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Conserved domains on  [gi|1039729385|ref|XP_017176834|]
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uncharacterized protein KIAA2012 homolog isoform X16 [Mus musculus]

Protein Classification

DUF4670 domain-containing protein( domain architecture ID 12174332)

DUF4670 domain-containing protein similar to Homo sapiens protein KIAA2012

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
504-1014 2.26e-157

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


:

Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 476.37  E-value: 2.26e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  504 SSRLAQAAESQGAPQSLEAAAQKTGEPQRCINKGLICSNEKEFYTRKLHIDMTPFLKERGSELDSHEEPGGPLRGNAKDS 583
Cdd:pfam15709    3 TSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQDS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  584 QDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKKLA----SETPRKKKKRRS-KLLNQ 657
Cdd:pfam15709   83 QDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEKLTavdtSLLPRAREGKTEpRLFNQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  658 KTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERN 736
Cdd:pfam15709  163 ETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  737 MEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSK 814
Cdd:pfam15709  243 LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  815 ALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 894
Cdd:pfam15709  323 ALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  895 QEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQ 974
Cdd:pfam15709  403 QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1039729385  975 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 1014
Cdd:pfam15709  483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
 
Name Accession Description Interval E-value
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
504-1014 2.26e-157

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 476.37  E-value: 2.26e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  504 SSRLAQAAESQGAPQSLEAAAQKTGEPQRCINKGLICSNEKEFYTRKLHIDMTPFLKERGSELDSHEEPGGPLRGNAKDS 583
Cdd:pfam15709    3 TSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQDS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  584 QDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKKLA----SETPRKKKKRRS-KLLNQ 657
Cdd:pfam15709   83 QDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEKLTavdtSLLPRAREGKTEpRLFNQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  658 KTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERN 736
Cdd:pfam15709  163 ETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  737 MEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSK 814
Cdd:pfam15709  243 LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  815 ALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 894
Cdd:pfam15709  323 ALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  895 QEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQ 974
Cdd:pfam15709  403 QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1039729385  975 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 1014
Cdd:pfam15709  483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
771-1033 2.70e-14

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEER-SHEDPSKALQDKKQQE-KASRDRIRIEKAEMRwlKVEQRRR 847
Cdd:COG1196    236 ELEAELEELEAELEeLEAELEELEAELAELEAELEELRlELEELELELEEAQAEEyELLAELARLEQDIAR--LEERRRE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  848 EQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEI 927
Cdd:COG1196    314 LEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  928 QRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1007
Cdd:COG1196    389 LEALRA-----AAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                          250       260
                   ....*....|....*....|....*.
gi 1039729385 1008 AQEQIRQKAALDKHLHFHQELSKEAS 1033
Cdd:COG1196    463 ELLAELLEEAALLEAALAELLEELAE 488
PTZ00121 PTZ00121
MAEBL; Provisional
804-1020 3.37e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 3.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRl 883
Cdd:PTZ00121  1572 AEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  884 rkqrLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM 963
Cdd:PTZ00121  1648 ----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729385  964 --AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA--LEEATKLAQEQIRQKAALDK 1020
Cdd:PTZ00121  1722 kkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIE 1782
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
900-1020 1.70e-10

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 63.71  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyQQQKLAAE 979
Cdd:TIGR02794   53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAE 131
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039729385  980 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1020
Cdd:TIGR02794  132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
943-1017 2.11e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 2.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729385  943 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:cd06503     43 EKAKEEAEELLAEYEEKLAEAraeAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
 
Name Accession Description Interval E-value
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
504-1014 2.26e-157

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 476.37  E-value: 2.26e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  504 SSRLAQAAESQGAPQSLEAAAQKTGEPQRCINKGLICSNEKEFYTRKLHIDMTPFLKERGSELDSHEEPGGPLRGNAKDS 583
Cdd:pfam15709    3 TSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQDS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  584 QDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKKLA----SETPRKKKKRRS-KLLNQ 657
Cdd:pfam15709   83 QDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEKLTavdtSLLPRAREGKTEpRLFNQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  658 KTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERN 736
Cdd:pfam15709  163 ETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  737 MEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSK 814
Cdd:pfam15709  243 LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  815 ALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 894
Cdd:pfam15709  323 ALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  895 QEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQ 974
Cdd:pfam15709  403 QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1039729385  975 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 1014
Cdd:pfam15709  483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
771-1033 2.70e-14

