NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|808355035|ref|NP_001293416|]
View 

non-specific serine/threonine protein kinase [Caenorhabditis elegans]

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
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-281 3.12e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 3.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   45 VAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHL 124
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  125 RNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASK 204
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355035  205 HGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 281
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 908-990 3.19e-37

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260052  Cd Length: 82  Bit Score: 134.39  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  908 ASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSL-SRTDQLLNEWAIHHPeqASVGNLCRILVELGRCDAR 986
Cdd:cd08782     1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLpSPTDRLLQEWTARPP--STIGALLRKLRELGRRDAA 78


                  ....
gi 808355035  987 DALY 990
Cdd:cd08782    79 DFLL 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-73 2.59e-09

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 2.59e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355035     1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVAnEKIDVDSINKtGETALHCAVES 73
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARS 71
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 381-499 1.67e-07

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd09914:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 161  Bit Score: 51.95  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  381 GSKYaPPHSQYTRGIDVQTVNI----NGCGEFSVWEFGGYEPMHTCYDHFVGNAdCIHLILYRTSDPTEVQykQILYWMN 456
Cdd:cd09914    23 GEKF-DGDESSTHGINVQDWKIpapeRKKIRLNVWDFGGQEIYHATHQFFLTSR-SLYLLVFDLRTGDEVS--RVPYWLR 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 808355035  457 FLKGRvtpfepighcgfsSRRSKVIIVGTHATSSLFPQMNQEG 499
Cdd:cd09914    99 QIKAF-------------GGVSPVILVGTHIDESCDEDILKKA 128
COR super family cl24610
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
 573-763 3.88e-04

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


The actual alignment was detected with superfamily member pfam16095:

Pssm-ID: 406489  Cd Length: 196  Bit Score: 42.62  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   573 NLVRKKHANFPVITWPDFIQLVRNeiNPLTGDAHCRQIVQQLQLIGELVYLRNDLCDADYVVLNAEWfgthiLGQLLSAE 652
Cdd:pfam16095    9 EALEKERQKKPYISYEEYRKICAE--NGIDDEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVILNPQW-----LTNAVYRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   653 FLSKASPN--GSYHTSSLAKIFPEIP----EQSDLMTILEVLQLC--APDARTGAHEFPVFIQTEAPDSIWRPYSlkeke 724
Cdd:pfam16095   82 LDSKHVLNnnGILTHEDLEQIWKDPGypreLHPYLLRLMEKFELCyeLPGDEEGTYLVPQLLPENPPELYDWDEE----- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 808355035   725 rdtvyggvRILPMRGMERSLH-STFPRIQVALRRSINDYQ 763
Cdd:pfam16095  157 --------NNLELRYQYDFLPkGIFSRLIVRLHKFIDDEL 188
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-281 3.12e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 3.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   45 VAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHL 124
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  125 RNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASK 204
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355035  205 HGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 281
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 908-990 3.19e-37

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260052  Cd Length: 82  Bit Score: 134.39  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  908 ASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSL-SRTDQLLNEWAIHHPeqASVGNLCRILVELGRCDAR 986
Cdd:cd08782     1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLpSPTDRLLQEWTARPP--STIGALLRKLRELGRRDAA 78


                  ....
gi 808355035  987 DALY 990
Cdd:cd08782    79 DFLL 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
133-225 2.71e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   133 LHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNgCDINHADhHGDTALHIASKHGLLQAVQ 212
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 808355035   213 TLCHCAVTVDSVN 225
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-270 9.61e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.47  E-value: 9.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   10 AEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVA---NEKIDVDSINKTGETALHCAVESADT-RVVRLLLQL 85
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRlllEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   86 RPRLDLPNASGDTVLH--LAADSINPRIVPLLVCLAPPLHLRNIREETPLHV--AAARGHVDCVQALLDANSPIDAVEQD 161
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  162 GKTALIIALEN--GNVDIASILITNGCDINHADHHGDTALHIASKHGLLQA--VQTLCHCAVTVDSVNANKKTALHLAAH 237
Cdd:PHA03095  187 FRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAV 266

                         250       260       270
                  ....*....|....*....|....*....|...
gi 808355035  238 YGHVDIIRVLLLARADVTLRGDDGLTAELVAVA 270
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
Death pfam00531
Death domain;
910-993 7.38e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 79.33  E-value: 7.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   910 RCELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDST----GQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 985
Cdd:pfam00531    1 RKQLDRLLDPPPPLGKDWRELARKLGLSEN--EIDEIesenPRLRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78


                   ....*...
gi 808355035   986 RDALYRTV 993
Cdd:pfam00531   79 AEKIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 906-992 2.42e-16

