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Conserved domains on  [gi|564359176|ref|XP_006241377|]
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protein phosphatase 1 regulatory subunit 12A isoform X8 [Rattus norvegicus]

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 ...
 873-972 2.09e-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: 155.54  E-value: 2.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  873 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 950
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 564359176  951 ADNQRLKDENGALIRVISKLSK 972
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.12e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 2.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaKSGGTAL 203
Cdd:COG0666  171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        250
                 ....*....|....*
gi 564359176 284 QKKQNLLHSEKRDKK 298
Cdd:COG0666  271 LLLALLLLAAALLDL 285
IPD_PPP1R12 super family cl40436
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 608-654 1.91e-13

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.


The actual alignment was detected with superfamily member cd21945:

Pssm-ID: 424067  Cd Length: 54  Bit Score: 65.49  E-value: 1.91e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564359176 608 RSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 654
Cdd:cd21945    8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 873-972 2.09e-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: 155.54  E-value: 2.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  873 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 950
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 564359176  951 ADNQRLKDENGALIRVISKLSK 972
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.12e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 2.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaKSGGTAL 203
Cdd:COG0666  171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        250
                 ....*....|....*
gi 564359176 284 QKKQNLLHSEKRDKK 298
Cdd:COG0666  271 LLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 1.65e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghISDVR 194
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMETVNKVGQ 266
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                 ....*.
gi 564359176 267 TAFDVA 272
Cdd:PHA03095 259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 3.97e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 3.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 564359176  127 GQGAHVGAVN 136
Cdd:pfam12796  82 EKGADINVKD 91
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 608-654 1.91e-13

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: 65.49  E-value: 1.91e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564359176 608 RSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 654
Cdd:cd21945    8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-220 5.34e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 139 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHISDVRHaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192  169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                 ..
gi 564359176 219 IQ 220
Cdd:cd22192  232 VQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-100 5.64e-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: 5.64e-06
                           10        20
                   ....*....|....*....|....*....
gi 564359176    72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 876-972 3.20e-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: 40.90  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 876 KLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSLLEMEKRERRALERRI-SEMEEELKMLPDL 949
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAEL 218

                         90       100
                 ....*....|....*....|...
gi 564359176 950 KADNQRLKDENGALIRVISKLSK 972
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAE 241
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 886-960 8.85e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.93  E-value: 8.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564359176  886 EKLKAQLHDTNMELTDLKLQLEKatQRQERFADRSLLEMEKRERRALERRISEMEEELKmlpDLKADNQRLKDEN 960
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLEL--QAREKAQSQALAEAQQQELVALEGLAAELEEKQQ---ELEAQLEQLQEKA 207
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 873-972 2.09e-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: 155.54  E-value: 2.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  873 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 950
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 564359176  951 ADNQRLKDENGALIRVISKLSK 972
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-298 2.12e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.96  E-value: 2.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 124 FLIGQGAHVGAVNsegdtpldiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaKSGGTAL 203
Cdd:COG0666  171 LLLEAGADVNARD------------------------------------------------------------NDGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEEL 283
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                        250
                 ....*....|....*
gi 564359176 284 QKKQNLLHSEKRDKK 298
Cdd:COG0666  271 LLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-331 1.85e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 1.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:COG0666   25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 124 FLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIEAARKEEERImlrdARQWLNSGhiSDV-RHAKSGGTA 202
Cdd:COG0666  105 LLLEAGADVNARDKDGETPL----------------------HLAAYNGNLEI----VKLLLEAG--ADVnAQDNDGNTP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 203 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEE 282
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564359176 283 LQKKQNLLHSEKRDKKSPLIESTANMENNQPQKTFKNKETLIIEPEKNA 331
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-269 1.04e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  39 DDGAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY 118
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 119 LDIAEFLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsghisdvrhaks 198
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDL----------------------------------------------------- 225

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359176 199 ggtalhvAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAF 269
Cdd:COG0666  226 -------AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-272 1.65e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALH-QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL-- 119
Cdd:PHA03095  53 LYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-----YLsg 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 120 -----DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVNRQGVDIEAARkeeeriMLRDArqwlnsghISDVR 194
Cdd:PHA03095 128 fninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LKSRNANVELLR------LLIDA--------GADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 195 HAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGkeeACR-ILVDNL----CDMETVNKVGQ 266
Cdd:PHA03095 182 AVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKrSLVLPLliagISINARNRYGQ 258


                 ....*.
gi 564359176 267 TAFDVA 272
Cdd:PHA03095 259 TPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 3.97e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 3.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176   47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENgANINQPDNeGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 564359176  127 GQGAHVGAVN 136
Cdd:pfam12796  82 EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-229 5.02e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176   77 LHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGahvgavnsegdtpldiaeeeameellq 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359176  157 nevnrqgvdieaarkeeerimlrdarqwlnsghisDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam12796  54 -----------------------------------DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 50-236 5.05e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 5.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  50 SGDTDEVLKLLHR-GADINYANVDGLTALHQACIDDNVD--MVKFLVENGANINQPDNEGWIPLHA-----AAScgyLDI 121
Cdd:PHA03095  93 NATTLDVIKLLIKaGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VEL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 122 AEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQN-EVNRQGVDiEAARKEEERIMLRDA-----------RQWLNSGH 189
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCD-PAATDMLGNTPLHSMatgssckrslvLPLLIAGI 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564359176 190 ISDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:PHA03095 249 SINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-240 1.39e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  55 EVLK-LLHRGADINYANVDGLTALH-----QACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC--GYLDIAEFLI 126
Cdd:PHA03100  49 DVVKiLLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 127 GQGAHVGAVNSEGDTPLDIAEEEAMEELL--QNEVNRqGVDIEAARKEEeriMLrdarqwLNSGHISDVRHAKsGGTALH 204
Cdd:PHA03100 129 DNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDK-GVDINAKNRVN---YL------LSYGVPINIKDVY-GFTPLH 197

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564359176 205 VAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAA 240
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-263 1.71e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.31  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  52 DTDEVLKLLHRGADINYANVDGL-TALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGA 130
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 131 HVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAArkeeerimlrdarqwlnsghiSDVRhaksGGTALHVAAAKg 210
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAK---------------------SYIL----GLTALHSSIKS- 279

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564359176 211 yTEVLKLLIQAGYDVNIKDYDGWTPLHAAA-HWGKEEACRILVDNLCDMETVNK 263
Cdd:PHA02878 280 -ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKRIKP 332
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-272 3.29e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.29e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  203 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNlCDMETVNKvGQTAFDVA 272
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-145 3.59e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  44 FLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQA--CIDDNVDMVKFLVENGANINQ----------------PDNE 105
Cdd:PHA03100 112 YAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVY 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564359176 106 GWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 8.05e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 69.61  E-value: 8.05e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564359176   73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 608-654 1.91e-13

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: 65.49  E-value: 1.91e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564359176 608 RSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 654
Cdd:cd21945    8 RSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-262 5.85e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  110 LHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdieaarkeeerimlrdarqwlnsgh 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL---------------------------------------------- 34

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359176  190 isdvrhaksggtalHVAAAKGYTEVLKLLIQAGyDVNIKDYdGWTPLHAAAHWGKEEACRILVDNLCDMETVN 262
Cdd:pfam12796  35 --------------HLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 600-655 5.88e-13

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: 64.16  E-value: 5.88e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564359176 600 SSPAGTQSRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 655
Cdd:cd21944    2 TSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 7.91e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 7.91e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564359176  199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV 252
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 47-272 1.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.94  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDnegwIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLY 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 127 GQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEAARKEEERIMLRDARQWLNSGHI-------SDVRHAKS- 198
Cdd:PHA02876 261 DAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrtlimlgADVNAADRl 340

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564359176 199 GGTALHVAAA-KGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA 272
Cdd:PHA02876 341 YITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 53-267 3.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 3.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  53 TDEVLKLLHRGADINYANV-DGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGY-----LDIAEFLI 126
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYkKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 127 GQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieAARKEeerimlrdarqwLNSGHI--------SDVRHAKS 198
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLY----------------------AISKK------------SNSYSIveylldngANVNIKNS 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 199 -GGTALHVAAAKGY--TEVLKLLIQAGYDVNIKD-------YD---------GWTPLHAAAHWGKEEACRILVDNLCDME 259
Cdd:PHA03100 140 dGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsYGvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPN 219


                 ....*...
gi 564359176 260 TVNKVGQT 267
Cdd:PHA03100 220 LVNKYGDT 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 52-272 6.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 6.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 132 VGAVNSEGDTPLDIAeeeameellqnevnrqgvdIEAARKEEERIMLRdarqwlNSGHISDvrHAKSGGTALHVAAAKGY 211
Cdd:PHA02874 183 ANVKDNNGESPLHNA-------------------AEYGDYACIKLLID------HGNHIMN--KCKNGFTPLHNAIIHNR 235

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564359176 212 TeVLKLLIQaGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMETVNKVGQTAFDVA 272
Cdd:PHA02874 236 S-AIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-287 1.36e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 126
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 127 GQGAHVGAVNSEGDTPLdiaeeeameellQNEV--NRQGVDIeaarkeeerimlrdarqWLNSGHISDvrHAKSGGTALH 204
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPL------------HNAIihNRSAIEL-----------------LINNASIND--QDIDGSTPLH 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 205 VAAAKGYT-EVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEAcrILVDNLCDMETVNKVGQtafdVADEDILGYLEEL 283
Cdd:PHA02874 260 HAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDP--VIKDIIANAVLIKEADK----LKDSDFLEHIEIK 333


                 ....
gi 564359176 284 QKKQ 287
Cdd:PHA02874 334 DNKE 337
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 606-656 4.06e-10

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: 56.20  E-value: 4.06e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564359176 606 QSRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSR 656
Cdd:cd21946    3 KRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-279 1.92e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQAC-IDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDI 121
Cdd:PHA02876 311 LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 122 AEFLIGQGAhvgavnsegdtpldiaeeeameellqnevnrqgvDIEAArkeeerimlrdarqwlnsghisdvrhAKSGGT 201
Cdd:PHA02876 391 INTLLDYGA----------------------------------DIEAL--------------------------SQKIGT 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 202 ALHVA--AAKGYTEVlKLLIQAGYDVNIKDYDGWTPLHAAAHWG-KEEACRILVDNLCDMETVNKVGQTAFDVAdediLG 278
Cdd:PHA02876 411 ALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA----LE 485


                 .
gi 564359176 279 Y 279
Cdd:PHA02876 486 Y 486
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-145 2.89e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564359176   92 LVENG-ANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 3.19e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 3.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564359176   59 LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAA 113
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 608-650 8.20e-09

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: 52.34  E-value: 8.20e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564359176 608 RSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEK 650
Cdd:cd21930    5 RSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-254 9.21e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 9.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  50 SGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQ 128
Cdd:PHA02874  11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 129 GAHVG----------AVNSEGDTPLDIAEEEAMEELLQNEVNRQGvDIEAARkeeeriMLRDARQWLNsghISDVrhakS 198
Cdd:PHA02874  91 GVDTSilpipciekdMIKTILDCGIDVNIKDAELKTFLHYAIKKG-DLESIK------MLFEYGADVN---IEDD----N 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564359176 199 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDN 254
Cdd:PHA02874 157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-268 9.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 9.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  47 ACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGA--NINQPDNEGwiPLHAAASCGYLDIAEF 124
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 125 LIGQGAHVGAV-NSEGDTPLDIAEEEameellqnevnrQGVDIeaarkeeerimlrdARQWLNSGHISDVRHAKSgGTAL 203
Cdd:PHA02875  87 LLDLGKFADDVfYKDGMTPLHLATIL------------KKLDI--------------MKLLIARGADPDIPNTDK-FSPL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564359176 204 HVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTA 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: 57.75  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  54 DEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVG 133
Cdd:PHA03100 173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....
gi 564359176 134 AVNS 137
Cdd:PHA03100 253 TIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-93 2.89e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564359176   43 VFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLV 93
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-141 8.14e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 8.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  45 LAAcsSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEF 124
Cdd:PTZ00322  89 LAA--SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                         90
                 ....*....|....*....
gi 564359176 125 LIG--QGAHVGAVNSEGDT 141
Cdd:PTZ00322 167 LSRhsQCHFELGANAKPDS 185
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-279 9.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 9.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  54 DEVLKLLHRGADINYANVDGLTALHQACI--------------------------------------------------- 82
Cdd:PHA02878  51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifkiiltnrykniqt 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  83 -----------DDNVD--MVKFLVENGANINQPD-NEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDiaee 148
Cdd:PHA02878 131 idlvyidkkskDDIIEaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH---- 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 149 eameellqnevnrqgvdiEAARKEEERIMlrdaRQWLNSGHISDVRHaKSGGTALHVAAA--KGYtEVLKLLIQAGYDVN 226
Cdd:PHA02878 207 ------------------HAVKHYNKPIV----HILLENGASTDARD-KCGNTPLHISVGycKDY-DILKLLLEHGVDVN 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564359176 227 IKDY-DGWTPLHAAAHwgKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878 263 AKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 606-651 1.30e-07

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


Pssm-ID: 412022  Cd Length: 50  Bit Score: 49.10  E-value: 1.30e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 564359176 606 QSRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKT 651
Cdd:cd22527    5 RRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-280 2.02e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 157 NEVNRQGVDIEAARKEEERIMLRDARQWLNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 236
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564359176 237 HAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA----DEDILGYL 280
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLL 139
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 2.98e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564359176  185 LNSGHISDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 239
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-104 3.63e-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: 3.63e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564359176   72 DGLTALHQACID-DNVDMVKFLVENGANINQPDN 104
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 52-236 6.27e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 53.38  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  52 DTDEVLKLLHRGADINYANVDGLTALHQACIDDNV--DMVKFLVENGANINQPDNEGWIPLHAAASCG------------ 117
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdn 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 118 --YLDIAEFLIGQGAHVGAVNSEGDTPL-------------DIAEEEAMEELLQNEVNRQGVDIEAARKEEERIM----- 177
Cdd:PHA02716 376 diRLDVIQCLISLGADITAVNCLGYTPLtsyictaqnymyyDIIDCLISDKVLNMVKHRILQDLLIRVDDTPCIIhhiia 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 178 --------LRDARQWLNSGHISDVRHAK------------SGGTALHVAA-----AKGYTEVLKLLIQAGYDVNIKDYDG 232
Cdd:PHA02716 456 kyniptdlYTDEYEPYDSTKIHDVYHCAiierynnavcetSGMTPLHVSIishtnANIVMDSFVYLLSIQYNINIPTKNG 535


                 ....
gi 564359176 233 WTPL 236
Cdd:PHA02716 536 VTPL 539
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 67-279 7.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 7.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  67 NYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASC-GYLDIAEFL--------------IGQGAH 131
Cdd:PHA02878  31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIrsinkcsvfytlvaIKDAFN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 132 VGAVNSEGDTPLDIAEeeameellqnevNRQGVDIEAARK--EEERIMLRDARQWLNSGHISDVRHAKSGGTALHVAAAK 209
Cdd:PHA02878 111 NRNVEIFKIILTNRYK------------NIQTIDLVYIDKksKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATEN 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 210 GYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGY 279
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-293 9.96e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 9.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 207 AAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVADEDILGYLEELQKK 286
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*..
gi 564359176 287 QNLLHSE 293
Cdd:PTZ00322 170 HSQCHFE 176
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-100 1.56e-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: 1.56e-06
                          10        20
                  ....*....|....*....|....*....
gi 564359176   72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-143 2.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  36 VKFDDGAVFLAACSSGDTDEVLK-LLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAA 114
Cdd:PHA02875  97 VFYKDGMTPLHLATILKKLDIMKlLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                         90       100
                 ....*....|....*....|....*....
gi 564359176 115 SCGYLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-145 2.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  55 EVLKLL-HRGADINYANVDGLTALHQAC--IDDNVDMVKFLVENGANINQPDNEGWIPLHAaascgYL------DIAEFL 125
Cdd:PHA02859 104 EILKILiDSGSSITEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYS-----YIlfhsdkKIFDFL 178

                         90       100
                 ....*....|....*....|
gi 564359176 126 IGQGAHVGAVNSEGDTPLDI 145
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDL 198
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-288 4.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  56 VLKLLHRGADINY----ANVDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAH 131
Cdd:PHA02876 124 ILKEAISGNDIHYdkinESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAD 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 132 VGAVNSEGDTPLDIAEEEAMEELLQNEV-NRQGVD------IEAARKE--EERIMLRDARQWLNSghISDVRHaksggTA 202
Cdd:PHA02876 204 VNIIALDDLSVLECAVDSKNIDTIKAIIdNRSNINkndlslLKAIRNEdlETSLLLYDAGFSVNS--IDDCKN-----TP 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 203 LHVAA-AKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKE-EACRILVDNLCDMETVNKVGQTAFDVA-----DED 275
Cdd:PHA02876 277 LHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAstldrNKD 356

                        250
                 ....*....|...
gi 564359176 276 ILGYLEELQKKQN 288
Cdd:PHA02876 357 IVITLLELGANVN 369
Ank_4 pfam13637
Ankyrin repeats (many copies);
232-280 4.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564359176  232 GWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA----DEDILGYL 280
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-220 5.34e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.40  E-value: 5.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  73 GLTALHQACIDDNVDMVKFLVENGANINQPDNEGWI--------------PLHAAASCGYLDIAEFLIGQGAHVGAVNSE 138
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 139 GDTPLDIaeeeaMEELLQNEVNRQGVDIeaarkeeerIMLRDARQwlNSGHISDVRHaKSGGTALHVAAAKGYTEVLKLL 218
Cdd:cd22192  169 GNTVLHI-----LVLQPNKTFACQMYDL---------ILSYDKED--DLQPLDLVPN-NQGLTPFKLAAKEGNIVMFQHL 231


                 ..
gi 564359176 219 IQ 220
Cdd:cd22192  232 VQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 72-100 5.64e-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: 5.64e-06
                           10        20
                   ....*....|....*....|....*....
gi 564359176    72 DGLTALHQACIDDNVDMVKFLVENGANIN 100
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 5.70e-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: 5.70e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 564359176  199 GGTALHVAAAK-GYTEVLKLLIQAGYDVNIKD 229
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-280 6.10e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 6.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  86 VDMVKFLVENGANINQPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrq 162
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPL------------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 163 gvdieaarkeeerimlrdarqwlnsghisdvrhaksggtalHVAAAKGYTE-VLKLLIQAGYDVNIKDYDGWTPLHA--A 239
Cdd:PHA03095  88 -----------------------------------------HLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylS 126

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564359176 240 AHWGKEEACRILVDNLCDMETVNKVGQTAFDV------ADEDILGYL 280
Cdd:PHA03095 127 GFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANVELLRLL 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 41-99 2.25e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564359176  41 GAVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDDNVDMVKFLVENGANI 99
Cdd:PLN03192 623 GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 47-227 2.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  47 ACSSGDTDEVLKLLHRGA---DINYAnvDGLTALHQACIDDNVDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE 123
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKfadDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 124 FLIGQGAHVGAVNSEGDTPLDIAEEEAmeellqnevnrqgvDIEAARkeeeriMLrdarqwLNSGHISDVRHAKSGGTAL 203
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKG--------------DIAICK------ML------LDSGANIDYFGKNGCVAAL 206

                        170       180
                 ....*....|....*....|....
gi 564359176 204 HVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:PHA02875 207 CYAIENNKIDIVRLFIKRGADCNI 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 185-301 4.19e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 185 LNSGHISDVRHAKsGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL--VDNLCDMETVN 262
Cdd:PLN03192 545 LKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAG 623

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564359176 263 KVGQTAfdvADEDILGYLEELQKKQNLLHSEKRDKKSPL 301
Cdd:PLN03192 624 DLLCTA---AKRNDLTAMKELLKQGLNVDSEDHQGATAL 659
PHA02798 PHA02798
ankyrin-like protein; Provisional
 53-237 4.21e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  53 TDEVLKLLHRGADINYANVDGLTALhqaC------IDDN--VDMVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE- 123
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL---CtilsniKDYKhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEi 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 124 --FLIGQGAHVGAVNSEGDTPLDIaeeeameellqnevnrqgvdieaarkeeerimlrdarqWLNSGHISDVrhaksggt 201
Cdd:PHA02798 128 llFMIENGADTTLLDKDGFTMLQV--------------------------------------YLQSNHHIDI-------- 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564359176 202 alhvaaakgytEVLKLLIQAGYDVN-IKDYDGWTPLH 237
Cdd:PHA02798 162 -----------EIIKLLLEKGVDINtHNNKEKYDTLH 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-140 5.55e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  47 ACSSGDTDEVLKLLHRGADINYANVDGLTAL----------------HQACIDD---------------NVDMVKFLVEN 95
Cdd:PLN03192 565 AASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASISDphaagdllctaakrnDLTAMKELLKQ 644

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564359176  96 GANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGD 140
Cdd:PLN03192 645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-272 5.68e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564359176  218 LIQAGY-DVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTAFDVA 272
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 42-132 7.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  42 AVFLAACSSGDTDEVLKLLHRGADINYANVDGLTALHQACIDD-NVDMVKFLVENGANINQPDNEGWIPLHAAasCGYLD 120
Cdd:PHA02876 411 ALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHG 488

                         90
                 ....*....|..
gi 564359176 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 1.11e-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: 1.11e-04
                           10        20
                   ....*....|....*....|....*..
gi 564359176   201 TALHVAAAKGYTEVLKLLIQAGYDVNI 227
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 66-220 2.25e-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: 45.18  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  66 INYANVD----GLTALHQACIDDNVDMVKFLVENGANINQPDNE--------------GWIPLHAAASCGYLDIAEFLIG 127
Cdd:cd22196   83 VNAAYTDsyykGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 128 ---QGAHVGAVNSEGDTPL--------DIAEEEAMEELLQNEVNRQGVDIEAARKEEErimlrdarqwlnsghISDvrha 196
Cdd:cd22196  163 nphSPADISARDSMGNTVLhalvevadNTPENTKFVTKMYNEILILGAKIRPLLKLEE---------------ITN---- 223

                        170       180
                 ....*....|....*....|....
gi 564359176 197 KSGGTALHVAAAKGYTEVLKLLIQ 220
Cdd:cd22196  224 KKGLTPLKLAAKTGKIGIFAYILG 247
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 80-143 4.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 4.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359176  80 ACIDD---NVDMVKFLVENGANIN-QPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPL 143
Cdd:PHA02859  57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-136 4.16e-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: 4.16e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564359176  105 EGWIPLHAAA-SCGYLDIAEFLIGQGAHVGAVN 136
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 89-145 4.74e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564359176  89 VKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-145 5.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.84e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 564359176  109 PLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 145
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 55-129 6.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  55 EVLKLL-HRGADINYANVD-GLTALHQ-ACIDDNV--DMVKFLVENGANINQPDNEGWIPLHA-AASCGY-LDIAEFLIG 127
Cdd:PHA02859  67 EILKFLiENGADVNFKTRDnNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMyMCNFNVrINVIKLLID 146


                 ..
gi 564359176 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 1.08e-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: 1.08e-03
                          10        20
                  ....*....|....*....|....*....
gi 564359176  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 1.36e-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: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  73 GLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIG---QGAHVGAV 135
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 136 NSEGDTPLDIAEEEAMEELLQNEVNRQGVDIeaarkeeerIMLRDARqWLNSGHISDVRHAKsGGTALHVAAAKGYTEVL 215
Cdd:cd22193  156 DSRGNTVLHALVTVADNTKENTKFVTRMYDM---------ILIRGAK-LCPTVELEEIRNND-GLTPLQLAAKMGKIEIL 224


                 ....*
gi 564359176 216 KLLIQ 220
Cdd:cd22193  225 KYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 231-263 1.37e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564359176  231 DGWTPLHAAA-HWGKEEACRILVDNLCDMETVNK 263
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-132 1.69e-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: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  43 VFLAAcSSGDTDEVLKLL-HRGADINYANVDGLTALHQACIDDNVDMVKFLVENGAN-INQPDN----EGWIPLHAAASC 116
Cdd:cd22192   21 LLLAA-KENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99

                         90
                 ....*....|....*.
gi 564359176 117 GYLDIAEFLIGQGAHV 132
Cdd:cd22192  100 QNLNLVRELIARGADV 115
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 73-145 1.87e-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: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  73 GLTALHQACIDDNVDMVKFLVENGANINQPDNE-------------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV---N 136
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALeaqD 152


                 ....*....
gi 564359176 137 SEGDTPLDI 145
Cdd:cd21882  153 SLGNTVLHA 161
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 206-268 2.47e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564359176 206 AAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMETVNKVGQTA 268
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 876-972 3.20e-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: 40.90  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 876 KLYEQILAENEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSLLEMEKRERRALERRI-SEMEEELKMLPDL 949
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAEL 218

                         90       100
                 ....*....|....*....|...
gi 564359176 950 KADNQRLKDENGALIRVISKLSK 972
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAE 241
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 70-216 3.30e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.28  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176  70 NVDGLTALHQACIDDNVDMVKFLVENGANIN--------QPDNE------GWIPLHAAASCGYLDIAEFLIGQGAHVGAV 135
Cdd:cd22194  138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359176 136 -NSEGDTPLDIAEEEAMEELLQNEVNRQGVDieaarkeeerIMLRDARQWlnsgHISDVRHaKSGGTALHVAAAKGYTEV 214
Cdd:cd22194  218 qDSRGNTVLHALVTVAEDSKTQNDFVKRMYD----------MILLKSENK----NLETIRN-NEGLTPLQLAAKMGKAEI 282


                 ..
gi 564359176 215 LK 216
Cdd:cd22194  283 LK 284
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 181-251 3.64e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 3.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359176 181 ARQWLNSGHISDVRHAkSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL 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 ...
 879-946 4.51e-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: 38.75  E-value: 4.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359176  879 EQILAENEKLKAQLHDTNMELTDLKLQLEKATQrQERFADRSLLEME---KRERRALERRISEMEEELKML 946
Cdd:pfam09744  39 ESLASRNQEHNVELEELREDNEQLETQYEREKA-LRKRAEEELEEIEdqwEQETKDLLSQVESLEEENRRL 108
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 886-960 8.85e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.93  E-value: 8.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564359176  886 EKLKAQLHDTNMELTDLKLQLEKatQRQERFADRSLLEMEKRERRALERRISEMEEELKmlpDLKADNQRLKDEN 960
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLEL--QAREKAQSQALAEAQQQELVALEGLAAELEEKQQ---ELEAQLEQLQEKA 207
 
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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