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Conserved domains on  [gi|350529366|ref|NP_001231919|]
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protein phosphatase 1 regulatory subunit 12A isoform c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.90e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 2.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghindvrhaKSGGTAL 203
Cdd:COG0666  171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        250
                 ....*....|....*
gi 350529366 284 QKKQNLLHSEKRDKK 298
Cdd:COG0666  271 LLLALLLLAAALLDL 285
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 922-995 2.76e-28

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: 109.32  E-value: 2.76e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350529366  922 SRLEKDdstdFKKRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK 995
Cdd:pfam15898  32 SQLERL----TQQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLRAENQRLKDENGALIRVISKLSK 102
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-714 7.50e-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: 83.80  E-value: 7.50e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 350529366 658 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 714
Cdd:cd21944    1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.90e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 2.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghindvrhaKSGGTAL 203
Cdd:COG0666  171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        250
                 ....*....|....*
gi 350529366 284 QKKQNLLHSEKRDKK 298
Cdd:COG0666  271 LLLALLLLAAALLDL 285
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 922-995 2.76e-28

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: 109.32  E-value: 2.76e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350529366  922 SRLEKDdstdFKKRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK 995
Cdd:pfam15898  32 SQLERL----TQQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLRAENQRLKDENGALIRVISKLSK 102
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 2.98e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghINDVR 194
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMEMVNKVGQ 266
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                 ....*.
gi 350529366 267 TAFDVA 272
Cdd:PHA03095 259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 350529366  127 GQGAHVGAVN 136
Cdd:pfam12796  82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-714 7.50e-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: 83.80  E-value: 7.50e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 350529366 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 5.77e-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: 5.77e-06
                           10        20
                   ....*....|....*....|....*....
gi 350529366    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: 49.24  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 139 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192  169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                 ..
gi 350529366 219 IQ 220
Cdd:cd22192  232 VQ 233
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.90e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 2.90e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghindvrhaKSGGTAL 203
Cdd:COG0666  171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        250
                 ....*....|....*
gi 350529366 284 QKKQNLLHSEKRDKK 298
Cdd:COG0666  271 LLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-331 3.01e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 3.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 124 FLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIEAARKEEERImlrdARQWLNSG-HINdvRHAKSGGTA 202
Cdd:COG0666  105 LLLEAGADVNARDKDGETPL----------------------HLAAYNGNLEI----VKLLLEAGaDVN--AQDNDGNTP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 203 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEE 282
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 350529366 283 LQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIEPEKNA 331
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-236 1.26e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 119 LDIAEFLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieAARKEEERIMlrdarQWLNSGHINDVRHAKS 198
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDL----------------------AAENGNLEIV-----KLLLEAGADLNAKDKD 251

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 350529366 199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:COG0666  252 GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 922-995 2.76e-28

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: 109.32  E-value: 2.76e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350529366  922 SRLEKDdstdFKKRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVISKLSK 995
Cdd:pfam15898  32 SQLERL----TQQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLRAENQRLKDENGALIRVISKLSK 102
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 2.98e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 2.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghINDVR 194
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMEMVNKVGQ 266
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                 ....*.
gi 350529366 267 TAFDVA 272
Cdd:PHA03095 259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.07e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 350529366  127 GQGAHVGAVN 136
Cdd:pfam12796  82 EKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 658-714 7.50e-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: 83.80  E-value: 7.50e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 350529366 658 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 714
Cdd:cd21944    1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-229 4.99e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366   77 LHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQgahvgavnsegdtpldiaeeeameellq 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350529366  157 nevnrqgvdieaarkeeerimlrdarqwlnsghiNDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam12796  53 ----------------------------------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-240 2.16e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.87  E-value: 2.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  55 EVLK-LLHRGADINYANVDGLTALH-----QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC--GYLDIAEFLI 126
Cdd:PHA03100  49 DVVKiLLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 127 GQGAHVGAVNSEGDTPLDIAEEEAMEELL--QNEVNRqGVDIEAARKEEeriMLrdarqwLNSG-HIN--DVRhaksGGT 201
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDK-GVDINAKNRVN---YL------LSYGvPINikDVY----GFT 194

