NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|410442518|ref|NP_001258547|]
View 

protein phosphatase 1 regulatory subunit 12C isoform b [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 681-780 1.97e-40

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: 143.60  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  681 FRTLYAELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 759
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 410442518  760 DNQRLKDENAALIRVISKLSK 780
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 2.49e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 2.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  52 AAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:COG0666   38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 132 NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdtrc 211
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA-------------AANG-NLEIVK-----LL------ 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 212 wLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTH 291
Cdd:COG0666  173 -LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410442518 292 AGQRPCDLADEEVLSLLEELARKQEDLRNQK 322
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 523-576 1.59e-27

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: 105.55  E-value: 1.59e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 410442518 523 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGK 576
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 371-617 9.11e-07

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 371 PPIQDED-EGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVLEEAPFSRRFGLLKTGSSGALGPPERRTAEGAPG------ 443
Cdd:PTZ00449 497 APIEEEDsDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSkiptls 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 444 ---AGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEpsvLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTA 520
Cdd:PTZ00449 577 kkpEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 521 PPADsrdrrRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLD-----PSRRPRV 595
Cdd:PTZ00449 654 IKSP-----KPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprplPPKLPRD 728

                        250       260
                 ....*....|....*....|..
gi 410442518 596 PgvENSDSPAQReaPDGQGPGP 617
Cdd:PTZ00449 729 E--EFPFEPIGD--PDAEQPDD 746
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 681-780 1.97e-40

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: 143.60  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  681 FRTLYAELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 759
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 410442518  760 DNQRLKDENAALIRVISKLSK 780
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 2.49e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 2.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  52 AAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:COG0666   38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 132 NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdtrc 211
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA-------------AANG-NLEIVK-----LL------ 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 212 wLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTH 291
Cdd:COG0666  173 -LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410442518 292 AGQRPCDLADEEVLSLLEELARKQEDLRNQK 322
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 523-576 1.59e-27

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: 105.55  E-value: 1.59e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 410442518 523 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGK 576
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-160 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518   95 DSTNADGISALHQACIDENLEVVRFLVEQGATvnQADNEGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-268 8.01e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 8.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 110 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASC--GYLDIARYLLSHGANIAAVNSDGDLPLDLA------ESDAMEG 181
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 182 LLKaeiarRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGW 261
Cdd:PHA03100 162 LID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                 ....*..
gi 410442518 262 TPLHAAA 268
Cdd:PHA03100 227 TPLHIAI 233
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 101-282 1.16e-07

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: 55.27  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVNQADNE-------------GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDg 167
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 168 dlplDLAESDAMEGLLkaEIARRGVDVEA-AKRAEEELLLHDTRcwLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLL 246
Cdd:cd21882  152 ----DSLGNTVLHALV--LQADNTPENSAfVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410442518 247 LQ----AGYDPELRDGDGWT--PLHAAAH-------WGVEDACRLLAEH 282
Cdd:cd21882  224 LQrefsGPYQPLSRKFTEWTygPVTSSLYdlseidsWEKNSVLELIAFS 272
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-160 3.55e-07

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: 46.81  E-value: 3.55e-07
                           10        20
                   ....*....|....*....|....*...
gi 410442518   133 EGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 371-617 9.11e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 371 PPIQDED-EGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVLEEAPFSRRFGLLKTGSSGALGPPERRTAEGAPG------ 443
Cdd:PTZ00449 497 APIEEEDsDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSkiptls 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 444 ---AGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEpsvLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTA 520
Cdd:PTZ00449 577 kkpEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 521 PPADsrdrrRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLD-----PSRRPRV 595
Cdd:PTZ00449 654 IKSP-----KPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprplPPKLPRD 728

                        250       260
                 ....*....|....*....|..
gi 410442518 596 PgvENSDSPAQReaPDGQGPGP 617
Cdd:PTZ00449 729 E--EFPFEPIGD--PDAEQPDD 746
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-270 1.49e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.62  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  101 GISALHQACIDENLEVVRFLVEQGATVNQADN--------------EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 166
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  167 GDlplDLAESDAMEGLLKAEiarrgvDVEAAKRAEEELLLHDTRCwlnggampeaRHPRT--------GASALHVAAAKG 238
Cdd:TIGR00870 208 GN---TLLHLLVMENEFKAE------YEELSCQMYNFALSLLDKL----------RDSKElevilnhqGLTPLKLAAKEG 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 410442518  239 YIEVMRLLLQAGYdpELRDGDGWT--PLHAAAHW 270
Cdd:TIGR00870 269 RIVLFRLKLAIKY--KQKKFVAWPngQQLLSLYW 300
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
686-780 1.61e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 686 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQR 763
Cdd:COG2433  423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLER 497

                         90       100
                 ....*....|....*....|....
gi 410442518 764 LKD-------ENAALIRVISKLSK 780
Cdd:COG2433  498 LKElwklehsGELVPVKVVEKFTK 521
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 634-780 6.25e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518   634 AEGEEAEPADRSQESSTLEGGPSARRQRWQRDLNPEPEPESEepdggFRTLYAELRRENERLREALTETTLRLAQL---- 709
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-----LREALDELRAELTLLNEEAANLRERLESLerri 833

