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Conserved domains on  [gi|583029556|emb|CDM63494|]
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non-specific serine/threonine protein kinase [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-323 3.19e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 3.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQ 251
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 583029556 252 AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 323
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 806-888 3.37e-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: 134.01  E-value: 3.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 806 ASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSL-SRTDQLLNEWAIHHPeqASVGNLCRILVELGRCDAR 884
Cdd:cd08782    1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLpSPTDRLLQEWTARPP--STIGALLRKLRELGRRDAA 78


                 ....
gi 583029556 885 DALY 888
Cdd:cd08782   79 DFLL 82
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 423-541 1.49e-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: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 423 GSKYaPPHSQYTRGIDVQTVNI----NGCGEFSVWEFGGYEPMHTCYDHFVGNAdCIHLILYRTSDPTEVQykQILYWMN 498
Cdd:cd09914   23 GEKF-DGDESSTHGINVQDWKIpapeRKKIRLNVWDFGGQEIYHATHQFFLTSR-SLYLLVFDLRTGDEVS--RVPYWLR 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 583029556 499 FLKGRvtpfepighcgfsSRRSKVIIVGTHATSSLFPQMNQEG 541
Cdd:cd09914   99 QIKAF-------------GGVSPVILVGTHIDESCDEDILKKA 128
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-323 3.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 3.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQ 251
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 583029556 252 AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 323
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 806-888 3.37e-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: 134.01  E-value: 3.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 806 ASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSL-SRTDQLLNEWAIHHPeqASVGNLCRILVELGRCDAR 884
Cdd:cd08782    1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLpSPTDRLLQEWTARPP--STIGALLRKLRELGRRDAA 78


                 ....
gi 583029556 885 DALY 888
Cdd:cd08782   79 DFLL 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-267 6.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 6.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  175 LHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNgCDINHADhHGDTALHIASKHGLLQAVQ 254
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 583029556  255 TLCHCAVTVDSVN 267
Cdd:pfam12796  79 LLLEKGADINVKD 91
Death pfam00531
Death domain;
808-891 6.31e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 79.33  E-value: 6.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  808 RCELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDST----GQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 883
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSEN--EIDEIesenPRLRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78


                  ....*...
gi 583029556  884 RDALYRTV 891
Cdd:pfam00531  79 AEKIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 804-890 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: 74.75  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556   804 QMASRCELACLLDPPhaMGRDWSILAVKLQLTDQVPDVDSTGQS---LSRTDQLLNEWAIHHPEQASVGNLCRILVELGR 880
Cdd:smart00005   1 PELTRQKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTEAPrdlAEQSVQLLRLWEQREGKNATLGTLLEALRKMGR 78

                           90
                   ....*....|
gi 583029556   881 CDARDALYRT 890
Cdd:smart00005  79 DDAVELLRSE 88
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 163-321 1.19e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 163 PDLCEcAREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITngCDINHADHHGDTALH 242
Cdd:PLN03192 551 PDIGD-SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH--FASISDPHAAGDLLC 627

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 243 IASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRG--DDGLTAELVAVAAERLEAHS 320
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtdDDFSPTELRELLQKRELGHS 707


                 .
gi 583029556 321 L 321
Cdd:PLN03192 708 I 708
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 423-541 1.49e-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: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 423 GSKYaPPHSQYTRGIDVQTVNI----NGCGEFSVWEFGGYEPMHTCYDHFVGNAdCIHLILYRTSDPTEVQykQILYWMN 498
Cdd:cd09914   23 GEKF-DGDESSTHGINVQDWKIpapeRKKIRLNVWDFGGQEIYHATHQFFLTSR-SLYLLVFDLRTGDEVS--RVPYWLR 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 583029556 499 FLKGRvtpfepighcgfsSRRSKVIIVGTHATSSLFPQMNQEG 541
Cdd:cd09914   99 QIKAF-------------GGVSPVILVGTHIDESCDEDILKKA 128
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 178-299 5.58e-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: 5.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  178 AAARGHVDCVQALLDANSP--IDAVEQDGKTALI-IALENGNVDIASILITNGCDInhadHHGDTALHIASKhGLLQAVQ 254
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFvAAIENENLELTELLLNLSCRG----AVGDTLLHAISL-EYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556  255 -TLCH------CAVTVDSVNANKK-------TALHLAAHYGHVDIIRVLLLARADVTLR 299
Cdd:TIGR00870  99 aILLHllaafrKSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 162-304 1.09e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 162 HPDLCE-CAREETPLHVAAARGHVDCVQALLDA-----NSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADH 235
Cdd:cd22192   41 SCDLFQrGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRA 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556 236 HGdTALHiASKHGLlqavqtlCHCAVTVdsvnankktaLHLAAHYGHVDIIRVLLLARADvtLRGDDGL 304
Cdd:cd22192  121 TG-TFFR-PGPKNL-------IYYGEHP----------LSFAACVGNEEIVRLLIEHGAD--IRAQDSL 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 203-231 3.92e-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: 38.34  E-value: 3.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 583029556   203 DGKTALIIALENGNVDIASILITNGCDIN 231
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 429-528 3.38e-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: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  429 PHSQYTRGIDV---QTVNINGCGE---FSVWEFGGYEPMHTCYDHFVGNADCIhLILYrtsDPTEvqYKQILYWMNFLKg 502
Cdd:pfam08477  26 PKYKSTIGVDFktkTVLENDDNGKkikLNIWDTAGQERFRSLHPFYYRGAAAA-LLVY---DSRT--FSNLKYWLRELK- 98