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 350529366 202 ALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAA 240
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 50-236 5.76e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 5.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  50 SGDTDEVLKLLHR-GADINYANVDGLTALHQACIDDNVD--MVKFLVENGANINQPDNEGWIPLHA-----AAScgyLDI 121
Cdd:PHA03095  93 NATTLDVIKLLIKaGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VEL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 122 AEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQN-EVNRQGVDiEAARKEEERIMLRDA-----------RQWLNSGH 189
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCD-PAATDMLGNTPLHSMatgssckrslvLPLLIAGI 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 350529366 190 INDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:PHA03095 249 SINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-272 7.16e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 7.16e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  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 2.26e-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: 2.26e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 350529366 660 TEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 713
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-263 2.45e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.92  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  52 DTDEVLKLLHRGADINYANVDGL-TALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGA 130
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 131 HVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerimlrdarqwlnsghindvrHAKS---GGTALHVAA 207
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDV----------------------------NAKSyilGLTALHSSI 277

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 350529366 208 AKgyTEVLKLLIQAGYDVNIKDYDGWTPLHAAA-HWGKEEACRILVDNLCDMEMVNK 263
Cdd:PHA02878 278 KS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKRIKP 332
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-145 3.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQA--CIDDNVDMVKFLVENGANINQ----------------PDNE 105
Cdd:PHA03100 112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVY 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 350529366 106 GWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 8.24e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.61  E-value: 8.24e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 350529366   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-262 5.49e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  181 ARQWLNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGyDVNIKDYdGWTPLHAAAHWGKEEACRILVDNLCDMEM 260
Cdd:pfam12796  13 VKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89


                  ..
gi 350529366  261 VN 262
Cdd:pfam12796  90 KD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 8.10e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 8.10e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 350529366  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV 252
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 663-715 5.74e-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: 5.74e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 350529366 663 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSR 715
Cdd:cd21946    1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-287 1.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 127 GQGAHVGAVNSEGDTPLdiaeeeameellQNEV--NRQGVDIeaarkeeerimlrdarqWLNSGHINDvrHAKSGGTALH 204
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPL------------HNAIihNRSAIEL-----------------LINNASIND--QDIDGSTPLH 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 205 VAAAKGYT-EVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEAcrILVDNLCDMEMVNKVGQtafdVADEDILGYLEEL 283
Cdd:PHA02874 260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDP--VIKDIIANAVLIKEADK----LKDSDFLEHIEIK 333


                 ....
gi 350529366 284 QKKQ 287
Cdd:PHA02874 334 DNKE 337
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 47-272 2.31e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDnegwIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 127 GQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHIN-------DVRHAKS- 198
Cdd:PHA02876 261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRtlimlgaDVNAADRl 340

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350529366 199 GGTALHVAAA-KGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA 272
Cdd:PHA02876 341 YITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-267 3.33e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 3.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  53 TDEVLKLLHRGADINYANV-DGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY-----LDIAEFLI 126
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 127 GQGAHVGAVNSEGDTPLDIAeeeameellqnevnrqgvdieAARKEEERIMLRDarqwLNSGHINDVRHAKSGGTALHVA 206
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYA---------------------ISKKSNSYSIVEY----LLDNGANVNIKNSDGENLLHLY 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 350529366 207 AAKGY--TEVLKLLIQAGYDVNIKD-------YD---------GWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQT 267
Cdd:PHA03100 149 LESNKidLKILKLLIDKGVDINAKNrvnyllsYGvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 52-272 1.32e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 132 VGAVNSEGDTPLDIAeeeameellqnevnrqgvdIEAARKEEERIMLRdarqwlNSGHINDvrHAKSGGTALHVAAAKGY 211
Cdd:PHA02874 183 ANVKDNNGESPLHNA-------------------AEYGDYACIKLLID------HGNHIMN--KCKNGFTPLHNAIIHNR 235

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 350529366 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 2.71e-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: 2.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 350529366 661 EVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKT 710
Cdd:cd22527    1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 663-709 4.73e-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: 4.73e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 350529366 663 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEK 709
Cdd:cd21930    1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-279 2.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQAC-IDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDI 121
Cdd:PHA02876 311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 122 AEFLIGQGAhvgavnsegdtpldiaeeeameellqnevnrqgvDIEAArkeeerimlrdarqwlnsghindvrhAKSGGT 201
Cdd:PHA02876 391 INTLLDYGA----------------------------------DIEAL--------------------------SQKIGT 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 202 ALHVA--AAKGYTEVlKLLIQAGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMEMVNKVGQTAFDVAdediLG 278
Cdd:PHA02876 411 ALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA----LE 485


