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Conserved domains on  [gi|1063713509|ref|NP_001325640|]
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AAA-type ATPase family protein / ankyrin repeat family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 143-350 1.30e-45

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 CHL00181:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 287  Bit Score: 159.50  E-value: 1.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 143 EQCGKTKAK--MELLEDELsniVGLSELKTQLRKWAKGMLLDERRRALGLNIGTrrpP--HMAFLGNPGTGKTMVARVLG 218
Cdd:CHL00181    7 EEYEKTQIQevLDILDEEL---VGLAPVKTRIREIAALLLIDRLRKNLGLTSSN---PglHMSFTGSPGTGKTTVALKMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 219 KLLNTVGILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEAEGGILFVDEAYRLIpmqKAD-DKDYGLEALEEIMSVMDT 297
Cdd:CHL00181   81 DILYKLGYIKKGHLLTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLY---KPDnERDYGSEAIEILLQVMEN 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063713509 298 GK--IVVIFAGYSEPMKRVIASNEGFCRRVTKFFNFSDFSAKELAQILHIKMNNQ 350
Cdd:CHL00181  158 QRddLVVIFAGYKDRMDKFYESNPGLSSRIANHVDFPDYTPEELLQIAKIMLEEQ 212
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-179 6.98e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 6.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWY 82
Cdd:COG0666   121 ETPLHLAAYNGNLEIVKLLLE-AGAD---VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  83 sitaKEISTVKTLLDHNADCSAKDNEGMTPLDHLPQGQGSEKLRELLRWFLQEQRKRSALEQCGKTKAKMELLEDELSNI 162
Cdd:COG0666   197 ----GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         170
                  ....*....|....*..
gi 1063713509 163 VGLSELKTQLRKWAKGM 179
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
cbbX CHL00181
CbbX; Provisional
 143-350 1.30e-45

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 159.50  E-value: 1.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 143 EQCGKTKAK--MELLEDELsniVGLSELKTQLRKWAKGMLLDERRRALGLNIGTrrpP--HMAFLGNPGTGKTMVARVLG 218
Cdd:CHL00181    7 EEYEKTQIQevLDILDEEL---VGLAPVKTRIREIAALLLIDRLRKNLGLTSSN---PglHMSFTGSPGTGKTTVALKMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 219 KLLNTVGILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEAEGGILFVDEAYRLIpmqKAD-DKDYGLEALEEIMSVMDT 297
Cdd:CHL00181   81 DILYKLGYIKKGHLLTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLY---KPDnERDYGSEAIEILLQVMEN 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063713509 298 GK--IVVIFAGYSEPMKRVIASNEGFCRRVTKFFNFSDFSAKELAQILHIKMNNQ 350
Cdd:CHL00181  158 QRddLVVIFAGYKDRMDKFYESNPGLSSRIANHVDFPDYTPEELLQIAKIMLEEQ 212
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 130-429 1.51e-43

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 160.40  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 130 RWFLQEQRKRSALEQCGKTKAKMELL---EDELSNIVGLSELKTQLRKWAKGMLLDERRRALGLNIgTRRPPHMAFLGNP 206
Cdd:TIGR03922 243 PWDPSSAPSRAEFVDPAAAERKAKLLaeaEAELAEQIGLERVKRQVAALKSSTAMALARAERGLPV-AQTSNHMLFAGPP 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 207 GTGKTMVARVLGKLLNTVGILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEAEGGILFVDEAYRLIPMQKADDKDYGLE 286
Cdd:TIGR03922 322 GTGKTTIARVVAKIYCGLGVLRKPLVREVSRADLIGQYIGESEAKTNEIIDSALGGVLFLDEAYTLVETGYGQKDPFGLE 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 287 ALEEIMSVM--DTGKIVVIFAGYSEPMKRVIASNEGFCRRVTKFFNFSDFSAKELAQILHiKMNNQGEDTLFYGFR--LH 362
Cdd:TIGR03922 402 AIDTLLARMenDRDRLVVIGAGYRKDLDKFLEVNEGLRSRFTRVIEFPSYSPDELVEIAR-RMATERDSVLDDAAAdaLL 480

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063713509 363 ESCTLQEIASLIEAETTEKQRKEM--NGGLVDTLLVNARENLDLRL----SFECVDTEEICTIKLEDLEAGLR 429
Cdd:TIGR03922 481 EAATTLAQDTTPDANGDLRRGLDIagNGRFVRNVVERAEEERDFRLdhsdRLDAVTVDDLMEITADDVARAVA 553
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 123-426 1.17e-36

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 138.51  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 123 EKLRELLRWFLQEQRKRSALEQCGKTKAKMELLEDELSNIVGLSELKTQLRKWAKGMLLDERRRAlglNIGTRRPPHMAF 202
Cdd:COG0464   120 ELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELRE---EYGLPPPRGLLL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 203 LGNPGTGKTMVARVLGKLLNtvgiLPtdkVTEVQRTDLVGEFVGHTGPKTRRKIQEAEG---GILFVDEAYRLIPMQKAD 279
Cdd:COG0464   197 YGPPGTGKTLLARALAGELG----LP---LIEVDLSDLVSKYVGETEKNLREVFDKARGlapCVLFIDEADALAGKRGEV 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 280 DKDYGLEALEEIMSVMD--TGKIVVIFAGYsepmkRVIASNEGFCRRVTKFFNFSDFSAKELAQILHIkmnnqgedtLFY 357
Cdd:COG0464   270 GDGVGRRVVNTLLTEMEelRSDVVVIAATN-----RPDLLDPALLRRFDEIIFFPLPDAEERLEIFRI---------HLR 335