                          90       100
                  ....*....|....*....|....*.
gi 583029556  503 rvtpfepiGHCGfssrRSKVIIVGTH 528
Cdd:pfam08477  99 --------KYAG----NSPVILVGNK 112
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-323 3.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 3.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQ 251
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 583029556 252 AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 323
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 806-888 3.37e-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: 134.01  E-value: 3.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 806 ASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGQSL-SRTDQLLNEWAIHHPeqASVGNLCRILVELGRCDAR 884
Cdd:cd08782    1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDSTSSPLpSPTDRLLQEWTARPP--STIGALLRKLRELGRRDAA 78


                 ....
gi 583029556 885 DALY 888
Cdd:cd08782   79 DFLL 82
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-323 6.52e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 6.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQ 251
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 583029556 252 AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLLK 323
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-322 9.79e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 9.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 169 AREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHG 248
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 583029556 249 LLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 322
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-306 1.64e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 1.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQ 251
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 583029556 252 AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTA 306
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
173-322 8.83e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.87  E-value: 8.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 173 TPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQA 252
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 253 VQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 322
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-267 6.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 6.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  175 LHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNgCDINHADhHGDTALHIASKHGLLQAVQ 254
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 583029556  255 TLCHCAVTVDSVN 267
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-299 6.93e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 6.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  208 LIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLC-HCAVTVDSvnaNKKTALHLAAHYGHVDII 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVNLKD---NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 583029556  287 RVLLLARADVTLR 299
Cdd:pfam12796  78 KLLLEKGADINVK 90
Death pfam00531
Death domain;
808-891 6.31e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 79.33  E-value: 6.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  808 RCELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDST----GQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 883
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSEN--EIDEIesenPRLRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78


                  ....*...
gi 583029556  884 RDALYRTV 891
Cdd:pfam00531  79 AEKIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 804-890 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: 74.75  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556   804 QMASRCELACLLDPPhaMGRDWSILAVKLQLTDQVPDVDSTGQS---LSRTDQLLNEWAIHHPEQASVGNLCRILVELGR 880
Cdd:smart00005   1 PELTRQKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTEAPrdlAEQSVQLLRLWEQREGKNATLGTLLEALRKMGR 78

                           90
                   ....*....|
gi 583029556   881 CDARDALYRT 890
Cdd:smart00005  79 DDAVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
166-234 3.90e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.90e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556  166 CECAREETPLHVAAARGHVDCVQALLDaNSPIDAVEqDGKTALIIALENGNVDIASILITNGCDINHAD 234
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 163-321 1.19e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 163 PDLCEcAREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITngCDINHADHHGDTALH 242
Cdd:PLN03192 551 PDIGD-SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH--FASISDPHAAGDLLC 627

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 243 IASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRG--DDGLTAELVAVAAERLEAHS 320
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtdDDFSPTELRELLQKRELGHS 707


                 .
gi 583029556 321 L 321
Cdd:PLN03192 708 I 708
Ank_2 pfam12796
Ankyrin repeats (3 copies);
241-318 3.35e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.35e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 583029556  241 LHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRvLLLARADVTLRgDDGLTAELVAVAAERLEA 318
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLK-DNGRTALHYAARSGHLEI 76
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
189-322 9.15e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 9.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 189 ALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNA 268
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 583029556 269 NKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 322
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 173-356 2.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 173 TPLHVAAAR--GHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVD--IASILITNGCDINHADHhgdtalhiaskhg 248
Cdd:PHA03100 108 TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR------------- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 249 llqaVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLE-AHSLLKMVKS 327
Cdd:PHA03100 175 ----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPS 250

