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Conserved domains on  [gi|1958803880|ref|XP_038940103|]
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BRCA1-associated RING domain protein 1 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 524-624 8.87e-39

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


:

Pssm-ID: 349352  Cd Length: 101  Bit Score: 138.27  E-value: 8.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 524 LFDGCYFFLGGNFKHH-PKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIVYEDLFNCHPER 602
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 1958803880 603 VRQGKVWMAPSTWLISCVMAFE 624
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-397 1.40e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSLLLL 397
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 423-499 6.25e-29

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


:

Pssm-ID: 349366  Cd Length: 80  Bit Score: 110.00  E-value: 6.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 423 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEE---AQSTLKCMLGILNGCWVLKFDWVKACLDSQERE 499
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
 
Name Accession Description Interval E-value
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 524-624 8.87e-39

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


Pssm-ID: 349352  Cd Length: 101  Bit Score: 138.27  E-value: 8.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 524 LFDGCYFFLGGNFKHH-PKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIVYEDLFNCHPER 602
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 1958803880 603 VRQGKVWMAPSTWLISCVMAFE 624
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-397 1.40e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSLLLL 397
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 423-499 6.25e-29

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 110.00  E-value: 6.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 423 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEE---AQSTLKCMLGILNGCWVLKFDWVKACLDSQERE 499
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
284-376 4.30e-28

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 107.89  E-value: 4.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 284 LHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTgyHNDSPLHDAAKNGHIDIVK 363
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958803880 364 VLLSHGASRNAVN 376
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 267-369 1.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                          90       100
                  ....*....|....*....|...
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHG 369
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLIDHG 213
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 280-383 7.04e-08

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: 55.40  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 280 GETLLHIASIKGDISSVEYLLQNG----NDPNVKD-HAGWTPLHEACSHGHLKIVELLLQHNALVNT---TG-------- 343
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAApelvNEPMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSpraTGtffrpgpk 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958803880 344 ---YHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPV 383
Cdd:cd22192   131 nliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
BRCT smart00292
breast cancer carboxy-terminal domain;
434-493 3.24e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 48.14  E-value: 3.24e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803880  434 QQKLLSKLETVLKAKKCAEFDN----TVTHVIVPDEEaQSTLKCMLGILNGCWVLKFDWVKACL 493
Cdd:smart00292  16 DKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPE-GGKLELLKAIALGIPIVKEEWLLDCL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 313-340 3.61e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 46.43  E-value: 3.61e-07
                           10        20
                   ....*....|....*....|....*...
gi 1958803880  313 GWTPLHEACSHGHLKIVELLLQHNALVN 340
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
BRCT smart00292
breast cancer carboxy-terminal domain;
522-620 3.26e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.36  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880  522 PKLFDGCYFFLGGNFKHHPKEDLLKLIAAAGGRILSRKPKPDsdvtqtintvayhakpdsdqrfcTQYIVYEDLFN--CH 599
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 1958803880  600 PERVRQGKVWMAPSTWLISCV 620
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 280-374 6.09e-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: 42.76  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 280 GETLLHIASiKGDISSVEYLLQ--------NGNDPNVKD------HAGWTPLHEACSHGHLKIVELLLQHNALVN----- 340
Cdd:TIGR00870  82 GDTLLHAIS-LEYVDAVEAILLhllaafrkSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVParacg 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958803880 341 ---------TTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNA 374
Cdd:TIGR00870 161 dffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILT 203
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 521-608 8.15e-03

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 35.80  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 521 LPKLFDGCYFFLGGnFKHHPKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYHAKPDSDQRFCTQYIvyedlFNChp 600
Cdd:pfam16589   1 LPNLFEPLRFYINA-IPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWI-----FDC-- 72


                  ....*...
gi 1958803880 601 erVRQGKV 608
Cdd:pfam16589  73 --VKKGKL 78
 
Name Accession Description Interval E-value
BRCT_Bard1_rpt2 cd17720
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ...
 524-624 8.87e-39

second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain.


Pssm-ID: 349352  Cd Length: 101  Bit Score: 138.27  E-value: 8.87e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 524 LFDGCYFFLGGNFKHH-PKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYhAKPDSDQRFCTQYIVYEDLFNCHPER 602
Cdd:cd17720     1 LFDGCHFYFHGTFKPPtTKDDLEQLVKAGGGTVLSREPKPDSDVTQTINTVAY-ARPDSDLANCTHYIIYDKLNDKKPAK 79

                          90       100
                  ....*....|....*....|..
gi 1958803880 603 VRQGKVWMAPSTWLISCVMAFE 624
Cdd:cd17720    80 VRQGKVRVVPVSWLLDCISQFK 101
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-397 1.40e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:COG0666   107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSLLLL 397
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-395 4.04e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 4.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERP----VDYTDAENIRSLL 395
Cdd:COG0666   154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPlhlaAENGHLEIVKLLL 206
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-397 2.90e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:COG0666   140 LEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSLLLL 397
Cdd:COG0666   220 KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 423-499 6.25e-29

first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain.


Pssm-ID: 349366  Cd Length: 80  Bit Score: 110.00  E-value: 6.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 423 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEE---AQSTLKCMLGILNGCWVLKFDWVKACLDSQERE 499
Cdd:cd17734     1 LVLLGSGLSSEQKKLLEKLAQLLKAKVVTEFSPEVTHVVVPADErgvCPRTMKYLMGILAGKWIVSFEWVEACLKAKKLV 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
284-376 4.30e-28

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 107.89  E-value: 4.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 284 LHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTgyHNDSPLHDAAKNGHIDIVK 363
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958803880 364 VLLSHGASRNAVN 376
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
265-395 2.30e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.80  E-value: 2.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 265 VKLSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGY 344
Cdd:COG0666    39 LLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958803880 345 HNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERP----VDYTDAENIRSLL 395
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlaAANGNLEIVKLLL 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
276-381 1.16e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 276 RNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAK 355
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                          90       100
                  ....*....|....*....|....*.
gi 1958803880 356 NGHIDIVKVLLSHGASRNAVNIFGER 381
Cdd:COG0666   262 AGAALIVKLLLLALLLLAAALLDLLT 287
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 267-369 1.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN 346
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                          90       100
                  ....*....|....*....|...
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHG 369
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLIDHG 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
262-342 1.50e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 262 PSTVK--LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNgNDPNVKDHaGWTPLHEACSHGHLKIVELLLQHNALV 339
Cdd:pfam12796  10 LELVKllLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 1958803880 340 NTT 342
Cdd:pfam12796  88 NVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 259-376 2.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 259 MSKPSTVK--LSSGIPARKRNHRGETLLHIA--SIKGDIS----------------SVEYLLQNGNDPNVKDHAGWTPLH 318
Cdd:PHA03100  118 SNSYSIVEylLDNGANVNIKNSDGENLLHLYleSNKIDLKilkllidkgvdinaknRVNYLLSYGVPINIKDVYGFTPLH 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958803880 319 EACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVN 376
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
282-333 7.91e-15

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 68.84  E-value: 7.91e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803880 282 TLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLL 333
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 261-392 1.58e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 261 KPSTVK--LSSGIPARKRNHRGETLLHIAS-----IKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSH--GHLKIVEL 331
Cdd:PHA03100   47 NIDVVKilLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958803880 332 LLQHNALVNTTGYHNDSPLHDAAKNGHID--IVKVLLSHGASRNA---VNIFGERPVDyTDAENIR 392
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAknrVNYLLSYGVP-INIKDVY 191
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 275-374 5.27e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 275 KRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAA 354
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242

                          90       100
                  ....*....|....*....|.
gi 1958803880 355 KN-GHIDIVKVLLSHGASRNA 374
Cdd:PHA02878  243 GYcKDYDILKLLLEHGVDVNA 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-382 5.49e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 5.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 282 TLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDI 361
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100
                  ....*....|....*....|.
gi 1958803880 362 VKVLLSHGASRNAVNIFGERP 382
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETP 123
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 265-384 5.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 265 VKLSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHlKIVELLLqHNALVNTTGY 344
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDI 252

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958803880 345 HNDSPLHDAAKNG-HIDIVKVLLSHGASRNAVNIFGERPVD 384
Cdd:PHA02874  253 DGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPID 293
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 283-368 9.17e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 68.00  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 283 LLHIASiKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIV 362
Cdd:PTZ00322   86 LCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....*.
gi 1958803880 363 KVLLSH 368
Cdd:PTZ00322  165 QLLSRH 170
BRCT_BRCA1_rpt1 cd17735
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ...
 425-508 1.26e-11

first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain.


Pssm-ID: 349367  Cd Length: 97  Bit Score: 61.21  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 425 LIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIV-PDEE--AQSTLKCMLGILNGCWVLKFDWVKACLDSQEREQE 501
Cdd:cd17735     3 MVASGLTPEELMLVQKFARKTGSTLTSQFTEETTHVIMkTDAElvCERTLKYFLGIAGRKWVVSYQWITQSIKEGKILPE 82


                  ....*..
gi 1958803880 502 EKYEVPG 508
Cdd:cd17735    83 HDFEVRG 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
313-366 1.74e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 1.74e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958803880 313 GWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLL 366
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 288-386 2.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 288 SIKGDIssVEYLLQNGNDPNVKD-HAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLL 366
Cdd:PHA02878  144 IIEAEI--TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221

                          90       100
                  ....*....|....*....|
gi 1958803880 367 SHGASRNAVNIFGERPVDYT 386
Cdd:PHA02878  222 ENGASTDARDKCGNTPLHIS 241
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 423-492 3.54e-11

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 58.91  E-value: 3.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 423 LVLIGSGLSSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVPDEEaqSTLKCMLGILNGCWVLKFDWVKAC 492
Cdd:cd00027     1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPS--GEKYYLAALAWGIPIVSPEWLLDC 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 279-382 2.20e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 279 RGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGH 358
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                          90       100
                  ....*....|....*....|....
gi 1958803880 359 IDIVKVLLSHGASrnaVNIFGERP 382
Cdd:PHA02875  181 IAICKMLLDSGAN---IDYFGKNG 201
BRCT_microcephalin_rpt2 cd17736
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ...
 431-500 6.70e-10

second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat.


Pssm-ID: 349368 [Multi-domain]  Cd Length: 76  Bit Score: 55.67  E-value: 6.70e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 431 SSQQQKLLSKLETVLKAKKCAEFDNTVTHVIVpdEEAQSTLKCMLGILNGCWVLKFDWVkacLDSQEREQ 500
Cdd:cd17736    10 SEEQELLESVVKKLGGFRVEDSVTEKTTHVVV--GSPRRTLNVLLGIARGCWILSPDWV---LESLEAGK 74
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 282-395 6.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 6.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 282 TLLHIASIKGDIssVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDI 361
Cdd:PHA02874   95 SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958803880 362 VKVLLSHGASRNAVNIFGERP----VDYTDAENIRSLL 395
Cdd:PHA02874  173 IKLLLEKGAYANVKDNNGESPlhnaAEYGDYACIKLLI 210
PHA03095 PHA03095
ankyrin-like protein; Provisional
 277-384 1.26e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 277 NHRGE---TLLHI---ASIKGDISSVEYLLQNGNDPNVKDHAGWTPLH-EACSHGHLKIVELLLQHNALVNTTGYHNDSP 349
Cdd:PHA03095   41 NFRGEygkTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTP 120

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958803880 350 LHD--AAKNGHIDIVKVLLSHGASRNAVNIFGERPVD 384
Cdd:PHA03095  121 LHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 236-375 1.44e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 236 DDSLSLSPGTPPSLLNNSTHRQMMSKPSTVKLSSGIPARKRNhrgeTLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWT 315
Cdd:PHA02875   95 DDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF----SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 316 PLHEACSHGHLKIVELLLQHNALVNTTGYHND-SPLHDAAKNGHIDIVKVLLSHGASRNAV 375
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 232-376 2.48e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 232 SNASDDSLSLSPGTPpslLNNSTHRQMMSKPSTVKLSSGIPARKRNHRGETLLHIASIKG-DISSVEYLLQNGNDPNVKD 310
Cdd:PHA02876  262 AGFSVNSIDDCKNTP---LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD 338

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958803880 311 HAGWTPLHEACSHGHLK-IVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVN 376
Cdd:PHA02876  339 RLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 281-409 4.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 4.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 281 ETLLHIASIKGDISSVEYLLQNG---NDPNVKDhaGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNG 357
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGkfaDDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958803880 358 HIDIVKVLLSHGASRNAVNIFGERP----VDYTDAENIRSLLLLPEKTDSFSTSQC 409
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPliiaMAKGDIAICKMLLDSGANIDYFGKNGC 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
332-385 7.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 7.06e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958803880 332 LLQH-NALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY 385
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 291-420 9.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 291 GDISSVEYLLQN-GNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHG 369
Cdd:PHA02874   12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 370 ASRNAVnifgerPVDYTDAENIRSLLllpektdsfstsQCSVQVNTGQRKS 420
Cdd:PHA02874   92 VDTSIL------PIPCIEKDMIKTIL------------DCGIDVNIKDAEL 124
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 280-383 7.04e-08

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: 55.40  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 280 GETLLHIASIKGDISSVEYLLQNG----NDPNVKD-HAGWTPLHEACSHGHLKIVELLLQHNALVNT---TG-------- 343
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAApelvNEPMTSDlYQGETALHIAVVNQNLNLVRELIARGADVVSpraTGtffrpgpk 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958803880 344 ---YHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPV 383
Cdd:cd22192   131 nliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 265-335 8.11e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 8.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 265 VKLSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQH 335
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 296-404 9.70e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 296 VEYLLQNGNDPNVKDHAGWTPLHeACSHG---HLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDI--VKVLLSHGA 370
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGA 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958803880 371 SRNAVNIFGERPVDY------TDAENIRSLLLL---PEKTDSF 404
Cdd:PHA03095  179 DVYAVDDRFRSLLHHhlqsfkPRARIVRELIRAgcdPAATDML 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 292-370 2.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 292 DISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHN-DSPLHDAAKNGHIDIVKVLLSHGA 370
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGA 126
BRCT smart00292
breast cancer carboxy-terminal domain;
434-493 3.24e-07

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 48.14  E-value: 3.24e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958803880  434 QQKLLSKLETVLKAKKCAEFDN----TVTHVIVPDEEaQSTLKCMLGILNGCWVLKFDWVKACL 493
Cdd:smart00292  16 DKEERDELKELIEALGGKVTSSlsskTTTHVIVGSPE-GGKLELLKAIALGIPIVKEEWLLDCL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 313-340 3.61e-07

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 46.43  E-value: 3.61e-07
                           10        20
                   ....*....|....*....|....*...
gi 1958803880  313 GWTPLHEACSHGHLKIVELLLQHNALVN 340
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 313-340 7.36e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 45.74  E-value: 7.36e-07
                          10        20
                  ....*....|....*....|....*....
gi 1958803880 313 GWTPLHEACSH-GHLKIVELLLQHNALVN 340
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 267-383 8.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 8.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEA-CSHGHLKIVELLLQHNALVNTTGYH 345
Cdd:PHA02876  362 LELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKD 441

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958803880 346 NDSPLHDAAKNG-HIDIVKVLLSHGASRNAVNIFGERPV 383
Cdd:PHA02876  442 LSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 283-365 9.73e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 9.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 283 LLHIASIkGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIV 362
Cdd:PLN03192  529 LLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIF 607


                  ...
gi 1958803880 363 KVL 365
Cdd:PLN03192  608 RIL 610
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 281-415 1.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 281 ETLLHIASIKGDISS-----VEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAK 355
Cdd:PHA02876  141 ESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 356 NGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENirSLLLLpekTDSFSTSQCSVQVNT 415
Cdd:PHA02876  221 SKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLET--SLLLY---DAGFSVNSIDDCKNT 275
BRCT_TopBP1_rpt7 cd17738
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ...
 428-496 1.18e-06

seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group.


Pssm-ID: 349370 [Multi-domain]  Cd Length: 75  Bit Score: 46.41  E-value: 1.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958803880 428 SGLSSQQQKLLSKLETVLKAKKC--AEFDNTVTHVIVpdEEAQSTLKCMLGILNGCWVLKFDWVKACLDSQ 496
Cdd:cd17738     7 SGFSEDEKKELISIIEKLGGKVLdsDEFDPKCTHLIC--GKPSRSEKFLAACAAGKWILHPSYIEASAKAG 75
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 345-374 1.58e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 1.58e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958803880  345 HNDSPLHDAAKNGHIDIVKVLLSHGASRNA 374
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 267-369 2.31e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTtgYHN 346
Cdd:PLN03192  545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAA 622

                          90       100
                  ....*....|....*....|...
gi 1958803880 347 DSPLHDAAKNGHIDIVKVLLSHG 369
Cdd:PLN03192  623 GDLLCTAAKRNDLTAMKELLKQG 645
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 313-341 2.42e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 44.17  E-value: 2.42e-06
                          10        20
                  ....*....|....*....|....*....
gi 1958803880 313 GWTPLHEACSHGHLKIVELLLQHNALVNT 341
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
299-351 2.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958803880 299 LLQNGN-DPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLH 351
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
346-385 2.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958803880 346 NDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY 385
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank_5 pfam13857
Ankyrin repeats (many copies);
276-320 3.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 3.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1958803880 276 RNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEA 320
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 293-386 3.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 293 ISSVEYLLQNG--NDPNVKDHAgwTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHI-----DIVKVL 365
Cdd:PHA03100   15 VKNIKYIIMEDdlNDYSYKKPV--LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLL 92

                          90       100
                  ....*....|....*....|.
gi 1958803880 366 LSHGASRNAVNIFGERPVDYT 386
Cdd:PHA03100   93 LEYGANVNAPDNNGITPLLYA 113
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 345-376 3.93e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 3.93e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958803880 345 HNDSPLHDAA-KNGHIDIVKVLLSHGASRNAVN 376
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
267-341 6.15e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.41  E-value: 6.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNT 341
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
PHA03095 PHA03095
ankyrin-like protein; Provisional
 274-385 6.28e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 6.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 274 RKRNHRGETLLHI----ASIKGDIssVEYLLQNGNDPNVKDHAGWTPLHeaC---SHG-HLKIVELLLQHNALVNTTGYH 345
Cdd:PHA03095  111 NAKDKVGRTPLHVylsgFNINPKV--IRLLLRKGADVNALDLYGMTPLA--VllkSRNaNVELLRLLIDAGADVYAVDDR 186

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958803880 346 NDSPLHDAAKNGHID--IVKVLLSHGASRNAVNIFGERPVDY 385
Cdd:PHA03095  187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHS 228
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 287-375 2.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 287 ASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLL 366
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88


                  ....*....
gi 1958803880 367 SHGASRNAV 375
Cdd:PHA02875   89 DLGKFADDV 97
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 329-441 2.52e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 329 VELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDYTDAENIRSL--LLLPEKTDSFST 406
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVvqLLSRHSQCHFEL 177

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958803880 407 SQCSV-QVNTGQRKS---GPLVLIGSGLSSQQQKLLSKL 441
Cdd:PTZ00322  178 GANAKpDSFTGKPPSledSPISSHHPDFSAVPQPMMGSL 216
BRCT smart00292
breast cancer carboxy-terminal domain;
522-620 3.26e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 42.36  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880  522 PKLFDGCYFFLGGNFKHHPKEDLLKLIAAAGGRILSRKPKPDsdvtqtintvayhakpdsdqrfcTQYIVYEDLFN--CH 599
Cdd:smart00292   1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKT-----------------------TTHVIVGSPEGgkLE 57

                           90       100
                   ....*....|....*....|.
gi 1958803880  600 PERVRQGKVWMAPSTWLISCV 620
Cdd:smart00292  58 LLKAIALGIPIVKEEWLLDCL 78
PHA02946 PHA02946
ankyin-like protein; Provisional
 289-373 3.32e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 289 IKG-DISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLH--DAAKNGHIDIVKVL 365
Cdd:PHA02946   47 IKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLL 126


                  ....*...
gi 1958803880 366 LSHGASRN 373
Cdd:PHA02946  127 VQYGAKIN 134
PHA03095 PHA03095
ankyrin-like protein; Provisional
 262-383 5.48e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 5.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 262 PSTVKL--SSGIPARKRNHRGETLLHI--ASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLK--IVELLLQH 335
Cdd:PHA03095  167 VELLRLliDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958803880 336 NALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPV 383
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-311 7.55e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 7.55e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958803880 279 RGETLLHIASIK-GDISSVEYLLQNGNDPNVKDH 311
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 267-371 7.62e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQ--------HNAL 338
Cdd:PHA03095  244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpsaetvAATL 323

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958803880 339 VNTTGYHNDSPLhDAAKnghIDIVKVLLSHGAS 371
Cdd:PHA03095  324 NTASVAGGDIPS-DATR---LCVAKVVLRGAFS 352
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 280-397 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 280 GETLLHIASIKGDISSVEYLLQNGNDPNVKDHAgwtpLHEACSHGHLKIVELLLQHNALVNTTGYHNDSPLHDAAKNGHI 359
Cdd:PHA02876  211 DLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSL 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958803880 360 D-IVKVLLSHGASRNAVNIFGERPV-----DYTDAENIRSLLLL 397
Cdd:PHA02876  287 SrLVPKLLERGADVNAKNIKGETPLylmakNGYDTENIRTLIML 330
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-308 1.72e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.72e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958803880 279 RGETLLHIASIKGDISSVEYLLQNGNDPNV 308
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 292-383 1.86e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.52  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 292 DISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLK--IVELLLQHNALVNTTGYHNDSPLH------------DAAKNG 357
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnilDPETDN 375

                          90       100
                  ....*....|....*....|....*...
gi 1958803880 358 HI--DIVKVLLSHGASRNAVNIFGERPV 383
Cdd:PHA02716  376 DIrlDVIQCLISLGADITAVNCLGYTPL 403
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 276-368 2.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 276 RNHRGETLLHIASIK-GDISSVEYLLQNGNDPNVKDHA-GWTPLHEACSHGhlKIVELLLQHNALVNTTGYHNDSPLHDA 353
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307

                          90
                  ....*....|....*.
gi 1958803880 354 AKNGH-IDIVKVLLSH 368
Cdd:PHA02878  308 VKQYLcINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-310 2.30e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 2.30e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958803880 280 GETLLHIASIKGDISSVEYLLQNGNDPNVKD 310
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 279-308 2.47e-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: 38.72  E-value: 2.47e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958803880  279 RGETLLHIASIKGDISSVEYLLQNGNDPNV 308
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
350-382 2.80e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 2.80e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958803880 350 LHDAAKNGHIDIVKVLLSHGASRNAVNIFGERP 382
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 280-351 3.26e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 280 GETLLHIASIKGDISSVEYLLQNGND------------PNVKD--HAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYH 345
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                  ....*.
gi 1958803880 346 NDSPLH 351
Cdd:cd22192   169 GNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 280-374 6.09e-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: 42.76  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 280 GETLLHIASiKGDISSVEYLLQ--------NGNDPNVKD------HAGWTPLHEACSHGHLKIVELLLQHNALVN----- 340
Cdd:TIGR00870  82 GDTLLHAIS-LEYVDAVEAILLhllaafrkSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVParacg 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958803880 341 ---------TTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNA 374
Cdd:TIGR00870 161 dffvksqgvDSFYHGESPLNAAACLGSPSIVALLSEDPADILT 203
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 278-347 6.75e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 6.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 278 HRGETLLHIASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSHGHLKIVELLLQHNALVNTTGYHND 347
Cdd:PLN03192  620 HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 345-374 9.99e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 9.99e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958803880 345 HNDSPLHDAAKNGHIDIVKVLLSHGASRNA 374
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-300 2.37e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 2.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958803880 267 LSSGIPARKRNHRGETLLHIASIKGDISSVEYLL 300
Cdd:pfam13637  21 LEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 267-350 3.83e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 267 LSSGIPARKRNHRGETLLH--IASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEACSH--GHLKIVELLLQHNAlVNTT 342
Cdd:PHA02946  160 MSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPSTD-VNKQ 238


                  ....*...
gi 1958803880 343 GYHNDSPL 350
Cdd:PHA02946  239 NKFGDSPL 246
PHA03095 PHA03095
ankyrin-like protein; Provisional
 261-386 3.90e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 261 KPSTVK--LSSGIPARKRNHRGETLLHI--ASIKGDISSVEYLLQNGNDPNVKDHAGWTPLHEAC--SHGHLKIVELLLQ 334
Cdd:PHA03095  131 NPKVIRllLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIR 210

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958803880 335 HNALVNTTGYHNDSPLHDAAKNG---HIDIVKvLLSHGASRNAVNIFGERPVDYT 386
Cdd:PHA03095  211 AGCDPAATDMLGNTPLHSMATGSsckRSLVLP-LLIAGISINARNRYGQTPLHYA 264
PHA02946 PHA02946
ankyin-like protein; Provisional
 317-475 4.67e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 317 LHEACSHGHL--KIVELLLQHNALVNTTGYHNDSPLHDAAKNGHIDIVKVLLSHGASRNAVNIFGERPVDY---TDAENI 391
Cdd:PHA02946   41 LHAYCGIKGLdeRFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgTDDEVI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 392 RSLLLLPEKTDSFSTSqcsvqvnTGQRKSGPLVligsGLSSQQQKLLSKLETV-LKAKKCAEF-DNTVTHVIVPDEEAQS 469
Cdd:PHA02946  121 ERINLLVQYGAKINNS-------VDEEGCGPLL----ACTDPSERVFKKIMSIgFEARIVDKFgKNHIHRHLMSDNPKAS 189


                  ....*.
gi 1958803880 470 TLKCML 475
Cdd:PHA02946  190 TISWMM 195
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 278-375 5.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 278 HRGETLLHIASIKGDISS--VEYLLQNGNDPNvkdHAGW--TPL------HEACSHGHLKIVELLLQHNALVNTTGYHND 347
Cdd:PHA02989   33 YRGNSILLLYLKRKDVKIkiVKLLIDNGADVN---YKGYieTPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFNGV 109

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958803880 348 SPLHDAAKNGHI---DIVKVLLSHGASRNAV 375
Cdd:PHA02989  110 SPIVCFIYNSNInncDMLRFLLSKGINVNDV 140
BRCT_2 pfam16589
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ...
 521-608 8.15e-03

BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown.


Pssm-ID: 465186 [Multi-domain]  Cd Length: 84  Bit Score: 35.80  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803880 521 LPKLFDGCYFFLGGnFKHHPKEDLLKLIAAAGGRILSRKPKPDSDVTQTINTVAYHAKPDSDQRFCTQYIvyedlFNChp 600
Cdd:pfam16589   1 LPNLFEPLRFYINA-IPSPSRSKLKRLIEANGGTVVDNINPAVYIVIAPYNKTDKLAENTKLGVVSPQWI-----FDC-- 72


                  ....*...
gi 1958803880 601 erVRQGKV 608
Cdd:pfam16589  73 --VKKGKL 78
 
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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