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 358 GFRLHESCTLQEIAslieaetteKQRKEMNGGLVDTLLVNAREnLDLRLSFECVDTEEIC-TIKLEDLEA 426
Cdd:COG0464   336 KRPLDEDVDLEELA---------EATEGLSGADIRNVVRRAAL-QALRLGREPVTTEDLLeALEREDIFL 395
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-179 6.98e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 6.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWY 82
Cdd:COG0666   121 ETPLHLAAYNGNLEIVKLLLE-AGAD---VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  83 sitaKEISTVKTLLDHNADCSAKDNEGMTPLDHLPQGQGSEKLRELLRWFLQEQRKRSALEQCGKTKAKMELLEDELSNI 162
Cdd:COG0666   197 ----GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         170
                  ....*....|....*..
gi 1063713509 163 VGLSELKTQLRKWAKGM 179
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-106 1.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   6 LHVSAGNGNVDIVKYLLawtgSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFieAKASNGMTPLHLAVWYsit 85
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL----ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARS--- 71

                          90       100
                  ....*....|....*....|.
gi 1063713509  86 aKEISTVKTLLDHNADCSAKD 106
Cdd:pfam12796  72 -GHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 5-167 1.93e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   5 PLHVSAGNGNVDIVKYLLawtgSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYSI 84
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLL----EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  85 TAKEistvktLLDHNADCSAKDNEGMTPLDHLPQGQGSEKLRELLRWF-----LQEQRKRSALEQCGKTKAKMELLEDEL 159
Cdd:PHA02874  236 SAIE------LLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHkadisIKDNKGENPIDTAFKYINKDPVIKDII 309


                  ....*...
gi 1063713509 160 SNIVGLSE 167
Cdd:PHA02874  310 ANAVLIKE 317
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 202-303 6.83e-12

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 62.61  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 202 FLGNPGTGKTMVARVLGKLLNTvgilptdKVTEVQRTDLVGEFVGHTGPKTRRKIQEAE---GGILFVDEAYRLIPMQKA 278
Cdd:pfam00004   3 LYGPPGTGKTTLAKAVAKELGA-------PFIEISGSELVSKYVGESEKRLRELFEAAKklaPCVIFIDEIDALAGSRGS 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063713509 279 DDKDYGLEALEEIMSVMD-----TGKIVVI 303
Cdd:pfam00004  76 GGDSESRRVVNQLLTELDgftssNSKVIVI 105
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 4-121 1.80e-10

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: 62.72  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAwTGSDKVELEAMNT-----------YGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNG 72
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIA-RGADVVSPRATGTffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063713509  73 MTPLHLAVwySITAKEISTVKTLLDHNADcsAKDNEGmtPLDHLPQGQG 121
Cdd:cd22192   170 NTVLHILV--LQPNKTFACQMYDLILSYD--KEDDLQ--PLDLVPNNQG 212
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 182-305 1.95e-09

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 56.00  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 182 DERRRALGLNIGTRRPPHMAFLGNPGTGKTMVARVLGKLLNTVG--ILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEA 259
Cdd:cd00009     4 EEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGapFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063713509 260 EGGILFVDEAYRLIPMQKADdkdyGLEALEEIMSVM-DTGKIVVIFA 305
Cdd:cd00009    84 KPGVLFIDEIDSLSRGAQNA----LLRVLETLNDLRiDRENVRVIGA 126
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 196-303 5.78e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.13  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  196 RPPHMAFLGNPGTGKTMVARVLGKLLNTVG----ILPTDKVTEVQRTDLVGEFVGHTGPKT---------RRKIQEAEGG 262
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGggviYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrlaLALARKLKPD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1063713509  263 ILFVDEAYRLIPMQKADDKDYGLEALEEIMSVMDTGKIVVI 303
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-138 1.49e-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: 44.30  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLA--------WTGSDKVELEAMNT--YGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNG 72
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLErgasvparACGDFFVKSQGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLG 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713509  73 MTPLHLAV---WYSITAKEIST-----VKTLLDHNadCSAKDNEGMTPLDHLPQGQ--GSEKLRELLRWFLQ---EQRK 138
Cdd:TIGR00870 209 NTLLHLLVmenEFKAEYEELSCqmynfALSLLDKL--RDSKELEVILNHQGLTPLKlaAKEGRIVLFRLKLAikyKQKK 285
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 38-67 2.61e-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: 2.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1063713509   38 YGETPLHMAAKNGCNEAAKLLLESGAFIEA 67
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
cbbX CHL00181
CbbX; Provisional
 143-350 1.30e-45

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 159.50  E-value: 1.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 143 EQCGKTKAK--MELLEDELsniVGLSELKTQLRKWAKGMLLDERRRALGLNIGTrrpP--HMAFLGNPGTGKTMVARVLG 218
Cdd:CHL00181    7 EEYEKTQIQevLDILDEEL---VGLAPVKTRIREIAALLLIDRLRKNLGLTSSN---PglHMSFTGSPGTGKTTVALKMA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 219 KLLNTVGILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEAEGGILFVDEAYRLIpmqKAD-DKDYGLEALEEIMSVMDT 297
Cdd:CHL00181   81 DILYKLGYIKKGHLLTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLY---KPDnERDYGSEAIEILLQVMEN 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063713509 298 GK--IVVIFAGYSEPMKRVIASNEGFCRRVTKFFNFSDFSAKELAQILHIKMNNQ 350
Cdd:CHL00181  158 QRddLVVIFAGYKDRMDKFYESNPGLSSRIANHVDFPDYTPEELLQIAKIMLEEQ 212
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 130-429 1.51e-43

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 160.40  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 130 RWFLQEQRKRSALEQCGKTKAKMELL---EDELSNIVGLSELKTQLRKWAKGMLLDERRRALGLNIgTRRPPHMAFLGNP 206
Cdd:TIGR03922 243 PWDPSSAPSRAEFVDPAAAERKAKLLaeaEAELAEQIGLERVKRQVAALKSSTAMALARAERGLPV-AQTSNHMLFAGPP 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 207 GTGKTMVARVLGKLLNTVGILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEAEGGILFVDEAYRLIPMQKADDKDYGLE 286
Cdd:TIGR03922 322 GTGKTTIARVVAKIYCGLGVLRKPLVREVSRADLIGQYIGESEAKTNEIIDSALGGVLFLDEAYTLVETGYGQKDPFGLE 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 287 ALEEIMSVM--DTGKIVVIFAGYSEPMKRVIASNEGFCRRVTKFFNFSDFSAKELAQILHiKMNNQGEDTLFYGFR--LH 362
Cdd:TIGR03922 402 AIDTLLARMenDRDRLVVIGAGYRKDLDKFLEVNEGLRSRFTRVIEFPSYSPDELVEIAR-RMATERDSVLDDAAAdaLL 480

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063713509 363 ESCTLQEIASLIEAETTEKQRKEM--NGGLVDTLLVNARENLDLRL----SFECVDTEEICTIKLEDLEAGLR 429
Cdd:TIGR03922 481 EAATTLAQDTTPDANGDLRRGLDIagNGRFVRNVVERAEEERDFRLdhsdRLDAVTVDDLMEITADDVARAVA 553
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 123-426 1.17e-36

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 138.51  E-value: 1.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 123 EKLRELLRWFLQEQRKRSALEQCGKTKAKMELLEDELSNIVGLSELKTQLRKWAKGMLLDERRRAlglNIGTRRPPHMAF 202
Cdd:COG0464   120 ELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRPELRE---EYGLPPPRGLLL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 203 LGNPGTGKTMVARVLGKLLNtvgiLPtdkVTEVQRTDLVGEFVGHTGPKTRRKIQEAEG---GILFVDEAYRLIPMQKAD 279
Cdd:COG0464   197 YGPPGTGKTLLARALAGELG----LP---LIEVDLSDLVSKYVGETEKNLREVFDKARGlapCVLFIDEADALAGKRGEV 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 280 DKDYGLEALEEIMSVMD--TGKIVVIFAGYsepmkRVIASNEGFCRRVTKFFNFSDFSAKELAQILHIkmnnqgedtLFY 357
Cdd:COG0464   270 GDGVGRRVVNTLLTEMEelRSDVVVIAATN-----RPDLLDPALLRRFDEIIFFPLPDAEERLEIFRI---------HLR 335

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 358 GFRLHESCTLQEIAslieaetteKQRKEMNGGLVDTLLVNAREnLDLRLSFECVDTEEIC-TIKLEDLEA 426
Cdd:COG0464   336 KRPLDEDVDLEELA---------EATEGLSGADIRNVVRRAAL-QALRLGREPVTTEDLLeALEREDIFL 395
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-179 6.98e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 6.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWY 82
Cdd:COG0666   121 ETPLHLAAYNGNLEIVKLLLE-AGAD---VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  83 sitaKEISTVKTLLDHNADCSAKDNEGMTPLDHLPQGQGSEKLRELLRWFLQEQRKRSALEQCGKTKAKMELLEDELSNI 162
Cdd:COG0666   197 ----GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272

                         170
                  ....*....|....*..
gi 1063713509 163 VGLSELKTQLRKWAKGM 179
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-113 5.07e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 5.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAwtgsDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYs 83
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLE----AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN- 163

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063713509  84 itaKEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:COG0666   164 ---GNLEIVKLLLEAGADVNARDNDGETPL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-106 1.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   6 LHVSAGNGNVDIVKYLLawtgSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFieAKASNGMTPLHLAVWYsit 85
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL----ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARS--- 71

                          90       100
                  ....*....|....*....|.
gi 1063713509  86 aKEISTVKTLLDHNADCSAKD 106
Cdd:pfam12796  72 -GHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-113 5.80e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 5.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   2 YHTPLHVSAGNGNVDIVKYLLAWtgsdKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVW 81
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAA----GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY 129

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063713509  82 YSITAkeisTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:COG0666   130 NGNLE----IVKLLLEAGADVNAQDNDGNTPL 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 5-167 1.93e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 1.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   5 PLHVSAGNGNVDIVKYLLawtgSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYSI 84
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLL----EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  85 TAKEistvktLLDHNADCSAKDNEGMTPLDHLPQGQGSEKLRELLRWF-----LQEQRKRSALEQCGKTKAKMELLEDEL 159
Cdd:PHA02874  236 SAIE------LLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHkadisIKDNKGENPIDTAFKYINKDPVIKDII 309


                  ....*...
gi 1063713509 160 SNIVGLSE 167
Cdd:PHA02874  310 ANAVLIKE 317
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-68 3.67e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 3.67e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLawtgsDKVELEaMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAK 68
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-----EHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-116 4.75e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 4.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGN---VDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEA-AKLLLESGAFIEAKASNGMTPLHLa 79
Cdd:PHA03095   49 TPLHLYLHYSSekvKDIVRLLLE-AGAD---VNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHV- 123

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063713509  80 vwYsITAKEI--STVKTLLDHNADCSAKDNEGMTPLDHL 116
Cdd:PHA03095  124 --Y-LSGFNInpKVIRLLLRKGADVNALDLYGMTPLAVL 159
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 4-113 2.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWtGSDkVELEAMNtyGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYS 83
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEY-GAD-VNIEDDN--GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063713509  84 itakEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA02874  202 ----DYACIKLLIDHGNHIMNKCKNGFTPL 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 9-113 1.68e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   9 SAGNGNVDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEAAK---LLLESGAFIEAKASNGMTPLHLavwYSIT 85
Cdd:PHA03095   21 NASNVTVEEVRRLLA-AGAD---VNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHL---YLYN 93

                          90       100
                  ....*....|....*....|....*...
gi 1063713509  86 AKEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA03095   94 ATTLDVIKLLIKAGADVNAKDKVGRTPL 121
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 4-113 2.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 2.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWTGsdkvELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYs 83
Cdd:PHA02878  170 TALHYATENKDQRLTELLLSYGA----NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063713509  84 itAKEISTVKTLLDHNADCSAKDN-EGMTPL 113
Cdd:PHA02878  245 --CKDYDILKLLLEHGVDVNAKSYiLGLTAL 273
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-130 4.24e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 4.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNV-DIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEA--AKLLLESGAFIEAKASNGMTPLHlaV 80
Cdd:PHA03095   85 TPLHLYLYNATTlDVIKLLIK-AGAD---VNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLA--V 158

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063713509  81 WYSITAKEISTVKTLLDHNADCSAKDNEGMTPLDHLPQG--QGSEKLRELLR 130
Cdd:PHA03095  159 LLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIR 210
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 4-113 6.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 6.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGN--GNVDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCN--EAAKLLLESGAFIEAKAS--------- 70
Cdd:PHA03100  108 TPLLYAISKksNSYSIVEYLLD-NGAN---VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyllsygv 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063713509  71 -------NGMTPLHLAVWYSitakEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA03100  184 pinikdvYGFTPLHYAVYNN----NPEFVKYLLDLGANPNLVNKYGDTPL 229
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 202-303 6.83e-12

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 62.61  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 202 FLGNPGTGKTMVARVLGKLLNTvgilptdKVTEVQRTDLVGEFVGHTGPKTRRKIQEAE---GGILFVDEAYRLIPMQKA 278
Cdd:pfam00004   3 LYGPPGTGKTTLAKAVAKELGA-------PFIEISGSELVSKYVGESEKRLRELFEAAKklaPCVIFIDEIDALAGSRGS 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063713509 279 DDKDYGLEALEEIMSVMD-----TGKIVVI 303
Cdd:pfam00004  76 GGDSESRRVVNQLLTELDgftssNSKVIVI 105
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-129 8.81e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  43 LHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAvwysITAKEISTVKTLLDHNAdcSAKDNEGMTPLdHLPQGQGS 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA----AKNGHLEIVKLLLEHAD--VNLKDNGRTAL-HYAARSGH 73


                  ....*..
gi 1063713509 123 EKLRELL 129
Cdd:pfam12796  74 LEIVKLL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 4-121 1.80e-10

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: 62.72  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAwTGSDKVELEAMNT-----------YGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNG 72
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIA-RGADVVSPRATGTffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063713509  73 MTPLHLAVwySITAKEISTVKTLLDHNADcsAKDNEGmtPLDHLPQGQG 121
Cdd:cd22192   170 NTVLHILV--LQPNKTFACQMYDLILSYD--KEDDLQ--PLDLVPNNQG 212
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
159-268 2.19e-10

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 60.67  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 159 LSNIVGLSELKTQLRKWAKGMLLDERRRALGLNIgtrrPPHMAFLGNPGTGKTMVARVLGKLLNtvgiLPtdkVTEVQRT 238
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWP----PRKILFYGPPGTGKTMLAEALAGELK----LP---LLTVRLD 69

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063713509 239 DLVGEFVGHTGPKTRRKIQEAE--GGILFVDE 268
Cdd:COG1223    70 SLIGSYLGETARNLRKLFDFARraPCVIFFDE 101
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 4-113 8.71e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 8.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWTGSdkveLEAMNTYGETPLHMAAKNGCN-EAAKLLLESGAFIEAKAS-NGMTPLHLAVw 81
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHILLENGAS----TDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSI- 277

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063713509  82 ysitaKEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA02878  278 -----KSERKLKLLLEYGADINSLNSYKLTPL 304
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 182-305 1.95e-09

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 56.00  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 182 DERRRALGLNIGTRRPPHMAFLGNPGTGKTMVARVLGKLLNTVG--ILPTDKVTEVQRTDLVGEFVGHTGPKTRRKIQEA 259
Cdd:cd00009     4 EEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGapFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063713509 260 EGGILFVDEAYRLIPMQKADdkdyGLEALEEIMSVM-DTGKIVVIFA 305
Cdd:cd00009    84 KPGVLFIDEIDSLSRGAQNA----LLRVLETLNDLRiDRENVRVIGA 126
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-113 2.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 2.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   1 MYHTPLHVSAGNGNVDIVKYLLAwTGSDkVELEAMNTYgeTPLHMAAKNGCN-----EAAKLLLESGAFIEAKASNGMTP 75
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLD-NGAD-INSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITP 109

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1063713509  76 LHLAVWYSITAKEIstVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA03100  110 LLYAISKKSNSYSI--VEYLLDNGANVNIKNSDGENLL 145
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 4-113 7.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 7.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAwtgSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVwys 83
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLD---LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV--- 143

                          90       100       110
                  ....*....|....*....|....*....|
gi 1063713509  84 iTAKEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA02875  144 -MMGDIKGIELLIDHKACLDIEDCCGCTPL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-107 8.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 8.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  14 NVDI-----VKYLLawtgSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYSItaKE 88
Cdd:PHA03100  166 GVDInaknrVNYLL----SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNN--KE 239

                          90
                  ....*....|....*....
gi 1063713509  89 IstVKTLLDHNADCSAKDN 107
Cdd:PHA03100  240 I--FKLLLNNGPSIKTIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-81 3.32e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 3.32e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063713509  41 TPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVW 81
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-107 1.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   2 YHTPLHVSAGNG-----NVDIVKYLLawtgSDKVELEAMNTYGETPLHMAA--KNGCNEAAKLLLESGAFIEAKASNGMT 74
Cdd:PHA03100   68 NSTPLHYLSNIKynltdVKEIVKLLL----EYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGEN 143

