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Conserved domains on  [gi|16417188|gb|AAL18609|]
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VMA1 precursor, partial [Saccharomyces sp. DH1-1A]

Protein Classification

Hint domain-containing protein( domain architecture ID 12061208)

Hint domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hom_end_hint pfam05203
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are ...
29-481 0e+00

Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life. The crystal structure of the homing nuclease PI-Sce revealed two domains: an endonucleolytic centre resembling the C-terminal domain of Drosophila melanogaster Hedgehog protein, and a second domain containing the protein-splicing active site. This Domain corresponds to the latter protein-splicing domain.


:

Pssm-ID: 368334 [Multi-domain]  Cd Length: 444  Bit Score: 651.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188    29 CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGSETMYSVVQKSQHRAHKSDSsrempeLLKFTCNATHE 108
Cdd:pfam05203   1 CFAKGTEVLMADGSIKSIEDIEVGDKVMGKDGTPREVVGLPRGRETMYEVTQKTQHRADESEG------LLSFTCNANHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   109 LVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYP-VSEGPERANelVESYRKASNKAYFEWTI 187
Cdd:pfam05203  75 LVLRTPQKIRVTEHVLRGKKYTSVTYFALEDTKTGDGRIIEIVKEVTKSFPhSSHGGERAA--AQEFAATIDKEPIEWTI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   188 EARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIegPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERV 267
Cdd:pfam05203 153 EARDLDLLGAHVRKATFQLINPVLYESGHLAQYLEKQGFDKSL--APELAYLLGLWVGDGTSDAAEFSVDSQDTELMERI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   268 TEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGVRNNLNTENPLWDAIIGLGFLKDG--VKNIPSFLSTDNIGTRET 345
Cdd:pfam05203 231 VEYGKALGLTATTKDEQEPLRAKTVNLHSGNERDGGNRNRLNTNNLFWDAVVSLGFRKDGdgEKQIPSFLASEDIEVREQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   346 FLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGtKHKISYAIYMSGGDVLLNVLSK 425
Cdd:pfam05203 311 FLAGLIDSDGYVKKDKGGSATIKTIYPSVMDGLVKLARSLGIKVSVTTESAKTDVGV-RHVSCYAITLSGGDALQSVLSK 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16417188   426 CAGSKKFRPAPVAtFVRECQGFYFELQELKENDYYGITLSDDSDHQFLLANQVVVH 481
Cdd:pfam05203 390 CALSRKKAPVPEP-FAREPVPFYFTLEKLEEDDYYGITLPEDSDHQFLLSNLALVH 444
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
1-38 1.08e-14

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 cd01134:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 288  Bit Score: 74.53  E-value: 1.08e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 16417188   1 PGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKG---TNVLM 38
Cdd:cd01134  82 PGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGnemAEVLE 122
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
475-516 1.95e-12

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 cd01134:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 288  Bit Score: 67.60  E-value: 1.95e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16417188 475 ANQVVVHNCGERGNEMAEVLMEFPELytKMSGTKEPIMKRTT 516
Cdd:cd01134 102 SDVVIYVGCGERGNEMAEVLEEFPEL--KDPITGESLMERTV 141
 
Name Accession Description Interval E-value
Hom_end_hint pfam05203
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are ...
29-481 0e+00

Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life. The crystal structure of the homing nuclease PI-Sce revealed two domains: an endonucleolytic centre resembling the C-terminal domain of Drosophila melanogaster Hedgehog protein, and a second domain containing the protein-splicing active site. This Domain corresponds to the latter protein-splicing domain.


