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Conserved domains on  [gi|564380748|ref|XP_006249942|]
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protein phosphatase 1 regulatory subunit 12B 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 ...
 708-815 1.74e-35

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: 129.73  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  708 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEmknlhqLK 787
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                          90       100
                  ....*....|....*....|....*...
gi 564380748  788 QIQTLKQMNEQLQAENRALTRVVARLSR 815
Cdd:pfam15898  75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-137 1.58e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaE 228

                         90
                 ....*....|....
gi 564380748 124 EGLVEHLEMLQKKQ 137
Cdd:COG0666  229 NGNLEIVKLLLEAG 242
IPD_PPP1R12 super family cl40436
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 441-493 6.46e-17

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: 75.12  E-value: 6.46e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380748 441 EPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 493
Cdd:cd21945    2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
375-576 2.81e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 375 VAPSTY---TSTYLKRTPYKSQADSTAERTDSGSSSTPLCVITNRPAPSTANGVPAATVLSSPAADASVEPREQRRSYLT 451
Cdd:PRK07003 340 LAPDEYagfTMTLLRMLAFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 452 PVRdEEAESLRKARSRQA-RQTRRSTQGVTLTDLQEAEKTFSRSRAERQAQE--QPGEKLEDSGELEGSTKKQ-EPSAAP 527
Cdd:PRK07003 420 ATR-AEAPPAAPAPPATAdRGDDAADGDAPVPAKANARASADSRCDERDAQPpaDSGSASAPASDAPPDAAFEpAPRAAA 498

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380748 528 TKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDKLTAPVSPSASRPSLYTG 576
Cdd:PRK07003 499 PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAG 547
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 708-815 1.74e-35

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: 129.73  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  708 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEmknlhqLK 787
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                          90       100
                  ....*....|....*....|....*...
gi 564380748  788 QIQTLKQMNEQLQAENRALTRVVARLSR 815
Cdd:pfam15898  75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-137 1.58e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaE 228

                         90
                 ....*....|....
gi 564380748 124 EGLVEHLEMLQKKQ 137
Cdd:COG0666  229 NGNLEIVKLLLEAG 242
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 441-493 6.46e-17

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: 75.12  E-value: 6.46e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380748 441 EPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 493
Cdd:cd21945    2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-133 2.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748   53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 564380748  132 ML 133
Cdd:pfam12796  79 LL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-124 4.35e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380748  57 AAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 124
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 8.45e-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: 37.18  E-value: 8.45e-04
                           10        20
                   ....*....|....*....|....*....
gi 564380748    49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 711-820 1.09e-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: 42.06  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 711 KLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEktsdrssVLEVEKRERRALERKMSEMEEEMKNLHqlKQIQ 790
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLE--KELA 209

                         90       100       110
                 ....*....|....*....|....*....|
gi 564380748 791 TLKQMNEQLQAENRALTRVVARLSRSVESS 820
Cdd:COG4942  210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 727-805 1.67e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380748  727 LQEAQLELADIKAKLEKMAQQKQEktsdRSSVLEVEKRERRALERKMSEMEEEMKNLHQlkQIQTLKQMNEQLQAENRA 805
Cdd:PRK11448  144 LHALQQEVLTLKQQLELQAREKAQ----SQALAEAQQQELVALEGLAAELEEKQQELEA--QLEQLQEKAAETSQERKQ 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-137 2.31e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD----------IRNKLGQTPFDV 121
Cdd:cd22192  140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldlVPNNQGLTPFKL 218

                         90
                 ....*....|....*..
gi 564380748 122 A-DEGLVEHLEMLQKKQ 137
Cdd:cd22192  219 AaKEGNIVMFQHLVQKR 235
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
375-576 2.81e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 375 VAPSTY---TSTYLKRTPYKSQADSTAERTDSGSSSTPLCVITNRPAPSTANGVPAATVLSSPAADASVEPREQRRSYLT 451
Cdd:PRK07003 340 LAPDEYagfTMTLLRMLAFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 452 PVRdEEAESLRKARSRQA-RQTRRSTQGVTLTDLQEAEKTFSRSRAERQAQE--QPGEKLEDSGELEGSTKKQ-EPSAAP 527
Cdd:PRK07003 420 ATR-AEAPPAAPAPPATAdRGDDAADGDAPVPAKANARASADSRCDERDAQPpaDSGSASAPASDAPPDAAFEpAPRAAA 498

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380748 528 TKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDKLTAPVSPSASRPSLYTG 576
Cdd:PRK07003 499 PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAG 547
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 708-815 1.74e-35

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: 129.73  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  708 DYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVEKRERRALERKMSEMEEEmknlhqLK 787
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTQQRQESFSDRSSLLETEKREKRALERKISEMEEE------LK 74

                          90       100
                  ....*....|....*....|....*...
gi 564380748  788 QIQTLKQMNEQLQAENRALTRVVARLSR 815
Cdd:pfam15898  75 VLEDLRAENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-137 1.58e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666  149 QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaE 228

                         90
                 ....*....|....
gi 564380748 124 EGLVEHLEMLQKKQ 137
Cdd:COG0666  229 NGNLEIVKLLLEAG 242
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 441-493 6.46e-17

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: 75.12  E-value: 6.46e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380748 441 EPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSR 493
Cdd:cd21945    2 DSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-133 8.04e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.92  E-value: 8.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA-D 123
Cdd:COG0666  116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaE 195

                         90
                 ....*....|
gi 564380748 124 EGLVEHLEML 133
Cdd:COG0666  196 NGHLEIVKLL 205
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 438-494 2.80e-16

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: 73.40  E-value: 2.80e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564380748 438 ASVEPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRS 494
Cdd:cd21944    1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 443-489 4.56e-16

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


Pssm-ID: 412018  Cd Length: 47  Bit Score: 72.76  E-value: 4.56e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564380748 443 REQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEK 489
Cdd:cd21930    1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-133 7.46e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 7.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  30 DARQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMD 109
Cdd:COG0666   68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                         90       100
                 ....*....|....*....|....*
gi 564380748 110 IRNKLGQTPFDVA-DEGLVEHLEML 133
Cdd:COG0666  148 AQDNDGNTPLHLAaANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-133 2.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748   53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEaLCDMDIRNKlGQTPFDVA-DEGLVEHLE 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAaRSGHLEIVK 78


                  ..
gi 564380748  132 ML 133
Cdd:pfam12796  79 LL 80
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 443-495 5.69e-15

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: 69.69  E-value: 5.69e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380748 443 REQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKTFSRSR 495
Cdd:cd21946    1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-122 4.99e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 4.99e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380748  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 441-490 1.17e-11

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: 60.27  E-value: 1.17e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380748 441 EPREQRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAEKT 490
Cdd:cd22527    1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 5.14e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.14e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564380748   51 TALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSIL 101
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-112 5.36e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.36e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564380748   49 GATALHVAAAKGYSEVLRLLIQAGyELNVQDHdGWTPLHAAAHWGVKEACSILAEALCDMDIRN 112
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-89 1.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564380748   35 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAA 89
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-134 7.44e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 51.88  E-value: 7.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  35 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                         90       100
                 ....*....|....*....|
gi 564380748 115 GQTPFDVADEGlvEHLEMLQ 134
Cdd:COG0666  120 GETPLHLAAYN--GNLEIVK 137
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-79 1.87e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.87e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 564380748   42 DVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQD 79
Cdd:pfam12796  54 DVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-124 4.35e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380748  57 AAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADE 124
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 2-122 4.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748   2 KDLLLEQVKK-QGVDLEQSRKEEEQQMLQDA--RQWLNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQ 78
Cdd:PHA02878 118 KIILTNRYKNiQTIDLVYIDKKSKDDIIEAEitKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIP 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 564380748  79 DHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA02878 198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-134 7.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 7.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564380748   82 GWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVADEGlvEHLEMLQ 134
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN--GNVEVLK 51
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-122 9.35e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 9.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380748  47 RSGATALHVAAAKGYSE--VLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA03095 220 MLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-80 9.39e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 9.39e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564380748   49 GATALHVAAAK-GYSEVLRLLIQAGYELNVQDH 80
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 707-823 1.01e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  707 RDYKKLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEKTSDRSSVLEVE------KRERRALERKMSEMEEEM 780
Cdd:pfam13851  43 ERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLEkelkdlKWEHEVLEQRFEKVERER 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 564380748  781 KNLHQlKQIQTLKQMNEQLQAENRALTRVVARLSRSVESSDTQ 823
Cdd:pfam13851 123 DELYD-KFEAAIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQ 164
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 47-136 2.20e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.56  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  47 RSGATALHVAAAKGYS---EVLRLLIQAGYELNVQDH-DGWTPLHAAAHWGVKEacsiLAEALC-----DMDIRNKLGQT 117
Cdd:PHA02736  53 RHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYE----LATWLCnqpgvNMEILNYAFKT 128

                         90       100
                 ....*....|....*....|
gi 564380748 118 PFDVA-DEGLVEHLEMLQKK 136
Cdd:PHA02736 129 PYYVAcERHDAKMMNILRAK 148
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-122 4.00e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  40 IEDVrqarSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQTPF 119
Cdd:PHA02874 152 IEDD----NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227


                 ...
gi 564380748 120 DVA 122
Cdd:PHA02874 228 HNA 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 49-77 8.45e-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: 37.18  E-value: 8.45e-04
                           10        20
                   ....*....|....*....|....*....
gi 564380748    49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-122 9.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 9.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380748  45 QARSGATALHVAAAKGYSeVLRLLIQaGYELNVQDHDGWTPLHAAAHWGV-KEACSILAEALCDMDIRNKLGQTPFDVA 122
Cdd:PHA02874 219 KCKNGFTPLHNAIIHNRS-AIELLIN-NASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTA 295
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 711-820 1.09e-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: 42.06  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 711 KLYESALTENQKLKTKLQEAQLELADIKAKLEKMAQQKQEktsdrssVLEVEKRERRALERKMSEMEEEMKNLHqlKQIQ 790
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA-------LLAELEEERAALEALKAERQKLLARLE--KELA 209

                         90       100       110
                 ....*....|....*....|....*....|
gi 564380748 791 TLKQMNEQLQAENRALTRVVARLSRSVESS 820
Cdd:COG4942  210 ELAAELAELQQEAEELEALIARLEAEAAAA 239
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-124 1.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  35 LNSGKIEDVRQARSgATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:PHA02874 111 LDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90
                 ....*....|
gi 564380748 115 GQTPFDVADE 124
Cdd:PHA02874 190 GESPLHNAAE 199
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-117 1.65e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  18 QSRKEEEQQMLQDARQW---LNSGKIEDVRQARSG-------ATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLH 87
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHhkeLHDLNVGDLLGDNGGehddpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                         90       100       110
                 ....*....|....*....|....*....|
gi 564380748  88 AAAHWGVKEACSILAEALCDMDIRNKLGQT 117
Cdd:PLN03192 564 IAASKGYEDCVLVLLKHACNVHIRDANGNT 593
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 727-805 1.67e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 42.25  E-value: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380748  727 LQEAQLELADIKAKLEKMAQQKQEktsdRSSVLEVEKRERRALERKMSEMEEEMKNLHQlkQIQTLKQMNEQLQAENRA 805
Cdd:PRK11448  144 LHALQQEVLTLKQQLELQAREKAQ----SQALAEAQQQELVALEGLAAELEEKQQELEA--QLEQLQEKAAETSQERKQ 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-137 2.31e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.54  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  53 LHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKE-ACSILaEALCDMD----------IRNKLGQTPFDV 121
Cdd:cd22192  140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfACQMY-DLILSYDkeddlqpldlVPNNQGLTPFKL 218

                         90
                 ....*....|....*..
gi 564380748 122 A-DEGLVEHLEMLQKKQ 137
Cdd:cd22192  219 AaKEGNIVMFQHLVQKR 235
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-117 2.59e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 2.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380748  45 QARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKLGQT 117
Cdd:COG0666  215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
375-576 2.81e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 41.37  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 375 VAPSTY---TSTYLKRTPYKSQADSTAERTDSGSSSTPLCVITNRPAPSTANGVPAATVLSSPAADASVEPREQRRSYLT 451
Cdd:PRK07003 340 LAPDEYagfTMTLLRMLAFEPAVTGGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAA 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 452 PVRdEEAESLRKARSRQA-RQTRRSTQGVTLTDLQEAEKTFSRSRAERQAQE--QPGEKLEDSGELEGSTKKQ-EPSAAP 527
Cdd:PRK07003 420 ATR-AEAPPAAPAPPATAdRGDDAADGDAPVPAKANARASADSRCDERDAQPpaDSGSASAPASDAPPDAAFEpAPRAAA 498

