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Conserved domains on  [gi|219842212|ref|NP_001137357|]
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protein phosphatase 1 regulatory subunit 12A isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 931-1030 4.57e-44

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: 154.77  E-value: 4.57e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   931 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 1008
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 219842212  1009 ADNQRLKDENGALIRVISKLSK 1030
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.90e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 2.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghindvrhaKSGGTAL 203
Cdd:COG0666   171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         250
                  ....*....|....*
gi 219842212  284 QKKQNLLHSEKRDKK 298
Cdd:COG0666   271 LLLALLLLAAALLDL 285
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-714 4.37e-20

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: 84.57  E-value: 4.37e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842212  658 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 714
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 931-1030 4.57e-44

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: 154.77  E-value: 4.57e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   931 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 1008
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 219842212  1009 ADNQRLKDENGALIRVISKLSK 1030
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.90e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 2.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghindvrhaKSGGTAL 203
Cdd:COG0666   171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         250
                  ....*....|....*
gi 219842212  284 QKKQNLLHSEKRDKK 298
Cdd:COG0666   271 LLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 3.11e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghINDVR 194
Cdd:PHA03095  128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMEMVNKVGQ 266
Cdd:PHA03095  182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                  ....*.
gi 219842212  267 TAFDVA 272
Cdd:PHA03095  259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212    47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 219842212   127 GQGAHVGAVN 136
Cdd:pfam12796   82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-714 4.37e-20

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: 84.57  E-value: 4.37e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842212  658 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 714
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-100 5.97e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 5.97e-06
                            10        20
                    ....*....|....*....|....*....
gi 219842212     72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-220 1.03e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  139 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192   169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                  ..
gi 219842212  219 IQ 220
Cdd:cd22192   232 VQ 233
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 867-1030 2.13e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  867 QEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPY-SSRLEKDDSTDFKK---LYEQILAE 942
Cdd:COG4942    68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlqYLKYLAPA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  943 NEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSLLEMEKRERRALERRI-SEMEEELKMLPDLKADNQRLKD 1016
Cdd:COG4942   148 RREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEA 227

                         170
                  ....*....|....
gi 219842212 1017 ENGALIRVISKLSK 1030
Cdd:COG4942   228 LIARLEAEAAAAAE 241
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 931-1030 4.57e-44

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: 154.77  E-value: 4.57e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   931 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 1008
Cdd:pfam15898    1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                           90       100
                   ....*....|....*....|..
gi 219842212  1009 ADNQRLKDENGALIRVISKLSK 1030
Cdd:pfam15898   81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.90e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 2.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghindvrhaKSGGTAL 203
Cdd:COG0666   171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                         250
                  ....*....|....*
gi 219842212  284 QKKQNLLHSEKRDKK 298
Cdd:COG0666   271 LLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-331 2.40e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 2.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  124 FLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIEAARKEEERImlrdARQWLNSG-HINdvRHAKSGGTA 202
Cdd:COG0666   105 LLLEAGADVNARDKDGETPL----------------------HLAAYNGNLEI----VKLLLEAGaDVN--AQDNDGNTP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  203 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEE 282
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 219842212  283 LQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNA 331
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-236 7.00e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.22  E-value: 7.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  119 LDIAEFLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieAARKEEERIMlrdarQWLNSGHINDVRHAKS 198
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDL----------------------AAENGNLEIV-----KLLLEAGADLNAKDKD 251

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 219842212  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 3.11e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 3.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095   53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghINDVR 194
Cdd:PHA03095  128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMEMVNKVGQ 266
Cdd:PHA03095  182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                  ....*.
gi 219842212  267 TAFDVA 272
Cdd:PHA03095  259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212    47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 219842212   127 GQGAHVGAVN 136
Cdd:pfam12796   82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-714 4.37e-20

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: 84.57  E-value: 4.37e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842212  658 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 714
Cdd:cd21944     1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-229 5.17e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212    77 LHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQgahvgavnsegdtpldiaeeeameellq 156
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219842212   157 nevnrqgvdieaarkeeerimlrdarqwlnsghiNDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam12796   53 ----------------------------------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-240 3.30e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.49  E-value: 3.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   55 EVLK-LLHRGADINYANVDGLTALH-----QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC--GYLDIAEFLI 126
Cdd:PHA03100   49 DVVKiLLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  127 GQGAHVGAVNSEGDTPLDIAEEEAMEELL--QNEVNRqGVDIEAARKEEeriMLrdarqwLNSG-HIN--DVRhaksGGT 201
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDK-GVDINAKNRVN---YL------LSYGvPINikDVY----GFT 194