                        170       180       190
                 ....*....|....*....|....*....|.
gi 583029556 328 QEIREEYISQL--YPLDTslrRIKLKLLGHS 356
Cdd:PHA03100 251 IKTIIETLLYFkdKDLNT---ITKIKMLKKS 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 172-322 4.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 4.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAV-EQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLL 250
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 583029556 251 QAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDG-LTAELVAVAAERLEAHSLL 322
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLF 221
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-224 4.64e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 4.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 583029556  173 TPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILI 224
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 154-356 8.01e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 8.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 154 LLNDISETHPDLCECAReetpLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHA 233
Cdd:PLN03192 512 LLGDNGGEHDDPNMASN----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 234 DHHGDTAL--HIASKHGllQAVQTLCHCAVTVDSVNANKktALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAV 311
Cdd:PLN03192 588 DANGNTALwnAISAKHH--KIFRILYHFASISDPHAAGD--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 583029556 312 AAERLEAHSLLKMVKSQEIREEYISQLYPldTSLRR-IKLKLLGHS 356
Cdd:PLN03192 664 AEDHVDMVRLLIMNGADVDKANTDDDFSP--TELRElLQKRELGHS 707
PHA03095 PHA03095
ankyrin-like protein; Provisional
 172-306 1.68e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 172 ETPLHVAAARGHVDC---VQALLDANSPIDAVEQDGKTALIIALENGNV-DIASILITNGCDINHADHHGDTALHI--AS 245
Cdd:PHA03095  48 KTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSG 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 583029556 246 KHGLLQAVQTLCHCAVTVDSVNANKKTALH--LAAHYGHVDIIRVLLLARADVTLRGDDGLTA 306
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 164-312 4.45e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 164 DLCEC-AREETPLHV--AAARGHVDCVQALLDANSPIDAVEQDGKTALIIALEN--GNVDIASILITNGCDINHADHHGD 238
Cdd:PHA03095 144 DVNALdLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGN 223

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 583029556 239 TALHIASKHGLLQA--VQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVA 312
Cdd:PHA03095 224 TPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-305 2.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 185 DCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVD 264
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 583029556 265 SVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLT 305
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 169-351 1.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 169 AREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHG 248
Cdd:PHA02874 122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 249 LLQAVQ-----------------TLCHCAV--------------TVDSVNANKKTALHLAAHYG-HVDIIRVLLLARADV 296
Cdd:PHA02874 202 DYACIKllidhgnhimnkckngfTPLHNAIihnrsaiellinnaSINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 583029556 297 TLRGDDGltAELVAVAAERLEAHSLLKMVKSQEIREEYISQLyPLDTSLRRIKLK 351
Cdd:PHA02874 282 SIKDNKG--ENPIDTAFKYINKDPVIKDIIANAVLIKEADKL-KDSDFLEHIEIK 333
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 807-882 1.18e-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: 1.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 583029556 807 SRCELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDSTGQSLSRTDQLLNEWAIHHPEqASVGNLCRILVELGRCD 882
Cdd:cd08312    1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYL--EIRNFERQSSPTERLLEDWETRPPG-ATVGNLLEILEELERKD 73
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 165-268 1.38e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 165 LCECAREETP------LHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGD 238
Cdd:PLN03192 610 LYHFASISDPhaagdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689

                         90       100       110
                 ....*....|....*....|....*....|
gi 583029556 239 taLHIASKHGLLQAvQTLCHCAVTVDSVNA 268
Cdd:PLN03192 690 --FSPTELRELLQK-RELGHSITIVDSVPA 716
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 423-541 1.49e-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: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 423 GSKYaPPHSQYTRGIDVQTVNI----NGCGEFSVWEFGGYEPMHTCYDHFVGNAdCIHLILYRTSDPTEVQykQILYWMN 498
Cdd:cd09914   23 GEKF-DGDESSTHGINVQDWKIpapeRKKIRLNVWDFGGQEIYHATHQFFLTSR-SLYLLVFDLRTGDEVS--RVPYWLR 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 583029556 499 FLKGRvtpfepighcgfsSRRSKVIIVGTHATSSLFPQMNQEG 541
Cdd:cd09914   99 QIKAF-------------GGVSPVILVGTHIDESCDEDILKKA 128
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 821-887 1.95e-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: 1.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 821 MGRDWSILAVKLQLTD---QVPDVDSTGQSLSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDARDAL 887
Cdd:cd01670    9 LGRDWKKLARKLGLSEgdiDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKL 78
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-256 3.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 583029556  206 TALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTL 256
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 803-887 6.39e-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: 6.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 803 LQMASRCELACLLDPPHAMGRDWSILAVKLQLTDQVPDVDSTGqslSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCD 882
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDRYINYFATKP---SPTEVILDLWEARNRDDGALNSLAAILREMGRHD 77


