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Conserved domains on  [gi|1972253392|ref|NP_001379325|]
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cGMP-dependent protein kinase interacting domain-containing protein [Caenorhabditis elegans]

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];
54-307 1.26e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   54 QDSDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGN 133
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  134 VAIVRYLCQHGADLSIVNSDkelaldlavdeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsqgeyrdiphhrt 213
Cdd:COG0666    166 LEIVKLLLEAGADVNARDND------------------------------------------------------------ 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  214 GGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVADKECID 293
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                          250
                   ....*....|....
gi 1972253392  294 YLVELADTVKVQNK 307
Cdd:COG0666    266 LIVKLLLLALLLLA 279
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 906-1019 2.03e-32

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: 121.26  E-value: 2.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  906 NYKALFEKERSECERLRREMEEMRRSQTadsyrgastQLAWRARNASPSAQPhnlSVAKSTSLASFDENERRSMERKISD 985
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELA---------ELKSQLERLTQQRQE---SFSDRSSLLETEKREKRALERKISE 68

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1972253392  986 LELQLKTATNLRMENQRLKEENGALVRVISKMTI 1019
Cdd:pfam15898   69 MEEELKVLEDLRAENQRLKDENGALIRVISKLSK 102
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 655-701 5.11e-14

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: 66.98  E-value: 5.11e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1972253392  655 TFSKPSRWQSKTVTESEAERRNNSRMQRQHRRSTQGVTKEQLEEASK 701
Cdd:cd21930      1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-307 1.26e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   54 QDSDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGN 133
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  134 VAIVRYLCQHGADLSIVNSDkelaldlavdeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsqgeyrdiphhrt 213
Cdd:COG0666    166 LEIVKLLLEAGADVNARDND------------------------------------------------------------ 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  214 GGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVADKECID 293
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                          250
                   ....*....|....
gi 1972253392  294 YLVELADTVKVQNK 307
Cdd:COG0666    266 LIVKLLLLALLLLA 279
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 906-1019 2.03e-32

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: 121.26  E-value: 2.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  906 NYKALFEKERSECERLRREMEEMRRSQTadsyrgastQLAWRARNASPSAQPhnlSVAKSTSLASFDENERRSMERKISD 985
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELA---------ELKSQLERLTQQRQE---SFSDRSSLLETEKREKRALERKISE 68

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1972253392  986 LELQLKTATNLRMENQRLKEENGALVRVISKMTI 1019
Cdd:pfam15898   69 MEEELKVLEDLRAENQRLKDENGALIRVISKLSK 102
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-151 5.24e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 5.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKgADVNAQDNeGWTPLHAAACCGNVAIVRYLC 141
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1972253392  142 QHGADLSIVN 151
Cdd:pfam12796   82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-280 5.12e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 5.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   60 LSACMSG----DEEEVEELLNKGANINTCTVDGLTALHQSVI-DSKPEMVRFLCEKGADVNAQDNEGWTPLHAaaCCGNV 134
Cdd:PHA03095    51 LHLYLHYssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHV--YLSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  135 AI----VRYLCQHGADLS-------------IVNSDKELA-LDLAVDEQCRDYLDDDYKRQMID--LDACRDQelqtmlK 194
Cdd:PHA03095   129 NInpkvIRLLLRKGADVNaldlygmtplavlLKSRNANVElLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPR------A 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  195 DVNMWMSQGEYRDIPHHRTGGTAMHVAA--GRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAE 272
Cdd:PHA03095   203 RIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282


                   ....*...
gi 1972253392  273 LSDLTFTG 280
Cdd:PHA03095   283 INAVSSDG 290
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 655-701 5.11e-14

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: 66.98  E-value: 5.11e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1972253392  655 TFSKPSRWQSKTVTESEAERRNNSRMQRQHRRSTQGVTKEQLEEASK 701
Cdd:cd21930      1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-235 3.05e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   69 EEVEELLNkganiNTCTVD---GLTALHQSVIDSKPEMVRFLCEKGADVNA-----------QDNE---GWTPLHAAACC 131
Cdd:cd22192     72 EAAPELVN-----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyyGEHPLSFAACV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  132 GNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQCRdylddDYKRQMIDLDACRDQELQTMLKDVnmwmsqgeyrdIPHH 211
Cdd:cd22192    147 GNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK-----TFACQMYDLILSYDKEDDLQPLDL-----------VPNN 210