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 75.14  E-value: 2.42e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    906 QMASRCELACLLDPPhaMGRDWSILAVKLQLTDQVPDVDSTGQS---LSRTDQLLNEWAIHHPEQASVGNLCRILVELGR 982
Cdd:smart00005    1 PELTRQKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTEAPrdlAEQSVQLLRLWEQREGKNATLGTLLEALRKMGR 78

                            90
                    ....*....|
gi 808355035    983 CDARDALYRT 992
Cdd:smart00005   79 DDAVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-73 2.59e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 2.59e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355035     1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVAnEKIDVDSINKtGETALHCAVES 73
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARS 71
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 381-499 1.67e-07

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 51.95  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  381 GSKYaPPHSQYTRGIDVQTVNI----NGCGEFSVWEFGGYEPMHTCYDHFVGNAdCIHLILYRTSDPTEVQykQILYWMN 456
Cdd:cd09914    23 GEKF-DGDESSTHGINVQDWKIpapeRKKIRLNVWDFGGQEIYHATHQFFLTSR-SLYLLVFDLRTGDEVS--RVPYWLR 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 808355035  457 FLKGRvtpfepighcgfsSRRSKVIIVGTHATSSLFPQMNQEG 499
Cdd:cd09914    99 QIKAF-------------GGVSPVILVGTHIDESCDEDILKKA 128
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-262 2.96e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  114 LLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDA-----NSPIDAVEQDGKTALIIALENGNVDIASILITNGCDI 188
Cdd:cd22192    36 LLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADV 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355035  189 NHADHHGdTALHiASKHGLlqavqtlCHCAVTVdsvnankktaLHLAAHYGHVDIIRVLLLARADvtLRGDDGL 262
Cdd:cd22192   116 VSPRATG-TFFR-PGPKNL-------IYYGEHP----------LSFAACVGNEEIVRLLIEHGAD--IRAQDSL 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 136-257 6.35e-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: 50.08  E-value: 6.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   136 AAARGHVDCVQALLDANSP--IDAVEQDGKTALI-IALENGNVDIASILITNGCDInhadHHGDTALHIASKhGLLQAVQ 212
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFvAAIENENLELTELLLNLSCRG----AVGDTLLHAISL-EYVDAVE 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 808355035   213 -TLCH------CAVTVDSVNANKK-------TALHLAAHYGHVDIIRVLLLARADVTLR 257
Cdd:TIGR00870   99 aILLHllaafrKSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
 573-763 3.88e-04

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 42.62  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   573 NLVRKKHANFPVITWPDFIQLVRNeiNPLTGDAHCRQIVQQLQLIGELVYLRNDLCDADYVVLNAEWfgthiLGQLLSAE 652
Cdd:pfam16095    9 EALEKERQKKPYISYEEYRKICAE--NGIDDEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVILNPQW-----LTNAVYRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   653 FLSKASPN--GSYHTSSLAKIFPEIP----EQSDLMTILEVLQLC--APDARTGAHEFPVFIQTEAPDSIWRPYSlkeke 724
Cdd:pfam16095   82 LDSKHVLNnnGILTHEDLEQIWKDPGypreLHPYLLRLMEKFELCyeLPGDEEGTYLVPQLLPENPPELYDWDEE----- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 808355035   725 rdtvyggvRILPMRGMERSLH-STFPRIQVALRRSINDYQ 763
Cdd:pfam16095  157 --------NNLELRYQYDFLPkGIFSRLIVRLHKFIDDEL 188
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 161-189 8.72e-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: 8.72e-04
                            10        20
                    ....*....|....*....|....*....
gi 808355035    161 DGKTALIIALENGNVDIASILITNGCDIN 189
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-62 1.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355035    2 HCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKT 62
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 387-486 3.77e-03

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 38.26  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   387 PHSQYTRGIDV---QTVNINGCGE---FSVWEFGGYEPMHTCYDHFVGNADCIhLILYrtsDPTEvqYKQILYWMNFLKg 460
Cdd:pfam08477   26 PKYKSTIGVDFktkTVLENDDNGKkikLNIWDTAGQERFRSLHPFYYRGAAAA-LLVY---DSRT--FSNLKYWLRELK- 98

                           90       100
                   ....*....|....*....|....*.
gi 808355035   461 rvtpfepiGHCGfssrRSKVIIVGTH 486
Cdd:pfam08477   99 --------KYAG----NSPVILVGNK 112
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
45-281 3.12e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 3.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   45 VAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHL 124
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  125 RNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASK 204
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355035  205 HGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 281
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-281 4.33e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 4.33e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   17 HMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASG 96
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   97 DTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVD 176
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  177 IASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTL 256
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                         250       260
                  ....*....|....*....|....*
gi 808355035  257 RGDDGLTAELVAVAAERLEAHSLLK 281
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-264 9.07e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 9.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    4 AAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLL 83
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   84 QLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGK 163
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  164 TALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDI 243
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                         250       260
                  ....*....|....*....|.
gi 808355035  244 IRVLLLARADVTLRGDDGLTA 264
Cdd:COG0666   268 VKLLLLALLLLAAALLDLLTL 288
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 908-990 3.19e-37