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410442518   710 ---KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKALSDLRADNQR----LKDENAALIRVISKLSK 780
Cdd:TIGR02168  834 aatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEalalLRSELEELSEELRELES 908
PTZ00121 PTZ00121
MAEBL; Provisional
 175-773 7.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  175 ESDAMEGLLKAEIARRGVDV---EAAKRAEEELLLHDTRCWLNGGAMPEARH---PRTGASALHVAAAKGYIEVMRLllq 248
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDARKaeeARKAEDAKKAEAARKAEEVRKA--- 1190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  249 agydPELRDGDGWTPLHAAAHWgvEDACRLLAEHGGGMDSLTHAGQRPCDLADEEVLSLLEELARKQEDLRNQKEASQSR 328
Cdd:PTZ00121 1191 ----EELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  329 GQEPQAPSSSKHRRSSVCRLSSREKISLQDLSKERRpggaggppIQDEDEGEEGPTEPPPAEPRTLNGVSSPPHPSPKSP 408
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE--------KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  409 VLEEApfsRRFGLLKTGSSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSvlSEVT 488
Cdd:PTZ00121 1337 KAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA--DELK 1411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  489 KPPPCLENSSPPSRIPEPESPAKPNVPTASTAPPAD-----SRDRRRSYQMPVRDEESESQRKARSRLmrqsrrstqgvt 563
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADeakkkAEEAKKAEEAKKKAEEAKKADEAKKKA------------ 1479

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  564 lTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQREAPDGQGPGPQAAREHRKVGKEWRGPAEGEEAEPAD 643
Cdd:PTZ00121 1480 -EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  644 RSQESSTLEggpSARRQRWQRDLNPEPEPESEEpdggfrtlyAELRRENERLREALTETTLRLAQLKVELERATQRQErf 723
Cdd:PTZ00121 1559 KAEEKKKAE---EAKKAEEDKNMALRKAEEAKK---------AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-- 1624

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 410442518  724 aerpalLELERFERRALERKAAELEEELKALSDLRADNQRLKDENAALIR 773
Cdd:PTZ00121 1625 ------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 681-780 1.97e-40

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: 143.60  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  681 FRTLYAELRRENERLREALTETTLRLAQLKVELERAT-QRQERFAERPALLELERFERRALERKAAELEEELKALSDLRA 759
Cdd:pfam15898   2 YKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSSLLETEKREKRALERKISEMEEELKVLEDLRA 81

                          90       100
                  ....*....|....*....|.
gi 410442518  760 DNQRLKDENAALIRVISKLSK 780
Cdd:pfam15898  82 ENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 2.49e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 2.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  52 AAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:COG0666   38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 132 NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdtrc 211
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA-------------AANG-NLEIVK-----LL------ 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 212 wLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTH 291
Cdd:COG0666  173 -LEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        250       260       270
                 ....*....|....*....|....*....|.
gi 410442518 292 AGQRPCDLADEEVLSLLEELARKQEDLRNQK 322
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-300 8.28e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 8.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  50 ERAAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQ 129
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 130 ADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdamegllkaeiARRGvDVEAAKraeeeLLlhdt 209
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA-------------AYNG-NLEIVK-----LL---- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 210 rcwLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSL 289
Cdd:COG0666  140 ---LEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        250
                 ....*....|.
gi 410442518 290 THAGQRPCDLA 300
Cdd:COG0666  216 DNDGKTALDLA 226
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 523-576 1.59e-27

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: 105.55  E-value: 1.59e-27
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 410442518 523 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGK 576
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-204 1.51e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 1.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  55 FLAACAGGDLDEARLMLRAadpgpGAELDPaappparavldsTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEG 134
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEA-----GADVNA------------RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 135 WTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEIARRGVDVEAAKRAEEEL 204
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-160 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.36e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518   95 DSTNADGISALHQACIDENLEVVRFLVEQGATvnQADNEGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 526-572 1.52e-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.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 76.61  E-value: 1.52e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 410442518 526 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 572
Cdd:cd21930    1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-257 2.07e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 2.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  105 LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHganiAAVNSDGDlpldlaesdamegllk 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN---------------- 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410442518  185 aeiarrgvdveaakraeeelllhdtrcwlnggampearhprtGASALHVAAAKGYIEVMRLLLQAGYDPELRD 257
Cdd:pfam12796  61 ------------------------------------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 523-577 2.20e-17

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: 76.48  E-value: 2.20e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 410442518 523 ADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKA 577
Cdd:cd21944    3 SEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-268 8.01e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 8.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 110 IDENLEVVRFLVEQGATVNQADNEGWTPLHVAASC--GYLDIARYLLSHGANIAAVNSDGDLPLDLA------ESDAMEG 181
Cdd:PHA03100  82 LTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnkiDLKILKL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 182 LLKaeiarRGVDVEAAKRAEeelllhdtrCWLNGGAMPEARHPRtGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGW 261
Cdd:PHA03100 162 LID-----KGVDINAKNRVN---------YLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226


                 ....*..
gi 410442518 262 TPLHAAA 268
Cdd:PHA03100 227 TPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-300 1.27e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  63 DLDEARLMLRAadpgpGAELDPAAPPparavldstnadGISALH-QACIDENLEVVRFLVEQGATVNQADNEGWTPLHVa 141
Cdd:PHA03095  62 VKDIVRLLLEA-----GADVNAPERC------------GFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 142 ascgYL-------DIARYLLSHGANIAAVNSDGDLPLDLaesdamegLLKaeiaRRGVDVEAAKraeeeLLlhdtrcwLN 214
Cdd:PHA03095 124 ----YLsgfninpKVIRLLLRKGADVNALDLYGMTPLAV--------LLK----SRNANVELLR-----LL-------ID 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 215 GGAMPEARHPRtGASALHVAA--AKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGvedACRL-----LAEHGGGMD 287
Cdd:PHA03095 176 AGADVYAVDDR-FRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKRslvlpLLIAGISIN 251

                        250
                 ....*....|...
gi 410442518 288 SLTHAGQRPCDLA 300
Cdd:PHA03095 252 ARNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
231-282 3.88e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.88e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 410442518  231 LHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEH 282
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
Ank_4 pfam13637
Ankyrin repeats (many copies);
103-154 3.93e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 64.22  E-value: 3.93e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 410442518  103 SALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLL 154
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 524-572 4.08e-13

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: 64.13  E-value: 4.08e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 410442518 524 DSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEK 572
Cdd:cd22527    1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEK 49
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 526-577 6.00e-13

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: 63.91  E-value: 6.00e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 410442518 526 RDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKA 577
Cdd:cd21946    1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRS 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 109-264 5.20e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 5.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 109 CIDENleVVRFLVEQGATVNQADNEGWTPLHV-----AAScgyLDIARYLLSHGANIAAVNSDGDLPLD-LAES-DAMEG 181
Cdd:PHA03095 129 NINPK--VIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VELLRLLIDAGADVYAVDDRFRSLLHhHLQSfKPRAR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 182 LLKaEIARRGVDVeAAKRAEEELLLHD----TRCW-------LNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAG 250
Cdd:PHA03095 204 IVR-ELIRAGCDP-AATDMLGNTPLHSmatgSSCKrslvlplLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALG 280

                        170
                 ....*....|....
gi 410442518 251 YDPELRDGDGWTPL 264
Cdd:PHA03095 281 ADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 114-266 1.78e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 114 LEVVRFLVEQGATVNQADNEGWTPLHVAASCG---YLDIARYLLSHGANIAAVNSDGDLPLDL-AESDAMEGLLKAEIaR 189
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI-K 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410442518 190 RGVDVEAAKRAeeelllhdtrcwlnggampearhprtGASALHVAAAKGYI--EVMRLLLQAGYDPELRDGDGWTPLHA 266
Cdd:PHA03095 106 AGADVNAKDKV--------------------------GRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
229-279 2.62e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.62e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 410442518  229 SALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLL 279
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-174 4.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  94 LDSTNADGISALHQA--CIDENLEVVRFLVEQGATVNQ----------------ADNEGWTPLHVAASCGYLDIARYLLS 155
Cdd:PHA03100 134 VNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLD 213

                         90
                 ....*....|....*....
gi 410442518 156 HGANIAAVNSDGDLPLDLA 174
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIA 232
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 2.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.59  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518  120 LVEQG-ATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-165 5.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 5.14e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410442518  94 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNS 165
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 120-287 6.99e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 6.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 120 LVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLdlaesdamegllkaeiarrgVDVEAAKR 199
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL--------------------WNAISAKH 603

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 200 AEEELLLHDtrcwlnggaMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLL 279
Cdd:PLN03192 604 HKIFRILYH---------FASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674


                 ....*...
gi 410442518 280 AEHGGGMD 287
Cdd:PLN03192 675 IMNGADVD 682
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-300 1.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 115 EVVRFLVEQGATVNQAD-NEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAeiarrgvd 193
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI-------- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 194 veaakraeeelllhdtrcWLNGGAMPEARHpRTGASALHVAAakGY---IEVMRLLLQAGYDPELRDG-DGWTPLHAAAH 269
Cdd:PHA02878 220 ------------------LLENGASTDARD-KCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYiLGLTALHSSIK 278

                        170       180       190
                 ....*....|....*....|....*....|.
gi 410442518 270 wgVEDACRLLAEHGGGMDSLTHAGQRPCDLA 300
Cdd:PHA02878 279 --SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 101-282 2.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESdame 180
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG---- 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 181 gllkaeiarRGVDVEAAKRaeeeLLLHdtrcwlngGAMPEARHPRTGASALHVAAAKGyiEVMRLLLQAGYDPELRDGDG 260
Cdd:PHA02878 244 ---------YCKDYDILKL----LLEH--------GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYK 300

                        170       180
                 ....*....|....*....|....
gi 410442518 261 WTPLHAAA--HWGVEdACRLLAEH 282
Cdd:PHA02878 301 LTPLSSAVkqYLCIN-IGRILISN 323
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 99-296 2.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  99 ADGISA-----LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLlshganIAAVNSDGDLPLDL 173
Cdd:PHA02878  30 STSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 174 AESDAMEG---------LLKAEIARRGVD-VEAAKRAEEELLLHD-TRCWLNGGAMPEARHPRTGASALHVAAAKGYIEV 242
Cdd:PHA02878 104 AIKDAFNNrnveifkiiLTNRYKNIQTIDlVYIDKKSKDDIIEAEiTKLLLSYGADINMKDRHKGNTALHYATENKDQRL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 410442518 243 MRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRP 296
Cdd:PHA02878 184 TELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-175 4.45e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 4.45e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 410442518 117 VRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAE 175
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 133-164 5.00e-08

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: 49.21  E-value: 5.00e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 410442518  133 EGWTPLHVAA-SCGYLDIARYLLSHGANIAAVN 164
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 101-282 1.16e-07

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: 55.27  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVNQADNE-------------GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDg 167
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 168 dlplDLAESDAMEGLLkaEIARRGVDVEA-AKRAEEELLLHDTRcwLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLL 246
Cdd:cd21882  152 ----DSLGNTVLHALV--LQADNTPENSAfVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHI 223

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 410442518 247 LQ----AGYDPELRDGDGWT--PLHAAAH-------WGVEDACRLLAEH 282
Cdd:cd21882  224 LQrefsGPYQPLSRKFTEWTygPVTSSLYdlseidsWEKNSVLELIAFS 272
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 210-282 3.09e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410442518 210 RCWLNGGAMPEARHpRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEH 282
Cdd:PTZ00322  99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 133-160 3.55e-07

