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Conserved domains on  [gi|1907164552|ref|XP_006535114|]
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ADP-ribosylation factor-like protein 9 isoform X2 [Mus musculus]

Protein Classification

Arl9_Arfrp2_like domain-containing protein( domain architecture ID 10134997)

Arl9_Arfrp2_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 489-654 3.70e-82

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


:

Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 256.22  E-value: 3.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04162     1 QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 569 KRLPEAKKYLHQLINPNPGLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRKLFLFGTQVTKNGSeiPSTMQDAKDLI 648
Cdd:cd04162    81 ERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGTSLDDDGS--PSRMEAVKDLL 158


                  ....*.
gi 1907164552 649 THLATD 654
Cdd:cd04162   159 SQLINL 164
PTZ00121 super family cl31754
MAEBL; Provisional
 340-463 1.09e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  340 RKSADLKTKETGKEKVEEKRKSADLKTKETGKEKVEEKRKSADLKTKETGKEKEEEKRKSADlktkETGKEKEEEKRKSA 419
Cdd:PTZ00121  1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD----EAKKKAEEAKKKAD 1500

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907164552  420 DLKTKENGKDKGKE----EEKRKNDE--KGKENGTGMEAKEEQGTEKEKE 463
Cdd:PTZ00121  1501 EAKKAAEAKKKADEakkaEEAKKADEakKAEEAKKADEAKKAEEKKKADE 1550
 
Name Accession Description Interval E-value
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 489-654 3.70e-82

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 256.22  E-value: 3.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04162     1 QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 569 KRLPEAKKYLHQLINPNPGLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRKLFLFGTQVTKNGSeiPSTMQDAKDLI 648
Cdd:cd04162    81 ERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGTSLDDDGS--PSRMEAVKDLL 158


                  ....*.
gi 1907164552 649 THLATD 654
Cdd:cd04162   159 SQLINL 164
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 490-632 1.45e-33

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 125.80  E-value: 1.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQHsTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADHK 569
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLKLGEIVT-TIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADRD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552 570 RLPEAKKYLHQLIN--PNPGLPLVVFANKQDLEAAYHITDIHDALALSEVgNDRKLFLFGTQVTK 632
Cdd:pfam00025  82 RIEEAKEELHALLNeeELADAPLLILANKQDLPGAMSEAEIRELLGLHEL-KDRPWEIQGCSAVT 145
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 489-631 4.14e-22

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 93.83  E-value: 4.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:smart00177  15 RILMVGLDAAGKTTILYKLKLGESV-TTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDR 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552  569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVgNDRKLFLFGTQVT 631
Cdd:smart00177  94 DRIDEAREELHRMLNEDElrDAVILVFANKQDLPDAMKAAEITEKLGLHSI-RDRNWYIQPTCAT 157
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 489-614 6.88e-21

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 90.41  E-value: 6.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:PLN00223   19 RILMVGLDAAGKTTILYKLKLGEIV-TTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALAL 614
Cdd:PLN00223   98 DRVVEARDELHRMLNEDElrDAVLLVFANKQDLPNAMNAAEITDKLGL 145
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
487-616 2.54e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 487 NKQILVLGLDGAGKTSVLHLLASNRVqhSTAPTQGLNAVHI-------NSEDRQMEFLEIGGSEPFRSYWEMYLPkgWL- 558
Cdd:COG1100     3 EKKIVVVGTGGVGKTSLVNRLVGDIF--SLEKYLSTNGVTIdkkelklDGLDVDLVIWDTPGQDEFRETRQFYAR--QLt 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907164552 559 ----LIFVVDSADHKRLPEAKKYLHQLINPNPGLPLVVFANKQDLeaaYHITDIHDALALSE 616
Cdd:COG1100    79 gaslYLFVVDGTREETLQSLYELLESLRRLGKKSPIILVLNKIDL---YDEEEIEDEERLKE 137
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 488-600 1.19e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 48.91  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 488 KQILVLGLDGAGKTSVLHLLASN-RVQHSTAPTQGLNA----VHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFV 562
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYvttvIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907164552 563 VDSADH-KRLPEAK-KYLHQLINPNP-GLPLVVFANKQDLE 600
Cdd:TIGR00231  82 FDIVILvLDVEEILeKQTKEIIHHADsGVPIILVGNKIDLK 122
PTZ00121 PTZ00121
MAEBL; Provisional
 340-463 1.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  340 RKSADLKTKETGKEKVEEKRKSADLKTKETGKEKVEEKRKSADLKTKETGKEKEEEKRKSADlktkETGKEKEEEKRKSA 419
Cdd:PTZ00121  1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD----EAKKKAEEAKKKAD 1500