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063713509  75 PLHLAVWYSITAKEIstVKTLLDHNADCSAKDN 107
Cdd:PHA03100  144 LLHLYLESNKIDLKI--LKLLIDKGVDINAKNR 174
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-129 1.34e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 52.65  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  34 AMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYsitaKEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:COG0666    49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN----GDLEIVKLLLEAGADVNARDKDGETPL 124

                          90
                  ....*....|....*.
gi 1063713509 114 dHLPQGQGSEKLRELL 129
Cdd:COG0666   125 -HLAAYNGNLEIVKLL 139
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 172-303 2.39e-07

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 49.97  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 172 LRKWAKGMLLDERRRALGLNIGTRRPPHMAFLGNPGTGKTMVARVLGKLLNTvgilptdKVTEVQRTDLVGEFVGHTGPK 251
Cdd:cd19481     1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGL-------PLIVVKLSSLLSKYVGESEKN 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713509 252 TRRKIQEAE---GGILFVDEAyRLIPMQKADDKD--YGLEALEEIMSVMD----TGKIVVI 303
Cdd:cd19481    74 LRKIFERARrlaPCILFIDEI-DAIGRKRDSSGEsgELRRVLNQLLTELDgvnsRSKVLVI 133
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-115 4.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   1 MYHTPLH-VSAGNGNVDIVKYLLAWTGSdkveLEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLA 79
Cdd:PHA02876  340 LYITPLHqASTLDRNKDIVITLLELGAN----VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063713509  80 VWysiTAKEISTVKTLLDHNADCSAKDNEGMTPLDH 115
Cdd:PHA02876  416 LC---GTNPYMSVKTLIDRGANVNSKNKDLSTPLHY 448
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 186-305 4.43e-07

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 49.60  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 186 RALGLnigtrRPPH-MAFLGNPGTGKTMVARVLGkllNTVGIlptdKVTEVQRTDLVGEFVGHTGPKTRRKIQEAEG--- 261
Cdd:cd19503    27 RALGL-----KPPRgVLLHGPPGTGKTLLARAVA---NEAGA----NFLSISGPSIVSKYLGESEKNLREIFEEARShap 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1063713509 262 GILFVDEAYRLIPMQKADDKDYGLEALEEIMSVMD----TGKIVVIFA 305
Cdd:cd19503    95 SIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDgmssRGKVVVIAA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
2-59 7.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 7.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063713509   2 YHTPLHVSAGNGNVDIVKYLLAwtgsDKVELEAMNTYGETPLHMAAKNGCNEAAKLLL 59
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE----KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-115 9.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 9.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLAWTGSDkveLEAMNTYGETPLHMAAKNGCN-EAAKLLLESGAFIEAKASNGMTPLHLAvw 81
Cdd:PHA02876  274 NTPLHHASQAPSLSRLVPKLLERGAD---VNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQA-- 348

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063713509  82 ySITAKEISTVKTLLDHNADCSAKDNEGMTPLDH 115
Cdd:PHA02876  349 -STLDRNKDIVITLLELGANVNARDYCDKTPIHY 381
Ank_5 pfam13857
Ankyrin repeats (many copies);
36-79 1.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1063713509  36 NTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLA 79
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 4-101 2.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWtgsdKVELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVWYs 83
Cdd:PHA02875  104 TPLHLATILKKLDIMKLLIAR----GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK- 178

                          90
                  ....*....|....*...
gi 1063713509  84 itaKEISTVKTLLDHNAD 101
Cdd:PHA02875  179 ---GDIAICKMLLDSGAN 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-80 5.70e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNG---NVDIVKYLLAwtGSDkveLEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAV 80
Cdd:PHA03095  224 TPLHSMATGSsckRSLVLPLLIA--GIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-67 7.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 7.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063713509   1 MYHTPLHVSAGNGNVDIVKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEA 67
Cdd:PHA03100  191 YGFTPLHYAVYNNNPEFVKYLLD-LGAN---PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-114 8.49e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 8.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713509  43 LHMAAKNGCNEAA-------KLLLESGAFIEAKASNGMTPLHLAVwysiTAKEISTVKTLLDHNADCSAKDNEGMTPLD 114
Cdd:PTZ00322   79 AHMLTVELCQLAAsgdavgaRILLTGGADPNCRDYDGRTPLHIAC----ANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-113 1.13e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  30 VELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAvwysITAKEISTVKTLLDHNADCSAKDNEG 109
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA----IKHNFFDIIKLLLEKGAYANVKDNNG 190


                  ....
gi 1063713509 110 MTPL 113
Cdd:PHA02874  191 ESPL 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 4-101 1.78e-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: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLawtGSDKVELEAMNTYGETPLHMAAKNGCNEAAKLLLES--GAFIEAKASN---GMTPLHL 78
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL---KCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapELVNEPMTSDlyqGETALHI 95

                          90       100
                  ....*....|....*....|...
gi 1063713509  79 AVwysiTAKEISTVKTLLDHNAD 101
Cdd:cd22192    96 AV----VNQNLNLVRELIARGAD 114
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 4-114 3.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWTGSDKVEleamNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPlhlAVWYS 83
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDIE----DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVA---ALCYA 209

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063713509  84 ITAKEISTVKTLLDHNADCS---AKDNEGMTPLD 114
Cdd:PHA02875  210 IENNKIDIVRLFIKRGADCNimfMIEGEECTILD 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 71-107 3.66e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 3.66e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1063713509  71 NGMTPLHLAVWYsitAKEISTVKTLLDHNADCSAKDN 107
Cdd:pfam00023   1 DGNTPLHLAAGR---RGNLEIVKLLLSKGADVNARDK 34
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 196-303 5.78e-05