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260052  Cd Length: 82  Bit Score: 134.39  E-value: 3.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  908 ASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSL-SRTDQLLNEWAIHHPeqASVGNLCRILVELGRCDAR 986
Cdd:cd08782     1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLpSPTDRLLQEWTARPP--STIGALLRKLRELGRRDAA 78


                  ....
gi 808355035  987 DALY 990
Cdd:cd08782    79 DFLL 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
133-225 2.71e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   133 LHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNgCDINHADhHGDTALHIASKHGLLQAVQ 212
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 808355035   213 TLCHCAVTVDSVN 225
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-257 3.26e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   166 LIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLC-HCAVTVDSvnaNKKTALHLAAHYGHVDII 244
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVNLKD---NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|...
gi 808355035   245 RVLLLARADVTLR 257
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-270 9.61e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.47  E-value: 9.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   10 AEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVA---NEKIDVDSINKTGETALHCAVESADT-RVVRLLLQL 85
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRlllEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   86 RPRLDLPNASGDTVLH--LAADSINPRIVPLLVCLAPPLHLRNIREETPLHV--AAARGHVDCVQALLDANSPIDAVEQD 161
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  162 GKTALIIALEN--GNVDIASILITNGCDINHADHHGDTALHIASKHGLLQA--VQTLCHCAVTVDSVNANKKTALHLAAH 237
Cdd:PHA03095  187 FRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAV 266

                         250       260       270
                  ....*....|....*....|....*....|...
gi 808355035  238 YGHVDIIRVLLLARADVTLRGDDGLTAELVAVA 270
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
Ank_2 pfam12796
Ankyrin repeats (3 copies);
100-192 4.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   100 LHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDaNSPIDAVEqDGKTALIIALENGNVDIAS 179
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 808355035   180 ILITNGCDINHAD 192
Cdd:pfam12796   79 LLLEKGADINVKD 91
Death pfam00531
Death domain;
910-993 7.38e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 79.33  E-value: 7.38e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   910 RCELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDST----GQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 985
Cdd:pfam00531    1 RKQLDRLLDPPPPLGKDWRELARKLGLSEN--EIDEIesenPRLRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78


                   ....*...
gi 808355035   986 RDALYRTV 993
Cdd:pfam00531   79 AEKIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 906-992 2.42e-16

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 75.14  E-value: 2.42e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    906 QMASRCELACLLDPPhaMGRDWSILAVKLQLTDQVPDVDSTGQS---LSRTDQLLNEWAIHHPEQASVGNLCRILVELGR 982
Cdd:smart00005    1 PELTRQKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTEAPrdlAEQSVQLLRLWEQREGKNATLGTLLEALRKMGR 78

                            90
                    ....*....|
gi 808355035    983 CDARDALYRT 992
Cdd:smart00005   79 DDAVELLRSE 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-258 1.96e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   19 KGGNICARDDNGDTPLHVACR--FAQHTVAGYVANEKIDVDSINKTGETALHCAVES--ADTRVVRLLLQLRPRLDLPNA 94
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSrnANVELLRLLIDAGADVYAVDD 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   95 SGDTVLHLAADSI--NPRIVPLLVCLAPPLHLRNIREETPLHVAAArgHVDC----VQALLDANSPIDAVEQDGKTALII 168
Cdd:PHA03095  186 RFRSLLHHHLQSFkpRARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCkrslVLPLLIAGISINARNRYGQTPLHY 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  169 ALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNAnkktALHLAAHYGHVDIIRVLL 248
Cdd:PHA03095  264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDIPSDATR 339

                         250
                  ....*....|
gi 808355035  249 LARADVTLRG 258
Cdd:PHA03095  340 LCVAKVVLRG 349
Ank_2 pfam12796
Ankyrin repeats (3 copies);
199-276 1.11e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.11e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355035   199 LHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRvLLLARADVTLRgDDGLTAELVAVAAERLEA 276
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLK-DNGRTALHYAARSGHLEI 76
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-314 5.08e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 5.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  108 NPRIVPLLVCLAPPLHLRNIREETPLHVAAAR--GHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVD--IASILIT 183
Cdd:PHA03100   85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLID 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  184 NGCDINHADHhgdtalhiaskhgllqaVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLT 263
Cdd:PHA03100  165 KGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808355035  264 AELVAVAAERLE-AHSLLKMVKSQEIREEYISQL--YPLDTslrRIKLKLLGHS 314
Cdd:PHA03100  228 PLHIAILNNNKEiFKLLLNNGPSIKTIIETLLYFkdKDLNT---ITKIKMLKKS 278
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-248 5.95e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   20 GGNICARDDNGDTPLHVACRFAQHT-VAGYVANEKIDVDSINKTGETALHCAVESA-DTRVVRLLLQLRPRLDLPNASGD 97
Cdd:PHA02876  263 GFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYI 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   98 TVLHLAAD-SINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVD 176
Cdd:PHA02876  343 TPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPY 422