                          170       180
                   ....*....|....*....|....
gi 1972253392  212 RtGGTAMHVAAGRGYTQLLELLIK 235
Cdd:cd22192    211 Q-GLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 120-149 4.49e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.49e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 1972253392   120 EGWTPLHAAACCGNVAIVRYLCQHGADLSI 149
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-307 1.26e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 1.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   54 QDSDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGN 133
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  134 VAIVRYLCQHGADLSIVNSDkelaldlavdeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsqgeyrdiphhrt 213
Cdd:COG0666    166 LEIVKLLLEAGADVNARDND------------------------------------------------------------ 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  214 GGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVADKECID 293
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                          250
                   ....*....|....
gi 1972253392  294 YLVELADTVKVQNK 307
Cdd:COG0666    266 LIVKLLLLALLLLA 279
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 906-1019 2.03e-32

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: 121.26  E-value: 2.03e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  906 NYKALFEKERSECERLRREMEEMRRSQTadsyrgastQLAWRARNASPSAQPhnlSVAKSTSLASFDENERRSMERKISD 985
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELA---------ELKSQLERLTQQRQE---SFSDRSSLLETEKREKRALERKISE 68

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1972253392  986 LELQLKTATNLRMENQRLKEENGALVRVISKMTI 1019
Cdd:pfam15898   69 MEEELKVLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-298 3.51e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 3.51e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   36 SEMNAEAARRTKRPKVQFQDSDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVN 115
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  116 AQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQcrdylDDDYKRQMIDLDAcrdqelqtmlkD 195
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-----NLEIVKLLLEAGA-----------D 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  196 VNMwmsqgeyrdipHHRTGGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSD 275
Cdd:COG0666    146 VNA-----------QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                          250       260
                   ....*....|....*....|...
gi 1972253392  276 LTFTGADVLGVADKECIDYLVEL 298
Cdd:COG0666    215 KDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-284 7.74e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 7.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLC 141
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  142 QHGADLSIVNSDkelaldlavdeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsqgeyrdiphhrtGGTAMHVA 221
Cdd:COG0666    207 EAGADVNAKDND------------------------------------------------------------GKTALDLA 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972253392  222 AGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVL 284
Cdd:COG0666    227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-151 5.24e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 5.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKgADVNAQDNeGWTPLHAAACCGNVAIVRYLC 141
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1972253392  142 QHGADLSIVN 151
Cdd:pfam12796   82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-280 5.12e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 5.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   60 LSACMSG----DEEEVEELLNKGANINTCTVDGLTALHQSVI-DSKPEMVRFLCEKGADVNAQDNEGWTPLHAaaCCGNV 134
Cdd:PHA03095    51 LHLYLHYssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHV--YLSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  135 AI----VRYLCQHGADLS-------------IVNSDKELA-LDLAVDEQCRDYLDDDYKRQMID--LDACRDQelqtmlK 194
Cdd:PHA03095   129 NInpkvIRLLLRKGADVNaldlygmtplavlLKSRNANVElLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPR------A 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  195 DVNMWMSQGEYRDIPHHRTGGTAMHVAA--GRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAE 272
Cdd:PHA03095   203 RIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282


                   ....*...
gi 1972253392  273 LSDLTFTG 280
Cdd:PHA03095   283 INAVSSDG 290
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 71-271 1.42e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   71 VEELLNKGANINTCTVDGLTALH-----QSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACC--GNVAIVRYLCQH 143
Cdd:PHA03100    51 VKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDN 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  144 GADLSIVNSDKELALDLAVdEQCRDYLDD-----DYKrqmIDLDAcrdqelqtmlKD-VNMWMSQGEYRDIPHHRtGGTA 217
Cdd:PHA03100   131 GANVNIKNSDGENLLHLYL-ESNKIDLKIlklliDKG---VDINA----------KNrVNYLLSYGVPINIKDVY-GFTP 195

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1972253392  218 MHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGA 271
Cdd:PHA03100   196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-251 2.62e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 2.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   64 MSGDEEEVEELL-NKGANINTCTVDGLTALHQ--SVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHA----AACcgNVAI 136
Cdd:PHA03095    92 YNATTLDVIKLLiKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksRNA--NVEL 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  137 VRYLCQHGADLSIVNSDKELALD------------------LAVDEQCRDYLDDDYKRQMIDLDACRDQELQTMLK---D 195
Cdd:PHA03095   170 LRLLIDAGADVYAVDDRFRSLLHhhlqsfkprarivrelirAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIagiS 249