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: 46.81  E-value: 3.55e-07
                           10        20
                   ....*....|....*....|....*...
gi 410442518   133 EGWTPLHVAASCGYLDIARYLLSHGANI 160
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 113-225 4.15e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 4.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 113 NLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDL-PLDLAESdamegLLKAEIARRG 191
Cdd:PLN03192 634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFsPTELREL-----LQKRELGHSI 708

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 410442518 192 VDVEAAKRAEEELLL--HDTRCWLNGGAMPEARHPR 225
Cdd:PLN03192 709 TIVDSVPADEPDLGRdgGSRPGRLQGTSSDNQCRPR 744
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-174 5.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.70e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 410442518  134 GWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-174 6.41e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 6.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  96 STNADGISALHQACIDENLE--VVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDL 173
Cdd:PHA03095 217 ATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296


                 .
gi 410442518 174 A 174
Cdd:PHA03095 297 M 297
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 371-617 9.11e-07

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.77  E-value: 9.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 371 PPIQDED-EGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVLEEAPFSRRFGLLKTGSSGALGPPERRTAEGAPG------ 443
Cdd:PTZ00449 497 APIEEEDsDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKESDEPKEGGKPGETKEGEVGKKPGPAKEHKPSkiptls 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 444 ---AGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEpsvLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTA 520
Cdd:PTZ00449 577 kkpEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPE---LLDIPKSPKRPESPKSPKRPPPPQRPSSPERPEGPKI 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 521 PPADsrdrrRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLD-----PSRRPRV 595
Cdd:PTZ00449 654 IKSP-----KPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFESILKETLPETPGTPFTtprplPPKLPRD 728

                        250       260
                 ....*....|....*....|..
gi 410442518 596 PgvENSDSPAQReaPDGQGPGP 617
Cdd:PTZ00449 729 E--EFPFEPIGD--PDAEQPDD 746
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 52-156 1.01e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  52 AAEFLAACAGGDLDEARLMLRA-ADPgpgaeldpaappparavlDSTNADGISALHQACIDENLEVVRFLVEQGATVNQA 130
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGgADP------------------NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|....*.
gi 410442518 131 DNEGWTPLHVAASCGYLDIARYLLSH 156
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 95-171 1.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410442518  95 DSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPL 171
Cdd:PHA02875 129 DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-270 1.49e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.62  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  101 GISALHQACIDENLEVVRFLVEQGATVNQADN--------------EGWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 166
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  167 GDlplDLAESDAMEGLLKAEiarrgvDVEAAKRAEEELLLHDTRCwlnggampeaRHPRT--------GASALHVAAAKG 238
Cdd:TIGR00870 208 GN---TLLHLLVMENEFKAE------YEELSCQMYNFALSLLDKL----------RDSKElevilnhqGLTPLKLAAKEG 268

                         170       180       190
                  ....*....|....*....|....*....|....
gi 410442518  239 YIEVMRLLLQAGYdpELRDGDGWT--PLHAAAHW 270
Cdd:TIGR00870 269 RIVLFRLKLAIKY--KQKKFVAWPngQQLLSLYW 300
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-267 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.52e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 410442518  225 RTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAA 267
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-297 1.65e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 100 DGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAV-NSDGDLPLDLAESDA 178
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 179 MEGLLKAEIARRG-VDVEAAKRAeeelllhdtrcwlnggampearhprtgaSALHVAAAKGYIEVMRLLLQAGYDPELRD 257
Cdd:PHA02875 114 KLDIMKLLIARGAdPDIPNTDKF----------------------------SPLHLAVMMGDIKGIELLIDHKACLDIED 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 410442518 258 GDGWTPLHAAAHWGVEDACRLLAEHGGGMDsltHAGQRPC 297
Cdd:PHA02875 166 CCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGC 202
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-283 1.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 113 NLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAvnsdgdLPLDLAESDAMEGLLKAeiarrGV 192
Cdd:PHA02874  47 DAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIPCIEKDMIKTILDC-----GI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 193 DVEAAKRAEEELL--------LHDTRCWLNGGAMPEARHPrTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPL 264
Cdd:PHA02874 116 DVNIKDAELKTFLhyaikkgdLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                        170
                 ....*....|....*....
gi 410442518 265 HAAAHWGVEDACRLLAEHG 283
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHG 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 94-300 3.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  94 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDL 173
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 174 AesdamegllkaeiarrgvdVEAAKRAEEELLLHDTRCWLNggampearHPRTGASALHVAAAKGYIEVMRLLLQAGYDp 253
Cdd:PHA02874 197 A-------------------AEYGDYACIKLLIDHGNHIMN--------KCKNGFTPLHNAIIHNRSAIELLINNASIN- 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 410442518 254 eLRDGDGWTPLHAAAHWGVE-DACRLLAEHGGGMDSLTHAGQRPCDLA 300
Cdd:PHA02874 249 -DQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 133-162 5.21e-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: 43.40  E-value: 5.21e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 410442518  133 EGWTPLHVAASCGYLDIARYLLSHGANIAA 162
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 104-287 5.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 5.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 104 ALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGAnIAAVNSDGdlpldlAESDAMEGLL 183
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPD------IESELHDAVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 184 KAEIarrgvdveaakRAEEELLLHDTrcWLNGGAMpearhpRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTP 263
Cdd:PHA02875  78 EGDV-----------KAVEELLDLGK--FADDVFY------KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                        170       180
                 ....*....|....*....|....
gi 410442518 264 LHAAAHWGVEDACRLLAEHGGGMD 287
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLD 162
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 381-658 1.61e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  381 EGPTEPPPAEPRTLNGVSSPPHPSPKSPVLEEAPFSRRFGLLKTGSSGALGPPerrtAEGAPGAGLQRSASSSWlEGTST 460
Cdd:PHA03307   66 EPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPP----PTPPPASPPPSPAPDLS-EMLRP 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  461 QAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLENSSPPSRIPEPESPAKPNVP-TASTAPPADSRDRRRSYQMPVRDE 539
Cdd:PHA03307  141 VGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPsTPPAAASPRPPRRSSPISASASSP 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  540 ESESQRKARSRLMRQSRRSTqgvtltdlKEAEKAAGKAPESEKPAQSLDPSRRPRVPG------VENSDSPAQREAPDGQ 613
Cdd:PHA03307  221 APAPGRSAADDAGASSSDSS--------SSESSGCGWGPENECPLPRPAPITLPTRIWeasgwnGPSSRPGPASSSSSPR 292