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 219842212  202 ALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAA 240
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 50-236 6.05e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 6.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   50 SGDTDEVLKLLHR-GADINYANVDGLTALHQACIDDNVD--MVKFLVENGANINQPDNEGWIPLHA-----AAScgyLDI 121
Cdd:PHA03095   93 NATTLDVIKLLIKaGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VEL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  122 AEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQN-EVNRQGVDiEAARKEEERIMLRDA-----------RQWLNSGH 189
Cdd:PHA03095  170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCD-PAATDMLGNTPLHSMatgssckrslvLPLLIAGI 248

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 219842212  190 INDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:PHA03095  249 SINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-272 7.42e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 7.42e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   203 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNlCDMEMVNKvGQTAFDVA 272
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 660-713 1.88e-15

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: 71.27  E-value: 1.88e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 219842212  660 TEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 713
Cdd:cd21945     1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-263 3.85e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 3.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   52 DTDEVLKLLHRGADINYANVDGL-TALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGA 130
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  131 HVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerimlrdarqwlnsghindvrHAKS---GGTALHVAA 207
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDV----------------------------NAKSyilGLTALHSSI 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842212  208 AKgyTEVLKLLIQAGYDVNIKDYDGWTPLHAAA-HWGKEEACRILVDNLCDMEMVNK 263
Cdd:PHA02878  278 KS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKRIKP 332
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-145 5.17e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQA--CIDDNVDMVKFLVENGANINQ----------------PDNE 105
Cdd:PHA03100  112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVY 191

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 219842212  106 GWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 8.53e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.61  E-value: 8.53e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 219842212    73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-262 5.69e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   181 ARQWLNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGyDVNIKDYdGWTPLHAAAHWGKEEACRILVDNLCDMEM 260
Cdd:pfam12796   13 VKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89


                   ..
gi 219842212   261 VN 262
Cdd:pfam12796   90 KD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 8.39e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 8.39e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 219842212   199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV 252
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 663-715 6.06e-12

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: 61.60  E-value: 6.06e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 219842212  663 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSR 715
Cdd:cd21946     1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-287 1.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  127 GQGAHVGAVNSEGDTPLdiaeeeameellQNEV--NRQGVDIeaarkeeerimlrdarqWLNSGHINDvrHAKSGGTALH 204
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPL------------HNAIihNRSAIEL-----------------LINNASIND--QDIDGSTPLH 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  205 VAAAKGYT-EVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEAcrILVDNLCDMEMVNKVGQtafdVADEDILGYLEEL 283
Cdd:PHA02874  260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDP--VIKDIIANAVLIKEADK----LKDSDFLEHIEIK 333


                  ....
gi 219842212  284 QKKQ 287
Cdd:PHA02874  334 DNKE 337
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 47-272 2.93e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDnegwIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02876  185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  127 GQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHIN-------DVRHAKS- 198
Cdd:PHA02876  261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRtlimlgaDVNAADRl 340

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219842212  199 GGTALHVAAA-KGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA 272
Cdd:PHA02876  341 YITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-267 5.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 5.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   53 TDEVLKLLHRGADINYANV-DGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY-----LDIAEFLI 126
Cdd:PHA03100   14 KVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  127 GQGAHVGAVNSEGDTPLDIAeeeameellqnevnrqgvdieAARKEEERIMLRDarqwLNSGHINDVRHAKSGGTALHVA 206
Cdd:PHA03100   94 EYGANVNAPDNNGITPLLYA---------------------ISKKSNSYSIVEY----LLDNGANVNIKNSDGENLLHLY 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219842212  207 AAKGY--TEVLKLLIQAGYDVNIKD-------YD---------GWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQT 267
Cdd:PHA03100  149 LESNKidLKILKLLIDKGVDINAKNrvnyllsYGvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 52-272 1.71e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  132 VGAVNSEGDTPLDIAeeeameellqnevnrqgvdIEAARKEEERIMLRdarqwlNSGHINDvrHAKSGGTALHVAAAKGY 211
Cdd:PHA02874  183 ANVKDNNGESPLHNA-------------------AEYGDYACIKLLID------HGNHIMN--KCKNGFTPLHNAIIHNR 235

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219842212  212 TeVLKLLIQaGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMEMVNKVGQTAFDVA 272
Cdd:PHA02874  236 S-AIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 661-710 2.98e-10

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: 56.42  E-value: 2.98e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 219842212  661 EVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKT 710
Cdd:cd22527     1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 663-709 4.06e-10