                 ....*
gi 583029556 883 ARDAL 887
Cdd:cd08781   78 AATIL 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 146-296 8.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 146 SSTTAFIQLLNDISETHPDLCECAREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIAL-----ENGNVDIA 220
Cdd:PHA03100  10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 221 SILITNGCDINHADHHGDTALHIAS--KHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVD--IIRVLLLARADV 296
Cdd:PHA03100  90 KLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 171-290 2.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 171 EETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIA-SILITNGCDINHADHHGDTALHIASKHGL 249
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKDLSTPLHYACKKNC 454

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 583029556 250 -LQAVQTLCHCAVTVDSVNANKKTALHLAAHYGhvDIIRVLL 290
Cdd:PHA02876 455 kLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILL 494
Ank_5 pfam13857
Ankyrin repeats (many copies);
154-211 2.73e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 583029556  154 LLNDISETHPDLCECarEETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIA 211
Cdd:pfam13857   1 LLEHGPIDLNRLDGE--GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 178-299 5.58e-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: 5.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  178 AAARGHVDCVQALLDANSP--IDAVEQDGKTALI-IALENGNVDIASILITNGCDInhadHHGDTALHIASKhGLLQAVQ 254
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFvAAIENENLELTELLLNLSCRG----AVGDTLLHAISL-EYVDAVE 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556  255 -TLCH------CAVTVDSVNANKK-------TALHLAAHYGHVDIIRVLLLARADVTLR 299
Cdd:TIGR00870  99 aILLHllaafrKSGPLELANDQYTseftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-306 6.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 583029556  258 HCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTA 306
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 173-305 8.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 8.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 173 TPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINhadhHGDTALHIASKHGLLQA 252
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLET 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 583029556 253 VQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLAR-ADVTLRGDDGLT 305
Cdd:PHA02876 256 SLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERgADVNAKNIKGET 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-290 1.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 583029556  237 GDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLL 290
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 162-304 1.09e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 162 HPDLCE-CAREETPLHVAAARGHVDCVQALLDA-----NSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADH 235
Cdd:cd22192   41 SCDLFQrGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRA 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556 236 HGdTALHiASKHGLlqavqtlCHCAVTVdsvnankktaLHLAAHYGHVDIIRVLLLARADvtLRGDDGL 304
Cdd:cd22192  121 TG-TFFR-PGPKNL-------IYYGEHP----------LSFAACVGNEEIVRLLIEHGAD--IRAQDSL 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-322 1.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 583029556  272 TALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 322
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 173-311 1.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 173 TPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASkhGLLQA 252
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKD 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 583029556 253 VQTLCHCAVTVDSVNANKK----TALHLAAHygHVDIIRVLLLARADVTLRGDDGLTAELVAV 311
Cdd:PHA02878 248 YDILKLLLEHGVDVNAKSYilglTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 124-231 1.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 124 RAADFVYPGQDRYSKLgSVPAYSSTTAFIQLLNDISETH--PDLCECareeTPLHVAAARGHVDCVQALLDANSPIDAVE 201
Cdd:PHA02875 124 RGADPDIPNTDKFSPL-HLAVMMGDIKGIELLIDHKACLdiEDCCGC----TPLIIAMAKGDIAICKMLLDSGANIDYFG 198

                         90       100       110
                 ....*....|....*....|....*....|.
gi 583029556 202 QDGK-TALIIALENGNVDIASILITNGCDIN 231
Cdd:PHA02875 199 KNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 152-290 1.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 152 IQLLNDISETHPDLCECAREET--PLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCD 229
Cdd:PHA02874  14 IEAIEKIIKNKGNCINISVDETttPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 230 -----------------------INHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDII 286
Cdd:PHA02874  94 tsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII 173


                 ....
gi 583029556 287 RVLL 290
Cdd:PHA02874 174 KLLL 177
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 810-888 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: 43.81  E-value: 1.56e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556 810 ELACLLDPPHAMGRDWSILAVKLQLTDQvpDVDSTGQSLSRTDQLLNEWAihHPEQASVGNLCRILVELGRCDARDALY 888
Cdd:cd08311    6 EEVEKLLNAGREGSDWRALAGELGYSAE--EIDSFAREADPCRALLTDWS--AQDGATLGVLLTALRKIGRDDIVEILQ 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 171-234 2.07e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 583029556 171 EETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILItnGCDINHAD 234
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--RHSQCHFE 176
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 211-296 3.17e-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: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 211 ALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVdsVNA-------NKKTALHLAAHYGHV 283
Cdd:cd22192   25 AKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL--VNEpmtsdlyQGETALHIAVVNQNL 102

                         90
                 ....*....|...
gi 583029556 284 DIIRVLLLARADV 296
Cdd:cd22192  103 NLVRELIARGADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 179-271 3.55e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 179 AARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCH 258
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                         90
                 ....*....|...
gi 583029556 259 CAVTVDSVNANKK 271
Cdd:PTZ00322 170 HSQCHFELGANAK 182
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 152-243 5.03e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 152 IQLLNDISETHPDLCECARE-------------ETPLHVAAARGHVDCVQALL----DANSP----------IDAVEQDG 204
Cdd:cd22192   57 VAALYDNLEAAVVLMEAAPElvnepmtsdlyqgETALHIAVVNQNLNLVRELIargaDVVSPratgtffrpgPKNLIYYG 136

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 583029556 205 KTALIIALENGNVDIASILITNGCDINHADHHGDTALHI 243
Cdd:cd22192  137 EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 220-290 5.44e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 5.44e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 583029556 220 ASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLL 290
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 172-234 7.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 7.82e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 583029556 172 ETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHAD 234
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 187-315 8.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 8.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 187 VQALLDANSPIDAVEQD-GKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDS 265
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 583029556 266 VNANKKTALHLAAHY-GHVDIIRVLLLARADVTLRGD-DGLTAELVAVAAER 315
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER 281
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 171-296 8.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 171 EETPLHVAAARGHVD-CVQALLDANSPIDAVEQDGKTALIIALENG-NVDIASILITNGCDINHADHHGDTALHIASKHG 248
Cdd:PHA02876 273 KNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLD 352

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 583029556 249 LLQ-AVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADV 296
Cdd:PHA02876 353 RNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
Ank_5 pfam13857
Ankyrin repeats (many copies);
190-244 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 583029556  190 LLDANSP-IDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTALHIA 244
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 153-290 1.32e-04

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: 45.84  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  153 QLLNDisethPDLCECAREETPLHVAAARGHVDCVQALLD--ANSPIDA-----VEQDGKTA-------LIIALENGNVD 218
Cdd:TIGR00870 115 ELAND-----QYTSEFTPGITALHLAAHRQNYEIVKLLLErgASVPARAcgdffVKSQGVDSfyhgespLNAAACLGSPS 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  219 IASILITNGCDINHADHHGDTALHIA-------------SKHGLLQAVQTLCHCAVTV---DSVNANKKTALHLAAHYGH 282
Cdd:TIGR00870 190 IVALLSEDPADILTADSLGNTLLHLLvmenefkaeyeelSCQMYNFALSLLDKLRDSKeleVILNHQGLTPLKLAAKEGR 269


                  ....*...
gi 583029556  283 VDIIRVLL 290
Cdd:TIGR00870 270 IVLFRLKL 277
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 185-242 1.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 1.37e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 185 DCVQALLDANSPIDAVEQDGKTALIIALENGNV--DIASILITNGCDINHADHHGDTALH 242
Cdd:PHA02859 104 EILKILIDSGSSITEEDEDGKNLLHMYMCNFNVriNVIKLLIDSGVSFLNKDFDNNNILY 163
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-299 2.60e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 583029556  269 NKKTALHLAA-HYGHVDIIRVLLLARADVTLR 299
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 211-295 2.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.49  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 211 ALENGNVDIASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHcAVTVDSVnANKKTALHLAAHYGHVDIIRVLL 290
Cdd:PHA02878  44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR-SINKCSV-FYTLVAIKDAFNNRNVEIFKIIL 121


                 ....*
gi 583029556 291 LARAD 295
Cdd:PHA02878 122 TNRYK 126
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
 802-887 2.93e-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: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 802 DLQMASRCELACLLDPPHAMGrdWSILAVKLQLT-DQVPDVDSTGQ-SLSRTDQLLNEWAIhhpEQASVGNLCRILVELG 879
Cdd:cd08309    5 NLPPWVLKRLCKVLDALELAG--WRQLASLIPYDqTDVRQIESMKQrGQSPTRELLWDWGT---QNATVQDLVQLLTQLG 79