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972253392  196 VNmwmsqgeYRDiphhRTGGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPL 251
Cdd:PHA03095   250 IN-------ARN----RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 655-701 5.11e-14

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: 66.98  E-value: 5.11e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1972253392  655 TFSKPSRWQSKTVTESEAERRNNSRMQRQHRRSTQGVTKEQLEEASK 701
Cdd:cd21930      1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-168 7.07e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 7.07e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972253392   92 LHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHgADLSIVNsDKELALDLAVDEQCRD 168
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-163 9.67e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 9.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   65 SGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKP--EMVRFLCEKGADVNAQ----------------DNEGWTPLH 126
Cdd:PHA03100   118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLH 197

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1972253392  127 AAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVD 163
Cdd:PHA03100   198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-294 1.11e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   92 LHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLcqhgadLSIVNSDKELALDLAVDEQCrdYLD 171
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLVAIKDAF--NNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  172 DDYKRQMIDLDACR------DQELQTMLKD-------VNMWMSQGEYRDIPHHRTGGTAMHVAAGRGYTQLLELLIKAGG 238
Cdd:PHA02878   113 NVEIFKIILTNRYKniqtidLVYIDKKSKDdiieaeiTKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGA 192

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972253392  239 NVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVADKECIDY 294
Cdd:PHA02878   193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
88-140 4.91e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 4.91e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1972253392   88 GLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYL 140
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 55-289 7.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 7.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   55 DSDIFLSACMsgDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNV 134
Cdd:PHA02874    93 DTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  135 AIVRYLCQHGADLSIVNSDKELALDLAVDeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsQGEYRDIPHHRTG 214
Cdd:PHA02874   171 DIIKLLLEKGAYANVKDNNGESPLHNAAE--------------------------------------YGDYACIKLLIDH 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  215 GTAMHVAAGRGYTQL----------LELLIKaGGNVRAQDVEGWTPLHAAAHW-AERDACKILLENGAELSDLTFTGADV 283
Cdd:PHA02874   213 GNHIMNKCKNGFTPLhnaiihnrsaIELLIN-NASINDQDIDGSTPLHHAINPpCDIDIIDILLYHKADISIKDNKGENP 291


                   ....*.
gi 1972253392  284 LGVADK 289
Cdd:PHA02874   292 IDTAFK 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 103-274 2.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 2.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  103 MVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQCRDYL-------DDDYK 175
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIkaiidnrSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  176 RQMIDLDACRDQELQT--MLKDVNMWM-SQGEYRDIPHHrtggtamHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLH 252
Cdd:PHA02876   240 NDLSLLKAIRNEDLETslLLYDAGFSVnSIDDCKNTPLH-------HASQAPSLSRLVPKLLERGADVNAKNIKGETPLY 312

                          170       180
                   ....*....|....*....|...
gi 1972253392  253 -AAAHWAERDACKILLENGAELS 274
Cdd:PHA02876   313 lMAKNGYDTENIRTLIMLGADVN 335
PHA03095 PHA03095
ankyrin-like protein; Provisional
 71-162 3.58e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 3.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   71 VEELLNKGANINTCTVDGLTALHQSVIDS--KPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLS 148
Cdd:PHA03095   205 VRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                           90
                   ....*....|....
gi 1972253392  149 IVNSDKELALDLAV 162
Cdd:PHA03095   285 AVSSDGNTPLSLMV 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-275 4.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 4.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   55 DSDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQ-SVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGN 133
Cdd:PHA02876   308 ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQaSTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  134 VAIVRYLCQHGADLSIVNSDKELALDLAVdeqcrdYLDDDYK--RQMIDLDAcrdqelqtmlkDVNmwmSQGEYRDIPHH 211
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFAL------CGTNPYMsvKTLIDRGA-----------NVN---SKNKDLSTPLH 447

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972253392  212 rtggtamHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWaeRDACKILLENGAELSD 275
Cdd:PHA02876   448 -------YACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGAELRD 502
Ank_2 pfam12796
Ankyrin repeats (3 copies);
218-306 5.50e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  218 MHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAelSDLTFTGADVLGVA----DKECID 293
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAarsgHLEIVK 78