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.13  E-value: 5.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  196 RPPHMAFLGNPGTGKTMVARVLGKLLNTVG----ILPTDKVTEVQRTDLVGEFVGHTGPKT---------RRKIQEAEGG 262
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGggviYIDGEDILEEVLDQLLLIIVGGKKASGsgelrlrlaLALARKLKPD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1063713509  263 ILFVDEAYRLIPMQKADDKDYGLEALEEIMSVMDTGKIVVI 303
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVIL 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 30-106 6.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 6.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063713509  30 VELEAMNTYGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHlavwYSITAKEISTVKTLLDHNADCSAKD 106
Cdd:PHA02876  169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE----CAVDSKNIDTIKAIIDNRSNINKND 241
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 4-113 8.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 8.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWTGsdkvELEAMNTYGETPLHMAAKnGCNE--AAKLLLESGAFIEAKASNGMTPLHLAVW 81
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGA----DIEALSQKIGTALHFALC-GTNPymSVKTLIDRGANVNSKNKDLSTPLHYACK 451

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063713509  82 YSItakEISTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA02876  452 KNC---KLDVIEMLLDNGADVNAINIQNQYPL 480
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 176-272 9.30e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 44.31  E-value: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 176 AKGMLLderRRAlglnIGTRRPPHMAFLGNPGTGKTMVARVLGK-------LLNTVgilpTDKVTEVqrtdlvgefvght 248
Cdd:PRK13342   22 GPGKPL---RRM----IEAGRLSSMILWGPPGTGKTTLARIIAGatdapfeALSAV----TSGVKDL------------- 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063713509 249 gpktRRKIQEAEGG-------ILFVDEAYRL 272
Cdd:PRK13342   78 ----REVIEEARQRrsagrrtILFIDEIHRF 104
PHA03095 PHA03095
ankyrin-like protein; Provisional
 3-113 9.88e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 9.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDI--VKYLLAwTGSDkveLEAMNTYGETPLHMAAKNGCNEAAKL--LLESGAFIEAKASNGMTPLHL 78
Cdd:PHA03095  153 MTPLAVLLKSRNANVelLRLLID-AGAD---VYAVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHS 228

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063713509  79 AVWYSITAKeiSTVKTLLDHNADCSAKDNEGMTPL 113
Cdd:PHA03095  229 MATGSSCKR--SLVLPLLIAGISINARNRYGQTPL 261
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
146-268 1.18e-04

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 44.25  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 146 GKTKAKMeLLEDEL----SNIVGLSELKTQLRKWAKGMLLDERRRALGLNIgtrrPPHMAFLGNPGTGKTMVARvlgkll 221
Cdd:PRK10733  135 GKSKARM-LTEDQIkttfADVAGCDEAKEEVAELVEYLREPSRFQKLGGKI----PKGVLMVGPPGTGKTLLAK------ 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063713509 222 ntvGILPTDKVT--EVQRTDLVGEFVGHTGPKTRRKIQEAEGG---ILFVDE 268
Cdd:PRK10733  204 ---AIAGEAKVPffTISGSDFVEMFVGVGASRVRDMFEQAKKAapcIIFIDE 252
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 197-305 1.29e-04

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 42.50  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 197 PPH-MAFLGNPGTGKTMVARVLGKLLNTVGilptDKVTEVQR--TDLVGEFVGHTGPKTRRKIQEA---EGGILFVDEAY 270
Cdd:cd19517    33 PPRgVLFHGPPGTGKTLMARALAAECSKGG----QKVSFFMRkgADCLSKWVGEAERQLRLLFEEAyrmQPSIIFFDEID 108

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063713509 271 RLIPMQKADDKDYGLEALEEIMSVMD----TGKIVVIFA 305
Cdd:cd19517   109 GLAPVRSSKQEQIHASIVSTLLALMDgldnRGQVVVIGA 147
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-138 1.49e-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: 44.30  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLA--------WTGSDKVELEAMNT--YGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNG 72
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLErgasvparACGDFFVKSQGVDSfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLG 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713509  73 MTPLHLAV---WYSITAKEIST-----VKTLLDHNadCSAKDNEGMTPLDHLPQGQ--GSEKLRELLRWFLQ---EQRK 138
Cdd:TIGR00870 209 NTLLHLLVmenEFKAEYEELSCqmynfALSLLDKL--RDSKELEVILNHQGLTPLKlaAKEGRIVLFRLKLAikyKQKK 285
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 147-268 1.64e-04

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 43.46  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 147 KTKAKMELLEDELSNIVGLSELKTQLRKwakgMLLDERRRA-LGLNIGTRRPPHMAFLGNPGTGKTMVARVL-----GKL 220
Cdd:COG1222    65 GTAVPAESPDVTFDDIGGLDEQIEEIRE----AVELPLKNPeLFRKYGIEPPKGVLLYGPPGTGKTLLAKAVagelgAPF 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063713509 221 LNTVGilptdkvtevqrTDLVGEFVGHTGPKTR---RKIQEAEGGILFVDE 268
Cdd:COG1222   141 IRVRG------------SELVSKYIGEGARNVRevfELAREKAPSIIFIDE 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 38-67 2.61e-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: 2.61e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1063713509   38 YGETPLHMAAKNGCNEAAKLLLESGAFIEA 67
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
 204-343 2.91e-04

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 42.25  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 204 GNPGTGKTMVARVLGKL-LNTVGILPTDKVTevqRTDLVGEFV--------GHTGPKTRRKIQEA---EGGILFVDEAYR 271
Cdd:COG2842    57 GESGVGKTTAAREYANRnPNVIYVTASPSWT---SKELLEELAeelgipapPGTIADLRDRILERlagTGRLLIIDEADH 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063713509 272 LIPmqkaddkdyglEALEEIMSVMDTGKIVVIFAGysepMKRVIASNEGFCR---RVTKFFNFSDFSAKELAQIL 343
Cdd:COG2842   134 LKP-----------KALEELRDIHDETGVGVVLIG----MERLPAKLKRYEQlysRIGFWVEFKPLSLEDVRALA 193
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-68 3.50e-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: 37.65  E-value: 3.50e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1063713509  38 YGETPLHMAA-KNGCNEAAKLLLESGAFIEAK 68
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
72-115 4.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 4.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1063713509  72 GMTPLHLAVWYSitAKEIstVKTLLDHNADCSAKDNEGMTPLDH 115
Cdd:pfam13857  16 GYTPLHVAAKYG--ALEI--VRVLLAYGVDLNLKDEEGLTALDL 55
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-63 4.76e-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: 37.24  E-value: 4.76e-04
                          10        20
                  ....*....|....*....|....*.
gi 1063713509  38 YGETPLHMAAKNGCNEAAKLLLESGA 63
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 3-80 6.32e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   3 HTPLHVSAGNGNVDIVKYLLAwTGSDkVELEAMNT-----------YGETPLHMAAKNGCNEAAKLLLESG---AFIEAK 68
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVE-NGAD-VSARATGRffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGaqpAALEAQ 151

                          90
                  ....*....|..
gi 1063713509  69 ASNGMTPLHLAV 80
Cdd:cd21882   152 DSLGNTVLHALV 163
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 36-113 8.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 8.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  36 NTYGETPLH--MAAKNGCNEAAKLLLESGAFIEAKA-SNGMTPLHLAVWYSITAkEISTVKTLLDHNADCSAKDNEGMTP 112
Cdd:PHA02859   48 NDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTrDNNLSALHHYLSFNKNV-EPEILKILIDSGSSITEEDEDGKNL 126


                  .
gi 1063713509 113 L 113
Cdd:PHA02859  127 L 127
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 161-305 8.67e-04

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 41.82  E-value: 8.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 161 NIVGLSELKTQLRKWAKgmlLDERRRALGLNIGTRRPPHMAFLGNPGTGKTMVARVLGKLLNTVGILptdkvteVQRTDL 240
Cdd:TIGR01243 179 DIGGLKEAKEKIREMVE---LPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFIS-------INGPEI 248

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063713509 241 VGEFVGHTGPKTRRKIQEAEG---GILFVDEAYRLIPMQKADDKDYGLEALEEIMSVMD----TGKIVVIFA 305
Cdd:TIGR01243 249 MSKYYGESEERLREIFKEAEEnapSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDglkgRGRVIVIGA 320
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 199-303 8.80e-04

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 39.20  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 199 HMAFLGNPGTGKTMVARVLGKLLNtvgilpTDKVTEVQ------RTDLVGEFVGHTGpKTRRKIQEA-----EGGILFVD 267
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALS------NRPVFYVQltrdttEEDLFGRRNIDPG-GASWVDGPLvraarEGEIAVLD 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1063713509 268 EAYRLIPmqkaddkdyglEALEEIMSVMDTGKIVVI 303
Cdd:pfam07728  74 EINRANP-----------DVLNSLLSLLDERRLLLP 98
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-131 9.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509  13 GNVDIVKYLLAWTGSDKVELEAmntyGETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAVwysiTAKEISTV 92
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYD----GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAV----EEGDVKAV 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1063713509  93 KTLLDHNA---DCSAKDneGMTPLDHLPQGQGSEKLRELLRW 131
Cdd:PHA02875   85 EELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIAR 124
Ank_5 pfam13857
Ankyrin repeats (many copies);
4-46 1.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1063713509   4 TPLHVSAGNGNVDIVKYLLAWTGSDKVEleamNTYGETPLHMA 46
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLK----DEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 4-80 2.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063713509   4 TPLHVSAGN-GNVDIVKYLLawtgSDKVELEAMNT-YGETPLHMAAKNgcNEAAKLLLESGAFIEAKASNGMTPLHLAV 80
Cdd:PHA02878  236 TPLHISVGYcKDYDILKLLL----EHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 2-59 2.34e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   2 YH--TPLHVSAGNGNVDIVKYLLAWtGSDkveLEAMNTYGETPLHMAAKNGCNEAAKLLL 59
Cdd:PTZ00322  113 YDgrTPLHIACANGHVQVVRVLLEF-GAD---PTLLDKDGKTPLELAEENGFREVVQLLS 168
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 168-305 3.08e-03

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 38.19  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 168 LKTQLRKWAKGMLLDERRRALGLNIGTRRPPHMAFLGNPGTGKTMVARVLGKLLNTVGILptdkvteVQRTDLVGEFVGH 247
Cdd:cd19519     5 CRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFL-------INGPEIMSKLAGE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063713509 248 TGPKTRRKIQEAEG---GILFVDEAYRLIPMQKADDKDYGLEALEEIMSVMD----TGKIVVIFA 305
Cdd:cd19519    78 SESNLRKAFEEAEKnapAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDglkqRAHVIVMAA 142
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 200-260 3.63e-03

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 38.24  E-value: 3.63e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063713509 200 MAFLGNPGTGKTMVARVLGKLLNtvGILPtdKVteVQRTDLVGEFVGHTGPKTRRKIQEAE 260
Cdd:cd19504    38 ILLYGPPGTGKTLMARQIGKMLN--AREP--KI--VNGPEILNKYVGESEANIRKLFADAE 92
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 2-109 5.02e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.26  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509   2 YHTPLH--VSAGNGNVDIVKYLLAwTGSDkVELEAMNtYGETPLH---MAAKNGCNEAAKLLLESGAFIEAKASNGMTPL 76
Cdd:PHA02859   51 YETPIFscLEKDKVNVEILKFLIE-NGAD-VNFKTRD-NNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLL 127

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063713509  77 HlaVWYSITAKEISTVKTLLDHNADCSAKDNEG 109
Cdd:PHA02859  128 H--MYMCNFNVRINVIKLLIDSGVSFLNKDFDN 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-115 5.23e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 5.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1063713509  72 GMTPLHLAvwysITAKEISTVKTLLDHNADCSAKDNEGMTPLDH 115
Cdd:pfam13637   1 ELTALHAA----AASGHLELLRLLLEKGADINAVDGNGETALHF 40
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 39-80 5.42e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 5.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1063713509  39 GETPLHMAAKNGCNEAAKLLLESGAFIEAKASNGMTPLHLAV 80
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-104 5.94e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 5.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1063713509   71 NGMTPLHLAVWYsitaKEISTVKTLLDHNADCSA 104
Cdd:smart00248   1 DGRTPLHLAAEN----GNLEVVKLLLDKGADINA 30
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 152-310 6.22e-03

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 39.12  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 152 MELLEDELSNIVGLSELKTQLRKWAKGMLldeRRRALGLNIGTRRPPHMAFLGNPGTGKTMVARvlgkllnTVGILPTDK 231
Cdd:TIGR01243 445 VEVPNVRWSDIGGLEEVKQELREAVEWPL---KHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAK-------AVATESGAN 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 232 VTEVQRTDLVGEFVGHTGPKTR---RKIQEAEGGILFVDEAYRLIPMQKADD----KDYGLEALEEIMSVMDTGKIVVIF 304
Cdd:TIGR01243 515 FIAVRGPEILSKWVGESEKAIReifRKARQAAPAIIFFDEIDAIAPARGARFdtsvTDRIVNQLLTEMDGIQELSNVVVI 594


                  ....*.
gi 1063713509 305 AGYSEP 310
Cdd:TIGR01243 595 AATNRP 600
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 6-76 6.76e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 38.74  E-value: 6.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063713509   6 LHVSAGNGNVDIvkYLLAWTGSDKVELEAMNTYGETPLH--MAAKNGCNEAAKLLLESGAFIEAKASNGMTPL 76
Cdd:PHA02716  181 LHAYLGNMYVDI--DILEWLCNNGVNVNLQNNHLITPLHtyLITGNVCASVIKKIIELGGDMDMKCVNGMSPI 251
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 181-343 7.00e-03

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 38.38  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 181 LDERRRALGLNIGTRRPPHMAFLGNPGTGKTMVARVLGKLLNTVGILPTDKVT------EVQRT------DLVGEFVGH- 247
Cdd:TIGR02928  24 IEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDVRVVtvyvncQILDTlyqvlvELANQLRGSg 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 248 -----TGPKTRR-------KIQEAEGGILFV-DEAYRLIpmQKADDKDYGLEALEEiMSVMDTGKIVVIF----AGYSEP 310
Cdd:TIGR02928 104 eevptTGLSTSEvfrrlykELNERGDSLIIVlDEIDYLV--GDDDDLLYQLSRARS-NGDLDNAKVGVIGisndLKFREN 180

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063713509 311 M-KRVIASnegFCRRVtkfFNFSDFSAKELAQIL 343
Cdd:TIGR02928 181 LdPRVKSS---LCEEE---IIFPPYDAEELRDIL 208
DUF2075 pfam09848
Schlafen group 3, DNA/RNA helicase domain; This domain is found in at the C terminus of group ...
 198-304 7.28e-03

Schlafen group 3, DNA/RNA helicase domain; This domain is found in at the C terminus of group 3 Schlafen proteins from mammals, and represents the DNA/RNA helicase domain. Schlafen proteins are involved in the control of cell proliferation, induction of immune responses, and in the regulation of viral replication. These proteins inhibit DNA replication and promote cell death in response to DNA damage. They play a role in genome surveillance to kill cells with defective replication. This domain is also found in various uncharacterized prokaryotic proteins fused to a DNA helicase, GIY-YIG or PD-(D/E)XK catalytic domain or HsdR-N(terminal) domain, which are similar to AAA DNA helicase, Type III restriction enzyme ATPase, RecD and RuvB helicase.


Pssm-ID: 430875 [Multi-domain]  Cd Length: 355  Bit Score: 38.42  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 198 PHMAFL-GNPGTGKTMVA-RVLGKLLNTVGILPTDKVT----EVQ--RTDLVGEFVGHTGPKTRRK----IQEAEGG--- 262
Cdd:pfam09848   1 KAVFLVtGGPGTGKTVIGlNLFAELEDSDLGRTAVYLSgnhpLVLvlYEALAGDLRKKRKKSAFQRptsfINNLHKThph 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063713509 263 --ILFVDEAYRLIPMQKADDKDYGLEALEEImsvMDTGKIVVIF 304
Cdd:pfam09848  81 edVVIFDEAHRLWDKSDPYNNFSGPNQLKEI---MKRAKVIVFL 121
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 161-268 8.79e-03

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 36.96  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 161 NIVGLSELKTQLRKWAKGmlLDERRRALGLNIgtrrPPHMAFLGNPGTGKTMVARVLGKLLNtvgiLPTDKVtEVQRtdL 240
Cdd:cd19507     1 DVGGLDNLKDWLKKRKAA--FSKQASAYGLPT----PKGLLLVGIQGTGKSLTAKAIAGVWQ----LPLLRL-DMGR--L 67

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063713509 241 VGEFVGHTGPKTRRKIQEAEG---GILFVDE 268
Cdd:cd19507    68 FGGLVGESESRLRQMIQTAEAiapCVLWIDE 98
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 176-272 9.34e-03

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 38.11  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063713509 176 AKGMLLderRRAlglnIGTRRPPHMAFLGNPGTGKTMVARVLGKL-------LNTVgilpTDKVTEVqrtdlvgefvght 248
Cdd:COG2256    35 GPGKPL---RRA----IEAGRLSSMILWGPPGTGKTTLARLIANAtdaefvaLSAV----TSGVKDI------------- 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063713509 249 gpktRRKIQEAE-----GG--ILFVDEAYRL 272
Cdd:COG2256    91 ----REVIEEARerrayGRrtILFVDEIHRF 117
 
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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