                 ....*...
gi 583029556 880 RCDARDAL 887
Cdd:cd08309   80 LFRAADLI 87
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 203-231 3.92e-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: 38.34  E-value: 3.92e-04
                           10        20
                   ....*....|....*....|....*....
gi 583029556   203 DGKTALIIALENGNVDIASILITNGCDIN 231
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 209-306 4.25e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 209 IIALENGNVDIASILITNGCDINHADHHGDTALHI---ASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHV-D 284
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlD 98

                         90       100
                 ....*....|....*....|..
gi 583029556 285 IIRVLLLARADVTLRGDDGLTA 306
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTP 120
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 269-298 6.40e-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: 37.95  E-value: 6.40e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 583029556   269 NKKTALHLAAHYGHVDIIRVLLLARADVTL 298
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 172-200 6.69e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 6.69e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 583029556  172 ETPLHVAAAR-GHVDCVQALLDANSPIDAV 200
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
 815-883 7.12e-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: 7.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 583029556 815 LDPPHAMGRDWSILAVKLQLTDQVPDVDSTGqslSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 883
Cdd:cd08800   13 LDPPCPRGADWRTLAQKLNLDSHLSFFASKS---SPTAMILNLWEAQHFPNGNLSQLAAVVAEIGKQDA 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 173-199 7.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 7.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 583029556   173 TPLHVAAARGHVDCVQALLDANSPIDA 199
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
274-322 1.41e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 583029556  274 LHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHSLL 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 256-322 1.42e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 256 LCHCAVTVDSVNA---------------NKKTALHLAAHYGHVDIIRVLLLARADVTLRGDDGLTAELVAVAAERLEAHS 320
Cdd:PTZ00322  86 LCQLAASGDAVGArilltggadpncrdyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                 ..
gi 583029556 321 LL 322
Cdd:PTZ00322 166 LL 167
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
 808-883 1.86e-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: 1.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 583029556 808 RCELACLLDPPHAMGRDWSILAVKLQLtDQVPDVDSTGQslSRTDQLLNEWAIHHPEQASVGNLCRILVELGRCDA 883
Cdd:cd08799    6 RQKLCGSLDAPQTRGNDWRMLAHKLNL-DRYLNYFATKS--SPTGVILDLWEAQHFPDGNLSRLAAVLEEMGRHET 78
Ank_2 pfam12796
Ankyrin repeats (3 copies);
162-199 1.95e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 1.95e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 583029556  162 HPDLCECAREETPLHVAAARGHVDCVQALLDANSPIDA 199
Cdd:pfam12796  52 HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 203-232 2.00e-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: 36.47  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 583029556  203 DGKTALIIALENGNVDIASILITNGCDINH 232
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-296 3.18e-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: 36.08  E-value: 3.18e-03
                          10        20
                  ....*....|....*....|....*...
gi 583029556  269 NKKTALHLAAHYGHVDIIRVLLLARADV 296
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 429-528 3.38e-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: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556  429 PHSQYTRGIDV---QTVNINGCGE---FSVWEFGGYEPMHTCYDHFVGNADCIhLILYrtsDPTEvqYKQILYWMNFLKg 502
Cdd:pfam08477  26 PKYKSTIGVDFktkTVLENDDNGKkikLNIWDTAGQERFRSLHPFYYRGAAAA-LLVY---DSRT--FSNLKYWLRELK- 98

                          90       100
                  ....*....|....*....|....*.
gi 583029556  503 rvtpfepiGHCGfssrRSKVIIVGTH 528
Cdd:pfam08477  99 --------KYAG----NSPVILVGNK 112
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-241 4.23e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 4.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 583029556 169 AREETPLHVAAARGHVDCVQALLDANSPIDAVEQDGKTALIIALENGNVDIASILITNGCDINHADHHGDTAL 241
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
223-277 4.63e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 583029556  223 LITNG-CDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLA 277
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 219-322 8.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 8.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 583029556 219 IASILITNGCDINHADHHGDTALHIASKHGLLQAVQTLCHCAVTVDSVNANKKTALHLAAHYGHVDIIRVLLLARADVTl 298
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN- 238

                         90       100
                 ....*....|....*....|....
gi 583029556 299 RGDDGLtaeLVAVAAERLEAHSLL 322
Cdd:PHA02876 239 KNDLSL---LKAIRNEDLETSLLL 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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