Pssm-ID: 368334 [Multi-domain]  Cd Length: 444  Bit Score: 651.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188    29 CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGSETMYSVVQKSQHRAHKSDSsrempeLLKFTCNATHE 108
Cdd:pfam05203   1 CFAKGTEVLMADGSIKSIEDIEVGDKVMGKDGTPREVVGLPRGRETMYEVTQKTQHRADESEG------LLSFTCNANHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   109 LVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYP-VSEGPERANelVESYRKASNKAYFEWTI 187
Cdd:pfam05203  75 LVLRTPQKIRVTEHVLRGKKYTSVTYFALEDTKTGDGRIIEIVKEVTKSFPhSSHGGERAA--AQEFAATIDKEPIEWTI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   188 EARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIegPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERV 267
Cdd:pfam05203 153 EARDLDLLGAHVRKATFQLINPVLYESGHLAQYLEKQGFDKSL--APELAYLLGLWVGDGTSDAAEFSVDSQDTELMERI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   268 TEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGVRNNLNTENPLWDAIIGLGFLKDG--VKNIPSFLSTDNIGTRET 345
Cdd:pfam05203 231 VEYGKALGLTATTKDEQEPLRAKTVNLHSGNERDGGNRNRLNTNNLFWDAVVSLGFRKDGdgEKQIPSFLASEDIEVREQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   346 FLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGtKHKISYAIYMSGGDVLLNVLSK 425
Cdd:pfam05203 311 FLAGLIDSDGYVKKDKGGSATIKTIYPSVMDGLVKLARSLGIKVSVTTESAKTDVGV-RHVSCYAITLSGGDALQSVLSK 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16417188   426 CAGSKKFRPAPVAtFVRECQGFYFELQELKENDYYGITLSDDSDHQFLLANQVVVH 481
Cdd:pfam05203 390 CALSRKKAPVPEP-FAREPVPFYFTLEKLEEDDYYGITLPEDSDHQFLLSNLALVH 444
Hop COG1372
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ...
236-502 8.88e-15

Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];


Pssm-ID: 440983 [Multi-domain]  Cd Length: 866  Bit Score: 77.24  E-value: 8.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188 236 LAYLLGLWIGDG-LSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYskvVRGNGVRnnlntenpL 314
Cdd:COG1372 212 LAYLLGLLLGDGsLSKRGAGRFTNADEELLEDVAEAAEELFGRADEGPRVEARRATVYEVR---VSSKPLA--------E 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188 315 WDAIIGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVtDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAE 394
Cdd:COG1372 281 LLEELGLFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSV-SNRGGRIRLSTTSRRLAEQVQLLLLRLGIVSRIYER 359
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188 395 PAKvdmNGtKHKISYAIYMSGGDVLLN-------------------------------VLSKCAGSKKFRPAPVATFVRE 443
Cdd:COG1372 360 RRP---DG-KGRTAYRLRISGGDNLRRfaerigfgssrkqerlaellaalrrrkddlvRARELANGRRLSRERLRRLALE 435
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16417188 444 CQ--------GFYF----ELQELKENDYYGITLSDdsDHQFlLANQVVVHNCGERgnEMAEVLMEFPELYT 502
Cdd:COG1372 436 DEalealadsDVYWdevvSIEPVGEEDVYDLTVPG--THNF-VANGIVVHNSGGA--LDDVGAAVLDEDLL 501
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
1-38 1.08e-14

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 74.53  E-value: 1.08e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 16417188   1 PGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKG---TNVLM 38
Cdd:cd01134  82 PGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGnemAEVLE 122
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
475-516 1.95e-12

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 67.60  E-value: 1.95e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16417188 475 ANQVVVHNCGERGNEMAEVLMEFPELytKMSGTKEPIMKRTT 516
Cdd:cd01134 102 SDVVIYVGCGERGNEMAEVLEEFPEL--KDPITGESLMERTV 141
NtpA COG1155
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ...
478-516 1.42e-09

Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 440769 [Multi-domain]  Cd Length: 583  Bit Score: 60.49  E-value: 1.42e-09
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16417188 478 VVVHNCGERGNEMAEVLMEFPELYTKMSGtkEPIMKRTT 516
Cdd:COG1155 256 VVYVGCGERGNEMTEVLEEFPELIDPKTG--RPLMERTV 292
HintN smart00306
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ...
28-133 1.95e-08

Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197642 [Multi-domain]  Cd Length: 100  Bit Score: 51.89  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188     28 GCFAKGTNVLMADGSIECIENIEVGNKVMGKDG-------RPREVIKLPRGSETMYSVVQKSQHrahksdssrempellK 100
Cdd:smart00306   1 GCFPGDTLVLTEDGGIKKIEELEEGDKVLALDEgtlkyspVKVFLVREPKGEKKFYRIKTENGR---------------E 65
                           90       100       110
                   ....*....|....*....|....*....|....
gi 16417188    101 FTCNATHELVVRTPRSVR-RLSRTIKGVEYFEVI 133
Cdd:smart00306  66 ITLTPDHLLLVRDGGKLVwVFASELKPGDYVLVP 99
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
478-516 3.14e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 56.33  E-value: 3.14e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 16417188  478 VVVHNCGERGNEMAEVLMEFPELytKMSGTKEPIMKRTT 516
Cdd:PRK04192 256 VIYVGCGERGNEMTEVLEEFPEL--IDPKTGRPLMERTV 292
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
1-29 4.89e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 55.56  E-value: 4.89e-08
                         10        20
                 ....*....|....*....|....*....
gi 16417188    1 PGAFGCGKTVISQSLSKYSNSDAIIYVGC 29
Cdd:PRK04192 233 PGPFGSGKTVTQHQLAKWADADIVIYVGC 261
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
236-515 3.57e-06

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 50.02  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   236 LAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLnlcaeykdrkepqvaktVNLYSKVVRGNGVRNNLNTENPLW 315
Cdd:PRK14698  393 LAEFLGYLIADGTLKPRTVAIYNNDESLLKRANELAMEL-----------------FGIEGKIVKERTVKALLIHSKALV 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   316 DAIIGLGF---LKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGiKATIKTIHTSVRDGLVSLARSLGLVASVN 392
Cdd:PRK14698  456 DFFKKLGIpgnKKARTWKVPKELLISEPEVVKAFIKAYIACDGYYDEEKG-EIEIVTASEEAAYGFSYLLAKLGIYAIIR 534
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   393 AEPakvdMNGtkhKISYAIYMSGGDVL--LNVLSKCAGSKKFRPAPV-------------ATFVREC---------QGFY 448
Cdd:PRK14698  535 EKI----IGD---KEYYRVVISGEANLekLGIEREARGYTSIDIVPVdveeiyealgrpyAELKKAGieihnylsgENMS 607
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   449 FE----------LQELKEN--------------------DYYGITlsdDSDHQFLLAN--------------------QV 478
Cdd:PRK14698  608 YEmfrkfakfvgLEEIAENhlqhilfdeiveinyisegqEVYDIT---TETHNFIGGNmptllhntvtqhqlakwsdaQV 684
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 16417188   479 VVH-NCGERGNEMAEVLMEFPELytKMSGTKEPIMKRT 515
Cdd:PRK14698  685 VIYiGCGERGNEMTDVLEEFPKL--KDPKTGKPLMERT 720
Hint cd00081
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ...
29-118 1.06e-05

Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.


Pssm-ID: 238035 [Multi-domain]  Cd Length: 136  Bit Score: 44.95  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188  29 CFAKGTNVLMADGSIECIENIEV--GNKVMGKD----GRPREVIKLPR--GSETMYSVVQKSQHrahksdssrempellK 100
Cdd:cd00081   1 CFTGDTLVLLEDGGRKKIEELVEkkGDKVLALDetgkLVFSKVLKVLRrdYEKKFYKIKTESGR---------------E 65
                        90
                ....*....|....*...
gi 16417188 101 FTCNATHELVVRTPRSVR 118
Cdd:cd00081  66 ITLTPDHLLFVLEDGELK 83
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
1-29 3.96e-04

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 41.96  E-value: 3.96e-04
                          10        20
                  ....*....|....*....|....*....
gi 16417188     1 PGAFGCGKTVISQSLSKYSNSDAIIYVGC 29
Cdd:pfam00006  20 FGGSGVGKTVLAGMIARQASADVVVYALI 48
 
Name Accession Description Interval E-value
Hom_end_hint pfam05203
Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are ...
29-481 0e+00

Hom_end-associated Hint; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life. The crystal structure of the homing nuclease PI-Sce revealed two domains: an endonucleolytic centre resembling the C-terminal domain of Drosophila melanogaster Hedgehog protein, and a second domain containing the protein-splicing active site. This Domain corresponds to the latter protein-splicing domain.


Pssm-ID: 368334 [Multi-domain]  Cd Length: 444  Bit Score: 651.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188    29 CFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGSETMYSVVQKSQHRAHKSDSsrempeLLKFTCNATHE 108
Cdd:pfam05203   1 CFAKGTEVLMADGSIKSIEDIEVGDKVMGKDGTPREVVGLPRGRETMYEVTQKTQHRADESEG------LLSFTCNANHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   109 LVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYP-VSEGPERANelVESYRKASNKAYFEWTI 187
Cdd:pfam05203  75 LVLRTPQKIRVTEHVLRGKKYTSVTYFALEDTKTGDGRIIEIVKEVTKSFPhSSHGGERAA--AQEFAATIDKEPIEWTI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   188 EARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIegPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERV 267
Cdd:pfam05203 153 EARDLDLLGAHVRKATFQLINPVLYESGHLAQYLEKQGFDKSL--APELAYLLGLWVGDGTSDAAEFSVDSQDTELMERI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   268 TEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGVRNNLNTENPLWDAIIGLGFLKDG--VKNIPSFLSTDNIGTRET 345
Cdd:pfam05203 231 VEYGKALGLTATTKDEQEPLRAKTVNLHSGNERDGGNRNRLNTNNLFWDAVVSLGFRKDGdgEKQIPSFLASEDIEVREQ 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   346 FLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGtKHKISYAIYMSGGDVLLNVLSK 425
Cdd:pfam05203 311 FLAGLIDSDGYVKKDKGGSATIKTIYPSVMDGLVKLARSLGIKVSVTTESAKTDVGV-RHVSCYAITLSGGDALQSVLSK 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16417188   426 CAGSKKFRPAPVAtFVRECQGFYFELQELKENDYYGITLSDDSDHQFLLANQVVVH 481
Cdd:pfam05203 390 CALSRKKAPVPEP-FAREPVPFYFTLEKLEEDDYYGITLPEDSDHQFLLSNLALVH 444
Hom_end pfam05204
Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found ...
330-435 2.10e-49

Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life.


Pssm-ID: 368335 [Multi-domain]  Cd Length: 110  Bit Score: 165.17  E-value: 2.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   330 NIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKVDMNGTKHKISY 409
Cdd:pfam05204   1 NIPSFLSSEAIEVREAFLAGLIDSDGYVDKAKNITASVKTEDKSVMEGIVKLARSLGIKASVKTKEEPIDAKGVNLQFTY 80
                          90       100
                  ....*....|....*....|....*.
gi 16417188   410 AIYMSGGDVLLNVLSKCAGSKKFRPA 435
Cdd:pfam05204  81 AITLSGGDALLSVLSKCALWNKRVEA 106
Hom_end pfam05204
Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found ...
223-324 1.09e-26

Homing endonuclease; Homing endonucleases are encoded by mobile DNA elements that are found inserted within host genes in all domains of life.


Pssm-ID: 368335 [Multi-domain]  Cd Length: 110  Bit Score: 103.93  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   223 KSKFHLTIEGPKVL-AYLLGLWIGDGLSDRA---TFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNL---Y 295
Cdd:pfam05204   1 NIPSFLSSEAIEVReAFLAGLIDSDGYVDKAkniTASVKTEDKSVMEGIVKLARSLGIKASVKTKEEPIDAKGVNLqftY 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 16417188   296 SKVVRGNGVRNNLNTENPLWDAIIG-LGFL 324
Cdd:pfam05204  81 AITLSGGDALLSVLSKCALWNKRVEaLGFL 110
Hop COG1372
Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, ...
236-502 8.88e-15

Intein/homing endonuclease [Replication, recombination and repair, Mobilome: prophages, transposons];


Pssm-ID: 440983 [Multi-domain]  Cd Length: 866  Bit Score: 77.24  E-value: 8.88e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188 236 LAYLLGLWIGDG-LSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYskvVRGNGVRnnlntenpL 314
Cdd:COG1372 212 LAYLLGLLLGDGsLSKRGAGRFTNADEELLEDVAEAAEELFGRADEGPRVEARRATVYEVR---VSSKPLA--------E 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188 315 WDAIIGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVtDEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAE 394
Cdd:COG1372 281 LLEELGLFGKRSGEKRIPDFVFRLSREQIRAFLRGLFDADGSV-SNRGGRIRLSTTSRRLAEQVQLLLLRLGIVSRIYER 359
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188 395 PAKvdmNGtKHKISYAIYMSGGDVLLN-------------------------------VLSKCAGSKKFRPAPVATFVRE 443
Cdd:COG1372 360 RRP---DG-KGRTAYRLRISGGDNLRRfaerigfgssrkqerlaellaalrrrkddlvRARELANGRRLSRERLRRLALE 435
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16417188 444 CQ--------GFYF----ELQELKENDYYGITLSDdsDHQFlLANQVVVHNCGERgnEMAEVLMEFPELYT 502
Cdd:COG1372 436 DEalealadsDVYWdevvSIEPVGEEDVYDLTVPG--THNF-VANGIVVHNSGGA--LDDVGAAVLDEDLL 501
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
1-38 1.08e-14

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 74.53  E-value: 1.08e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 16417188   1 PGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKG---TNVLM 38
Cdd:cd01134  82 PGPFGCGKTVISQSLSKWSNSDVVIYVGCGERGnemAEVLE 122
V_A-ATPase_A cd01134
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ...
475-516 1.95e-12

V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.


Pssm-ID: 410878 [Multi-domain]  Cd Length: 288  Bit Score: 67.60  E-value: 1.95e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16417188 475 ANQVVVHNCGERGNEMAEVLMEFPELytKMSGTKEPIMKRTT 516
Cdd:cd01134 102 SDVVIYVGCGERGNEMAEVLEEFPEL--KDPITGESLMERTV 141
NtpA COG1155
Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; ...
478-516 1.42e-09

Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 440769 [Multi-domain]  Cd Length: 583  Bit Score: 60.49  E-value: 1.42e-09
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 16417188 478 VVVHNCGERGNEMAEVLMEFPELYTKMSGtkEPIMKRTT 516
Cdd:COG1155 256 VVYVGCGERGNEMTEVLEEFPELIDPKTG--RPLMERTV 292
HintN smart00306
Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. ...
28-133 1.95e-08

Hint (Hedgehog/Intein) domain N-terminal region; Hedgehog/Intein domain, N-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197642 [Multi-domain]  Cd Length: 100  Bit Score: 51.89  E-value: 1.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188     28 GCFAKGTNVLMADGSIECIENIEVGNKVMGKDG-------RPREVIKLPRGSETMYSVVQKSQHrahksdssrempellK 100
Cdd:smart00306   1 GCFPGDTLVLTEDGGIKKIEELEEGDKVLALDEgtlkyspVKVFLVREPKGEKKFYRIKTENGR---------------E 65
                           90       100       110
                   ....*....|....*....|....*....|....
gi 16417188    101 FTCNATHELVVRTPRSVR-RLSRTIKGVEYFEVI 133
Cdd:smart00306  66 ITLTPDHLLLVRDGGKLVwVFASELKPGDYVLVP 99
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
478-516 3.14e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 56.33  E-value: 3.14e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 16417188  478 VVVHNCGERGNEMAEVLMEFPELytKMSGTKEPIMKRTT 516
Cdd:PRK04192 256 VIYVGCGERGNEMTEVLEEFPEL--IDPKTGRPLMERTV 292
PRK04192 PRK04192
V-type ATP synthase subunit A; Provisional
1-29 4.89e-08

V-type ATP synthase subunit A; Provisional


Pssm-ID: 235248 [Multi-domain]  Cd Length: 586  Bit Score: 55.56  E-value: 4.89e-08
                         10        20
                 ....*....|....*....|....*....
gi 16417188    1 PGAFGCGKTVISQSLSKYSNSDAIIYVGC 29
Cdd:PRK04192 233 PGPFGSGKTVTQHQLAKWADADIVIYVGC 261
PRK14698 PRK14698
V-type ATP synthase subunit A; Provisional
236-515 3.57e-06

V-type ATP synthase subunit A; Provisional


Pssm-ID: 184795 [Multi-domain]  Cd Length: 1017  Bit Score: 50.02  E-value: 3.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   236 LAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLnlcaeykdrkepqvaktVNLYSKVVRGNGVRNNLNTENPLW 315
Cdd:PRK14698  393 LAEFLGYLIADGTLKPRTVAIYNNDESLLKRANELAMEL-----------------FGIEGKIVKERTVKALLIHSKALV 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   316 DAIIGLGF---LKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGiKATIKTIHTSVRDGLVSLARSLGLVASVN 392
Cdd:PRK14698  456 DFFKKLGIpgnKKARTWKVPKELLISEPEVVKAFIKAYIACDGYYDEEKG-EIEIVTASEEAAYGFSYLLAKLGIYAIIR 534
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   393 AEPakvdMNGtkhKISYAIYMSGGDVL--LNVLSKCAGSKKFRPAPV-------------ATFVREC---------QGFY 448
Cdd:PRK14698  535 EKI----IGD---KEYYRVVISGEANLekLGIEREARGYTSIDIVPVdveeiyealgrpyAELKKAGieihnylsgENMS 607
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   449 FE----------LQELKEN--------------------DYYGITlsdDSDHQFLLAN--------------------QV 478
Cdd:PRK14698  608 YEmfrkfakfvgLEEIAENhlqhilfdeiveinyisegqEVYDIT---TETHNFIGGNmptllhntvtqhqlakwsdaQV 684
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 16417188   479 VVH-NCGERGNEMAEVLMEFPELytKMSGTKEPIMKRT 515
Cdd:PRK14698  685 VIYiGCGERGNEMTDVLEEFPKL--KDPKTGKPLMERT 720
Hint cd00081
Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins ...
29-118 1.06e-05

Hedgehog/Intein domain, found in Hedgehog proteins as well as proteins which contain inteins and undergo protein splicing (e.g. DnaB, RIR1-2, GyrA and Pol). In protein splicing an intervening polypeptide sequence - the intein - is excised from a protein, and the flanking polypeptide sequences - the exteins - are joined by a peptide bond. In addition to the autocatalytic splicing domain, many inteins contain an inserted endonuclease domain, which plays a role in spreading inteins. Hedgehog proteins are a major class of intercellular signaling molecules, which control inductive interactions during animal development. The mature signaling forms of hedgehog proteins are the N-terminal fragments, which are covalently linked to cholesterol at their C-termini. This modification is the result of an autoprocessing step catalyzed by the C-terminal fragments, which are aligned here.


Pssm-ID: 238035 [Multi-domain]  Cd Length: 136  Bit Score: 44.95  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188  29 CFAKGTNVLMADGSIECIENIEV--GNKVMGKD----GRPREVIKLPR--GSETMYSVVQKSQHrahksdssrempellK 100
Cdd:cd00081   1 CFTGDTLVLLEDGGRKKIEELVEkkGDKVLALDetgkLVFSKVLKVLRrdYEKKFYKIKTESGR---------------E 65
                        90
                ....*....|....*...
gi 16417188 101 FTCNATHELVVRTPRSVR 118
Cdd:cd00081  66 ITLTPDHLLFVLEDGELK 83
Intein_splicing pfam14890
Intein splicing domain; Inteins are segments of protein which excise themselves from a ...
256-482 3.68e-04

Intein splicing domain; Inteins are segments of protein which excise themselves from a precursor protein and mediate the rejoining of the remainder of the precursor (the extein). Most inteins consist of a splicing domain which is split into two segments by a homing endonuclease domain. This domain represents the splicing domain.


Pssm-ID: 434290 [Multi-domain]  Cd Length: 378  Bit Score: 42.83  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   256 VDSRDTSLMERVTEYAEKLnlcaeYKDRKEPQVAKTVNLYSKV--VRGNGVRNNLNTENPLWDAIIGLGFLKDGVKNIPS 333
Cdd:pfam14890 142 KYTREIPLKELIEWIEEEL-----FGDVINPRIKPERKFWYQVglVAGDGLTHDKKNPIAKWLESLEIFGLLSYNKFIPE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   334 FLSTDNIGTRETFLAGLIDSDGYVTdEHGIKATIKTIHTSVRDGLVSLARSLGLVASVNAEPAKvDMNGtkhkisYAIYM 413
Cdd:pfam14890 217 FVFSLPKGAIASFIRGYFDTDGCIS-KRNPGIYLSSTSERLAEDVQLLLLSLGINARLSKINGK-GRNV------YHVLI 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188   414 SGGDVLLNVLSKCAGSKKFRPAPVATFV-------RECQGFYFELQELKENDYY-----GITLSDD---------SDHQF 472
Cdd:pfam14890 289 TGKSSLEKFKEKIGAYLQIKKEKLEEILnkykqsnAESSEVKDFLEWLINSDVYwdkvkSIEVLDEeeyvydltvEGYHN 368
                         250
                  ....*....|
gi 16417188   473 LLANQVVVHN 482
Cdd:pfam14890 369 FVANGIIVHN 378
ATP-synt_ab pfam00006
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ...
1-29 3.96e-04

ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.


Pssm-ID: 425417 [Multi-domain]  Cd Length: 212  Bit Score: 41.96  E-value: 3.96e-04
                          10        20
                  ....*....|....*....|....*....
gi 16417188     1 PGAFGCGKTVISQSLSKYSNSDAIIYVGC 29
Cdd:pfam00006  20 FGGSGVGKTVLAGMIARQASADVVVYALI 48
HintC smart00305
Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. ...
444-486 2.33e-03

Hint (Hedgehog/Intein) domain C-terminal region; Hedgehog/Intein domain, C-terminal region. Domain has been split to accommodate large insertions of endonucleases.


Pssm-ID: 197641  Cd Length: 46  Bit Score: 36.00  E-value: 2.33e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 16417188    444 CQGFYF----ELQELKENDYYGITLSDDsdHQFLlANQVVVHNCGER 486
Cdd:smart00305   1 EGDFRFvrvkSIEETEYTGVYDPTVTEN--HNFI-ANGILVHNCAEI 44
PRK14898 PRK14898
DNA-directed RNA polymerase subunit A''; Provisional
236-366 2.55e-03

DNA-directed RNA polymerase subunit A''; Provisional


Pssm-ID: 237854 [Multi-domain]  Cd Length: 858  Bit Score: 40.65  E-value: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16417188  236 LAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNL-CAEYKDRKEPQVAKTVNLYSKVvrgngvrnnlntenpL 314
Cdd:PRK14898 245 TGYFVGAYLAEGSLTDHYVSISNVDETFQNRVRAFAERFDLsVNEYENDSGFATGYDIRLNGTV---------------L 309
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16417188  315 WDAIIGLGfLKDGVKNIPSFLstdnIGTRETFLAGLI----DSDGYV-TDEHGIKAT 366
Cdd:PRK14898 310 SDFLRNFC-TDDGEKKIPDFA----FGANKEFVRGLLqgyfDGDGNVgTNKKAIRIS 361
 
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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