                           90
                   ....*....|...
gi 1972253392  294 YLVELADTVKVQN 306
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-273 1.08e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  125 LHAAACCGNVAIVRYLCQHGADLSIVNSDkelaldlavdeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsqge 204
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKN--------------------------------------------------- 29

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972253392  205 yrdiphhrtGGTAMHVAAGRGYTQLLELLIKaGGNVRAQDvEGWTPLHAAAHWAERDACKILLENGAEL 273
Cdd:pfam12796   30 ---------GRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 70-152 3.22e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 3.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   70 EVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSI 149
Cdd:PHA03100   174 RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253


                   ...
gi 1972253392  150 VNS 152
Cdd:PHA03100   254 IIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 65-274 1.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   65 SGDEEEVEELL-NKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQH 143
Cdd:PHA02874    11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  144 GADLSIV------NSDKELALDLAVDEQCRDYLDDDYKRQMI---DLDAcrdqeLQTMLK---DVNMWMSQGEYrdiphh 211
Cdd:PHA02874    91 GVDTSILpipcieKDMIKTILDCGIDVNIKDAELKTFLHYAIkkgDLES-----IKMLFEygaDVNIEDDNGCY------ 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972253392  212 rtggtAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELS 274
Cdd:PHA02874   160 -----PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM 217
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 110-308 1.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  110 KGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQCRD----YLDDDYKRQMIDLDACR 185
Cdd:PHA02874    24 KGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiiklLIDNGVDTSILPIPCIE 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  186 DQELQTMLK---DVNMwmsqgeyRDiphhRTGGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDA 262
Cdd:PHA02874   104 KDMIKTILDcgiDVNI-------KD----AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1972253392  263 CKILLENGAELSDLTFTGADVLGVA----DKECIDYLVELADTVKVQNKR 308
Cdd:PHA02874   173 IKLLLEKGAYANVKDNNGESPLHNAaeygDYACIKLLIDHGNHIMNKCKN 222
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 59-274 2.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 2.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   59 FLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVidSKPEMVRF---LCEKGADVNAQDNEGWTPLHAAACCG-NV 134
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS--QAPSLSRLvpkLLERGADVNAKNIKGETPLYLMAKNGyDT 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  135 AIVRYLCQHGADL--------------SIVNSDKELA---LDLAVDEQCRDYldddYKRQMIDLDACRDQELQtmlkdVN 197
Cdd:PHA02876   322 ENIRTLIMLGADVnaadrlyitplhqaSTLDRNKDIVitlLELGANVNARDY----CDKTPIHYAAVRNNVVI-----IN 392

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972253392  198 MWMSQGEYRDIPHHRTgGTAMHVA-AGRGYTQLLELLIKAGGNVRAQDVEGWTPLH-AAAHWAERDACKILLENGAELS 274
Cdd:PHA02876   393 TLLDYGADIEALSQKI-GTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVN 470
Ank_5 pfam13857
Ankyrin repeats (many copies);
112-161 2.64e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 2.64e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1972253392  112 ADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLA 161
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-271 4.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGA--DVNAQDNEgwTPLHAAACCGNVAIVry 139
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAV-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  140 lcqhgadlsivnsdkELALDLAvdeqcrDYLDDD-YKRQMIDLdacrdqELQTMLKDVNMW---MSQGEYRDIPH-HRTg 214
Cdd:PHA02875    85 ---------------EELLDLG------KFADDVfYKDGMTPL------HLATILKKLDIMkllIARGADPDIPNtDKF- 136

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972253392  215 gTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGA 271
Cdd:PHA02875   137 -SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-162 4.78e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 4.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   67 DEEEVEELLNKGANINTCTVDGLTALHQSVIDSKP-EMVRFLCEKGADVNAQDN-EGWTPLHAAACCGNVaiVRYLCQHG 144
Cdd:PHA02878   213 NKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYG 290

                           90
                   ....*....|....*...
gi 1972253392  145 ADLSIVNSDKELALDLAV 162
Cdd:PHA02878   291 ADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
214-267 9.25e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 9.25e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1972253392  214 GGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILL 267
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-128 1.38e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 1.38e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972253392   74 LLNKG-ANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAA 128
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 120-151 1.43e-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: 48.44  E-value: 1.43e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1972253392  120 EGWTPLHAAAC-CGNVAIVRYLCQHGADLSIVN 151
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 104-184 1.55e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  104 VRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQCRDY--LDDDYKRQMIDL 181
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVvqLLSRHSQCHFEL 177


                   ...
gi 1972253392  182 DAC 184
Cdd:PTZ00322   178 GAN 180
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-235 3.05e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   69 EEVEELLNkganiNTCTVD---GLTALHQSVIDSKPEMVRFLCEKGADVNA-----------QDNE---GWTPLHAAACC 131
Cdd:cd22192     72 EAAPELVN-----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLiyyGEHPLSFAACV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  132 GNVAIVRYLCQHGADLSIVNSDKELALDLAVDEQCRdylddDYKRQMIDLDACRDQELQTMLKDVnmwmsqgeyrdIPHH 211
Cdd:cd22192    147 GNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK-----TFACQMYDLILSYDKEDDLQPLDL-----------VPNN 210

                          170       180
                   ....*....|....*....|....
gi 1972253392  212 RtGGTAMHVAAGRGYTQLLELLIK 235
Cdd:cd22192    211 Q-GLTPFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-194 7.79e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 7.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   67 DEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLH-AAACCGNVAIVRYLCQHGA 145
Cdd:PHA02878   180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGV 259

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1972253392  146 DLSIVNSDKEL-ALDLAVDEQCRDYLDDDYKRQMIDLDACRDQELQTMLK 194
Cdd:PHA02878   260 DVNAKSYILGLtALHSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
56-107 1.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.06e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1972253392   56 SDIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFL 107
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-269 1.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   67 DEEEVEELLNKGANINTCTVDGL-TALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGA 145
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  146 DLSIVNSDKELALDLAVDeQCRDYldddykrqmidldacrdqelqTMLKdvnMWMSQGEYRDIPHHRTGGTAMHVAAGRg 225
Cdd:PHA02878   226 STDARDKCGNTPLHISVG-YCKDY---------------------DILK---LLLEHGVDVNAKSYILGLTALHSSIKS- 279

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1972253392  226 yTQLLELLIKAGGNVRAQDVEGWTPLHAAA-HWAERDACKILLEN 269
Cdd:PHA02878   280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
PHA03095 PHA03095
ankyrin-like protein; Provisional
 67-297 2.03e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   67 DEEEVEELLNKGANINTCTVDGLTALHQ---SVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAaaccgnvaivrYLCqh 143
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHL-----------YLY-- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  144 gadlsivNSDKElaldlavdeqcrdyldddykrqmidldacrdqelqtmlkdvnmwmsqgeyrdiphhrtggtamhvaag 223
Cdd:PHA03095    93 -------NATTL-------------------------------------------------------------------- 97

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  224 rgytQLLELLIKAGGNVRAQDVEGWTPLHA--AAHWAERDACKILLENGAELSDLTFTGADVLGV------ADKECIDYL 295
Cdd:PHA03095    98 ----DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANVELLRLL 173


                   ..
gi 1972253392  296 VE 297
Cdd:PHA03095   174 ID 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 120-149 4.49e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.49e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 1972253392   120 EGWTPLHAAACCGNVAIVRYLCQHGADLSI 149
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 120-149 4.50e-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: 44.17  E-value: 4.50e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1972253392  120 EGWTPLHAAACCGNVAIVRYLCQHGADLSI 149
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 669-701 4.93e-06

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: 44.69  E-value: 4.93e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1972253392  669 ESEAERRNNSRMQRQHRRSTQGVTKEQLEEASK 701
Cdd:cd21945     18 ESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 50
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 88-146 5.41e-06

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: 50.26  E-value: 5.41e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972253392   88 GLTALHQSVIDSKPEMVRFLCEKGADVNAQDNE-------------GWTPLHAAACCGNVAIVRYLCQHGAD 146
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ 144
PHA02798 PHA02798
ankyrin-like protein; Provisional
 71-166 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.06  E-value: 1.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   71 VEELLNKGANINTCTVD---GLTALHQSVID--SKPEMVRFLCEKGADVNAQDNEGWTPLhaaaCC-------GNVAIVR 138
Cdd:PHA02798    54 VKLFINLGANVNGLDNEystPLCTILSNIKDykHMLDIVKILIENGADINKKNSDGETPL----YCllsngyiNNLEILL 129

                           90       100
                   ....*....|....*....|....*...
gi 1972253392  139 YLCQHGADLSIVNSDKELALDLAVDEQC 166
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNH 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 66-168 1.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   66 GDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKpEMVRFLCEKgADVNAQDNEGWTPLHAA---ACcgNVAIVRYLCQ 142
Cdd:PHA02874   201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinpPC--DIDIIDILLY 276