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380748 528 TKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDKLTAPVSPSASRPSLYTG 576
Cdd:PRK07003 499 PSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAG 547
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-89 2.92e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748   1 MKDLLLEQVKKQGV---DLEQSRKEEEQQMLQDARQWL-----NSGKIEDVRQAR--------SGATALHVAAAKGYSEV 64
Cdd:PLN03192 494 LKNFLQHHKELHDLnvgDLLGDNGGEHDDPNMASNLLTvastgNAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDC 573

                         90       100
                 ....*....|....*....|....*
gi 564380748  65 LRLLIQAGYELNVQDHDGWTPLHAA 89
Cdd:PLN03192 574 VLVLLKHACNVHIRDANGNTALWNA 598
PHA03095 PHA03095
ankyrin-like protein; Provisional
 47-121 3.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  47 RSGATALHVAAAKGYSE-VLRLLIQAGYELNVQDHDGWTPLHA-----AAHWGVKEacsILAEALCDMDIRNKLGQTPFD 120
Cdd:PHA03095  81 RCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVylsgfNINPKVIR---LLLRKGADVNALDLYGMTPLA 157


                 .
gi 564380748 121 V 121
Cdd:PHA03095 158 V 158
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-113 3.71e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564380748   81 DGWTPLHAAA-HWGVKEACSILAEALCDMDIRNK 113
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 49-77 4.33e-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: 35.31  E-value: 4.33e-03
                          10        20
                  ....*....|....*....|....*....
gi 564380748   49 GATALHVAAAKGYSEVLRLLIQAGYELNV 77
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03369 PHA03369
capsid maturational protease; Provisional
 331-618 5.91e-03

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 40.37  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 331 RRLSGTSDIEEKENRESAVNLVRSGSHTRQLWRDEAKGNETPQTVAPSTYTSTYLKRTPYKSQADSTAERTDSGSS---- 406
Cdd:PHA03369 326 QYLIEGRKLFSTINGLKAHNEILKTASLTAPSRVLAAAAKVAVIAAPQTHTGPADRQRPQRPDGIPYSVPARSPMTaypp 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 407 -----STPLCVITNRPAPSTaNGVPAATVLSSPAAdaSVEPREQRRSYLTPVRDEEAeslrkarSRQARQTRRSTQGVTL 481
Cdd:PHA03369 406 vpqfcGDPGLVSPYNPQSPG-TSYGPEPVGPVPPQ--PTNPYVMPISMANMVYPGHP-------QEHGHERKRKRGGELK 475

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748 482 TDLQEAEKTFSRSRAERQAQEQPGEKLEDSGELEgSTKKQEPSAAPTKEAGEGQQPWGRSLDEEPIYHRLRCPTQPDklt 561
Cdd:PHA03369 476 EELIETLKLVKKLKEEQESLAKELEATAHKSEIK-KIAESEFKNAGAKTAAANIEPNCSADAAAPATKRARPETKTE--- 551

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564380748 562 apvspSASRPSLYTGSQLLHTSRASVPDPEATTNTTAAKEMDTSEKEEADLDDQSSN 618
Cdd:PHA03369 552 -----LEAVVRFPYQIRNMESPAFVHSFTSTTLAAAAGQGSDTAEALAGAIETLLTQ 603
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 35-122 6.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380748  35 LNSGKIEDVRQARSGATALHVAAAKGYSEVLRLLIQAGYELNVQDHDGWTPLHAAAHWGVKEACSILAEALCDMDIRNKL 114
Cdd:PHA02875  88 LDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167


                 ....*...
gi 564380748 115 GQTPFDVA 122
Cdd:PHA02875 168 GCTPLIIA 175
 
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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