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355035  177 IA-SILITNGCDINHADHHGDTALHIASKHGL-LQAVQTLCHCAVTVDSVNANKKTALHLAAHYGhvDIIRVLL 248
Cdd:PHA02876  423 MSvKTLIDRGANVNSKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILL 494
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 19-192 9.64e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 9.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   19 KGGNICARDDNGDTPLHVA--CRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVvrlllqlrprldlpnasg 96
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL------------------ 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   97 dTVLHL---------AADSINprivpLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALI 167
Cdd:PHA03100  157 -KILKLlidkgvdinAKNRVN-----YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230

                         170       180
                  ....*....|....*....|....*
gi 808355035  168 IALENGNVDIASILITNGCDINHAD 192
Cdd:PHA03100  231 IAILNNNKEIFKLLLNNGPSIKTII 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 4-309 4.40e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    4 AAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKID-----VDSINK-TGETALHCAVEsADTR 77
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpIPCIEKdMIKTILDCGID-VNIK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   78 vvrlllqlrprldlpNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDA 157
Cdd:PHA02874  121 ---------------DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  158 VEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGlLQAVQTLCHCAvTVDSVNANKKTALHLAAH 237
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLINNA-SINDQDIDGSTPLHHAIN 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355035  238 YG-HVDIIRVLLLARADVTLRGDDGltAELVAVAAERLEAHSLLKMVKSQEIREEYISQLyPLDTSLRRIKLK 309
Cdd:PHA02874  264 PPcDIDIIDILLYHKADISIKDNKG--ENPIDTAFKYINKDPVIKDIIANAVLIKEADKL-KDSDFLEHIEIK 333
PHA03095 PHA03095
ankyrin-like protein; Provisional
 102-264 4.72e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  102 LAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDC---VQALLDANSPIDAVEQDGKTALIIALENGNV-DI 177
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  178 ASILITNGCDINHADHHGDTALHI--ASKHGLLQAVQTLCHCAVTVDSVNANKKTALH--LAAHYGHVDIIRVLLLARAD 253
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGAD 179

                         170
                  ....*....|.
gi 808355035  254 VTLRGDDGLTA 264
Cdd:PHA03095  180 VYAVDDRFRSL 190
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 130-280 5.08e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  130 ETPLHVAAARGHVDCVQALLDANSPIDAV-EQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLL 208
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355035  209 QAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDG-LTAELVAVAAERLEAHSLL 280
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 136-314 9.62e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 9.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  136 AAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTAL--HIASKHGllQAVQT 213
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAISAKHH--KIFRI 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  214 LCHCAVTVDSVNANKktALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLKMVKSQEIREEYI 293
Cdd:PLN03192  610 LYHFASISDPHAAGD--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687

                         170       180
                  ....*....|....*....|..
gi 808355035  294 SQLYPldTSLRR-IKLKLLGHS 314
Cdd:PLN03192  688 DDFSP--TELRElLQKRELGHS 707
Ank_4 pfam13637
Ankyrin repeats (many copies);
131-182 1.31e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 808355035   131 TPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILI 182
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-73 2.59e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 2.59e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355035     1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVAnEKIDVDSINKtGETALHCAVES 73
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARS 71
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-189 5.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 5.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   57 DSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVA 136
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808355035  137 AARGHVDCVQALLDANSPIDAVEQDGK-TALIIALENGNVDIASILITNGCDIN 189
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 29-199 5.69e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 5.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   29 NGDTPLHVACRFaQHTVAGYVANEKIDVDSINKTG-ETALHCAVESADTRVVRLLLQLRPRLDLP-NASGDTVLHLAADS 106
Cdd:PHA02875   34 DGISPIKLAMKF-RDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATIL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  107 INPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGC 186
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192

                         170
                  ....*....|...
gi 808355035  187 DINHADHHGDTAL 199
Cdd:PHA02875  193 NIDYFGKNGCVAA 205
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-179 1.27e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    2 HCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTV--------AGyvaNEKIDVDSInktGETALHCAVES 73
Cdd:PHA03095  124 YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVellrllidAG---ADVYAVDDR---FRSLLHHHLQS 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   74 ADTR--VVRLLLQLRPRLDLPNASGDTVLHLAADSINPR---IVPLLVCLApPLHLRNIREETPLHVAAARGHVDCVQAL 148
Cdd:PHA03095  198 FKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrslVLPLLIAGI-SINARNRYGQTPLHYAAVFNNPRACRRL 276

                         170       180       190
                  ....*....|....*....|....*....|.
gi 808355035  149 LDANSPIDAVEQDGKTALIIALENGNVDIAS 179
Cdd:PHA03095  277 IALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 53-226 2.10e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   53 KIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLApplhlrniREETP 132
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA--------SISDP 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  133 ------LHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDtaLHIASKHG 206
Cdd:PLN03192  620 haagdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD--FSPTELRE 697

                         170       180
                  ....*....|....*....|
gi 808355035  207 LLQAvQTLCHCAVTVDSVNA 226
Cdd:PLN03192  698 LLQK-RELGHSITIVDSVPA 716
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-197 6.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVVR 80
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   81 LLLQLRPRLDLPNASGDTVLHLAAdSINPRIVPLLVCLApPLHLRNIREETPLHVAAARG-HVDCVQALLDANSPIDAVE 159
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINNA-SINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 808355035  160 QDGKTALIIALENGNVD-IASILITNGCDINHADHHGDT 197
Cdd:PHA02874  286 NKGENPIDTAFKYINKDpVIKDIIANAVLIKEADKLKDS 324
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 19-254 1.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   19 KGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDlpnaSGDT 98
Cdd:PHA02876  167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   99 VLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVD-CVQALLDANSPIDAVEQDGKTALIIALENG-NVD 176
Cdd:PHA02876  243 SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTE 322

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355035  177 IASILITNGCDINHADHHGDTALHIASKHGLLQ-AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADV 254
Cdd:PHA02876  323 NIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 909-984 1.32e-07

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260026  Cd Length: 79  Bit Score: 49.91  E-value: 1.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355035  909 SRCELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDSTGQSLSRTDQLLNEWAIHHPEqASVGNLCRILVELGRCD 984
Cdd:cd08312     1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYL--EIRNFERQSSPTERLLEDWETRPPG-ATVGNLLEILEELERKD 73
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-176 1.33e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   10 AEVFNYFHMKGGNICARDDNGDTPLHVACRFAqHTVAGYV---ANEKIDVDSINKTGETALHCAVESADTR--VVRLLLQ 84
Cdd:PHA03095  167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQSF-KPRARIVrelIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLI 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   85 LRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQdgkt 164
Cdd:PHA03095  246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA---- 321

                         170
                  ....*....|..
gi 808355035  165 ALIIALENGNVD 176
Cdd:PHA03095  322 TLNTASVAGGDI 333
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 381-499 1.67e-07

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 51.95  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  381 GSKYaPPHSQYTRGIDVQTVNI----NGCGEFSVWEFGGYEPMHTCYDHFVGNAdCIHLILYRTSDPTEVQykQILYWMN 456
Cdd:cd09914    23 GEKF-DGDESSTHGINVQDWKIpapeRKKIRLNVWDFGGQEIYHATHQFFLTSR-SLYLLVFDLRTGDEVS--RVPYWLR 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 808355035  457 FLKGRvtpfepighcgfsSRRSKVIIVGTHATSSLFPQMNQEG 499
Cdd:cd09914    99 QIKAF-------------GGVSPVILVGTHIDESCDEDILKKA 128
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 923-989 2.60e-07

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 49.20  E-value: 2.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  923 MGRDWSILAVKLQLTD---QVPDVDSTGQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDARDAL 989
Cdd:cd01670     9 LGRDWKKLARKLGLSEgdiDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKL 78
Ank_5 pfam13857
Ankyrin repeats (many copies);
114-169 3.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 808355035   114 LLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIA 169
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-269 3.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 3.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINktgetALHCAVESADTRVVR 80
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY-----TLVAIKDAFNNRNVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   81 LLLQLRPRLDLPNASGDTVL---HLAADSINPRIVPLLVCLAPPLHLRNI-REETPLHVAAARGHVDCVQALLDANSPID 156
Cdd:PHA02878  116 IFKIILTNRYKNIQTIDLVYidkKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  157 AVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASkhGLLQAVQTLCHCAVTVDSVNANKK----TAL 232
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDILKLLLEHGVDVNAKSYilglTAL 273

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 808355035  233 HLAAHygHVDIIRVLLLARADVTLRGDDGLTAELVAV 269
Cdd:PHA02878  274 HSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 905-989 6.45e-07

Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260051  Cd Length: 83  Bit Score: 48.04  E-value: 6.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  905 LQMASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGqslSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCD 984
Cdd:cd08781     1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDRYINYFATKP---SPTEVILDLWEARNRDDGALNSLAAILREMGRHD 77


                  ....*
gi 808355035  985 ARDAL 989
Cdd:cd08781    78 AATIL 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 101-192 7.73e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  101 HLAA--DSINPRIvpLLVCLAPPlHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIA 178
Cdd:PTZ00322   88 QLAAsgDAVGARI--LLTGGADP-NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                          90
                  ....*....|....
gi 808355035  179 SILItnGCDINHAD 192
Cdd:PTZ00322  165 QLLS--RHSQCHFE 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
164-214 9.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 9.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 808355035   164 TALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTL 214
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 110-263 2.01e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  110 RIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDIN 189
Cdd:PHA02876  159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808355035  190 hadhHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLAR-ADVTLRGDDGLT 263
Cdd:PHA02876  239 ----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERgADVNAKNIKGET 309
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-262 2.96e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  114 LLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALLDA-----NSPIDAVEQDGKTALIIALENGNVDIASILITNGCDI 188
Cdd:cd22192    36 LLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADV 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355035  189 NHADHHGdTALHiASKHGLlqavqtlCHCAVTVdsvnankktaLHLAAHYGHVDIIRVLLLARADvtLRGDDGL 262
Cdd:cd22192   116 VSPRATG-TFFR-PGPKNL-------IYYGEHP----------LSFAACVGNEEIVRLLIEHGAD--IRAQDSL 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 94-201 3.83e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 3.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   94 ASGDTVLHLAADSINPRIVPLLVCLAPPLhlrnIRE---------ETPLHVAAARGHVDCVQALL----DANSP------ 154
Cdd:cd22192    49 ALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlyqgETALHIAVVNQNLNLVRELIargaDVVSPratgtf 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808355035  155 ----IDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHI 201
Cdd:cd22192   125 frpgPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 136-257 6.35e-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: 50.08  E-value: 6.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   136 AAARGHVDCVQALLDANSP--IDAVEQDGKTALI-IALENGNVDIASILITNGCDInhadHHGDTALHIASKhGLLQAVQ 212
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFvAAIENENLELTELLLNLSCRG----AVGDTLLHAISL-EYVDAVE 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 808355035   213 -TLCH------CAVTVDSVNANKK-------TALHLAAHYGHVDIIRVLLLARADVTLR 257
Cdd:TIGR00870   99 aILLHllaafrKSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
216-264 1.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.29e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 808355035   216 HCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTA 264
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 912-990 1.56e-05

Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260025  Cd Length: 80  Bit Score: 44.20  E-value: 1.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355035  912 ELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDSTGQSLSRTDQLLNEWAihHPEQASVGNLCRILVELGRCDARDALY 990
Cdd:cd08311     6 EEVEKLLNAGREGSDWRALAGELGYSAE--EIDSFAREADPCRALLTDWS--AQDGATLGVLLTALRKIGRDDIVEILQ 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
96-149 2.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.10e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 808355035    96 GDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAARGHVDCVQALL 149
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
195-248 2.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 808355035   195 GDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLL 248
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
230-280 2.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 808355035   230 TALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 280
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 137-229 3.43e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  137 AARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCH 216
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                          90
                  ....*....|...
gi 808355035  217 CAVTVDSVNANKK 229
Cdd:PTZ00322  170 HSQCHFELGANAK 182
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-254 4.02e-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: 47.70  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  169 ALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVdsVNA-------NKKTALHLAAHYGHV 241
Cdd:cd22192    25 AKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL--VNEpmtsdlyQGETALHIAVVNQNL 102

                          90
                  ....*....|...
gi 808355035  242 DIIRVLLLARADV 254
Cdd:cd22192   103 NLVRELIARGADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 178-248 5.53e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355035  178 ASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLL 248
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
1-48 8.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 8.48e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 808355035     1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGY 48
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 145-273 9.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 9.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  145 VQALLDANSPIDAVEQD-GKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDS 223
Cdd:PHA02878  150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808355035  224 VNANKKTALHLAAHY-GHVDIIRVLLLARADVTLRGD-DGLTAELVAVAAER 273
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER 281
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 143-200 1.53e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  143 DCVQALLDANSPIDAVEQDGKTALIIALENGNV--DIASILITNGCDINHADHHGDTALH 200
Cdd:PHA02859  104 EILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSGVSFLNKDFDNNNILY 163
Ank_5 pfam13857
Ankyrin repeats (many copies);
148-202 2.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.63e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 808355035   148 LLDANSP-IDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIA 202
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
 904-989 3.27e-04

Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260023  Cd Length: 88  Bit Score: 40.41  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  904 DLQMASRCELACLLDPPHAMGrdWSILAVKLQLT-DQVPDVDSTGQ-SLSRTDQLLNEWAIhhpEQASVGNLCRILVELG 981
Cdd:cd08309     5 NLPPWVLKRLCKVLDALELAG--WRQLASLIPYDqTDVRQIESMKQrGQSPTRELLWDWGT---QNATVQDLVQLLTQLG 79


                  ....*...
gi 808355035  982 RCDARDAL 989
Cdd:cd08309    80 LFRAADLI 87
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
 573-763 3.88e-04

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 42.62  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   573 NLVRKKHANFPVITWPDFIQLVRNeiNPLTGDAHCRQIVQQLQLIGELVYLRNDLCDADYVVLNAEWfgthiLGQLLSAE 652
Cdd:pfam16095    9 EALEKERQKKPYISYEEYRKICAE--NGIDDEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVILNPQW-----LTNAVYRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   653 FLSKASPN--GSYHTSSLAKIFPEIP----EQSDLMTILEVLQLC--APDARTGAHEFPVFIQTEAPDSIWRPYSlkeke 724
Cdd:pfam16095   82 LDSKHVLNnnGILTHEDLEQIWKDPGypreLHPYLLRLMEKFELCyeLPGDEEGTYLVPQLLPENPPELYDWDEE----- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 808355035   725 rdtvyggvRILPMRGMERSLH-STFPRIQVALRRSINDYQ 763
Cdd:pfam16095  157 --------NNLELRYQYDFLPkGIFSRLIVRLHKFIDDEL 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-204 4.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   62 TGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNIREETPLHVAAAR-G 140
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808355035  141 HVDCVQALLDANSPIDAVEQ-DGKTALIIALENGnvDIASILITNGCDINHADHHGDTALHIASK 204
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-257 5.80e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 5.80e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 808355035   227 NKKTALHLAA-HYGHVDIIRVLLLARADVTLR 257
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
 917-985 6.98e-04

Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). UNC5A is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a critical role in neuronal development and differentiation, as well as axon-guidance. It also plays a role in regulating apoptosis in non-neuronal cells as a downstream target of p53. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260065  Cd Length: 84  Bit Score: 39.49  E-value: 6.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355035  917 LDPPHAMGRDWSILAVKLQLTDQVPDVDSTGqslSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 985
Cdd:cd08800    13 LDPPCPRGADWRTLAQKLNLDSHLSFFASKS---SPTAMILNLWEAQHFPNGNLSQLAAVVAEIGKQDA 78
PHA03095 PHA03095
ankyrin-like protein; Provisional
 167-264 7.86e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 7.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  167 IIALENGNVDIASILITNGCDINHADHHGDTALHI---ASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHV-D 242
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlD 98

                          90       100
                  ....*....|....*....|..
gi 808355035  243 IIRVLLLARADVTLRGDDGLTA 264
Cdd:PHA03095   99 VIKLLIKAGADVNAKDKVGRTP 120
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 161-189 8.72e-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: 8.72e-04
                            10        20
                    ....*....|....*....|....*....
gi 808355035    161 DGKTALIIALENGNVDIASILITNGCDIN 189
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 96-248 1.02e-03

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: 43.15  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035    96 GDTVLHLAA----DSINPRIVPLLV----CLAPPLHL-----RNIREETPLHVAAARGHVDCVQALLD--ANSPIDA--- 157
Cdd:TIGR00870   82 GDTLLHAISleyvDAVEAILLHLLAafrkSGPLELANdqytsEFTPGITALHLAAHRQNYEIVKLLLErgASVPARAcgd 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   158 --VEQDGKTA-------LIIALENGNVDIASILITNGCDINHADHHGDTALHIA-------------SKHGLLQAVQTLC 215
Cdd:TIGR00870  162 ffVKSQGVDSfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkaeyeelSCQMYNFALSLLD 241

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 808355035   216 HCAVTV---DSVNANKKTALHLAAHYGHVDIIRVLL 248
Cdd:TIGR00870  242 KLRDSKeleVILNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 28-186 1.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   28 DNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADS- 106
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYc 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  107 INPRIVPLLVCLAPPLHLRN-IREETPLHVAAARGHVdcVQALLDANSPIDAVEQDGKTALIIA-LENGNVDIASILITN 184
Cdd:PHA02878  246 KDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAvKQYLCINIGRILISN 323


                  ..
gi 808355035  185 GC 186
Cdd:PHA02878  324 IC 325
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-37 1.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.30e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 808355035     1 MHCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVA 37
Cdd:pfam13857   20 LHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-62 1.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355035    2 HCAAKYGHAEVFNYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKT 62
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 214-280 1.35e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  214 LCHCAVTVDSVNA---------------NKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHS 278
Cdd:PTZ00322   86 LCQLAASGDAVGArilltggadpncrdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                  ..
gi 808355035  279 LL 280
Cdd:PTZ00322  166 LL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 227-256 1.40e-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: 37.18  E-value: 1.40e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 808355035    227 NKKTALHLAAHYGHVDIIRVLLLARADVTL 256
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 130-158 1.52e-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: 36.88  E-value: 1.52e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 808355035   130 ETPLHVAAAR-GHVDCVQALLDANSPIDAV 158
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 131-157 1.60e-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: 1.60e-03
                            10        20
                    ....*....|....*....|....*..
gi 808355035    131 TPLHVAAARGHVDCVQALLDANSPIDA 157
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 114-247 1.75e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.41  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  114 LLVCLAPPLHLRNIREETPLHVAAARGHV------------DCVQALLDAnspidaVEQDGKTALIIALENGN----VDI 177
Cdd:PHA02741    6 FMTCLEEMIAEKNSEGENFFHEAARCGCFdiiarftpfirgDCHAAALNA------TDDAGQMCIHIAAEKHEaqlaAEI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355035  178 ASILITNGCDINHADH-HGDTALHIASKHGLLQAVQTLC-HCAVTVDSVNANKKTALHLAAHYGHVDIIRVL 247
Cdd:PHA02741   80 IDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQIL 151
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
 910-985 2.07e-03

Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). UNC5C is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5C plays a critical role in the development of spinal accessory motor neurons. Methylation of the UNC5C gene is associated with early stages of colorectal carcinogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260064  Cd Length: 83  Bit Score: 38.07  E-value: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355035  910 RCELACLLDPPHAMGRDWSILAVKLQLtDQVPDVDSTGQslSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 985
Cdd:cd08799     6 RQKLCGSLDAPQTRGNDWRMLAHKLNL-DRYLNYFATKS--SPTGVILDLWEAQHFPDGNLSRLAAVLEEMGRHET 78
Ank_4 pfam13637
Ankyrin repeats (many copies);
30-79 2.48e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 808355035    30 GDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVV 79
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-79 2.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 2.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355035   14 NYFHMKGGNICARDDNGDTPLHVACRFAQHTVAGYVANEKIDVDSINKTGETALHCAVESADTRVV 79
Cdd:PHA03100  176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIF 241
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 20-79 2.68e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 2.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355035   20 GGNICARDD-NGDTPLHVACRFAQHTVAGYVANE-KIDVDSINKTGETALHCAVESADTRVV 79
Cdd:PHA02736   81 GADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMM 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
232-280 2.75e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 2.75e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 808355035   232 LHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 280
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-311 3.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   57 DSINKTGETALHCAVESADTRVVRLLLQLRPRLDLPNASGDTVLHLAADSINPRIVPLLVCLAPPLHLRNirEETPLHVA 136
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY--TLVAIKDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  137 AARGHVDCVQALL----DANSPIDAVEQDGKTALIIAlengNVDIASILITNGCDINHADHH-GDTALHIASKHGLLQAV 211
Cdd:PHA02878  109 FNNRNVEIFKIILtnryKNIQTIDLVYIDKKSKDDII----EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035  212 QTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAaeRLEAHSLLKMVKSQEIR-- 289
Cdd:PHA02878  185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG--YCKDYDILKLLLEHGVDvn 262

                         250       260
                  ....*....|....*....|....
gi 808355035  290 -EEYISQLYPLDTSLR-RIKLKLL 311
Cdd:PHA02878  263 aKSYILGLTALHSSIKsERKLKLL 286
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 387-486 3.77e-03

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 38.26  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355035   387 PHSQYTRGIDV---QTVNINGCGE---FSVWEFGGYEPMHTCYDHFVGNADCIhLILYrtsDPTEvqYKQILYWMNFLKg 460
Cdd:pfam08477   26 PKYKSTIGVDFktkTVLENDDNGKkikLNIWDTAGQERFRSLHPFYYRGAAAA-LLVY---DSRT--FSNLKYWLRELK- 98

                           90       100
                   ....*....|....*....|....*.
gi 808355035   461 rvtpfepiGHCGfssrRSKVIIVGTH 486
Cdd:pfam08477   99 --------KYAG----NSPVILVGNK 112
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 161-190 4.79e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 4.79e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 808355035   161 DGKTALIIALENGNVDIASILITNGCDINH 190
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-254 7.53e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.53e-03
                           10        20
                   ....*....|....*....|....*...
gi 808355035   227 NKKTALHLAAHYGHVDIIRVLLLARADV 254
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
181-235 9.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 9.39e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 808355035   181 LITNG-CDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLA 235
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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