                           90       100
                   ....*....|....*....|....*.
gi 1972253392  143 HGADLSIVNSDKELALDLAVDEQCRD 168
Cdd:PHA02874   277 HKADISIKDNKGENPIDTAFKYINKD 302
Ank_5 pfam13857
Ankyrin repeats (many copies);
204-254 2.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1972253392  204 EYRDIPHHRT---GGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAA 254
Cdd:pfam13857    3 EHGPIDLNRLdgeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 65-143 2.58e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.58e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972253392   65 SGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQH 143
Cdd:PTZ00322    92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 69-155 2.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 2.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   69 EEVEELLNKGANINTCTVD-GLTALHQSVIDSK---PEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAI--VRYLCQ 142
Cdd:PHA02859    67 EILKFLIENGADVNFKTRDnNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRInvIKLLID 146

                           90
                   ....*....|...
gi 1972253392  143 HGAdlSIVNSDKE 155
Cdd:PHA02859   147 SGV--SFLNKDFD 157
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 87-119 3.17e-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: 41.89  E-value: 3.17e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1972253392   87 DGLTALHQSVIDSK-PEMVRFLCEKGADVNAQDN 119
Cdd:pfam00023    1 DGNTPLHLAAGRRGnLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-119 4.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 4.54e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   60 LSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDN 119
Cdd:PHA03100   197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 107-343 4.59e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  107 LCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAVdeqcrdyldddykrqmidldACRD 186
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI--------------------SAKH 603

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  187 QELQTMLKdvnmwmsqgEYRDIPHHRTGGTAMHVAAGRGYTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKIL 266
Cdd:PLN03192   604 HKIFRILY---------HFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  267 LENGAEL----SDLTFTGADVLGVADKECIDYLVELADTVKVQNKRKSPGSGSQP----PTSILQEKNHRMPSHEEHVLt 338
Cdd:PLN03192   675 IMNGADVdkanTDDDFSPTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPgrlqGTSSDNQCRPRVSIYKGHPL- 753


                   ....*
gi 1972253392  339 sERKR 343
Cdd:PLN03192   754 -LRNE 757
PHA02741 PHA02741
hypothetical protein; Provisional
 102-165 5.18e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.03  E-value: 5.18e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972253392  102 EMVRFLCEKGADVNAQDN-EGWTPLHAAACCGNVAIVRYLC-QHGADLSIVNSDKELALDLAVDEQ 165
Cdd:PHA02741    78 EIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNE 143
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-158 5.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVRYLC 141
Cdd:PHA02875   109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                           90
                   ....*....|....*..
gi 1972253392  142 QHGADLSIVNSDKELAL 158
Cdd:PHA02875   189 DSGANIDYFGKNGCVAA 205
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 62-277 1.26e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTALH-----------QSVIDSKP------------------EMVRFLCEKGA 112
Cdd:PHA02876   185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLEcavdsknidtiKAIIDNRSninkndlsllkairnedlETSLLLYDAGF 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  113 DVNAQDNEGWTPLHAAACCGNVA-IVRYLCQHGADLSIVNSDKELALDLavdeQCRDYLDDDYKRQMIDLDAcrdqelqt 191
Cdd:PHA02876   265 SVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL----MAKNGYDTENIRTLIMLGA-------- 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  192 mlkDVNmwmsqgeyrdiPHHRTGGTAMHVAAGRG-YTQLLELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENG 270
Cdd:PHA02876   333 ---DVN-----------AADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398


                   ....*..
gi 1972253392  271 AELSDLT 277
Cdd:PHA02876   399 ADIEALS 405
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 87-116 4.89e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 4.89e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1972253392   87 DGLTALHQSVIDSKPEMVRFLCEKGADVNA 116
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 87-151 4.91e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 4.91e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972253392   87 DGLTALH----QSVIDSKpEMVRFLCEKGADVNAQDN-EGWTPLHAAACCGNVAIVRYLCQH-GADLSIVN 151
Cdd:PHA02736    54 HGKQCVHivsnPDKADPQ-EKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILN 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-162 5.08e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.08e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1972253392  121 GWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELALDLAV 162
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 62-157 7.47e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 7.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   62 ACMSGDEEEVEELLNKGANINTCTVDGLTAL-------HQSVID--------SKP----------------EMVRFLCEK 110
Cdd:PLN03192   565 AASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRilyhfasiSDPhaagdllctaakrndlTAMKELLKQ 644