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 410442518  614 GPGPQAAREHRKVGKEWRGPAEGEEAEPADRSQESSTLEGGPSAR 658
Cdd:PHA03307  293 ERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSR 337
PHA03247 PHA03247
large tegument protein UL36; Provisional
 312-649 1.73e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  312 ARKQEDLRNQKEASQSRGQEPQAPSSSKHRRSSVCRLSSREKISLQDLSKERRPggAGGPPIQDEDEGEEGPTEPPPAEP 391
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR--AARPTVGSLTSLADPPPPPPTPEP 2710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  392 RTLNGVSSPPHPSPKSPVLEEAPFSRRFGLLKTGSSGALGP--------------PERRTAEGAPGAGLQRSASSSWLEG 457
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPggparparppttagPPAPAPPAAPAAGPPRRLTRPAVAS 2790

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  458 TSTQAKELRLAR-------ITPTPSPKLPEPSVLSEVTKPPPCLENSSPPsriPEPESPAKPNVPTASTAPPADSRdRRR 530
Cdd:PHA03247 2791 LSESRESLPSPWdpadppaAVLAPAAALPPAASPAGPLPPPTSAQPTAPP---PPPGPPPPSLPLGGSVAPGGDVR-RRP 2866

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  531 SYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPgvenSDSPAQREAP 610
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----PPPPPRPQPP 2942

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 410442518  611 DGQGPGPQAAREHRKVGKEWRGPAEGEEAEPADRSQESS 649
Cdd:PHA03247 2943 LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQ 2981
PRK13335 PRK13335
superantigen-like protein SSL3; Reviewed;
424-542 1.94e-05

superantigen-like protein SSL3; Reviewed;


Pssm-ID: 139494 [Multi-domain]  Cd Length: 356  Bit Score: 47.43  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 424 TGSSGALGPPERRTA--EGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLenSSPPS 501
Cdd:PRK13335  60 SATTQAANTRQERTPklEKAPNTNEEKTSASKIEKISQPKQEEQKSLNISATPAPKQEQSQTTTESTTPKTKV--TTPPS 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 410442518 502 -RIPEPESPAKPNVPTASTAPPADS------RDRRRSYQMPVRDEESE 542
Cdd:PRK13335 138 tNTPQPMQSTKSDTPQSPTIKQAQTdmtpkyEDLRAYYTKPSFEFEKQ 185
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-141 2.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 410442518   94 LDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVA 141
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-171 3.13e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVNQA-----------DNE---GWTPLHVAASCGYLDIARYLLSHGANIAAVNSD 166
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*
gi 410442518 167 GDLPL 171
Cdd:cd22192  169 GNTVL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-252 5.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 100 DGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAesdam 179
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA----- 175

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410442518 180 egllkaeIARRGVDVeaakraeeelllhdTRCWLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYD 252
Cdd:PHA02875 176 -------MAKGDIAI--------------CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02795 PHA02795
ankyrin-like protein; Provisional
 114-174 6.27e-05

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 46.14  E-value: 6.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410442518 114 LEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVA 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-268 7.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 7.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  94 LDSTNADGISA--------------LHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLD-IARYLLSHGA 158
Cdd:PHA02876 219 VDSKNIDTIKAiidnrsninkndlsLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 159 NIAAVNSDGDLPLDLAESDAMEGLLKAEIARRGVDVEAAKRaeeellLHDTrcwlnggampearhPRTGASALhvaaaKG 238
Cdd:PHA02876 299 DVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADR------LYIT--------------PLHQASTL-----DR 353

                        170       180       190
                 ....*....|....*....|....*....|
gi 410442518 239 YIEVMRLLLQAGYDPELRDGDGWTPLHAAA 268
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCDKTPIHYAA 383
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 93-174 9.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 9.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  93 VLDSTN------ADGISALHQACIdENLEVVRFLVEQgATVNQADNEGWTPLHVAAS--CGyLDIARYLLSHGANIAAVN 164
Cdd:PHA02874 209 LIDHGNhimnkcKNGFTPLHNAII-HNRSAIELLINN-ASINDQDIDGSTPLHHAINppCD-IDIIDILLYHKADISIKD 285

                         90
                 ....*....|
gi 410442518 165 SDGDLPLDLA 174
Cdd:PHA02874 286 NKGENPIDTA 295
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-128 1.09e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 1.09e-04
                          10        20
                  ....*....|....*....|....*....
gi 410442518  100 DGISALHQACIDENLEVVRFLVEQGATVN 128
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-132 1.17e-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: 39.97  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 410442518  100 DGISALHQACIDE-NLEVVRFLVEQGATVNQADN 132
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 235-300 1.32e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518 235 AAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLA 300
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 112-268 1.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 112 ENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEIARRG 191
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 192 ---------VDVEAAKRAEEELLLHDTRCWLNG----------------------------GAMPEARHPRtGASALHVA 234
Cdd:PHA02876 236 ninkndlslLKAIRNEDLETSLLLYDAGFSVNSiddckntplhhasqapslsrlvpkllerGADVNAKNIK-GETPLYLM 314