                 .
gi 350529366 279 Y 279
Cdd:PHA02876 486 Y 486
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-145 2.96e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.96e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 350529366   92 LVENG-ANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 3.27e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 3.27e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 350529366   59 LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAA 113
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-254 6.30e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 6.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  50 SGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQ 128
Cdd:PHA02874  11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 129 GAHVG----------AVNSEGDTPLDIAEEEAMEELLQNEVNRQGvDIEAARkeeeriMLRDARQWLNSGHINdvrhaks 198
Cdd:PHA02874  91 GVDTSilpipciekdMIKTILDCGIDVNIKDAELKTFLHYAIKKG-DLESIK------MLFEYGADVNIEDDN------- 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 350529366 199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDN 254
Cdd:PHA02874 157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-268 1.24e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGA--NINQPDNEGwiPLHAAASCGYLDIAEF 124
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 125 LIGQGAHVGAV-NSEGDTPLDIAEEEameellqnevnrQGVDIeaarkeeerimlrdARQWLNSGHINDVRHAKSgGTAL 203
Cdd:PHA02875  87 LLDLGKFADDVfYKDGMTPLHLATIL------------KKLDI--------------MKLLIARGADPDIPNTDK-FSPL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 350529366 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTA 268
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA 204
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 54-137 1.68e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  54 DEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVG 133
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....
gi 350529366 134 AVNS 137
Cdd:PHA03100 253 TIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-93 2.95e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 350529366   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLV 93
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-141 8.46e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 8.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  45 LAAcsSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEF 124
Cdd:PTZ00322  89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                         90
                 ....*....|....*....
gi 350529366 125 LIG--QGAHVGAVNSEGDT 141
Cdd:PTZ00322 167 LSRhsQCHFELGANAKPDS 185
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-279 1.33e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  54 DEVLKLLHRGADINYANVDGLTALHQACI--------------------------------------------------- 82
Cdd:PHA02878  51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltnrykniqt 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  83 -----------DDNVD--MVKFLVENGANINQPD-NEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDiaee 148
Cdd:PHA02878 131 idlvyidkkskDDIIEaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH---- 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 149 eameellqnevnrqgvdiEAARKEEERIMlrdaRQWLNSGHINDVRHaKSGGTALHVAAA--KGYtEVLKLLIQAGYDVN 226
Cdd:PHA02878 207 ------------------HAVKHYNKPIV----HILLENGASTDARD-KCGNTPLHISVGycKDY-DILKLLLEHGVDVN 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 350529366 227 IKDY-DGWTPLHAAAHwgKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878 263 AKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-280 1.55e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 157 NEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 350529366 237 HAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 280
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLL 139
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 52-236 1.86e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.30  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAAASCG------------ 117
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 118 --YLDIAEFLIGQGAHVGAVNSEGDTPL-------------DIAEEEAMEELLQNEVNRQGVDIEAARKEEERIM----- 177
Cdd:PHA02716 376 diRLDVIQCLISLGADITAVNCLGYTPLtsyictaqnymyyDIIDCLISDKVLNMVKHRILQDLLIRVDDTPCIIhhiia 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 178 --------LRDARQWLNSGHINDVRHAK------------SGGTALHVAA-----AKGYTEVLKLLIQAGYDVNIKDYDG 232
Cdd:PHA02716 456 kyniptdlYTDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKNG 535


                 ....
gi 350529366 233 WTPL 236
Cdd:PHA02716 536 VTPL 539
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 1.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 350529366  185 LNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 239
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-104 3.71e-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: 3.71e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 350529366   72 DGLTALHQACID-DNVDMVKFLVENGANINQPDN 104
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-293 5.31e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 207 AAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKK 286
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*..
gi 350529366 287 QNLLHSE 293
Cdd:PTZ00322 170 HSQCHFE 176
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-279 8.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 8.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  67 NYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC-GYLDIAEFL--------------IGQGAH 131
Cdd:PHA02878  31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIrsinkcsvfytlvaIKDAFN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 132 VGAVNSEGDTPLDIAEeeameellqnevNRQGVDIEAARK--EEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAK 209
Cdd:PHA02878 111 NRNVEIFKIILTNRYK------------NIQTIDLVYIDKksKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATEN 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 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 1.60e-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: 1.60e-06
                          10        20
                  ....*....|....*....|....*....
gi 350529366   72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
232-280 2.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 350529366  232 GWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 280
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-143 2.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  36 VKFDDGAVFLAACSSGDTDEVLK-LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAA 114
Cdd:PHA02875  97 VFYKDGMTPLHLATILKKLDIMKlLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                         90       100
                 ....*....|....*....|....*....
gi 350529366 115 SCGYLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-145 2.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.05  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  55 EVLKLL-HRGADINYANVDGLTALHQAC--IDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL------DIAEFL 125
Cdd:PHA02859 104 EILKILiDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                         90       100
                 ....*....|....*....|
gi 350529366 126 IGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDL 198
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-288 3.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 3.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  56 VLKLLHRGADINY----ANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02876 124 ILKEAISGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 132 VGAVNSEGDTPLDIAEEEAMEELLQNEV-NRQGVD------IEAARKE--EERIMLRDARQWLNSghINDVRHaksggTA 202
Cdd:PHA02876 204 VNIIALDDLSVLECAVDSKNIDTIKAIIdNRSNINkndlslLKAIRNEdlETSLLLYDAGFSVNS--IDDCKN-----TP 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 203 LHVAA-AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKE-EACRILVDNLCDMEMVNKVGQTAFDVA-----DED 275
Cdd:PHA02876 277 LHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAstldrNKD 356

                        250
                 ....*....|...
gi 350529366 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 5.77e-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: 5.77e-06
                           10        20
                   ....*....|....*....|....*....
gi 350529366    72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 5.83e-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: 5.83e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 350529366  199 GGTALHVAAAK-GYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-280 9.10e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 9.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  86 VDMVKFLVENGANINQPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrq 162
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPL------------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 163 gvdieaarkeeerimlrdarqwlnsghindvrhaksggtalHVAAAKGYTE-VLKLLIQAGYDVNIKDYDGWTPLHA--A 239
Cdd:PHA03095  88 -----------------------------------------HLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylS 126

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 350529366 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: 49.24  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 139 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192  169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                 ..
gi 350529366 219 IQ 220
Cdd:cd22192  232 VQ 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-272 1.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 350529366  218 LIQAGY-DVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA 272
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 103-309 1.80e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 103 DNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqGVDIEAARKEEERIMLRDAR 182
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-------------------WNAISAKHHKIFRILYHFAS 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 183 qwLNSGHIndvrhaksGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVN 262
Cdd:PLN03192 616 --ISDPHA--------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 350529366 263 kvgqtafdvADEDILGY-LEELQKKQNLLHSEKRDKKSPLIESTANMD 309
Cdd:PLN03192 686 ---------TDDDFSPTeLRELLQKRELGHSITIVDSVPADEPDLGRD 724
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 41-99 2.32e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 350529366  41 GAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANI 99
Cdd:PLN03192 623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02798 PHA02798
ankyrin-like protein; Provisional
 53-267 4.72e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 4.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  53 TDEVLKLLHRGADINYANVDGLTALhqaC------IDDN--VDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE- 123
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 124 --FLIGQGAHVGAVNSEGDTPLDIaeEEAMEELLQNEVNR----QGVDIEAARKEE-------------ERIMLRDARQW 184
Cdd:PHA02798 128 llFMIENGADTTLLDKDGFTMLQV--YLQSNHHIDIEIIKllleKGVDINTHNNKEkydtlhcyfkyniDRIDADILKLF 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 185 LNSGHI---NDVRHAKSGGTALH--VAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDME 259
Cdd:PHA02798 206 VDNGFIinkENKSHKKKFMEYLNslLYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN 285


                 ....*...
gi 350529366 260 MVNKVGQT 267
Cdd:PHA02798 286 IITELGNT 293
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 186-275 6.11e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 186 NSGHINDVRHAK--------SGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV----- 252
Cdd:PLN03192 537 NAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYhfasi 616