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1972253392  111 GADVNAQDNEGWTPLHAAACCGNVAIVRYLCQHGADLSIVNSDKELA 157
Cdd:PLN03192   645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFS 691
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 669-701 1.28e-03

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: 37.96  E-value: 1.28e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1972253392  669 ESEAERRNNSRMQRQHRRSTQGVTKEQLEEASK 701
Cdd:cd21944     20 ESESQRKARSRQARQSRRSTQGVTLTDLQEAEK 52
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 57-116 1.35e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.35e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   57 DIFLSACMSGDEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNA 116
Cdd:PLN03192   624 DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 88-231 1.60e-03

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: 42.44  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   88 GLTALHQSVIDSKPEMVRFLCEKGADVNAQ----------DNEGW----TPLHAAACCGNVAIVRYLCQHGADlsIVNSD 153
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEIVQLLMEKEST--DITSQ 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  154 KEL------ALdLAVDEQCRDYldDDYKRQMID--LDACRDQELQTMlkdvnmwmsqgeyrdipHHRTGGTAMHVAAGRG 225
Cdd:cd22194    219 DSRgntvlhAL-VTVAEDSKTQ--NDFVKRMYDmiLLKSENKNLETI-----------------RNNEGLTPLQLAAKMG 278


                   ....*.
gi 1972253392  226 YTQLLE 231
Cdd:cd22194    279 KAEILK 284
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 231-307 1.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 1.66e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972253392  231 ELLIKAGGNVRAQDVEGWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVA-DKECIDYLVELADTVKVQNK 307
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvDSKNIDTIKAIIDNRSNINK 239
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 88-152 1.67e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.49  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   88 GLTALHQSVIDSKPEMVRFLCEKGADVNAQDNE--------------GWTPLHAAACCGNVAIVRYLCQH---GADLSIV 150
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISAR 173


                   ..
gi 1972253392  151 NS 152
Cdd:cd22196    174 DS 175
PHA02946 PHA02946
ankyin-like protein; Provisional
 67-252 2.64e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 2.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392   67 DEEEVEELLNKGANINTCTVDGLTALHQSVIDSKPEMVRFLCEKGADVNAQDNEGWTPLHAAACCGNVAIVR--YLCQHG 144
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERinLLVQYG 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253392  145 ADLSivNSdkelaldlaVDEQ-CRDYLdddykrqmidldACRDQElQTMLKDVnmwMSQG-EYRDIPHHRTGGTAMHVAA 222
Cdd:PHA02946   131 AKIN--NS---------VDEEgCGPLL------------ACTDPS-ERVFKKI---MSIGfEARIVDKFGKNHIHRHLMS 183

                          170       180       190
                   ....*....|....*....|....*....|
gi 1972253392  223 GRGYTQLLELLIKAGGNVRAQDVEGWTPLH 252
Cdd:PHA02946   184 DNPKASTISWMMKLGISPSKPDHDGNTPLH 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 246-273 3.12e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.12e-03
                           10        20
                   ....*....|....*....|....*....
gi 1972253392  246 EGWTPLHAAAHWAER-DACKILLENGAEL 273
Cdd:pfam00023    1 DGNTPLHLAAGRRGNlEIVKLLLSKGADV 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 88-142 4.81e-03

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: 40.93  E-value: 4.81e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972253392   88 GLTALHQSVIDSKPEMVRFLCEKGADVNAQDNE--------------GWTPLHAAACCGNVAIVRYLCQ 142
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
247-296 6.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 6.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1972253392  247 GWTPLHAAAHWAERDACKILLENGAELSDLTFTGADVLGVA----DKECIDYLV 296
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLLL 54
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 669-701 9.32e-03

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: 35.24  E-value: 9.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1972253392  669 ESEAERRNNSRMQRQHRRSTQGVTKEQLEEASK 701
Cdd:cd22527     17 EAEAQRKARSRHARQSRRSTQGVTLTDLKEAEK 49
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 246-274 9.53e-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: 34.54  E-value: 9.53e-03
                           10        20
                   ....*....|....*....|....*....
gi 1972253392  246 EGWTPLHAAAHWAERDACKILLENGAELS 274
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
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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