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 410442518 235 AAKGY-IEVMRLLLQAGYDPELRDGDGWTPLHAAA 268
Cdd:PHA02876 315 AKNGYdTENIRTLIMLGADVNAADRLYITPLHQAS 349
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
686-780 1.61e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 686 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPAllELERFERR--ALERkaaELEEELKALSDLRADNQR 763
Cdd:COG2433  423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR--EISRLDREieRLER---ELEEERERIEELKRKLER 497

                         90       100
                 ....*....|....*....|....
gi 410442518 764 LKD-------ENAALIRVISKLSK 780
Cdd:COG2433  498 LKElwklehsGELVPVKVVEKFTK 521
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-257 1.62e-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: 39.58  E-value: 1.62e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 410442518  227 GASALHVAAAK-GYIEVMRLLLQAGYDPELRD 257
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 114-167 1.95e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 1.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 410442518 114 LEVVRFLVEQGATVNQADNEGWTPLHVAASCGY---LDIARYLLSHGANIAAVNSDG 167
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDG 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-131 2.01e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 2.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410442518   57 AACAGGDLDEARLMLRAADpgpgaeldpaappparavLDSTNaDGISALHQACIDENLEVVRFLVEQGATVNQAD 131
Cdd:pfam12796  36 LAAKNGHLEIVKLLLEHAD------------------VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 683-780 2.52e-04

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: 43.98  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 683 TLYAELRRENERLREALTETTLRLAQLKVELERATQRQERF-----AERPALLELERFERRALERKAAELEEELKALSDL 757
Cdd:COG4942  139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                         90       100
                 ....*....|....*....|...
gi 410442518 758 RADNQRLKDENAALIRVISKLSK 780
Cdd:COG4942  219 QQEAEELEALIARLEAEAAAAAE 241
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 93-171 3.77e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.13  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  93 VLDSTNADGISALHQACIDENL--EVVRFLVEQGATVNQADNEGWTPLHVAASCG--------------YLDIARYLLSH 156
Cdd:PHA02716 309 KLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLISL 388

                         90
                 ....*....|....*
gi 410442518 157 GANIAAVNSDGDLPL 171
Cdd:PHA02716 389 GADITAVNCLGYTPL 403
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 228-283 5.43e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 5.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518 228 ASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHG 283
Cdd:PLN03192 526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 436-705 6.00e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 43.35  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 436 RTAEGAPGAGL--------QRSASSSWLEGTSTQAKELRLARIT----PTPSPKLPEPSVLSEVTKPPPCLENSSPPSRI 503
Cdd:PRK12678  13 DTAPRARGGGLagmklpelRALAKQLGIKGTSGMRKGELIAAIKeargGGAAAAAATPAAPAAAARRAARAAAAARQAEQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 504 PEPESPAKP--NVPTASTAPPADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESE 581
Cdd:PRK12678  93 PAAEAAAAKaeAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDER 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 582 KPAQSLDPSRRPRVPGVENSDSPAQREAPDGQGPGPQAAREHRKVGKewrgpaEGEEAEPADRSQESStlEGGPSARRQR 661
Cdd:PRK12678 173 RRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERG------RRDGGDRRGRRRRRD--RRDARGDDNR 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 410442518 662 WQRDLNPEPEPESEEPDGGFRTLYAELRRENERLREALTETTLR 705
Cdd:PRK12678 245 EDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELR 288
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 634-780 6.25e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518   634 AEGEEAEPADRSQESSTLEGGPSARRQRWQRDLNPEPEPESEepdggFRTLYAELRRENERLREALTETTLRLAQL---- 709
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-----LREALDELRAELTLLNEEAANLRERLESLerri 833

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410442518   710 ---KVELERATQRQERFAERPALLELERFErraLERKAAELEEELKALSDLRADNQR----LKDENAALIRVISKLSK 780
Cdd:TIGR02168  834 aatERRLEDLEEQIEELSEDIESLAAEIEE---LEELIEELESELEALLNERASLEEalalLRSELEELSEELRELES 908
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 101-171 6.85e-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: 43.26  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVN-QADNE-------------GWTPLHVAASCGYLDIARYLLSH---GANIAAV 163
Cdd:cd22196   94 GQTALHIAIERRNMHLVELLVQNGADVHaRASGEffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphsPADISAR 173


                 ....*...
gi 410442518 164 NSDGDLPL 171
Cdd:cd22196  174 DSMGNTVL 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 227-255 7.32e-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: 37.57  E-value: 7.32e-04
                           10        20
                   ....*....|....*....|....*....
gi 410442518   227 GASALHVAAAKGYIEVMRLLLQAGYDPEL 255
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-265 7.33e-04

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: 43.08  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGAT-VNQADN----EGWTPLHvaascgyldiaryllshganIAAVNSDgdlpldlae 175
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALH--------------------IAVVNQN--------- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 176 sdamEGLLKAEIaRRGVDVEAAkRAEEELLLHDTRCWLNGGampeaRHPrtgasaLHVAAAKGYIEVMRLLLQAGYDPEL 255
Cdd:cd22192  102 ----LNLVRELI-ARGADVVSP-RATGTFFRPGPKNLIYYG-----EHP------LSFAACVGNEEIVRLLIEHGADIRA 164