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907164552  420 DLKTKENGKDKGKE----EEKRKNDE--KGKENGTGMEAKEEQGTEKEKE 463
Cdd:PTZ00121  1501 EAKKAAEAKKKADEakkaEEAKKADEakKAEEAKKADEAKKAEEKKKADE 1550
 
Name Accession Description Interval E-value
Arl9_Arfrp2_like cd04162
Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first ...
 489-654 3.70e-82

Arf-like 9 (Arl9)/Arfrp2-like GTPase; Arl9/Arfrp2-like subfamily. Arl9 (Arf-like 9) was first identified as part of the Human Cancer Genome Project. It maps to chromosome 4q12 and is sometimes referred to as Arfrp2 (Arf-related protein 2). This is a novel subfamily identified in human cancers that is uncharacterized to date.


Pssm-ID: 133362 [Multi-domain]  Cd Length: 164  Bit Score: 256.22  E-value: 3.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04162     1 QILVLGLDGAGKTSLLHSLSSERSLESVVPTTGFNSVAIPTQDAIMELLEIGGSQNLRKYWKRYLSGSQGLIFVVDSADS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 569 KRLPEAKKYLHQLINPNPGLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRKLFLFGTQVTKNGSeiPSTMQDAKDLI 648
Cdd:cd04162    81 ERLPLARQELHQLLQHPPDLPLVVLANKQDLPAARSVQEIHKELELEPIARGRRWILQGTSLDDDGS--PSRMEAVKDLL 158


                  ....*.
gi 1907164552 649 THLATD 654
Cdd:cd04162   159 SQLINL 164
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 489-628 7.37e-34

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 126.54  E-value: 7.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd00878     1 RILMLGLDGAGKTTILYKLKLGEVV-TTIPTIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSDR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVGnDRKLFLFGT 628
Cdd:cd00878    80 ERIEEAKNELHKLLNEEElkGAPLLILANKQDLPGALTESELIELLGLESIK-GRRWHIQPC 140
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
 490-632 1.45e-33

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 125.80  E-value: 1.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQHsTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADHK 569
Cdd:pfam00025   3 ILILGLDNAGKTTILYKLKLGEIVT-TIPTIGFNVETVTYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSADRD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552 570 RLPEAKKYLHQLIN--PNPGLPLVVFANKQDLEAAYHITDIHDALALSEVgNDRKLFLFGTQVTK 632
Cdd:pfam00025  82 RIEEAKEELHALLNeeELADAPLLILANKQDLPGAMSEAEIRELLGLHEL-KDRPWEIQGCSAVT 145
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
 477-615 6.08e-32

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 121.73  E-value: 6.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 477 IKTLYPPPVENKQILVLGLDGAGKTSVLHLLASNRVQHsTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKG 556
Cdd:cd04155     5 LRKLKPSSRQEVRILLLGLDNAGKTTILKQLASEDISH-ITPTQGFNIKNVQADGFKLNVWDIGGQRKIRPYWRNYFENT 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907164552 557 WLLIFVVDSADHKRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALS 615
Cdd:cd04155    84 DVLIYVIDSADRKRFEEAGQELVELLEEEKlaGVPVLVFANKQDLLTAAPAEEVAEALNLH 144
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
 489-632 1.52e-28

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.


Pssm-ID: 206718 [Multi-domain]  Cd Length: 158  Bit Score: 111.73  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04151     1 RILILGLDGAGKTTILYRLQVGEVV-TTIPTIGFNVETVTYKNLKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTDR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVgNDRKLFLFGTQVTK 632
Cdd:cd04151    80 DRLGISKSELHAMLEEEElkDAVLLVFANKQDMPGALSEAEVAEKLGLSEL-KDRTWQIFKTSATK 144
Arl10_like cd04159
Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from ...
 490-642 6.86e-27

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.


Pssm-ID: 206724 [Multi-domain]  Cd Length: 159  Bit Score: 107.02  E-value: 6.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADHK 569
Cdd:cd04159     2 ITLVGLQNSGKTTLVNVIASGQFSEDTIPTVGFNMRKVTKGNVTIKVWDLGGQPRFRSMWERYCRGVNAIVYVVDAADRE 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552 570 RLPEAKKYLHQLIN-PN-PGLPLVVFANKQDLEAAYHITDIHDALALSEVGnDRKLFLFGTQVtKNGSEIPSTMQ 642
Cdd:cd04159    82 KLEVAKNELHDLLEkPSlEGIPLLVLGNKNDLPGALSVDELIEQMNLKSIT-DREVSCYSISA-KEKTNIDIVLD 154
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
 475-627 5.33e-26

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 105.12  E-value: 5.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 475 TSIKTLYPPPVENKqILVLGLDGAGKTSVLHLLASNRVQHsTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLP 554
Cdd:cd04153     4 SSLWSLFFPRKEYK-VIIVGLDNAGKTTILYQFLLGEVVH-TSPTIGSNVEEIVYKNIRFLMWDIGGQESLRSSWNTYYT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552 555 KGWLLIFVVDSADHKRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVgNDRKLFLFG 627
Cdd:cd04153    82 NTDAVILVIDSTDRERLPLTKEELYKMLAHEDlrKAVLLVLANKQDLKGAMTPAEISESLGLTSI-RDHTWHIQG 155
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
 489-625 5.48e-23

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 95.95  E-value: 5.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLaSNRVQHSTAPTQGLNAVHINSEDR-QMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSAD 567
Cdd:cd04156     1 QVLLLGLDSAGKSTLLYKL-KHAELVTTIPTVGFNVEMLQLEKHlSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSD 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 568 HKRLPEAKKYL-HQLINPN-PGLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRKLFL 625
Cdd:cd04156    80 EARLDESQKELkHILKNEHiKGVPVVLLANKQDLPGALTAEEITRRFKLKKYCSDRDWYV 139
Arl4_Arl7 cd04152
Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular ...
 490-621 7.43e-23

Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206719 [Multi-domain]  Cd Length: 183  Bit Score: 96.41  E-value: 7.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQHsTAPTQGLNAVHI-----NSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVD 564
Cdd:cd04152     6 IVMLGLDSAGKTTVLYRLKFNEFVN-TVPTKGFNTEKIkvslgNAKGVTFHFWDVGGQEKLRPLWKSYTRCTDGIVFVVD 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907164552 565 SADHKRLPEAKKYLHQL--INPNPGLPLVVFANKQDLEAAYHITDIHDALALSEVGNDR 621
Cdd:cd04152    85 SVDVERMEEAKTELHKItkFSENQGVPVLVLANKQDLPNALPVSEVEKLLALHELSSST 143
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
 489-619 1.22e-22

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 95.23  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04149    11 RILMLGLDAAGKTTILYKLKLGQSV-TTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSADR 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVGN 619
Cdd:cd04149    90 DRIDEARQELHRIINDREmrDALLLVFANKQDLPDAMKPHEIQEKLGLTRIRD 142
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
 490-602 2.66e-22

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 95.04  E-value: 2.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVqHSTAPTQglnavHINSED---RQMEF--LEIGGSEPFRSYWEMYLPKGWLLIFVVD 564
Cdd:cd00879    22 IVFLGLDNAGKTTLLHMLKDDRL-AQHVPTL-----HPTSEEltiGNVKFttFDLGGHEQARRVWKDYFPEVDGIVFLVD 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907164552 565 SADHKRLPEAKKYLHQLINPN--PGLPLVVFANKQDLEAA 602
Cdd:cd00879    96 AADPERFQESKEELDSLLNDEelANVPILILGNKIDKPGA 135
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
 489-631 4.14e-22

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 93.83  E-value: 4.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:smart00177  15 RILMVGLDAAGKTTILYKLKLGESV-TTIPTIGFNVETVTYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDSNDR 93

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552  569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVgNDRKLFLFGTQVT 631
Cdd:smart00177  94 DRIDEAREELHRMLNEDElrDAVILVFANKQDLPDAMKAAEITEKLGLHSI-RDRNWYIQPTCAT 157
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
 490-626 4.30e-22

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725 [Multi-domain]  Cd Length: 168  Bit Score: 93.56  E-value: 4.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQ-------HSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFV 562
Cdd:cd04160     2 VLILGLDNAGKTTFLEQTKTKFSKnykglnpSKITPTVGLNIGTIEVGKARLMFWDLGGQEELRSLWDKYYAESHGVIYV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907164552 563 VDSADHKRLPEAKKYLHQLINpNP---GLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRKLFLF 626
Cdd:cd04160    82 IDSTDRERFNESKSAFEKVIN-NEaleGVPLLVLANKQDLPDALSVAEIKEVFDDCIALIGRRDCLV 147
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 489-619 5.87e-21

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 90.18  E-value: 5.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVL-HLLASNRVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSAD 567
Cdd:cd04157     1 NILVLGLDNSGKTTIInQLKPSNAQSQNIVPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSSD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907164552 568 HKRLPEAKKYLHQLIN----PNPGLPLVVFANKQDLEAAYHITDIHDALALSEVGN 619
Cdd:cd04157    81 RLRMVVAKDELELLLNhpdiKHRRIPILFYANKMDLPDALTAVKITQLLCLENIKD 136
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
 489-614 6.88e-21

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 90.41  E-value: 6.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:PLN00223   19 RILMVGLDAAGKTTILYKLKLGEIV-TTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALAL 614
Cdd:PLN00223   98 DRVVEARDELHRMLNEDElrDAVLLVFANKQDLPNAMNAAEITDKLGL 145
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
 489-631 3.84e-20

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).


Pssm-ID: 206717 [Multi-domain]  Cd Length: 159  Bit Score: 87.85  E-value: 3.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04150     2 RILMVGLDAAGKTTILYKLKLGEIV-TTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552 569 KRLPEAKKYLHQLINPNPGLP--LVVFANKQDLEAAYHITDIHDALALSEVGNdRKLFLFGTQVT 631
Cdd:cd04150    81 ERIGEAREELQRMLNEDELRDavLLVFANKQDLPNAMSAAEVTDKLGLHSLRN-RNWYIQATCAT 144
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 489-631 2.50e-19

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 86.05  E-value: 2.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQhSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:PTZ00133   19 RILMVGLDAAGKTTILYKLKLGEVV-TTIPTIGFNVETVEYKNLKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDSNDR 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVGNdRKLFLFGTQVT 631
Cdd:PTZ00133   98 ERIGDAREELERMLSEDElrDAVLLVFANKQDLPNAMSTTEVTEKLGLHSVRQ-RNWYIQGCCAT 161
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
 490-619 1.52e-18

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.


Pssm-ID: 206720 [Multi-domain]  Cd Length: 173  Bit Score: 83.53  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLaSNRVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADHK 569
Cdd:cd04154    17 ILMLGLDNAGKTTILKKF-NGEDISTISPTLGFNIKTLEYNGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVDSSDRA 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907164552 570 RLPEAKKYLHQLINPN--PGLPLVVFANKQDLEAAYHITDIHDALALSEVGN 619
Cdd:cd04154    96 RLEDCKRELQKLLVEErlAGATLLIFANKQDLPGALSPEEIREVLELDSIKS 147
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
 490-622 5.97e-18

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 81.67  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNrVQHSTAPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADHK 569
Cdd:cd04161     2 LLTVGLDNAGKTTLVSALQGE-IPKKVAPTVGFTPTKLRLDKYEVCIFDLGGGANFRGIWVNYYAEAHGLVFVVDSSDDD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907164552 570 RLPEAKKYLHQLINpNP---GLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRK 622
Cdd:cd04161    81 RVQEVKEILRELLQ-HPrvsGKPILVLANKQDKKNALLGADVIEYLSLEKLVNENK 135
SAR smart00178
Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene ...
 489-614 5.97e-14

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 197556 [Multi-domain]  Cd Length: 184  Bit Score: 70.73  E-value: 5.97e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  489 QILVLGLDGAGKTSVLHLLASNR-VQHStaPTQglnavHINSEDR---QMEF--LEIGGSEPFRSYWEMYLPKGWLLIFV 562
Cdd:smart00178  19 KILFLGLDNAGKTTLLHMLKNDRlAQHQ--PTQ-----HPTSEELaigNIKFttFDLGGHQQARRLWKDYFPEVNGIVYL 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907164552  563 VDSADHKRLPEAKKYLHQLINPN--PGLPLVVFANKQDLEAAYHITDIHDALAL 614
Cdd:smart00178  92 VDAYDKERFAESKRELDALLSDEelATVPFLILGNKIDAPYAASEDELRYALGL 145
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
 489-627 1.17e-13

(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membrane. Two Tyr-based motifs in the Arf domain are responsible for Golgi localization, while the GAP domain controls lysosomal localization.


Pssm-ID: 206723 [Multi-domain]  Cd Length: 169  Bit Score: 69.29  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQHSTaPTQGLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDSADH 568
Cdd:cd04158     1 RVVTLGLDGAGKTTILFKLKQDEFMQPI-PTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDSSHR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907164552 569 KRLPEAKKYLHQLINPNP--GLPLVVFANKQDLEAAYHITDIHDALALSEVGNDRKLFLFG 627
Cdd:cd04158    80 DRVSEAHSELAKLLTEKElrDALLLIFANKQDVAGALSVEEMTELLSLHKLCCGRSWYIQG 140
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 491-643 7.77e-08

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 52.46  E-value: 7.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 491 LVLGLDGAGKTSVLHLLA---SNRVQHSTAPTQGLNAVH--INSEDRQMEFLEIGGSEPFRSYWEMYLPKGW-----LLI 560
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLggeVGEVSDVPGTTRDPDVYVkeLDKGKVKLVLVDTPGLDEFGGLGREELARLLlrgadLIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 561 FVVDSADHKRLPEAKKYLHQLINpNPGLPLVVFANKQDLEAAyhiTDIHDALALSEVGNDRKLFLFGTQVtKNGSEIPST 640
Cdd:cd00882    81 LVVDSTDRESEEDAKLLILRRLR-KEGIPIILVGNKIDLLEE---REVEELLRLEELAKILGVPVFEVSA-KTGEGVDEL 155


                  ...
gi 1907164552 641 MQD 643
Cdd:cd00882   156 FEK 158
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
487-616 2.54e-07

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 51.14  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 487 NKQILVLGLDGAGKTSVLHLLASNRVqhSTAPTQGLNAVHI-------NSEDRQMEFLEIGGSEPFRSYWEMYLPkgWL- 558
Cdd:COG1100     3 EKKIVVVGTGGVGKTSLVNRLVGDIF--SLEKYLSTNGVTIdkkelklDGLDVDLVIWDTPGQDEFRETRQFYAR--QLt 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907164552 559 ----LIFVVDSADHKRLPEAKKYLHQLINPNPGLPLVVFANKQDLeaaYHITDIHDALALSE 616
Cdd:COG1100    79 gaslYLFVVDGTREETLQSLYELLESLRRLGKKSPIILVLNKIDL---YDEEEIEDEERLKE 137
SR_beta cd04105
Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms ...
 490-612 5.02e-07

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.


Pssm-ID: 206691 [Multi-domain]  Cd Length: 202  Bit Score: 50.78  E-value: 5.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVqHSTAPTQGLNAVHINSE---DRQMEFLEIGGSEPFRSYWEMYLPKGWL-LIFVVDS 565
Cdd:cd04105     3 VLLLGPSDSGKTALFTKLTTGKV-RSTVTSIEPNVASFYSNsskGKKLTLVDVPGHEKLRDKLLEYLKASLKaIVFVVDS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907164552 566 AD-HKRLPEAKKYLHQLI----NPNPGLPLVVFANKQDLEAAYHITDIHDAL 612
Cdd:cd04105    82 ATfQKNIRDVAEFLYDILtdleKIKNKIPILIACNKQDLFTAKPAKKIKELL 133
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 488-600 1.19e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 48.91  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 488 KQILVLGLDGAGKTSVLHLLASN-RVQHSTAPTQGLNA----VHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFV 562
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGNkGSITEYYPGTTRNYvttvIEEDGKTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907164552 563 VDSADH-KRLPEAK-KYLHQLINPNP-GLPLVVFANKQDLE 600
Cdd:TIGR00231  82 FDIVILvLDVEEILeKQTKEIIHHADsGVPIILVGNKIDLK 122
PTZ00121 PTZ00121
MAEBL; Provisional
 340-463 1.09e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  340 RKSADLKTKETGKEKVEEKRKSADLKTKETGKEKVEEKRKSADLKTKETGKEKEEEKRKSADlktkETGKEKEEEKRKSA 419
Cdd:PTZ00121  1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD----EAKKKAEEAKKKAD 1500

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907164552  420 DLKTKENGKDKGKE----EEKRKNDE--KGKENGTGMEAKEEQGTEKEKE 463
Cdd:PTZ00121  1501 EAKKAAEAKKKADEakkaEEAKKADEakKAEEAKKADEAKKAEEKKKADE 1550
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 490-598 3.34e-05

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


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 43.65  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQHSTAPTQGLN-----AVHINSEDRQMEFlEI---GGSEPFRSYWEMYLPKGWLLIF 561
Cdd:pfam08477   2 VVLLGDSGVGKTSLLKRFVDDTFDPKYKSTIGVDfktktVLENDDNGKKIKL-NIwdtAGQERFRSLHPFYYRGAAAALL 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907164552 562 VVDSADHKRLpeaKKYLHQLINPNPGLPLVVFANKQD 598
Cdd:pfam08477  81 VYDSRTFSNL---KYWLRELKKYAGNSPVILVGNKID 114
RSR1 cd04177
RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that ...
 489-616 1.10e-04

RSR1/Bud1p family GTPase; RSR1/Bud1p is a member of the Rap subfamily of the Ras family that is found in fungi. In budding yeasts, RSR1 is involved in selecting a site for bud growth on the cell cortex, which directs the establishment of cell polarization. The Rho family GTPase cdc42 and its GEF, cdc24, then establish an axis of polarized growth by organizing the actin cytoskeleton and secretory apparatus at the bud site. It is believed that cdc42 interacts directly with RSR1 in vivo. In filamentous fungi, polar growth occurs at the tips of hypha and at novel growth sites along the extending hypha. In Ashbya gossypii, RSR1 is a key regulator of hyphal growth, localizing at the tip region and regulating in apical polarization of the actin cytoskeleton. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 133377 [Multi-domain]  Cd Length: 168  Bit Score: 43.24  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQHSTAPT-QGLNAVHINSEDRQ--MEFLEIGGSEPFRSYWEMYLP--KGWLLIF-V 562
Cdd:cd04177     3 KIVVLGAGGVGKSALTVQFVQNVFIESYDPTiEDSYRKQVEIDGRQcdLEILDTAGTEQFTAMRELYIKsgQGFLLVYsV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907164552 563 VDSADHKRLPEAKKYLHQlINPNPGLPLVVFANKQDLEAAYHItDIHDALALSE 616
Cdd:cd04177    83 TSEASLNELGELREQVLR-IKDSDNVPMVLVGNKADLEDDRQV-SREDGVSLSQ 134
PTZ00121 PTZ00121
MAEBL; Provisional
 339-488 3.03e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 3.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  339 KRKSADLKTKETGKEKVEEKRKSADLKTK-ETGKEKVEEKRKSADLKTKETGKEKEEEKRKSADLKTKETGKEKEEEKRK 417
Cdd:PTZ00121  1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907164552  418 SADLKTKENGK---DKGKEEEKRKNDEKGKENgTGMEAKEEQGTEKEKEQVTEQVKENTSTSIKTLYPPPVENK 488
Cdd:PTZ00121  1536 ADEAKKAEEKKkadELKKAEELKKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 490-600 1.85e-03

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 39.42  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 490 ILVLGLDGAGKTSVLHLLASNRVQHSTAPTQGLN----AVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKGWLLIFVVDS 565
Cdd:pfam00071   2 LVLVGDGGVGKSSLLIRFTQNKFPEEYIPTIGVDfytkTIEVDGKTVKLQIWDTAGQERFRALRPLYYRGADGFLLVYDI 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907164552 566 ADHKRLPEAKKYLHQLIN-PNPGLPLVVFANKQDLE 600
Cdd:pfam00071  82 TSRDSFENVKKWVEEILRhADENVPIVLVGNKCDLE 117
Rhes_like cd04143
Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); ...
 489-633 3.78e-03

Ras homolog enriched in striatum (Rhes) and activator of G-protein signaling 1 (Dexras1/AGS1); This subfamily includes Rhes (Ras homolog enriched in striatum) and Dexras1/AGS1 (activator of G-protein signaling 1). These proteins are homologous, but exhibit significant differences in tissue distribution and subcellular localization. Rhes is found primarily in the striatum of the brain, but is also expressed in other areas of the brain, such as the cerebral cortex, hippocampus, inferior colliculus, and cerebellum. Rhes expression is controlled by thyroid hormones. In rat PC12 cells, Rhes is farnesylated and localizes to the plasma membrane. Rhes binds and activates PI3K, and plays a role in coupling serpentine membrane receptors with heterotrimeric G-protein signaling. Rhes has recently been shown to be reduced under conditions of dopamine supersensitivity and may play a role in determining dopamine receptor sensitivity. Dexras1/AGS1 is a dexamethasone-induced Ras protein that is expressed primarily in the brain, with low expression levels in other tissues. Dexras1 localizes primarily to the cytoplasm, and is a critical regulator of the circadian master clock to photic and nonphotic input. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins.


Pssm-ID: 133343 [Multi-domain]  Cd Length: 247  Bit Score: 39.73  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552 489 QILVLGLDGAGKTSVLHLLASNRVQHSTAPTQ---GLNAVHINSEDRQMEFLEIGGSEPFRSYWEMYLPKG--WLLIFVV 563
Cdd:cd04143     2 RMVVLGASKVGKTAIVSRFLGGRFEEQYTPTIedfHRKLYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGdvFILVFSL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907164552 564 DSADH----KRLP----EAKKYLHQLINPNPGLPLVVFANKQDLEaAYHITDIHDALALseVGNDRKLFLFGTQVTKN 633
Cdd:cd04143    82 DNRESfeevCRLReqilETKSCLKNKTKENVKIPMVICGNKADRD-FPREVQRDEVEQL--VGGDENCAYFEVSAKKN 156
PTZ00121 PTZ00121
MAEBL; Provisional
 285-464 4.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  285 KTKENGKDKGKEEEKKKSVDLKtKENGKDKEKEEKKRKSADLKTKETGKEKEEEKRKSADLKTKETGKEKVEEKRKSADL 364
Cdd:PTZ00121  1390 KKKADEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907164552  365 KTK-ETGKEKVEEKRKSADLKTKETGKEKEEEK-RKSADLKTKETGKEKEEEKRKSADLKTKENGK---DKGKEEEKRKN 439
Cdd:PTZ00121  1469 AKKaDEAKKKAEEAKKADEAKKKAEEAKKKADEaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkadEAKKAEEKKKA 1548

                          170       180
                   ....*....|....*....|....*..
gi 1907164552  440 DE--KGKENGTGMEAKEEQGTEKEKEQ 464
Cdd:PTZ00121  1549 DElkKAEELKKAEEKKKAEEAKKAEED 1575
 
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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