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: 55.81  E-value: 4.06e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 219842212  663 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEK 709
Cdd:cd21930     1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-145 3.07e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 3.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 219842212    92 LVENG-ANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-279 3.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQA-CIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDI 121
Cdd:PHA02876  311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  122 AEFLIGQGAhvgavnsegdtpldiaeeeameellqnevnrqgvDIEAArkeeerimlrdarqwlnsghindvrhAKSGGT 201
Cdd:PHA02876  391 INTLLDYGA----------------------------------DIEAL--------------------------SQKIGT 410

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  202 ALHVA--AAKGYTEVlKLLIQAGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMEMVNKVGQTAFDVAdediLG 278
Cdd:PHA02876  411 ALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA----LE 485


                  .
gi 219842212  279 Y 279
Cdd:PHA02876  486 Y 486
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 3.38e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 3.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 219842212    59 LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAA 113
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-254 7.57e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 7.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   50 SGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQ 128
Cdd:PHA02874   11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  129 GAHVG----------AVNSEGDTPLDIAEEEAMEELLQNEVNRQGvDIEAARkeeeriMLRDARQWLNSGHINdvrhaks 198
Cdd:PHA02874   91 GVDTSilpipciekdMIKTILDCGIDVNIKDAELKTFLHYAIKKG-DLESIK------MLFEYGADVNIEDDN------- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 219842212  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDN 254
Cdd:PHA02874  157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-268 1.64e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGA--NINQPDNEGwiPLHAAASCGYLDIAEF 124
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  125 LIGQGAHVGAV-NSEGDTPLDIAEEEameellqnevnrQGVDIeaarkeeerimlrdARQWLNSGHINDVRHAKSgGTAL 203
Cdd:PHA02875   87 LLDLGKFADDVfYKDGMTPLHLATIL------------KKLDI--------------MKLLIARGADPDIPNTDK-FSPL 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219842212  204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTA 268
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 54-137 2.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   54 DEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVG 133
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ....
gi 219842212  134 AVNS 137
Cdd:PHA03100  253 TIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-93 3.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 219842212    43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLV 93
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-141 8.84e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 8.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   45 LAAcsSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEF 124
Cdd:PTZ00322   89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|....*....
gi 219842212  125 LIG--QGAHVGAVNSEGDT 141
Cdd:PTZ00322  167 LSRhsQCHFELGANAKPDS 185
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 1.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 219842212   185 LNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 239
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 52-236 2.03e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.30  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAAASCG------------ 117
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  118 --YLDIAEFLIGQGAHVGAVNSEGDTPL-------------DIAEEEAMEELLQNEVNRQGVDIEAARKEEERIM----- 177
Cdd:PHA02716  376 diRLDVIQCLISLGADITAVNCLGYTPLtsyictaqnymyyDIIDCLISDKVLNMVKHRILQDLLIRVDDTPCIIhhiia 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  178 --------LRDARQWLNSGHINDVRHAK------------SGGTALHVAA-----AKGYTEVLKLLIQAGYDVNIKDYDG 232
Cdd:PHA02716  456 kyniptdlYTDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKNG 535


                  ....
gi 219842212  233 WTPL 236
Cdd:PHA02716  536 VTPL 539
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-279 2.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   54 DEVLKLLHRGADINYANVDGLTALHQACI--------------------------------------------------- 82
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltnrykniqt 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   83 -----------DDNVD--MVKFLVENGANINQPD-NEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDiaee 148
Cdd:PHA02878  131 idlvyidkkskDDIIEaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH---- 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  149 eameellqnevnrqgvdiEAARKEEERIMlrdaRQWLNSGHINDVRHaKSGGTALHVAAA--KGYtEVLKLLIQAGYDVN 226
Cdd:PHA02878  207 ------------------HAVKHYNKPIV----HILLENGASTDARD-KCGNTPLHISVGycKDY-DILKLLLEHGVDVN 262

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 219842212  227 IKDY-DGWTPLHAAAHwgKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878  263 AKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-280 2.89e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.42  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  157 NEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 219842212  237 HAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 280
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLL 139
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-104 3.84e-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: 47.28  E-value: 3.84e-07
                           10        20        30
                   ....*....|....*....|....*....|....
gi 219842212    72 DGLTALHQACID-DNVDMVKFLVENGANINQPDN 104
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-293 5.55e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  207 AAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKK 286
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                  ....*..
gi 219842212  287 QNLLHSE 293
Cdd:PTZ00322  170 HSQCHFE 176
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-279 1.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   67 NYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC-GYLDIAEFL--------------IGQGAH 131
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIrsinkcsvfytlvaIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  132 VGAVNSEGDTPLDIAEeeameellqnevNRQGVDIEAARK--EEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAK 209
Cdd:PHA02878  111 NRNVEIFKIILTNRYK------------NIQTIDLVYIDKksKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATEN 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  210 GYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878  179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-100 1.66e-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: 45.33  E-value: 1.66e-06
                           10        20
                   ....*....|....*....|....*....
gi 219842212    72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
232-280 2.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.62e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 219842212   232 GWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 280
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-143 3.13e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   36 VKFDDGAVFLAACSSGDTDEVLK-LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAA 114
Cdd:PHA02875   97 VFYKDGMTPLHLATILKKLDIMKlLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                          90       100
                  ....*....|....*....|....*....
gi 219842212  115 SCGYLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02875  177 AKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-145 3.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.05  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   55 EVLKLL-HRGADINYANVDGLTALHQAC--IDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL------DIAEFL 125
Cdd:PHA02859  104 EILKILiDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                          90       100
                  ....*....|....*....|
gi 219842212  126 IGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA02859  179 TSLGIDINETNKSGYNCYDL 198
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-288 4.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   56 VLKLLHRGADINY----ANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02876  124 ILKEAISGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  132 VGAVNSEGDTPLDIAEEEAMEELLQNEV-NRQGVD------IEAARKE--EERIMLRDARQWLNSghINDVRHaksggTA 202
Cdd:PHA02876  204 VNIIALDDLSVLECAVDSKNIDTIKAIIdNRSNINkndlslLKAIRNEdlETSLLLYDAGFSVNS--IDDCKN-----TP 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  203 LHVAA-AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKE-EACRILVDNLCDMEMVNKVGQTAFDVA-----DED 275
Cdd:PHA02876  277 LHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAstldrNKD 356

                         250
                  ....*....|...
gi 219842212  276 ILGYLEELQKKQN 288
Cdd:PHA02876  357 IVITLLELGANVN 369
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-100 5.97e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.73  E-value: 5.97e-06
                            10        20
                    ....*....|....*....|....*....
gi 219842212     72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 6.04e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 6.04e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 219842212   199 GGTALHVAAAK-GYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-280 9.49e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   86 VDMVKFLVENGANINQPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrq 162
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPL------------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  163 gvdieaarkeeerimlrdarqwlnsghindvrhaksggtalHVAAAKGYTE-VLKLLIQAGYDVNIKDYDGWTPLHA--A 239
Cdd:PHA03095   88 -----------------------------------------HLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylS 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 219842212  240 AHWGKEEACRILVDNLCDMEMVNKVGQTAFDV------ADEDILGYL 280
Cdd:PHA03095  127 GFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANVELLRLL 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-220 1.03e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  139 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192   169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                  ..
gi 219842212  219 IQ 220
Cdd:cd22192   232 VQ 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-272 1.70e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 219842212   218 LIQAGY-DVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA 272
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 103-309 1.91e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  103 DNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqGVDIEAARKEEERIMLRDAR 182
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-------------------WNAISAKHHKIFRILYHFAS 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  183 qwLNSGHIndvrhaksGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVN 262
Cdd:PLN03192  616 --ISDPHA--------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 219842212  263 kvgqtafdvADEDILGY-LEELQKKQNLLHSEKRDKKSPLIESTANMD 309
Cdd:PLN03192  686 ---------TDDDFSPTeLRELLQKRELGHSITIVDSVPADEPDLGRD 724
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 41-99 2.44e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 219842212   41 GAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANI 99
Cdd:PLN03192  623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02798 PHA02798
ankyrin-like protein; Provisional
 36-267 5.45e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   36 VKFDDGAVFLAACssgDTDEVL-------KLLHRGA---DI------NYANVDGLTA--------LHQACIDDN--VDMV 89
Cdd:PHA02798   16 VKLSTVKLLIKSC---NPNEIVneysifqKYLQRDSpstDIvklfinLGANVNGLDNeystplctILSNIKDYKhmLDIV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   90 KFLVENGANINQPDNEGWIPLHAAASCGYLDIAE---FLIGQGAHVGAVNSEGDTPLDIaeEEAMEELLQNEVNR----Q 162
Cdd:PHA02798   93 KILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLDKDGFTMLQV--YLQSNHHIDIEIIKllleK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  163 GVDIEAARKEE-------------ERIMLRDARQWLNSGHI---NDVRHAKSGGTALH--VAAAKGYTEVLKLLIQAGYD 224
Cdd:PHA02798  171 GVDINTHNNKEkydtlhcyfkyniDRIDADILKLFVDNGFIinkENKSHKKKFMEYLNslLYDNKRFKKNILDFIFSYID 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 219842212  225 VNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQT 267
Cdd:PHA02798  251 INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNT 293
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 186-275 6.54e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  186 NSGHINDVRHAK--------SGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV----- 252
Cdd:PLN03192  537 NAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYhfasi 616

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 219842212  253 -------DNLC------DMEMVNKVGQTAFDVADED 275
Cdd:PLN03192  617 sdphaagDLLCtaakrnDLTAMKELLKQGLNVDSED 652
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-132 8.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 8.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   42 AVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDD-NVDMVKFLVENGANINQPDNEGWIPLHAAasCGYLD 120
Cdd:PHA02876  411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                          90
                  ....*....|..
gi 219842212  121 IAEFLIGQGAHV 132
Cdd:PHA02876  489 IVNILLHYGAEL 500
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-227 1.18e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.18e-04
                            10        20
                    ....*....|....*....|....*..
gi 219842212    201 TALHVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 66-143 3.57e-04

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: 44.41  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   66 INYANVD----GLTALHQACIDDNVDMVKFLVENGANINQPDNE--------------GWIPLHAAASCGYLDIAEFLIG 127
Cdd:cd22196    83 VNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                          90
                  ....*....|....*....
gi 219842212  128 ---QGAHVGAVNSEGDTPL 143
Cdd:cd22196   163 nphSPADISARDSMGNTVL 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-136 4.41e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.41e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 219842212   105 EGWIPLHAAA-SCGYLDIAEFLIGQGAHVGAVN 136
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 80-143 5.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 5.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219842212   80 ACIDD---NVDMVKFLVENGANIN-QPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02859   57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 89-145 5.13e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 5.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842212   89 VKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-145 6.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 219842212   109 PLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-263 7.00e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 7.00e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 219842212   231 DGWTPLHAAA-HWGKEEACRILVDNLCDMEMVNK 263
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-129 9.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   55 EVLKLL-HRGADINYANVD-GLTALHQ-ACIDDNV--DMVKFLVENGANINQPDNEGWIPLHA-AASCGY-LDIAEFLIG 127
Cdd:PHA02859   67 EILKFLiENGADVNFKTRDnNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMyMCNFNVrINVIKLLID 146


                  ..
gi 219842212  128 QG 129
Cdd:PHA02859  147 SG 148
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-227 1.14e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.14e-03
                           10        20
                   ....*....|....*....|....*....
gi 219842212   199 GGTALHVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 73-220 1.41e-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: 42.48  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   73 GLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIG---QGAHVGAV 135
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  136 NSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerIMLRDARqWLNSGHINDVRHAKsGGTALHVAAAKGYTEVL 215
Cdd:cd22193   156 DSRGNTVLHALVTVADNTKENTKFVTRMYDM---------ILIRGAK-LCPTVELEEIRNND-GLTPLQLAAKMGKIEIL 224


                  ....*
gi 219842212  216 KLLIQ 220
Cdd:cd22193   225 KYILQ 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 206-268 1.55e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219842212  206 AAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTA 268
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-132 1.81e-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: 42.31  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   43 VFLAAcSSGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGAN-INQPDN----EGWIPLHAAASC 116
Cdd:cd22192    21 LLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99

                          90
                  ....*....|....*.
gi 219842212  117 GYLDIAEFLIGQGAHV 132
Cdd:cd22192   100 QNLNLVRELIARGADV 115
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 73-145 2.00e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNE-------------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV---N 136
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaqD 152


                  ....*....
gi 219842212  137 SEGDTPLDI 145
Cdd:cd21882   153 SLGNTVLHA 161
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 867-1030 2.13e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  867 QEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPY-SSRLEKDDSTDFKK---LYEQILAE 942
Cdd:COG4942    68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlqYLKYLAPA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842212  943 NEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSLLEMEKRERRALERRI-SEMEEELKMLPDLKADNQRLKD 1016
Cdd:COG4942   148 RREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEA 227

                         170
                  ....*....|....
gi 219842212 1017 ENGALIRVISKLSK 1030
Cdd:COG4942   228 LIARLEAEAAAAAE 241
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 181-251 5.97e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219842212  181 ARQWLNSGHINDVRHAkSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL 251
Cdd:PTZ00322   98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 937-1004 6.94e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 38.37  E-value: 6.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219842212   937 EQILAENEKLKAQLHDTNMELTDLKLQLEKATQrQERFADRSLLEME---KRERRALERRISEMEEELKML 1004
Cdd:pfam09744   39 ESLASRNQEHNVELEELREDNEQLETQYEREKA-LRKRAEEELEEIEdqwEQETKDLLSQVESLEEENRRL 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 231-260 8.22e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 8.22e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 219842212    231 DGWTPLHAAAHWGKEEACRILVDNLCDMEM 260
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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