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 350529366 253 -------DNLC------DMEMVNKVGQTAFDVADED 275
Cdd:PLN03192 617 sdphaagDLLCtaakrnDLTAMKELLKQGLNVDSED 652
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-132 7.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  42 AVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDD-NVDMVKFLVENGANINQPDNEGWIPLHAAasCGYLD 120
Cdd:PHA02876 411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                         90
                 ....*....|..
gi 350529366 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 1.14e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.14e-04
                           10        20
                   ....*....|....*....|....*..
gi 350529366   201 TALHVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 66-143 3.43e-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: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  66 INYANVD----GLTALHQACIDDNVDMVKFLVENGANINQPDNE--------------GWIPLHAAASCGYLDIAEFLIG 127
Cdd:cd22196   83 VNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                         90
                 ....*....|....*....
gi 350529366 128 ---QGAHVGAVNSEGDTPL 143
Cdd:cd22196  163 nphSPADISARDSMGNTVL 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-136 4.26e-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: 4.26e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 350529366  105 EGWIPLHAAA-SCGYLDIAEFLIGQGAHVGAVN 136
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 80-143 4.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 4.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350529366  80 ACIDD---NVDMVKFLVENGANIN-QPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02859  57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 89-145 4.92e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 350529366  89 VKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-145 5.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 350529366  109 PLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-263 6.76e-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: 6.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 350529366  231 DGWTPLHAAA-HWGKEEACRILVDNLCDMEMVNK 263
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-129 7.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  55 EVLKLL-HRGADINYANVD-GLTALHQ-ACIDDNV--DMVKFLVENGANINQPDNEGWIPLHA-AASCGY-LDIAEFLIG 127
Cdd:PHA02859  67 EILKFLiENGADVNFKTRDnNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMyMCNFNVrINVIKLLID 146


                 ..
gi 350529366 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 1.10e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 350529366  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 1.40e-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: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  73 GLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIG---QGAHVGAV 135
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 136 NSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerIMLRDARqWLNSGHINDVRHAKsGGTALHVAAAKGYTEVL 215
Cdd:cd22193  156 DSRGNTVLHALVTVADNTKENTKFVTRMYDM---------ILIRGAK-LCPTVELEEIRNND-GLTPLQLAAKMGKIEIL 224


                 ....*
gi 350529366 216 KLLIQ 220
Cdd:cd22193  225 KYILQ 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 206-268 1.46e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 350529366 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 1.73e-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: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  43 VFLAAcSSGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGAN-INQPDN----EGWIPLHAAASC 116
Cdd:cd22192   21 LLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99

                         90
                 ....*....|....*.
gi 350529366 117 GYLDIAEFLIGQGAHV 132
Cdd:cd22192  100 QNLNLVRELIARGADV 115
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 73-145 1.92e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  73 GLTALHQACIDDNVDMVKFLVENGANINQPDNE-------------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV---N 136
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaqD 152


                 ....*....
gi 350529366 137 SEGDTPLDI 145
Cdd:cd21882  153 SLGNTVLHA 161
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 181-251 5.74e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 350529366 181 ARQWLNSGHINDVRHAkSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL 251
Cdd:PTZ00322  98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 231-260 7.94e-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: 7.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 350529366   231 DGWTPLHAAAHWGKEEACRILVDNLCDMEM 260
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 43-276 9.42e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 9.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366  43 VFLAACSSGDTDE--VLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCG--Y 118
Cdd:PHA02946  40 ILHAYCGIKGLDErfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 119 LDIAEFLIGQGAHV-GAVNSEGDTPLDIAEEEAMEELLQnevnRQGVDIEA------ARKEEERIMLRDARQ-----WLN 186
Cdd:PHA02946 120 IERINLLVQYGAKInNSVDEEGCGPLLACTDPSERVFKK----IMSIGFEArivdkfGKNHIHRHLMSDNPKastisWMM 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 350529366 187 SGHINDVRHAKSGGTALHVAAAKGY--TEVLKLLIQAGyDVNIKDYDGWTPLhaaahwgkeeacRILVDNLCDMEMVNKV 264
Cdd:PHA02946 196 KLGISPSKPDHDGNTPLHIVCSKTVknVDIINLLLPST-DVNKQNKFGDSPL------------TLLIKTLSPAHLINKL 262

                        250
                 ....*....|..
gi 350529366 265 GQTAFDVADEDI 276
Cdd:PHA02946 263 LSTSNVITDQTV 274
 
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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