                        170
                 ....*....|
gi 410442518 256 RDGDGWTPLH 265
Cdd:cd22192  165 QDSLGNTVLH 174
PHA02798 PHA02798
ankyrin-like protein; Provisional
 111-171 7.89e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 7.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518 111 DENLEVVRFLVEQGATVNQADNEGWTPLHVAASC-----GYLDIARYLLSHGANIAAVNSDGDLPL 171
Cdd:PHA02798  48 SPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPL 113
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-164 8.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 8.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410442518  94 LDSTNADGISALHQA-CIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVN 164
Cdd:PHA02876 334 VNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 101-267 9.44e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.53  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVN-QADNE------------GWTPLHVAASCGYLDIARYLLSHGANIAAV---N 164
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHaRACGRffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLqaqD 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 165 SDGDLPL--------DLAESDAMEGLLKAEIARRGVDVEAAKRAEEelllhdtrcwlnggaMPEarhpRTGASALHVAAA 236
Cdd:cd22197  174 SLGNTVLhalvmiadNSPENSALVIKMYDGLLQAGARLCPTVQLEE---------------ISN----HEGLTPLKLAAK 234

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 410442518 237 KGYIEVMRLLLQ----AGYDPELRDGDGWT--PLHAA 267
Cdd:cd22197  235 EGKIEIFRHILQrefsGPYQHLSRKFTEWCygPVRVS 271
PHA03247 PHA03247
large tegument protein UL36; Provisional
 471-661 1.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  471 TPTPSPKLPEPSVLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTAstAPPADSRDRRRSYQMPVRDEESESQRKARSR 550
Cdd:PHA03247 2570 PPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSP--LPPDTHAPDPPPPSPSPAANEPDPHPPPTVP 2647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  551 LMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENS-DSPAQREAPDGQGPGPQAAREHRKVGKE 629
Cdd:PHA03247 2648 PPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLaDPPPPPPTPEPAPHALVSATPLPPGPAA 2727

                         170       180       190
                  ....*....|....*....|....*....|..
gi 410442518  630 WRGPAEGEEAEPADRSQESSTLEGGPSARRQR 661
Cdd:PHA03247 2728 ARQASPALPAAPAPPAVPAGPATPGGPARPAR 2759
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 694-771 1.14e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.69  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  694 RLREALTETTLR---LAQLKVELERATQRQERF--AERPALLELERfERRALERKAAELEEELKALSDLradNQRLKDEN 768
Cdd:pfam08614  61 QLREELAELYRSrgeLAQRLVDLNEELQELEKKlrEDERRLAALEA-ERAQLEEKLKDREEELREKRKL---NQDLQDEL 136


                  ...
gi 410442518  769 AAL 771
Cdd:pfam08614 137 VAL 139
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 101-256 1.21e-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: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 101 GISALHQACIDENLEVVRFLVEQGATVNQADNE--------------GWTPLHVAASCGYLDIARYLLSHG---ANIAAV 163
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 164 NSDGDLPLdlaesDAMegllkAEIARRGVDVEA-AKRAEEELLLHDTRcWLNGGAMPEARHpRTGASALHVAAAKGYIEV 242
Cdd:cd22193  156 DSRGNTVL-----HAL-----VTVADNTKENTKfVTRMYDMILIRGAK-LCPTVELEEIRN-NDGLTPLQLAAKMGKIEI 223

                        170
                 ....*....|....*
gi 410442518 243 MRLLLQAGY-DPELR 256
Cdd:cd22193  224 LKYILQREIkEPELR 238
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-128 1.24e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.24e-03
                           10        20
                   ....*....|....*....|....*....
gi 410442518   100 DGISALHQACIDENLEVVRFLVEQGATVN 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 686-778 1.27e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 686 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERFE-RRALERKAAELEEELKALSDLRADNQRL 764
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaEEALLEAEAELAEAEEELEELAEELLEA 391

                         90
                 ....*....|....
gi 410442518 765 KDENAALIRVISKL 778
Cdd:COG1196  392 LRAAAELAAQLEEL 405
PHA03247 PHA03247
large tegument protein UL36; Provisional
 360-660 1.29e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  360 SKERRPGGAGGP-----PIQDEDE--GEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVLEEAPFSRRFGLLKTGSSGALGP 432
Cdd:PHA03247 2584 SRARRPDAPPQSarpraPVDDRGDprGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSR 2663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  433 PERRTAEGAPgaglqrSASSSWLEGTSTQAKELRLARIT----PTPSPKLPEPSVLSEVTKPP-PCLENSSPPSRIPEPE 507
Cdd:PHA03247 2664 PRRARRLGRA------AQASSPPQRPRRRAARPTVGSLTsladPPPPPPTPEPAPHALVSATPlPPGPAAARQASPALPA 2737

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  508 SPAKPNVPTASTAPPADSR-DRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQS 586
Cdd:PHA03247 2738 APAPPAVPAGPATPGGPARpARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410442518  587 LDPSRRPrVPGVENSDSPAQREAPDGQGPGPQAAREHRKVGK----EWRGPAEGEEAEPADRSQESSTLEGGPSARRQ 660
Cdd:PHA03247 2818 LPPAASP-AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPggdvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRS 2894
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 108-171 1.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 410442518 108 ACIDE---NLEVVRFLVEQGATVN-QADNEGWTPLHvaascGYL--------DIARYLLSHGANIAAVNSDGDLPL 171
Cdd:PHA02859  57 SCLEKdkvNVEILKFLIENGADVNfKTRDNNLSALH-----HYLsfnknvepEILKILIDSGSSITEEDEDGKNLL 127
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 97-168 1.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  97 TNADGISALHQ-ACIDENL--EVVRFLVEQGATVNQADNEGWTPLHVaascgYLD-------IARYLLSHGANIAAVNSD 166
Cdd:PHA02859  83 TRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM-----YMCnfnvrinVIKLLIDSGVSFLNKDFD 157


                 ..
gi 410442518 167 GD 168
Cdd:PHA02859 158 NN 159
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 682-779 1.97e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 682 RTLYAELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpaLLELERFERRALERKAAELEEELKALSDLRADN 761
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER--LEELEEELAELEEELEELEEELEELEEELEEAE 350

                         90
                 ....*....|....*...
gi 410442518 762 QRLKDENAALIRVISKLS 779
Cdd:COG1196  351 EELEEAEAELAEAEEALL 368
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 103-174 2.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 410442518 103 SALHQACIDEN-LEVVRFLVEQGATVNQADNEGWTPLHVAA--SCGyLDIARYLLSHGANIAAVNSDGDLPLDLA 174
Cdd:PHA02876 410 TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACkkNCK-LDVIEMLLDNGADVNAINIQNQYPLLIA 483
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 360-542 3.60e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 360 SKERRPGGAGGPPIQDEDEGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVLE--------------EAPFSRRFGLLKTG 425
Cdd:PRK07764 610 EEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDasdggdgwpakaggAAPAAPPPAPAPAA 689

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 426 SSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEP------SVLSEVTKPPPCLENSSP 499
Cdd:PRK07764 690 PAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPddppdpAGAPAQPPPPPAPAPAAA 769

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 410442518 500 PSRIPEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRDEESE 542
Cdd:PRK07764 770 PAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAEEVAMELLEEE 812
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
685-776 3.71e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 685 YAELRRENERLREALTETTLRLAQLKVE---LERATQRQERFAERPALL-ELERFERR--ALERKAAELEEELKALSDLR 758
Cdd:COG4717   90 YAELQEELEELEEELEELEAELEELREElekLEKLLQLLPLYQELEALEaELAELPERleELEERLEELRELEEELEELE 169

                         90
                 ....*....|....*...
gi 410442518 759 ADNQRLKDENAALIRVIS 776
Cdd:COG4717  170 AELAELQEELEELLEQLS 187
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 685-779 3.99e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 685 YAELRRENERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKALSDLRAD-NQR 763
Cdd:COG1196  290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEEELEELEEELEEAEEELEEAEAELAEaEEA 366

                         90
                 ....*....|....*.
gi 410442518 764 LKDENAALIRVISKLS 779
Cdd:COG1196  367 LLEAEAELAEAEEELE 382
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 686-778 7.12e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 686 AELRRENERLREALTETTLRLAQLKVELERATQRQERF-AERPALLELERFERRALERKAAELEEELKALSDLRADNQRL 764
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                         90
                 ....*....|....
gi 410442518 765 KDENAALIRVISKL 778
Cdd:COG1196  462 LELLAELLEEAALL 475
PTZ00121 PTZ00121
MAEBL; Provisional
 175-773 7.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  175 ESDAMEGLLKAEIARRGVDV---EAAKRAEEELLLHDTRCWLNGGAMPEARH---PRTGASALHVAAAKGYIEVMRLllq 248
Cdd:PTZ00121 1114 ARKAEEAKKKAEDARKAEEArkaEDARKAEEARKAEDAKRVEIARKAEDARKaeeARKAEDAKKAEAARKAEEVRKA--- 1190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  249 agydPELRDGDGWTPLHAAAHWgvEDACRLLAEHGGGMDSLTHAGQRPCDLADEEVLSLLEELARKQEDLRNQKEASQSR 328
Cdd:PTZ00121 1191 ----EELRKAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  329 GQEPQAPSSSKHRRSSVCRLSSREKISLQDLSKERRpggaggppIQDEDEGEEGPTEPPPAEPRTLNGVSSPPHPSPKSP 408
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE--------KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  409 VLEEApfsRRFGLLKTGSSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSvlSEVT 488
Cdd:PTZ00121 1337 KAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA--DELK 1411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  489 KPPPCLENSSPPSRIPEPESPAKPNVPTASTAPPAD-----SRDRRRSYQMPVRDEESESQRKARSRLmrqsrrstqgvt 563
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADeakkkAEEAKKAEEAKKKAEEAKKADEAKKKA------------ 1479

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  564 lTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQREAPDGQGPGPQAAREHRKVGKEWRGPAEGEEAEPAD 643
Cdd:PTZ00121 1480 -EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK 1558

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518  644 RSQESSTLEggpSARRQRWQRDLNPEPEPESEEpdggfrtlyAELRRENERLREALTETTLRLAQLKVELERATQRQErf 723
Cdd:PTZ00121 1559 KAEEKKKAE---EAKKAEEDKNMALRKAEEAKK---------AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-- 1624

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 410442518  724 aerpalLELERFERRALERKAAELEEELKALSDLRADNQRLKDENAALIR 773
Cdd:PTZ00121 1625 ------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 259-283 7.80e-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: 34.57  E-value: 7.80e-03
                          10        20
                  ....*....|....*....|....*.
gi 410442518  259 DGWTPLHAAA-HWGVEDACRLLAEHG 283
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKG 26
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 693-770 8.46e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 8.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410442518  693 ERLREALTETTLRLAQLKVELERATQRQERFAERpalLELERFERRALERKAAELEEELKAlsdLRADNQRLKDENAA 770
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQAL---AEAQQQELVALEGLAAELEEKQQE---LEAQLEQLQEKAAE 209
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 686-770 9.35e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410442518 686 AELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERF----ERRALERKAAELEEELKALSDLRADN 761
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEeaeeELEEAEAELAEAEEALLEAEAELAEA 377


                 ....*....
gi 410442518 762 QRLKDENAA 770
Cdd:COG1196  378 EEELEELAE 386
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH