NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|635767620|gb|KDF49128|]
View 

Mg chelatase-like protein [Enterobacter kobei]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK09862 super family cl32426
ATP-dependent protease;
1-496 0e+00

ATP-dependent protease;


The actual alignment was detected with superfamily member PRK09862:

Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 974.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   1 MSLSVVYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGR 80
Cdd:PRK09862   1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  81 YDLPIAIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAGRQIIVANENASEVSLIAEKGCLVAGHL 160
Cdd:PRK09862  81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLINGEGCLIADHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 161 QEVCAWLEGRHELSEPEECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNH 240
Cdd:PRK09862 161 QAVCAFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 241 EALESAAIYSLISSTSLQKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIES 320
Cdd:PRK09862 241 EALESAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIES 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 321 GEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQGNHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKGITG 400
Cdd:PRK09862 321 GQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVVPG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 401 ESSADVRERVIAAQTRQYARQNRLNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIADVEGCSDI 480
Cdd:PRK09862 401 ESSATVKQRVMAARERQFKRQNKLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIADIDQSDII 480

                        490
                 ....*....|....*.
gi 635767620 481 QRKHLQEALSYRAIDR 496
Cdd:PRK09862 481 TRQHLQEAVSYRAIDR 496
 
Name Accession Description Interval E-value
PRK09862 PRK09862
ATP-dependent protease;
1-496 0e+00

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 974.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   1 MSLSVVYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGR 80
Cdd:PRK09862   1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  81 YDLPIAIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAGRQIIVANENASEVSLIAEKGCLVAGHL 160
Cdd:PRK09862  81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLINGEGCLIADHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 161 QEVCAWLEGRHELSEPEECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNH 240
Cdd:PRK09862 161 QAVCAFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 241 EALESAAIYSLISSTSLQKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIES 320
Cdd:PRK09862 241 EALESAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIES 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 321 GEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQGNHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKGITG 400
Cdd:PRK09862 321 GQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVVPG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 401 ESSADVRERVIAAQTRQYARQNRLNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIADVEGCSDI 480
Cdd:PRK09862 401 ESSATVKQRVMAARERQFKRQNKLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIADIDQSDII 480

                        490
                 ....*....|....*.
gi 635767620 481 QRKHLQEALSYRAIDR 496
Cdd:PRK09862 481 TRQHLQEAVSYRAIDR 496
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 3-495 0e+00

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 778.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   3 LSVVYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGRYD 82
Cdd:COG0606    2 LARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  83 LPIAIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAG-RQIIVANENASEVSLIAEKGCLVAGHLQ 161
Cdd:COG0606   82 LPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGiRRLIVPAANAAEAALVPGIEVYGASSLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 162 EVCAWLEGRHELSEPE-ECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNH 240
Cdd:COG0606  162 EVVAFLRGEQPLPPAEpDAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 241 EALESAAIYSLISSTSL-QKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIE 319
Cdd:COG0606  242 EALEVTAIHSVAGLLPPdGGLIRRRPFRAPHHTASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 320 SGEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQ--GNHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKG 397
Cdd:COG0606  322 DGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGdpDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSAP 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 398 iTGESSADVRERVIAAQTRQYARQN----RLNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIAD 473
Cdd:COG0606  402 -PGESSAEVRERVAAARERQLERFGgtgiRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIAD 480

                        490       500
                 ....*....|....*....|..
gi 635767620 474 VEGCSDIQRKHLQEALSYRAID 495
Cdd:COG0606  481 LAGSERIEREHLAEALQYRRLD 502
TIGR00368 TIGR00368
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ...
 6-492 0e+00

Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]


Pssm-ID: 129465 [Multi-domain]  Cd Length: 499  Bit Score: 711.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620    6 VYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGRYDLPI 85
Cdd:TIGR00368   1 VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   86 AIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAGRQ-IIVANENASEVSLIAEKGCLVAGHLQEVC 164
Cdd:TIGR00368  81 AIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKfIIVPKENAEEASLIDGLNIYGADHLKEVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  165 AWLEGRHEL-----SEPEECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNN 239
Cdd:TIGR00368 161 KFLEGSEKLpprtnTKPKSIINKSYIIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  240 HEALESAAIYSLISSTSLQKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIE 319
Cdd:TIGR00368 241 EEAIETARIWSLVGKLIDRKQIKQRPFRSPHHSASKPALVGGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  320 SGEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQG--NHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKG 397
Cdd:TIGR00368 321 DGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGknTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  398 iTGESSADVRERVIAAQTRQYARQNR-----LNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIA 472
Cdd:TIGR00368 401 -SGESSAEVKQRVIKAREIQNIRYEKfaninKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVARTIA 479

                         490       500
                  ....*....|....*....|
gi 635767620  473 DVEGCSDIQRKHLQEALSYR 492
Cdd:TIGR00368 480 DLKEEKNISREHLAEAIEYR 499
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 189-393 5.42e-125

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 363.39  E-value: 5.42e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  189 DLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNHEALESAAIYSLISSTSLQKQWRRRPFRS 268
Cdd:pfam01078   1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLGGDGGLIRRRPFRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  269 PHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRAKISYPAQFQLVAAMNPSP 348
Cdd:pfam01078  81 PHHSASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPCP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 635767620  349 SGHYQGNHNRC--TPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLL 393
Cdd:pfam01078 161 CGYLGDPNKRCrcSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 195-387 3.44e-08

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 52.53  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 195 GQEQGKRALEITA--AGGHNLLLIGPPGTGKTMLASRLSgllpplnnHEALESAAIYSLISSTSLQKQWRRRPFRSPHHS 272
Cdd:cd00009    2 GQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIA--------NELFRPGAPFLYLNASDLLEGLVVAELFGHFLV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 273 ASLAAMVgggsipgpgeiSLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRakisypaQFQLVAAMNPSPsghy 352
Cdd:cd00009   74 RLLFELA-----------EKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-------NVRVIGATNRPL---- 131

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 635767620 353 qgnhnrctpeqtlryLGKLSGPFLDRFDLSLEIPL 387
Cdd:cd00009  132 ---------------LGDLDRALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 210-348 5.93e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.13  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   210 GHNLLLIGPPGTGKTMLASRLSGLLPPLNnhealesaAIYSLISSTSLQKQWRRRpfRSPHHSASLAAMVGGGSIPGpGE 289
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPG--------GGVIYIDGEDILEEVLDQ--LLLIIVGGKKASGSGELRLR-LA 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635767620   290 ISLAHN---GILFLDELPEFERRVLDALREPIESgeihiSRTRAKISYPAQFQLVAAMNPSP 348
Cdd:smart00382  71 LALARKlkpDVLILDEITSLLDAEQEALLLLLEE-----LRLLLLLKSEKNLTVILTTNDEK 127
 
Name Accession Description Interval E-value
PRK09862 PRK09862
ATP-dependent protease;
1-496 0e+00

ATP-dependent protease;


Pssm-ID: 182120 [Multi-domain]  Cd Length: 506  Bit Score: 974.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   1 MSLSVVYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGR 80
Cdd:PRK09862   1 MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEYPAKKITINLAPADLPKEGGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  81 YDLPIAIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAGRQIIVANENASEVSLIAEKGCLVAGHL 160
Cdd:PRK09862  81 YDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVPGAISSATEAIKSGRKIIVAKDNEDEVGLINGEGCLIADHL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 161 QEVCAWLEGRHELSEPEECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNH 240
Cdd:PRK09862 161 QAVCAFLEGKHALERPKPTDAVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 241 EALESAAIYSLISSTSLQKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIES 320
Cdd:PRK09862 241 EALESAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFLDELPEFERRTLDALREPIES 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 321 GEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQGNHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKGITG 400
Cdd:PRK09862 321 GQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCTPEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVVPG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 401 ESSADVRERVIAAQTRQYARQNRLNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIADVEGCSDI 480
Cdd:PRK09862 401 ESSATVKQRVMAARERQFKRQNKLNAWLDSPEIRQFCKLESEDARWLEETLIHLGLSIRAWQRLLKVARTIADIDQSDII 480

                        490
                 ....*....|....*.
gi 635767620 481 QRKHLQEALSYRAIDR 496
Cdd:PRK09862 481 TRQHLQEAVSYRAIDR 496
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 3-495 0e+00

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 778.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   3 LSVVYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGRYD 82
Cdd:COG0606    2 LARVYSVALLGIEAPLVEVEVDISNGLPGFTIVGLPDTAVKESRERVRAALKNSGFEFPAKRITVNLAPADLPKEGSRFD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  83 LPIAIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAG-RQIIVANENASEVSLIAEKGCLVAGHLQ 161
Cdd:COG0606   82 LPIALGILAASGQIPAEALEDYVFLGELSLDGSLRPVRGVLPAALAAREAGiRRLIVPAANAAEAALVPGIEVYGASSLL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 162 EVCAWLEGRHELSEPE-ECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNH 240
Cdd:COG0606  162 EVVAFLRGEQPLPPAEpDAPPAEPPYEPDLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLARRLPGILPPLTEE 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 241 EALESAAIYSLISSTSL-QKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIE 319
Cdd:COG0606  242 EALEVTAIHSVAGLLPPdGGLIRRRPFRAPHHTASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFSRRVLEALRQPLE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 320 SGEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQ--GNHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKG 397
Cdd:COG0606  322 DGEVTISRANGSVTYPARFQLVAAMNPCPCGYLGdpDRECRCSPRQIRRYLSRLSGPLLDRIDLHVEVPPVPYEELSSAP 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 398 iTGESSADVRERVIAAQTRQYARQN----RLNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIAD 473
Cdd:COG0606  402 -PGESSAEVRERVAAARERQLERFGgtgiRLNAQLPGRELRKYCRLDAEARALLERALERLGLSARAYDRILRVARTIAD 480

                        490       500
                 ....*....|....*....|..
gi 635767620 474 VEGCSDIQRKHLQEALSYRAID 495
Cdd:COG0606  481 LAGSERIEREHLAEALQYRRLD 502
TIGR00368 TIGR00368
Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase ...
 6-492 0e+00

Mg chelatase-related protein; The N-terminal end matches very strongly a pfam Mg_chelatase domain. [Unknown function, General]


Pssm-ID: 129465 [Multi-domain]  Cd Length: 499  Bit Score: 711.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620    6 VYTRAALGVKAPLISVEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGRYDLPI 85
Cdd:TIGR00368   1 VYSRSSLGVEAPLITIEVDISKGLPGITIVGLPETTVKESRERVKSAIKNSGFHFPAKRITINLAPADLPKEGGRFDLPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   86 AIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAGRQ-IIVANENASEVSLIAEKGCLVAGHLQEVC 164
Cdd:TIGR00368  81 AIGILAASEQLDAKNLGEYLFLGELALDGKLRGIKGVLPAIALAQKSGRKfIIVPKENAEEASLIDGLNIYGADHLKEVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  165 AWLEGRHEL-----SEPEECDNVIADTPEDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNN 239
Cdd:TIGR00368 161 KFLEGSEKLpprtnTKPKSIINKSYIIDLDLKDIKGQQHAKRALEIAAAGGHNLLLFGPPGSGKTMLASRLQGILPPLTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  240 HEALESAAIYSLISSTSLQKQWRRRPFRSPHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIE 319
Cdd:TIGR00368 241 EEAIETARIWSLVGKLIDRKQIKQRPFRSPHHSASKPALVGGGPIPLPGEISLAHNGVLFLDELPEFKRSVLDALREPIE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  320 SGEIHISRTRAKISYPAQFQLVAAMNPSPSGHYQG--NHNRCTPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLLRQKG 397
Cdd:TIGR00368 321 DGSISISRASAKIFYPARFQLVAAMNPCPCGHYGGknTHCRCSPQQISRYWNKLSGPFLDRIDLSVEVPLLPPEKLLSTG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  398 iTGESSADVRERVIAAQTRQYARQNR-----LNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIA 472
Cdd:TIGR00368 401 -SGESSAEVKQRVIKAREIQNIRYEKfaninKNADLNSDEIEQFCKLSAIDANDLEGALNKLGLSSRATHRILKVARTIA 479

                         490       500
                  ....*....|....*....|
gi 635767620  473 DVEGCSDIQRKHLQEALSYR 492
Cdd:TIGR00368 480 DLKEEKNISREHLAEAIEYR 499
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 189-393 5.42e-125

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 363.39  E-value: 5.42e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  189 DLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPLNNHEALESAAIYSLISSTSLQKQWRRRPFRS 268
Cdd:pfam01078   1 DLADVKGQEQAKRALEIAAAGGHNLLMIGPPGSGKTMLAKRLPGILPPLTEAEALEVTAIHSVAGLGGDGGLIRRRPFRA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  269 PHHSASLAAMVGGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRAKISYPAQFQLVAAMNPSP 348
Cdd:pfam01078  81 PHHSASAAALVGGGSIPRPGEISLAHNGVLFLDELPEFKRRVLESLRQPLEDGEITISRARAKVTFPARFQLVAAMNPCP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 635767620  349 SGHYQGNHNRC--TPEQTLRYLGKLSGPFLDRFDLSLEIPLPPPGLL 393
Cdd:pfam01078 161 CGYLGDPNKRCrcSPRQIRRYLSRLSGPLLDRIDLQVEVPRLPGEEL 207
ChlI pfam13541
Subunit ChlI of Mg-chelatase;
21-142 2.57e-57

Subunit ChlI of Mg-chelatase;


Pssm-ID: 433293 [Multi-domain]  Cd Length: 121  Bit Score: 186.12  E-value: 2.57e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   21 VEVHLSNGLPGLTLVGLPETTVKEARDRVRSAIINSGYTFAAKKITINLAPADLPKEGGRYDLPIAIALLAASEQlnTTR 100
Cdd:pfam13541   1 VEVDVSKGLPAFTIVGLPDTAVKESKERVRAALKNSGFEFPPKRITVNLAPADLKKEGSSFDLPIAIGILAAQGQ--IPV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 635767620  101 LGSYEFVGELALTGALRGVPGAISGALEAIRAG-RQIIVANEN 142
Cdd:pfam13541  79 LEETIFLGELSLDGSLRPVRGALPIALAARKHGfRGLIVPKEN 121
Mg_chelatase_C pfam13335
Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative ...
 400-492 2.97e-37

Magnesium chelatase, subunit ChlI C-terminal; This is a family of the C-terminal of putative bacterial magnesium chelatase subunit ChlI proteins. Most members have the associated pfam01078.


Pssm-ID: 433125  Cd Length: 93  Bit Score: 132.13  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  400 GESSADVRERVIAAQTRQYARQNRLNARLDNAGIRQFCSLNMEDAVWLEETLTRFGLSIRAWQRLLKVARTIADVEGCSD 479
Cdd:pfam13335   1 GESSAEVRERVAAARERQAERFGGENAQLPGRELRRFCRLDAAARALLERALERLGLSARAYDRILRVARTIADLAGSER 80

                          90
                  ....*....|...
gi 635767620  480 IQRKHLQEALSYR 492
Cdd:pfam13335  81 IGREHLAEALQYR 93
ChlI COG1239
Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];
190-488 8.41e-13

Mg-chelatase subunit ChlI [Coenzyme transport and metabolism];


Pssm-ID: 440852 [Multi-domain]  Cd Length: 344  Bit Score: 69.39  E-value: 8.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 190 LSEIMGQEQGKRALEITAA----GGhnLLLIGPPGTGKTMLASRLSGLLPPL------------NNHEALESAAIYSLIS 253
Cdd:COG1239    8 FTAIVGQEEMKLALLLNAVdpgiGG--VLIRGEKGTAKSTAVRALAALLPPIevvkgcpyncdpDDPDELCPDCRERLAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 254 STSLQKQWRRRPFRSPHHSASLAAMVGGGSIP-----G-----PGEISLAHNGILFLDELPEFERRVLDALREPIESGEI 323
Cdd:COG1239   86 GEELPTETRPVPVVELPLGATEDRVVGSLDLEkalkeGekafePGLLARAHRGILYVDEVNLLDDHLVDVLLDAAAMGRN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 324 HISRTRAKISYPAQFQLVAAMNPSpsghyqgnhnrctpEQTLRylgklsgP-FLDRFDLSLEiplpppgllrqkgITGES 402
Cdd:COG1239  166 TVEREGVSVSHPARFVLVGTMNPE--------------EGELR-------PqLLDRFGLSVE-------------VEGPR 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 403 SADVR----ERVIA------AQTRQYARQNR-LNARLDNAgiRQFC-SLNMEDAVWLE--ETLTRFGL-SIRAWQRLLKV 467
Cdd:COG1239  212 DPEERveivRRRLAfeadpeAFAAEYAEEQAeLRERIAAA--RELLpEVTIPDELLRYiaELCIALGVdGHRADIVIARA 289

                        330       340
                 ....*....|....*....|.
gi 635767620 468 ARTIADVEGCSDIQRKHLQEA 488
Cdd:COG1239  290 ARALAALEGRTEVTAEDIRRA 310
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 193-476 1.70e-11

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 64.80  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 193 IMGQEQGKRALEIT-AAGGHnLLLIGPPGTGKTMLA-----------SRL---SGLLPplnnhealeSAAIYSLIsstsL 257
Cdd:COG0714   14 YVGQEELIELVLIAlLAGGH-LLLEGVPGVGKTTLAkalaralglpfIRIqftPDLLP---------SDILGTYI----Y 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 258 QKQWRRRPFRsphhsaslaamvgggsiPGPgeisLAHNgILFLDEL----PEFErrvlDALREPIESGEIHISRTRAKIS 333
Cdd:COG0714   80 DQQTGEFEFR-----------------PGP----LFAN-VLLADEInrapPKTQ----SALLEAMEERQVTIPGGTYKLP 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 334 YPaqFQLVAAMNPSPSghyqgnhnrctpEQTLRylgkLSGPFLDRFDLSLEIPLPPPGLLRQ--KGITGESSADVrERVI 411
Cdd:COG0714  134 EP--FLVIATQNPIEQ------------EGTYP----LPEAQLDRFLLKLYIGYPDAEEEREilRRHTGRHLAEV-EPVL 194

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 412 AAQTRQYARQNRLNARLDNAGIRQFCSL-----NMEDAvwleetltRFGLSIRAWQRLLKVARTIADVEG 476
Cdd:COG0714  195 SPEELLALQELVRQVHVSEAVLDYIVDLvratrEHPDL--------RKGPSPRASIALLRAARALALLDG 256
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 212-351 2.90e-11

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 61.15  E-value: 2.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  212 NLLLIGPPGTGKTMLASRLSGLLPPLNnheaLESAAIYSLISSTSLQKQWRRRPFRSPHHSASLAAMVGGGsipgpgeis 291
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRP----VFYVQLTRDTTEEDLFGRRNIDPGGASWVDGPLVRAAREG--------- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635767620  292 lahnGILFLDELPEFERRVLDALREPIESGEIHI--SRTRAKISyPAQFQLVAAMNPSPSGH 351
Cdd:pfam07728  68 ----EIAVLDEINRANPDVLNSLLSLLDERRLLLpdGGELVKAA-PDGFRLIATMNPLDRGL 124
MCM pfam00493
MCM P-loop domain;
192-381 1.64e-08

MCM P-loop domain;


Pssm-ID: 459830 [Multi-domain]  Cd Length: 224  Bit Score: 55.23  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  192 EIMGQEQGKRAL--------EITAAGGH------NLLLIGPPGTGKTMLASRLSGLLPPlnnhealesaAIYSLISSTSl 257
Cdd:pfam00493  25 SIYGHEDVKKAIllqlfggvKKILPDGTrlrgdiNVLLVGDPGTAKSQLLKYVEKIAPR----------AVYTSGKGSS- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  258 qkqwrrrpfrsphhSASLAAMV-----GGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIESGEIHISrtRAKI 332
Cdd:pfam00493  94 --------------AAGLTAAVvrdpvTGEFVLEAGALVLADGGVCCIDEFDKMNDEDRVALHEAMEQQTISIA--KAGI 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 635767620  333 SY--PAQFQLVAAMNPSpSGHYQGNHnrcTPEQTLRylgkLSGPFLDRFDL 381
Cdd:pfam00493 158 VAtlNARCSILAAANPI-FGRYDPKK---SIAENIN----LPPPLLSRFDL 200
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 195-387 3.44e-08

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 52.53  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 195 GQEQGKRALEITA--AGGHNLLLIGPPGTGKTMLASRLSgllpplnnHEALESAAIYSLISSTSLQKQWRRRPFRSPHHS 272
Cdd:cd00009    2 GQEEAIEALREALelPPPKNLLLYGPPGTGKTTLARAIA--------NELFRPGAPFLYLNASDLLEGLVVAELFGHFLV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 273 ASLAAMVgggsipgpgeiSLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRakisypaQFQLVAAMNPSPsghy 352
Cdd:cd00009   74 RLLFELA-----------EKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDLRIDRE-------NVRVIGATNRPL---- 131

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 635767620 353 qgnhnrctpeqtlryLGKLSGPFLDRFDLSLEIPL 387
Cdd:cd00009  132 ---------------LGDLDRALYDRLDIRIVIPL 151
MCM6 cd17757
DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in ...
 212-488 5.61e-08

DNA replication licensing factor Mcm6; Mcm6 is a helicase that play an important role in replication. It is part of the heterohexameric ring-shaped Mcm2-7 complex, which is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases.


Pssm-ID: 350663 [Multi-domain]  Cd Length: 307  Bit Score: 54.30  E-value: 5.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 212 NLLLIGPPGTGKTMLASRLSGLLPplnnhealesAAIYSLISSTSlqkqwrrrpfrsphhSASLAAMV-----GGGSIPG 286
Cdd:cd17757   43 NVCIVGDPSTAKSQFLKYVEEFSP----------RAVYTSGKASS---------------AAGLTAAVvrdeeTGDFVIE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 287 PGEISLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRAKISYPAQFQLVAAMNPSpSGHYQgnhnrctPEQTLR 366
Cdd:cd17757   98 AGALMLADNGICCIDEFDKMDIKDQVAIHEAMEQQTISITKAGIQATLNARTSILAAANPV-GGRYD-------RSKSLK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 367 YLGKLSGPFLDRFDLSLeIPLPPPG---------------LLRQKGITGESSADVRERVIAaqtrqYARQNR--LNARLD 429
Cdd:cd17757  170 QNINISAPIMSRFDLFF-VLLDECNevtdyaiashivdlhSKREEAIEPPFTAEQLKRYIA-----YARTFKpkLTKEAK 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 635767620 430 NAGIRQFCSLNMEDAVwlEETLTRFGLSIRAWQRLLKVARTIADVEGCSDIQRKHLQEA 488
Cdd:cd17757  244 DELVEQYKELRQDDAS--GSTRSSYRITVRQLESLIRLSEAIARLHCSDEVTPEHVEEA 300
MCM cd17706
MCM helicase family; MCM helicases are a family of helicases that play an important role in ...
 192-381 8.84e-08

MCM helicase family; MCM helicases are a family of helicases that play an important role in replication and homologous recombination repair. The heterohexameric ring-shaped Mcm2-7 complex is part of the replicative helicase that unwinds parental double-stranded DNA at a replication fork to provide single-stranded DNA templates for the replicative polymerases. Mcm8 and Mcm9, form a complex required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350658 [Multi-domain]  Cd Length: 311  Bit Score: 53.89  E-value: 8.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 192 EIMGQEQGKRAL---------EITAAGGH-----NLLLIGPPGTGKTMLASRLSGLLPplnnhealesAAIYSLISSTSl 257
Cdd:cd17706    9 SIYGHEDVKKAVllqlfggvqKILEDGTRirgdiHILLVGDPGTAKSQILKYVLKIAP----------RGVYTSGKGSS- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 258 qkqwrrrpfrsphhSASLAAMV-----GGGSIPGPGEISLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRAKI 332
Cdd:cd17706   78 --------------GAGLTAAVvrdseTGEWYLEAGALVLADGGVCCIDEFDKMKELDRTALHEAMEQQTISIAKAGIVT 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 635767620 333 SYPAQFQLVAAMNPSpSGHYQgnhnrctPEQTLRYLGKLSGPFLDRFDL 381
Cdd:cd17706  144 TLNARCSILAAANPK-GGRYN-------PKLSPIENINLPSPLLSRFDL 184
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
190-232 4.09e-05

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 45.26  E-value: 4.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 635767620 190 LSEIMGQEQGKRALEI----------------TAAggHNLLLIGPPGTGKTMLASRLSG 232
Cdd:COG1223    1 LDDVVGQEEAKKKLKLiikelrrrenlrkfglWPP--RKILFYGPPGTGKTMLAEALAG 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 210-348 5.93e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 43.13  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620   210 GHNLLLIGPPGTGKTMLASRLSGLLPPLNnhealesaAIYSLISSTSLQKQWRRRpfRSPHHSASLAAMVGGGSIPGpGE 289
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPG--------GGVIYIDGEDILEEVLDQ--LLLIIVGGKKASGSGELRLR-LA 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635767620   290 ISLAHN---GILFLDELPEFERRVLDALREPIESgeihiSRTRAKISYPAQFQLVAAMNPSP 348
Cdd:smart00382  71 LALARKlkpDVLILDEITSLLDAEQEALLLLLEE-----LRLLLLLKSEKNLTVILTTNDEK 127
chlI CHL00081
Mg-protoporyphyrin IX chelatase
 193-416 9.90e-05

Mg-protoporyphyrin IX chelatase


Pssm-ID: 177020 [Multi-domain]  Cd Length: 350  Bit Score: 44.59  E-value: 9.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 193 IMGQEQGKRALEITAA----GGhnLLLIGPPGTGKTMLASRLSGLLP--------PLNNHealesAAIYSLISSTSLQKQ 260
Cdd:CHL00081  19 IVGQEEMKLALILNVIdpkiGG--VMIMGDRGTGKSTTIRALVDLLPeievvkddPFNSH-----PSDPELMSDEVREAI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 261 WRRRPFRSPHHSASLAAMVGG-------GSI-------PG-----PGEISLAHNGILFLDELPEFERRVLDALREPIESG 321
Cdd:CHL00081  92 QNGETIETEKIKIPMVDLPLGatedrvcGTIdiekaltEGvkafePGLLAKANRGILYVDEVNLLDDHLVDILLDSAASG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 322 EIHISRTRAKISYPAQFQLVAAmnpspsghyqGNhnrctPEQtlrylGKLSGPFLDRFDLSLEIPLPPPGLLRQKgITGE 401
Cdd:CHL00081 172 WNTVEREGISIRHPARFVLVGS----------GN-----PEE-----GELRPQLLDRFGMHAEIRTVKDPELRVK-IVEQ 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 635767620 402 SSA-----------------DVRERVIAAQTR 416
Cdd:CHL00081 231 RTSfdknpqefrekyeesqeELRSKIVAAQNL 262
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 86-234 1.40e-04

ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];


Pssm-ID: 440273 [Multi-domain]  Cd Length: 514  Bit Score: 44.20  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  86 AIALLAASEQLNTTRLgsyefvgELALTGALRGVPGAISGALEAIRAGRQIIVANENASEVSLIAEKGclVAGHLQEvca 165
Cdd:COG0507   32 AALLSRAAGEGHTFPL-------EDLAAARLLGVAEDIEAALAALVESGPLVLDGRRYLTRLLEAEQR--LARRLRR--- 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635767620 166 wleGRHELSEPEECDNVIADTPEDLSEIMGQEQgKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLL 234
Cdd:COG0507  100 ---LARPALDEADVEAALAALEPRAGITLSDEQ-REAVALALTTRRVSVLTGGAGTGKTTTLRALLAAL 164
MCM8 cd17759
DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a ...
 191-381 1.70e-04

DNA helicase Mcm8; Mcm8 plays an important role homologous recombination repair. It forms a complex with Mcm9 that is required for homologous recombination (HR) repair induced by DNA interstrand crosslinks (ICLs).


Pssm-ID: 350665 [Multi-domain]  Cd Length: 289  Bit Score: 43.68  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 191 SEIMGQEQGKRALEITAAGGH----------------NLLLIGPPGTGKTMLASRLSGLLPplnnhealESAAIYSLISS 254
Cdd:cd17759    8 PAIYGHELVKAGLLLSLFGGKqkyaddknripirgdpHVLIVGDPGLGKSQMLQAACNIAP--------RGVYVCGNTTT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 255 TSLQKQWRRRPFRSPHHSASLAAMVgggsipgpgeisLAHNGILFLDELPEFERRvLDALREPIESGEIHISRTRAKISY 334
Cdd:cd17759   80 TSGLTVTLTKDGRSGDFALEAGALV------------LGDQGICGIDEFDKMGSQ-HQALLEAMEQQSVSLAKAGVVCSL 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 635767620 335 PAQFQLVAAMNPSpSGHYqgNHNRCTPEQTlrylgKLSGPFLDRFDL 381
Cdd:cd17759  147 PARTSVIAAANPV-GGHY--NKGKTVSENL-----KMGPALLSRFDL 185
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 187-228 3.54e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.76  E-value: 3.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 635767620 187 PEDLSEIMGQE----QGK---RALEitaAGG-HNLLLIGPPGTGKTMLAS 228
Cdd:PRK13342   8 PKTLDEVVGQEhllgPGKplrRMIE---AGRlSSMILWGPPGTGKTTLAR 54
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 210-234 4.23e-04

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 40.73  E-value: 4.23e-04
                         10        20
                 ....*....|....*....|....*
gi 635767620 210 GHNLLLIGPPGTGKTMLASRLSGLL 234
Cdd:cd19481   26 PKGILLYGPPGTGKTLLAKALAGEL 50
MCM_arch cd17761
archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the ...
 209-381 4.73e-04

archaeal MCM protein; archaeal MCM proteins form a homohexameric ring homologous to the eukaryotic Mcm2-7 helicase and also function as the replicative helicase at the replication fork


Pssm-ID: 350667 [Multi-domain]  Cd Length: 308  Bit Score: 42.05  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 209 GGHNLLLIGPPGTGKTMLASRLSGLLPplnnhealesAAIYSLISSTSlqkqwrrrpfrsphhSASLAAMV------GGG 282
Cdd:cd17761   41 GDIHILLVGDPGTAKSQLLKYVSKVAP----------RAVYTTGKGST---------------AAGLTAAVvrdegtGEW 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 283 SIPGpGEISLAHNGILFLDELPEFERRVLDALREPIESGEIHISRTRAKISYPAQFQLVAAMNPSpSGHYqgNHNRCTPE 362
Cdd:cd17761   96 YLEA-GALVLADKGIAVVDEIDKMRKEDRSALHEAMEQQTISIAKAGIVATLNARAAVLAAANPK-FGRF--DSYRPVAE 171

                        170
                 ....*....|....*....
gi 635767620 363 QTlrylgKLSGPFLDRFDL 381
Cdd:cd17761  172 QI-----DLPPTLLSRFDL 185
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 187-227 5.12e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 42.35  E-value: 5.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 635767620 187 PEDLSEIMGQEQ----GK---RALEitaAGG-HNLLLIGPPGTGKTMLA 227
Cdd:COG2256   21 PRTLDEVVGQEHllgpGKplrRAIE---AGRlSSMILWGPPGTGKTTLA 66
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 213-262 9.19e-04

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 40.03  E-value: 9.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 635767620 213 LLLIGPPGTGKTMLASRLsgllpplnnheALESAAIYSLISSTSLQKQWR 262
Cdd:cd19509   35 ILLYGPPGTGKTLLARAV-----------ASESGSTFFSISASSLVSKWV 73
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 82-234 9.24e-04

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


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 41.44  E-value: 9.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  82 DLPIAIALLAASEQLNTTRLGSYEFVGELALTGALRGVPGAISGALEAIRAGRQIIVANENASEVSLIAEKGCLVAGHLQ 161
Cdd:COG0464   48 LLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 162 EVCAWLEGRHELSEPEECDNVIADTPEDLSEIMGQEQGKRALEITAAG---------------GHNLLLIGPPGTGKTML 226
Cdd:COG0464  128 ALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALplkrpelreeyglppPRGLLLYGPPGTGKTLL 207


                 ....*...
gi 635767620 227 ASRLSGLL 234
Cdd:COG0464  208 ARALAGEL 215
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
210-227 1.12e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.53  E-value: 1.12e-03
                         10
                 ....*....|....*...
gi 635767620 210 GHNLLLIGPPGTGKTMLA 227
Cdd:COG1484   99 GENLILLGPPGTGKTHLA 116
PRK04195 PRK04195
replication factor C large subunit; Provisional
 187-227 1.12e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 41.44  E-value: 1.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 635767620 187 PEDLSEIMGQEQGKRALE--ITA-AGGHN---LLLIGPPGTGKTMLA 227
Cdd:PRK04195  10 PKTLSDVVGNEKAKEQLRewIESwLKGKPkkaLLLYGPPGVGKTSLA 56
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 213-262 1.20e-03

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 39.97  E-value: 1.20e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 635767620 213 LLLIGPPGTGKTMLASRLsgllpplnnheALESAAIYSLISSTSLQKQWR 262
Cdd:cd19522   36 VLMVGPPGTGKTLLAKAV-----------ATECGTTFFNVSSSTLTSKYR 74
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 213-387 1.28e-03

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 39.11  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  213 LLLIGPPGTGKTMLASRLSGLLpplnnhealeSAAIYSLISSTSLQKQWRRRPfrsphhsASLAAMVGGGSIPGPgeisl 292
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVSKYVGESE-------KRLRELFEAAKKLAP----- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  293 ahnGILFLDEL-----------PEFERRVLDALREPIESGEIHISRTRakisypaqfqLVAAMNpspsghyqgnhnrctp 361
Cdd:pfam00004  59 ---CVIFIDEIdalagsrgsggDSESRRVVNQLLTELDGFTSSNSKVI----------VIAATN---------------- 109

                         170       180
                  ....*....|....*....|....*.
gi 635767620  362 eqtlrYLGKLSGPFLDRFDLSLEIPL 387
Cdd:pfam00004 110 -----RPDKLDPALLGRFDRIIEFPL 130
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 186-234 1.31e-03

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 41.19  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635767620 186 TPEDLSE-----IMGQEQGKRAL---------EITAAGGH---------NLLLIGPPGTGKTMLASRLSGLL 234
Cdd:COG1219   62 KPKEIKAfldeyVIGQERAKKVLsvavynhykRLNSGSKDdddveleksNILLIGPTGSGKTLLAQTLARIL 133
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
187-227 1.84e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 40.56  E-value: 1.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 635767620 187 PEDLSEIMGQEQGKRALEITAAGG---HNLLLIGPPGTGKTMLA 227
Cdd:COG2812    6 PQTFDDVVGQEHVVRTLKNALASGrlaHAYLFTGPRGVGKTTLA 49
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
186-234 2.03e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 40.53  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635767620 186 TPEDLSEIM-----GQEQGKRAL---------EITAAGGH---------NLLLIGPPGTGKTMLASRLSGLL 234
Cdd:PRK05342  61 TPKEIKAHLdqyviGQERAKKVLsvavynhykRLRHGDKKdddvelqksNILLIGPTGSGKTLLAQTLARIL 132
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 203-236 2.04e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 39.30  E-value: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 635767620  203 LEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPP 236
Cdd:pfam12775  24 LDLLLKNGKPVLLVGPTGTGKTVIIQNLLRKLDK 57
bpMoxR pfam20030
MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the ...
 203-234 2.08e-03

MoxR domain in the MoxR-vWA-beta-propeller ternary systems; Core MoxR component domain of the MoxR-vWA-beta-propeller ternary systems, a class of NTP-dependent biological conflict systems.


Pssm-ID: 437862 [Multi-domain]  Cd Length: 205  Bit Score: 39.53  E-value: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 635767620  203 LEITAAGGHNLLLIGPPGTGKTMLASRLSGLL 234
Cdd:pfam20030  24 LGLALVARENLFLLGPPGTAKSALVRRLAARL 55
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 213-232 2.43e-03

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 39.99  E-value: 2.43e-03
                         10        20
                 ....*....|....*....|
gi 635767620 213 LLLIGPPGTGKTMLASRLSG 232
Cdd:COG1222  115 VLLYGPPGTGKTLLAKAVAG 134
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
187-227 2.52e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.11  E-value: 2.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 635767620 187 PEDLSEIMGQEQGKRALE--ITAAGGHN-----LLLIGPPGTGKTMLA 227
Cdd:PRK00080  21 PKSLDEFIGQEKVKENLKifIEAAKKRGealdhVLLYGPPGLGKTTLA 68
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
188-234 2.92e-03

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 39.61  E-value: 2.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 635767620 188 EDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLL 234
Cdd:PRK09984   8 EKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI 54
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 187-227 3.40e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 38.25  E-value: 3.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 635767620  187 PEDLSEIMGQEQGKRALE--ITAAGGHN-----LLLIGPPGTGKTMLA 227
Cdd:pfam05496   3 PRTLDEYIGQEKVKENLKifIEAAKQRGealdhVLLYGPPGLGKTTLA 50
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 192-261 4.23e-03

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 38.29  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 192 EIMGQEQGKRAL-EITA-------------AGGHNLLLIGPPGTGKTMLASRLsgllpplnnheALESAAIYSLISSTSL 257
Cdd:cd19524    1 DIAGQDLAKQALqEMVIlpslrpelftglrAPARGLLLFGPPGNGKTMLAKAV-----------AAESNATFFNISAASL 69


                 ....
gi 635767620 258 QKQW 261
Cdd:cd19524   70 TSKY 73
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 188-237 4.63e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 38.32  E-value: 4.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 635767620 188 EDLSEIMGQEQGKRALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPL 237
Cdd:PRK13539   6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA 55
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
214-227 4.81e-03

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 39.63  E-value: 4.81e-03
                         10
                 ....*....|....
gi 635767620 214 LLIGPPGTGKTMLA 227
Cdd:COG0465  179 LLVGPPGTGKTLLA 192
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 213-309 5.16e-03

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 37.79  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 213 LLLIGPPGTGKTMLASRLsgllpplnnheALESAAIYSLISSTSLQKQWRrrpfrspHHSASLAAMVgggsipgpgeISL 292
Cdd:cd19520   38 VLLYGPPGCGKTMLAKAT-----------AKEAGARFINLQVSSLTDKWY-------GESQKLVAAV----------FSL 89

                         90       100
                 ....*....|....*....|
gi 635767620 293 AHN---GILFLDELPEFERR 309
Cdd:cd19520   90 ASKlqpSIIFIDEIDSFLRQ 109
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 187-227 5.29e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 38.91  E-value: 5.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 635767620 187 PEDLSEIMGQEQGKRALE--ITAAGGHN-----LLLIGPPGTGKTMLA 227
Cdd:COG2255   24 PKRLDEYIGQEKVKENLKifIEAAKKRGealdhVLLYGPPGLGKTTLA 71
rfc PRK00440
replication factor C small subunit; Reviewed
 187-227 7.62e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 38.32  E-value: 7.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 635767620 187 PEDLSEIMGQEQGKRALEITAAGGH--NLLLIGPPGTGKTMLA 227
Cdd:PRK00440  13 PRTLDEIVGQEEIVERLKSYVKEKNmpHLLFAGPPGTGKTTAA 55
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 190-496 8.45e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 38.44  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  190 LSEIMGQEQGKRALE--ITAAGGHN-----LLLIGPPGTGKTMLASRLsgllpplnnheALESAAIYSLISSTSLQKQwr 262
Cdd:TIGR00635   3 LAEFIGQEKVKEQLQlfIEAAKMRQealdhLLLYGPPGLGKTTLAHII-----------ANEMGVNLKITSGPALEKP-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  263 rrpfrsphhsASLAAMVGGgsipgpgeisLAHNGILFLDELPEFERRVLDALREPIESGEIHI-------SRTRaKISYP 335
Cdd:TIGR00635  70 ----------GDLAAILTN----------LEEGDVLFIDEIHRLSPAVEELLYPAMEDFRLDIvigkgpsARSV-RLDLP 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  336 aQFQLVAAmnpspsghyqgnhnrctpeqTLRyLGKLSGPFLDRFDLSLEIPLPPPGLLrqkgitgessadvrERVIAaqt 415
Cdd:TIGR00635 129 -PFTLVGA--------------------TTR-AGMLTSPLRDRFGIILRLEFYTVEEL--------------AEIVS--- 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620  416 rQYARQnrLNARLDNAGIrqfcslnmedavwlEETLTRFGLSIRAWQRLLKVARTIADVEGCSDIQRKHLQEALSYRAID 495
Cdd:TIGR00635 170 -RSAGL--LNVEIEPEAA--------------LEIARRSRGTPRIANRLLRRVRDFAQVRGQKIINRDIALKALEMLMID 232


                  .
gi 635767620  496 R 496
Cdd:TIGR00635 233 E 233
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 201-321 9.14e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 36.84  E-value: 9.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635767620 201 RALEITAAGGHNLLLIGPPGTGKTMLASRLSGLLPPlnnheALESAAIYSLISSTSLQKQWRRRPFRSPHHS------AS 274
Cdd:cd00267   16 DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP-----TSGEILIDGKDIAKLPLEELRRRIGYVPQLSggqrqrVA 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 635767620 275 LAAMvgggsipgpgeisLAHN-GILFLDEL-----PEFERRVLDALREPIESG 321
Cdd:cd00267   91 LARA-------------LLLNpDLLLLDEPtsgldPASRERLLELLRELAEEG 130
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 193-234 9.65e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 37.96  E-value: 9.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 635767620 193 IMGQEQGKRALEItAAGGH--------------------NLLLIGPPGTGKTMLASRLSGLL 234
Cdd:cd19497   14 VIGQERAKKVLSV-AVYNHykrirnnlkqkdddveleksNILLIGPTGSGKTLLAQTLAKIL 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH