RQDNE----GWTPLHATASCGFVSIARYLVENGADVAAvnsd 144
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDsfyhGESPLNAAACLGSPSIVALLSEDPADILT---- 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   145 gdlALDLAIDVQHMAMI------DYME---KMVQELNINVDEARKAEEL-AMLNDAkkwlrsdaaevdrphpktGATALH 214
Cdd:TIGR00870  204 ---ADSLGNTLLHLLVMenefkaEYEElscQMYNFALSLLDKLRDSKELeVILNHQ------------------GLTPLK 262

                          170
                   ....*....|....*.
gi 386771204   215 VAAAKGYTKVLGLLLA 230
Cdd:TIGR00870  263 LAAKEGRIVLFRLKLA 278
PHA02795 PHA02795
ankyrin-like protein; Provisional
 92-154 1.15e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 1.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386771204   92 LDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAID 154
Cdd:PHA02795  201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVD 263
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 79-143 1.36e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 1.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386771204   79 GLTALHQACIDDNLDMVEFLVERGADINRQDNE-------------GWTPLHATASCGFVSIARYLVENGADVAAVNS 143
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-138 1.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   51 LAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDD-NLDMVEFLVERGADINRQDNEGWTPLhaTASCGFVSIAR 129
Cdd:PHA02876  414 FALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVN 491


                  ....*....
gi 386771204  130 YLVENGADV 138
Cdd:PHA02876  492 ILLHYGAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-153 2.14e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   57 GDKDEVVQLLDQGADINTANVDGLTALHQACIdDNLDMVEFLVErGADINRQDNEGWTPLHATAS--CGfVSIARYLVEN 134
Cdd:PHA02874  201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLIN-NASINDQDIDGSTPLHHAINppCD-IDIIDILLYH 277

                          90
                  ....*....|....*....
gi 386771204  135 GADVAAVNSDGDLALDLAI 153
Cdd:PHA02874  278 KADISIKDNKGENPIDTAF 296
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-290 2.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.47e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386771204   242 GWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVA----DRKIVKFL 290
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-144 2.50e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   52 AACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHaTASCG---FVSIa 128
Cdd:PHA02876  348 ASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALH-FALCGtnpYMSV- 425

                          90
                  ....*....|....*.
gi 386771204  129 RYLVENGADVAAVNSD 144
Cdd:PHA02876  426 KTLIDRGANVNSKNKD 441
PHA02741 PHA02741
hypothetical protein; Provisional
 72-168 2.66e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.11  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   72 INTANVDGLTALHQACIDDN----LDMVEFLVERGADINRQDN-EGWTPLHATASCGFVSIARYLV-ENGADVAAVNSDG 145
Cdd:PHA02741   53 LNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADN 132

                          90       100
                  ....*....|....*....|...
gi 386771204  146 DLALDLAIDVQHMAMIDYMEKMV 168
Cdd:PHA02741  133 KSPFELAIDNEDVAMMQILREIV 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-164 2.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386771204   112 GWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYM 164
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 58-135 3.64e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQLLDQGADINTANVDGLTALH---QACIDDNLDMVEFLVERGADINRQDN-EGWTPLHA----TASCGFVSIAR 129
Cdd:PHA02798  124 NLEILLFMIENGADTTLLDKDGFTMLQvylQSNHHIDIEIIKLLLEKGVDINTHNNkEKYDTLHCyfkyNIDRIDADILK 203


                  ....*.
gi 386771204  130 YLVENG 135
Cdd:PHA02798  204 LFVDNG 209
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 61-151 4.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   61 EVVQLL-DQGADINTANVDGLTALHQAC--IDDNLDMVEFLVERGADINRQDNEGWTPLHATascgFV-----SIARYLV 132
Cdd:PHA02859  104 EILKILiDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYSY----ILfhsdkKIFDFLT 179

                          90
                  ....*....|....*....
gi 386771204  133 ENGADVAAVNSDGDLALDL 151
Cdd:PHA02859  180 SLGIDINETNKSGYNCYDL 198
Ank_5 pfam13857
Ankyrin repeats (many copies);
209-249 7.45e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 7.45e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 386771204   209 GATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAA 249
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 58-145 1.35e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.98  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   58 DKDEVVQLLDQGADINTANVDGLTALHQACIDDNL--DMVEFLVERGADINRQDNEGWTPLHATASCGFV---------- 125
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLSVvnildpetdn 375

                          90       100
                  ....*....|....*....|....
gi 386771204  126 ----SIARYLVENGADVAAVNSDG 145
Cdd:PHA02716  376 dirlDVIQCLISLGADITAVNCLG 399
PHA02791 PHA02791
ankyrin-like protein; Provisional
 71-166 1.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   71 DINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEgwTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALD 150
Cdd:PHA02791   22 DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALY 99

                          90
                  ....*....|....*.
gi 386771204  151 LAIDVQHMAMIDYMEK 166
Cdd:PHA02791  100 YAVDSGNMQTVKLFVK 115
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 51-146 2.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   51 LAACLSGDK--DEVVQLL-DQGADIN-TANVDGLTALHQ-ACIDDNL--DMVEFLVERGADINRQDNEGWTPLHATAsCG 123
Cdd:PHA02859   55 IFSCLEKDKvnVEILKFLiENGADVNfKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYM-CN 133

                          90       100
                  ....*....|....*....|....*.
gi 386771204  124 F---VSIARYLVENGADVAAVNSDGD 146
Cdd:PHA02859  134 FnvrINVIKLLIDSGVSFLNKDFDNN 159
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-138 2.51e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.51e-03
                            10        20
                    ....*....|....*....|....*...
gi 386771204    111 EGWTPLHATASCGFVSIARYLVENGADV 138
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
 89-149 2.85e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386771204   89 DDNLDMVEFLVERGADINRQDNEGWTPLhatasCGFVS----------IARYLVENGADVAAVNSDGDLAL 149
Cdd:PHA02798   48 SPSTDIVKLFINLGANVNGLDNEYSTPL-----CTILSnikdykhmldIVKILIENGADINKKNSDGETPL 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 241-270 3.61e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.61e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 386771204    241 DGWTPLHAASHWGQRETAEMLVESLADMDI 270
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-117 4.30e-03

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: 41.15  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204   53 ACLSGDKDEVVQLLDQGADINTANVDGlTALHQ----------------ACIdDNLDMVEFLVERGADINRQDNEGWTPL 116
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPgpknliyygehplsfaACV-GNEEIVRLLIEHGADIRAQDSLGNTVL 173


                  .
gi 386771204  117 H 117
Cdd:cd22192   174 H 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 123-296 8.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  123 GFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQELNINVDEAR-------------KAEELAMLND 189
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIEselhdaveegdvkAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386771204  190 AkkwlrsdaaeVDRPHPKTGATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMD 269
Cdd:PHA02875   93 F----------ADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                         170       180       190
                  ....*....|....*....|....*....|.
gi 386771204  270 IRNYAGQSCIDVA----DRKIVKFLEELRAN 296
Cdd:PHA02875  163 IEDCCGCTPLIIAmakgDIAICKMLLDSGAN 193
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 209-240 8.23e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 8.23e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 386771204   209 GATALHVAAAK-GYTKVLGLLLAGRGNVDRQDN 240
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
 
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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