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 77.67  E-value: 2.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEER-SHEDPSKALQDKKQQE-KASRDRIRIEKAEMRwlKVEQRRR 847
Cdd:COG1196    236 ELEAELEELEAELEeLEAELEELEAELAELEAELEELRlELEELELELEEAQAEEyELLAELARLEQDIAR--LEERRRE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  848 EQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEI 927
Cdd:COG1196    314 LEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  928 QRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1007
Cdd:COG1196    389 LEALRA-----AAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                          250       260
                   ....*....|....*....|....*.
gi 1039729385 1008 AQEQIRQKAALDKHLHFHQELSKEAS 1033
Cdd:COG1196    463 ELLAELLEEAALLEAALAELLEELAE 488
PTZ00121 PTZ00121
MAEBL; Provisional
804-1020 3.37e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 3.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRl 883
Cdd:PTZ00121  1572 AEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  884 rkqrLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM 963
Cdd:PTZ00121  1648 ----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729385  964 --AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA--LEEATKLAQEQIRQKAALDK 1020
Cdd:PTZ00121  1722 kkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIE 1782
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
819-1036 1.08e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.66  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  819 KKQQEKASR-----DRIRIEKAEMRWLKVEQRRREQEELtwlhKEQLEKAEKMKEELEleQQRRTEENRLRKqrleeerq 893
Cdd:COG1196    206 ERQAEKAERyrelkEELKELEAELLLLKLRELEAELEEL----EAELEELEAELEELE--AELAELEAELEE-------- 271
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  894 qqeeaekkRRLQLQAARERARQQQEELRRKLQEIQR--KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEE----- 966
Cdd:COG1196    272 --------LRLELEELELELEEAQAEEYELLAELARleQDIARLEERRRELEERLEELEEELAELEEELEELEEEleele 343
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  967 ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1036
Cdd:COG1196    344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
904-1017 3.00e-12

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 69.84  E-value: 3.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  904 LQLQAARERARQQQEElRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 983
Cdd:PRK09510    92 LQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039729385  984 QEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:PRK09510   171 AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
793-1020 3.21e-12

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 70.92  E-value: 3.21e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  793 QATDVASDMECEEERSHEDPSKALQDKKQQ-EKASRDRIRIEKAEMRWLKVEQRRREQEELTWlhKEQLEKAEKMKEELE 871
Cdd:pfam17380  332 QAAIYAEQERMAMERERELERIRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVKILEE 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  872 LEQqrRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKlQEIQRKKQQEAAERAEAEKQRQKELEM 951
Cdd:pfam17380  410 ERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDR 486
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  952 QLAEEQKRLM----------EMAEEER--------LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 1013
Cdd:pfam17380  487 KRAEEQRRKIlekeleerkqAMIEEERkrkllekeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566

                   ....*..
gi 1039729385 1014 QKAALDK 1020
Cdd:pfam17380  567 RLEAMER 573
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
815-1036 7.80e-12

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 7.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  815 ALQDKKQQEKASRDRIRIEKAEmrwlkvEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 894
Cdd:COG1196    231 LLKLRELEAELEELEAELEELE------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  895 QEEaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAeKQRQKELEMQLAEEQKRLMEMAEE--ERLEYQ 972
Cdd:COG1196    305 ARL--EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAElaEAEEEL 381
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729385  973 QQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1036
Cdd:COG1196    382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
771-1026 1.18e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.20  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQVAiDGRLSSIQATDVASDMECEEERSHEDPSKALQDKK-QQEKASRDRIRIEKAEMRWLKVEQRRREQ 849
Cdd:COG1196    257 ELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEEELEEL 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  850 EELTwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEI 927
Cdd:COG1196    336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAelAAQLEELEEAEEAL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  928 QRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmemAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1007
Cdd:COG1196    413 LERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
                          250
                   ....*....|....*....
gi 1039729385 1008 AQEQIRQKAALDKHLHFHQ 1026
Cdd:COG1196    490 AARLLLLLEAEADYEGFLE 508
PTZ00121 PTZ00121
MAEBL; Provisional
804-1036 2.55e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 2.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKALQDKKQQEKASRDRIR----IEKAEMRwLKVEQRRREQEELTWLHKE-----QLEKAEKMKEELELEQ 874
Cdd:PTZ00121  1525 DEAKKAEEAKKADEAKKAEEKKKADELKkaeeLKKAEEK-KKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLYEE 1603
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  875 QRRTEENRLRKQRLEEERQQQ---EEAEKKRRLQLQAARERARQQQEELRRKLQEIQ------RKKQQEAAERAEAEKQR 945
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKA 1683
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  946 QKElEMQLAEEQKRlmeMAEEERLEYQQQKLAAEEKARQE----AEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKH 1021
Cdd:PTZ00121  1684 EED-EKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
                          250
                   ....*....|....*
gi 1039729385 1022 LHFHQELSKEASGLQ 1036
Cdd:PTZ00121  1760 AHLKKEEEKKAEEIR 1774
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
814-1036 3.66e-11

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.65  E-value: 3.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE-NRLRKqrleeer 892
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElEEAQA------- 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  893 qqQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-QKELEMQLAEEQKRLMEMAEEERLEY 971
Cdd:COG1196    289 --EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEA 366
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729385  972 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1036
Cdd:COG1196    367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
908-1032 4.19e-11

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 65.98  E-value: 4.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  908 AARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMaEEERLEYQQQKLAAEEKARQEAE 987
Cdd:PRK09510    60 VVEQYNRQQQQQKSAKRAEEQRKKKE---------QQQAEELQQKQAAEQERLKQL-EKERLAAQEQKKQAEEAAKQAAL 129
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729385  988 ERRKQEEEAAKLA-------------LEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1032
Cdd:PRK09510   130 KQKQAEEAAAKAAaaakakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
900-1020 1.70e-10

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 63.71  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyQQQKLAAE 979
Cdd:TIGR02794   53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAE 131
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039729385  980 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1020
Cdd:TIGR02794  132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
814-1005 3.73e-10

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 63.99  E-value: 3.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEqleKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 893
Cdd:pfam17380  399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRK 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  894 QQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY 971
Cdd:pfam17380  476 KLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1039729385  972 QQQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT 1005
Cdd:pfam17380  556 EQMRKATEERSRLEAMEREREmmrqivESEKARAEYEATT 595
PTZ00121 PTZ00121
MAEBL; Provisional
804-1020 8.96e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 8.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQL----EKAEKMKEELELEQQRRTE 879
Cdd:PTZ00121  1215 EEARKAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKAD 1293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  880 ENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE------IQRKKQQEAAERAEAEKQRQKELEMQL 953
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakkaaeAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  954 AEEQKR---LMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEEEAAKlaLEEATKLAQEQIRQKAALDK 1020
Cdd:PTZ00121  1374 EEAKKKadaAKKKAEEKKKADEAKKKAEEDK--KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKK 1439
PTZ00121 PTZ00121
MAEBL; Provisional
804-1016 9.03e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 9.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENR- 882
Cdd:PTZ00121  1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  883 ---LRKQRLEEERQQQEEAEKKRRLQLQAARE--RARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQ 957
Cdd:PTZ00121  1554 aeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEE 1631
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  958 KRLMEM-----------AEEERLEYQQQKLAAEEKARQEAEERRKQEEeaAKLAlEEATKLAQEQIRQKA 1016
Cdd:PTZ00121  1632 KKKVEQlkkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKA-EEDEKKAAEALKKEA 1698
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
907-1032 1.69e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 57.55  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEM-----AEEERLEYQQQKLAAEEK 981
Cdd:TIGR02794   47 AVAQQANRIQQQKKPAAKKEQERQKKL---------EQQAEEAEKQRAAEQARQKELeqraaAEKAAKQAEQAAKQAEEK 117
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039729385  982 ARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1032
Cdd:TIGR02794  118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA 168
PTZ00121 PTZ00121
MAEBL; Provisional
801-1020 1.97e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  801 MECEEERSHEDPSKALQDKKQQEKASRDRIRiekaemrwlKVEQRRREQEELTwlHKEQLEKAEKMKEELELEQQRRTEE 880
Cdd:PTZ00121  1272 IKAEEARKADELKKAEEKKKADEAKKAEEKK---------KADEAKKKAEEAK--KADEAKKKAEEAKKKADAAKKKAEE 1340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  881 NRLRKQRLEEERQQQEEAEKKRRLQLQAAR---ERARQQQEELRRKLQEIqrKKQQEAAERAEAEKQRQKELEMQLAEEQ 957
Cdd:PTZ00121  1341 AKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKK 1418
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729385  958 K--RLMEMAEEERLEYQQQKLAAE----EKARQEAEERRKQEE-----EAAKLAlEEATKLAQEQIRQKAALDK 1020
Cdd:PTZ00121  1419 KadEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEakkkaEEAKKA-DEAKKKAEEAKKADEAKKK 1491
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
772-1050 3.63e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 3.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  772 LSLELDALESQ-VAIDGRLSSIQA--TDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQR--R 846
Cdd:TIGR02169  228 LLKEKEALERQkEAIERQLASLEEelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  847 REQEELtwlhKEQLEKAEKmkeeleleQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE 926
Cdd:TIGR02169  308 RSIAEK----ERELEDAEE--------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  927 IQRKKQqeaaERAEAEKQRQKELEM------QLAEEQKRLMEMAE---------EERLEYQQQKLAAEEKARQEAEERRK 991
Cdd:TIGR02169  376 VDKEFA----ETRDELKDYREKLEKlkreinELKRELDRLQEELQrlseeladlNAAIAGIEAKINELEEEKEDKALEIK 451
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729385  992 QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQWTQNISRPWVYSYF 1050
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
814-1014 4.26e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.44  E-value: 4.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQEKASR---DRIRIEKAEmRWLKVEQRRR--------------------EQEELTWLHKEQLEKAEKMKEEL 870
Cdd:pfam17380  282 KAVSERQQQEKFEKmeqERLRQEKEE-KAREVERRRKleeaekarqaemdrqaaiyaEQERMAMERERELERIRQEERKR 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  871 ELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRL--QLQAAReRARQQQEELRRKLQEIQRKKQQeaaERAEAEKQRQKE 948
Cdd:pfam17380  361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVrqELEAAR-KVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQRE 436
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729385  949 LEmQLAEEQKRLMEMAEEERLEYQQQKlaaeEKARQEAEERRKQEEEAAKlaLEEATKLAQEQIRQ 1014
Cdd:pfam17380  437 VR-RLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRK 495
PTZ00121 PTZ00121
MAEBL; Provisional
683-1030 4.33e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 4.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  683 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQGL 762
Cdd:PTZ00121  1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  763 LRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV 842
Cdd:PTZ00121  1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  843 EQRRREQEELTwlhKEQLEKAEKMKEELELEQQRRTEENRLR---KQRLEEERQQQEEAEKKRRLQLQAARERarqQQEE 919
Cdd:PTZ00121  1401 EEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKAEEAKKKAEEAK---KADE 1474
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  920 LRRKLQEIQRK---KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEE-- 994
Cdd:PTZ00121  1475 AKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADElk 1552
                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1039729385  995 EAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 1030
Cdd:PTZ00121  1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
814-1011 9.57e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 9.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHK-EQLEKAEKMKEELELEQQRRTEENRLRKQRLEEER 892
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  893 QQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRK--KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEerLE 970
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--IE 862
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039729385  971 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQ 1011
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
907-1017 1.89e-07

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 54.88  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEyQQQKLAAEEKARQEA 986
Cdd:COG2268    241 EAEAELAKKKAEERRE--AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1039729385  987 EERRKQEEEAAKLALEEATKLAQ-EQIRQKAA 1017
Cdd:COG2268    317 EKQAAEAEAEAEAEAIRAKGLAEaEGKRALAE 348
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
810-1020 3.79e-07

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 53.72  E-value: 3.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  810 EDPSKAL--QDKKQQEKASRDRiRIEKAEMRW---LKVEQRRREQEEltwlhkEQLEKAEKMKEELELEQQRRTEEnrlr 884
Cdd:COG2268    180 EDENNYLdaLGRRKIAEIIRDA-RIAEAEAEReteIAIAQANREAEE------AELEQEREIETARIAEAEAELAK---- 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  885 kqrleeerqqqeeaeKKRRLQLQAARERARQQQE-ELRR--KLQEIQRKKQQEaaeraeaekQRQKELEMQLAEEQKRLM 961
Cdd:COG2268    249 ---------------KKAEERREAETARAEAEAAyEIAEanAEREVQRQLEIA---------EREREIELQEKEAEREEA 304
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729385  962 EMAEEERLEYQQQKLAAEEKARQEAE-ERRKQEEEA-AKLALEEATKLAQEQIRQKAALDK 1020
Cdd:COG2268    305 ELEADVRKPAEAEKQAAEAEAEAEAEaIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIEK 365
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
877-1032 8.12e-07

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.23  E-value: 8.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  877 RTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQ-EAAERAEAEKQRQKELEMQLAE 955
Cdd:COG4717     64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAE 143
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729385  956 EQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1032
Cdd:COG4717    144 LPERLEEL--EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
806-1017 1.17e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 51.84  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  806 ERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRK 885
Cdd:pfam13868  108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  886 qrleeerqqqeeaekkRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM------QLAEEQKR 959
Cdd:pfam13868  188 ----------------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELqqareeQIELKERR 251
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729385  960 LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAA 1017
Cdd:pfam13868  252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR-RELEKQIEEREEQRAA 308
Caldesmon pfam02029
Caldesmon;
817-1017 1.92e-06

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 51.79  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  817 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 896
Cdd:pfam02029  143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  897 EAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERleyqqqkl 976
Cdd:pfam02029  223 TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKK----REERR-------- 290
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1039729385  977 aaeeKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:pfam02029  291 ----KLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRA 327
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
760-1010 3.00e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  760 QGLLRSHSAAGQLSLELDALESQVAidgRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRdRIRIEKAEMRW 839
Cdd:COG1196    302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEAELAEA 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  840 LKVEQRRREQEEltwlhkeQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEE 919
Cdd:COG1196    378 EEELEELAEELL-------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  920 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKL 999
Cdd:COG1196    451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
                          250
                   ....*....|.
gi 1039729385 1000 ALEEATKLAQE 1010
Cdd:COG1196    531 GVEAAYEAALE 541
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
911-1000 3.60e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.73  E-value: 3.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  911 ERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY-QQQKLAAEEKARQEAE-- 987
Cdd:pfam05672   39 EEERLRKEELRRRAEE-ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKEEAEAKAREEAErq 117
                           90
                   ....*....|....*..
gi 1039729385  988 ----ERRKQEEEAAKLA 1000
Cdd:pfam05672  118 rqerEKIMQQEEQERLE 134
PRK12704 PRK12704
phosphodiesterase; Provisional
900-1010 3.69e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.93  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ------RQKELEMQLAEEQKRL------------- 960
Cdd:PRK12704    78 RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKqqelekKEEELEELIEEQLQELerisgltaeeake 157
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039729385  961 --MEMAEEErleyqqqklaaeekARQEAEERRKQEEEAAKlalEEATKLAQE 1010
Cdd:PRK12704   158 ilLEKVEEE--------------ARHEAAVLIKEIEEEAK---EEADKKAKE 192
PRK12704 PRK12704
phosphodiesterase; Provisional
900-1031 4.24e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.55  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQE-ELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRlmemaeEERLEYQQQKLAA 978
Cdd:PRK12704    56 KEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRL--------LQKEENLDRKLELLEKR------EEELEKKEKELEQ 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729385  979 E----EKARQEAEERRKQE----EEAAKLALEEATKLAQEQIRQKAALDKHLHFHQ--ELSKE 1031
Cdd:PRK12704   122 KqqelEKKEEELEELIEEQlqelERISGLTAEEAKEILLEKVEEEARHEAAVLIKEieEEAKE 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
771-1008 4.84e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.83  E-value: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQVAI-DGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMRWLKVEQR 845
Cdd:TIGR02168  292 ALANEISRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEelaeLEEKLEELKEELESLEAELEELEAELEELE 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  846 RREQEEltwlhKEQLEKAEKMKEELEleQQRRTEENRLRkqrleeerqqqeeAEKKRRLQLQAARERARQQQEELRRKLQ 925
Cdd:TIGR02168  372 SRLEEL-----EEQLETLRSKVAQLE--LQIASLNNEIE-------------RLEARLERLEDRRERLQQEIEELLKKLE 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  926 EIQRKKQQEA----AERAEAEKQRQKELEMQLAEEQKRLMEMAEEER-LEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 1000
Cdd:TIGR02168  432 EAELKELQAEleelEEELEELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDSLERLQENLEGFSEGVKAL 511

                   ....*...
gi 1039729385 1001 LEEATKLA 1008
Cdd:TIGR02168  512 LKNQSGLS 519
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
802-987 5.05e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.51  E-value: 5.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  802 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKaekmkeeLELEQQRRTEEN 881
Cdd:pfam17380  421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK-------EKRDRKRAEEQR 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  882 R-LRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRL 960
Cdd:pfam17380  494 RkILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ------EMEERRRIQEQMRKATEERSR 567
                          170       180
                   ....*....|....*....|....*..
gi 1039729385  961 MEMAEEERLEYQQqkLAAEEKARQEAE 987
Cdd:pfam17380  568 LEAMEREREMMRQ--IVESEKARAEYE 592
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
820-1031 5.14e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.92  E-value: 5.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  820 KQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRrtEENRLRKQRLEEERQQQEEAE 899
Cdd:pfam13868   26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI--EEREQKRQEEYEEKLQEREQM 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAE-----EQKRLMEMAEEERLEYQQQ 974
Cdd:pfam13868  104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkekAEREEEREAEREEIEEEKE 183
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729385  975 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 1031
Cdd:pfam13868  184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
843-1020 5.44e-06

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 49.84  E-value: 5.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  843 EQRRREQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 922
Cdd:TIGR02794   61 PAAKKEQERQ-----KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  923 KLQEIQRKKQQEAaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEaEERRKQEEEAAKLALE 1002
Cdd:TIGR02794  136 AEAEAERKAKEEA------AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKAKAAAE 208
                          170
                   ....*....|....*...
gi 1039729385 1003 EATKLAQEQIRQKAALDK 1020
Cdd:TIGR02794  209 AAAKAEAEAAAAAAAEAE 226
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
819-1036 5.78e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 5.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  819 KKQQEKASRDR-IRIEKAEMRW----LKVEQRRREQEELtwlhKEQLEKAEKMKEELELEQQRRTEE-NRLRKQrleeer 892
Cdd:TIGR02168  206 ERQAEKAERYKeLKAELRELELallvLRLEELREELEEL----QEELKEAEEELEELTAELQELEEKlEELRLE------ 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  893 qqqEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEE-ERLEY 971
Cdd:TIGR02168  276 ---VSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEElAELEE 344
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729385  972 QQQKLAAE--------EKARQEAEERRKQEEEAAKLALEEATKLAQEQiRQKAALDKHLhfhQELSKEASGLQ 1036
Cdd:TIGR02168  345 KLEELKEElesleaelEELEAELEELESRLEELEEQLETLRSKVAQLE-LQIASLNNEI---ERLEARLERLE 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
804-1001 5.84e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 5.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwLKVEQRRREQEELTWLHKEQLEKAEkmkeeleleQQRRTEENRL 883
Cdd:COG4717     81 KEAEEKEEEYAELQEELEELEEELEELEAELEE---LREELEKLEKLLQLLPLYQELEALE---------AELAELPERL 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  884 RKQRLEEerqqqeeaekKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEm 963
Cdd:COG4717    149 EELEERL----------EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE- 217
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039729385  964 aEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAL 1001
Cdd:COG4717    218 -AQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
814-1018 6.05e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQ-EKASRDRIRIEKAEMRWL--KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEE 890
Cdd:COG4717     49 ERLEKEADElFKPQGRKPELNLKELKELeeELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  891 ERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLE 970
Cdd:COG4717    129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-----LAELQEELEELLEQLSLATEEELQDLAEELEE 203
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1039729385  971 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 1018
Cdd:COG4717    204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
791-1003 6.69e-06

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 49.53  E-value: 6.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  791 SIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwlkveQRRREQEELTwlhkEQLEKAEKMKEEL 870
Cdd:pfam13868  135 FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEE-------EKEREIARLR----AQQEKAQDEKAER 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  871 ELEQQRRTEENRLRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEA 941
Cdd:pfam13868  204 DELRAKLYQEEQERKERQKEREEAE----KKARQRQELQQAREEQIELKERRLAEEAEReeeefermlRKQAEDEEIEQE 279
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039729385  942 EKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEE 1003
Cdd:pfam13868  280 EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
814-1024 6.87e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 49.76  E-value: 6.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE--NRLRKQRLE 889
Cdd:COG4942     37 AELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  890 EERQQQE-------EAEKKRRLQLQAARERARQQQ-EELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLm 961
Cdd:COG4942    117 GRQPPLAlllspedFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAE-----LEAERAELEALLAELEEERAAL- 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729385  962 emaeeERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHF 1024
Cdd:COG4942    191 -----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
804-1013 1.10e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 1.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwlHKEQLE-KAEKMKEELELEQQRRTEENR 882
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE----ELEKLTeEISELEKRLEEIEQLLEELNK 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  883 lrkqRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLME 962
Cdd:TIGR02169  280 ----KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREIEEERKRRDK 354
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729385  963 MAEE-----ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 1013
Cdd:TIGR02169  355 LTEEyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
905-1017 1.63e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.29  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  905 QLQAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERlEYQQQKlAAEEKARQ 984
Cdd:COG3883    137 ELKADKAELEAKKAELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAEEA-AAEAQL-AELEAELA 206
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039729385  985 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:COG3883    207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
811-1020 1.93e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  811 DPSKALQD--KKQQEKASRDRirieKAEMRWLKVEQRRREQEEltwlhkEQLEkaekmkeeleleQQRRTEENRLRKQRL 888
Cdd:PRK09510    56 DPGAVVEQynRQQQQQKSAKR----AEEQRKKKEQQQAEELQQ------KQAA------------EQERLKQLEKERLAA 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  889 EEERQQQEEAEKKRRLQLQAARERARQQQEElrrklqeiqrkkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEEER 968
Cdd:PRK09510   114 QEQKKQAEEAAKQAALKQKQAEEAAAKAAAA----------------------AKAKAEAEAKRAAAAAKKAAAEAKKKA 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039729385  969 LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1020
Cdd:PRK09510   172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
PRK12705 PRK12705
hypothetical protein; Provisional
900-1027 2.04e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 48.55  E-value: 2.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQQQ 974
Cdd:PRK12705    33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEkldnlENQLEEREK 112
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039729385  975 KLAAEEKARQEAEERRKQE-EEAAKLALEEATKL--------AQEQIRQKAALDKH-LHFHQE 1027
Cdd:PRK12705   113 ALSARELELEELEKQLDNElYRVAGLTPEQARKLllklldaeLEEEKAQRVKKIEEeADLEAE 175
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
843-1020 2.57e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.43  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  843 EQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQL--QAARERARQQQEEL 920
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdyLKLNEERIDLLQEL 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  921 RRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 1000
Cdd:pfam02463  246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
                          170       180
                   ....*....|....*....|
gi 1039729385 1001 LEEATKLAQEQIRQKAALDK 1020
Cdd:pfam02463  326 AEKELKKEKEEIEELEKELK 345
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
874-1022 3.32e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 47.69  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  874 QQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKqrqkelemQL 953
Cdd:pfam05262  204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDK--------QV 275
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729385  954 AEEQKRLMEMAEEE----RLEYQQQKLAAEEKARQEA---EERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1022
Cdd:pfam05262  276 AENQKREIEKAQIEikknDEEALKAKDHKAFDLKQESkasEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSL 351
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
821-1031 3.71e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.81  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  821 QQEKASRDRIRIEKAEmrwlKVEQRRREQEeltwlhKEQLEKaekmkeelelEQQRRTEENRLRKQRLEEERQQQEEAEK 900
Cdd:pfam17380  279 QHQKAVSERQQQEKFE----KMEQERLRQE------KEEKAR----------EVERRRKLEEAEKARQAEMDRQAAIYAE 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  901 KRRLQLQAARERARQQQEELRRKLQEI----------------------QRKKQQEAAERAEAEKQRQKELEMQ-LAEEQ 957
Cdd:pfam17380  339 QERMAMERERELERIRQEERKRELERIrqeeiameisrmrelerlqmerQQKNERVRQELEAARKVKILEEERQrKIQQQ 418
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729385  958 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 1031
Cdd:pfam17380  419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
814-1032 8.91e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.07  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  814 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 893
Cdd:pfam13868   35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK---RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  894 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEY 971
Cdd:pfam13868  112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiaRLRA 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039729385  972 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEAtKLAQEQIRQKAALDKHLHFHQELSKEA 1032
Cdd:pfam13868  192 QQEKAQDEKAERDELRAKLYQEEQERKERQKER-EEAEKKARQRQELQQAREEQIELKERR 251
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
789-1040 1.01e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.50  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  789 LSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV-EQRRREQEELTWLHKEQLEKAEKMK 867
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrKVDDEEKLKESEKEKKKAEKELKKE 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  868 EELELEQQRRTEENRLRKQRLEEERQQqeeaekkrrlqlqaarerARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQK 947
Cdd:pfam02463  334 KEEIEELEKELKELEIKREAEEEEEEE------------------LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  948 ELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEaAKLALEEATKLAQEQIRQKAALDKHLHFHQE 1027
Cdd:pfam02463  396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDELELKKSEDLL 474
                          250
                   ....*....|...
gi 1039729385 1028 LSKEASGLQWTQN 1040
Cdd:pfam02463  475 KETQLVKLQEQLE 487
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
922-996 1.02e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 44.26  E-value: 1.02e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729385  922 RKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQ-QQKLAAEEKARQEA---EERRKQEEEA 996
Cdd:pfam09756    1 KKLGAKKRAKLELKEA-----KRQQREAEEEEREEREKLEEKREEEYKEREeREEEAEKEKEEEERkqeEEQERKEQEE 74
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
905-1029 1.08e-04

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 46.59  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  905 QLQAARERAR----------QQQEELRRKLQEIQRKKQ----------QEAAERAEAEKQRQK----ELEM-QL-AEEQK 958
Cdd:PRK10929   124 QAQQEQDRAReisdslsqlpQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKalvdELELaQLsANNRQ 203
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729385  959 RLMEMAEE------ERLEYQQQKLaaeekaRQEAEERRKQEeeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELS 1029
Cdd:PRK10929   204 ELARLRSElakkrsQQLDAYLQAL------RNQLNSQRQRE---AERALESTELLAEQSGDLPKSIVAQFKINRELS 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
759-1040 1.12e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  759 HQGLLRSHSAAGQLSLELDALESQV-AIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQekasrdRIRIEKAEM 837
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ------QKQILRERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  838 RWLKVEQRRREqeeltwlhkEQLEKAEkmkeELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 917
Cdd:TIGR02168  312 ANLERQLEELE---------AQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  918 EELRRKLQEIQRKKQQEAAERAeaekqRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 997
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039729385  998 K--LALEEATKLAQEQIRQK-AALDKHLHFHQELSKEASGLQWTQN 1040
Cdd:TIGR02168  454 EelERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQE 499
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
911-1014 1.12e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.49  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  911 ERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERR 990
Cdd:pfam05672   10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE 89
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039729385  991 -----------KQEEEAAKLALEEATKLAQEQIRQ 1014
Cdd:pfam05672   90 qreqeeqerlqKQKEEAEAKAREEAERQRQEREKI 124
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
683-1017 1.14e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  683 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELtpkKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTshQGL 762
Cdd:COG1196    448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL---LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL--RGL 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  763 LRSHSAAGQLSLELDALEsQVAIDGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMR 838
Cdd:COG1196    523 AGAVAVLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAV 601
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  839 WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLR-KQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 917
Cdd:COG1196    602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLReVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  918 EELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 997
Cdd:COG1196    682 EELAERLAEEELELEE---------ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
                          330       340
                   ....*....|....*....|
gi 1039729385  998 KLALEEATKLAQEQIRQKAA 1017
Cdd:COG1196    753 LEELPEPPDLEELERELERL 772
Macoilin pfam09726
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ...
900-1031 1.17e-04

Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.


Pssm-ID: 462859 [Multi-domain]  Cd Length: 670  Bit Score: 46.00  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARerarQQQEELRRKL-----------QEIQRKKQ-----QEAAERAEAEKQRQKE--------------- 948
Cdd:pfam09726  405 KKLKAELQASR----QTEQELRSQIssltslerslkSELGQLRQendllQTKLHNAVSAKQKDKQtvqqlekrlkaeqea 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  949 ---LEMQLAEEQKRLMEmaEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFH 1025
Cdd:pfam09726  481 rasAEKQLAEEKKRKKE--EEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKY 558

                   ....*.
gi 1039729385 1026 QELSKE 1031
Cdd:pfam09726  559 KESEKD 564
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
771-1005 1.46e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQVaidgrLSSIQATDVASDMECEEERSHEDPSKaLQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQE 850
Cdd:pfam02463  268 AQVLKENKEEEKE-----KKLQEEELKLLAKEEEELKSELLKLE-RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  851 ELTWLHKEQLEKAEKMKEEleLEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR----ERARQQQEELRRKLQE 926
Cdd:pfam02463  342 KELKELEIKREAEEEEEEE--LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkseeEKEAQLLLELARQLED 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  927 IQRKKQQEAAERAEAEKQRQKELEMQLAEEQ-KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 1005
Cdd:pfam02463  420 LLKEEKKEELEILEEEEESIELKQGKLTEEKeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
802-1032 1.53e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 46.12  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  802 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEEN 881
Cdd:pfam02463  195 LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  882 RLRKQRLEEERQQQEEAEKKRRlQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQ--KELE 950
Cdd:pfam02463  275 KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERRKVDDEEKLKESEKekkkaekelKKEKEEIEELEKELKELeiKREA 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  951 MQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRkqEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 1030
Cdd:pfam02463  354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431

                   ..
gi 1039729385 1031 EA 1032
Cdd:pfam02463  432 LE 433
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
819-1043 1.54e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.98  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  819 KKQQEKASRDRIRIEKAEMRWLK-----VEQRRREQEELTwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 893
Cdd:pfam12128  311 SAADAAVAKDRSELEALEDQHGAfldadIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  894 QQEEAEKKRRlqlQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQ 972
Cdd:pfam12128  390 RDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQL 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  973 QQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT-KLAQEQIR---QKAALDKHLH--------FHQELSKEASG 1034
Cdd:pfam12128  467 ENFDERIERAREEQEAANAEverlqsELRQARKRRDQASeALRQASRRleeRQSALDELELqlfpqagtLLHFLRKEAPD 546

                   ....*....
gi 1039729385 1035 lqWTQNISR 1043
Cdd:pfam12128  547 --WEQSIGK 553
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
943-1017 2.11e-04

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 42.42  E-value: 2.11e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729385  943 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:cd06503     43 EKAKEEAEELLAEYEEKLAEAraeAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
817-1008 2.17e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.34  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  817 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 896
Cdd:TIGR00618  208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH--AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  897 EAEKKRRLQL---QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQkrLMEMAEEERLEYQQ 973
Cdd:TIGR00618  286 INRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--LHSQEIHIRDAHEV 363
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1039729385  974 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLA 1008
Cdd:TIGR00618  364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
901-999 2.25e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.83  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  901 KRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyqQQKLAAEE 980
Cdd:pfam20492   13 ERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLE--AELAEAQE 90
                           90
                   ....*....|....*....
gi 1039729385  981 KARQEAEERRKQEEEAAKL 999
Cdd:pfam20492   91 EIARLEEEVERKEEEARRL 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
823-1036 2.26e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  823 EKASRDRIRIEKAEMRWLK-----VEQRRREQEELTWL--HKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQ 895
Cdd:COG4913    220 EPDTFEAADALVEHFDDLEraheaLEDAREQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  896 EEAEKKRrlqLQAARERARQQQEELRRKLQEIQRKKQQEAAeraeaekQRQKELEMQLAEEQKRLMEmAEEERLEYQQQK 975
Cdd:COG4913    300 LRAELAR---LEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLEREIERLERELEE-RERRRARLEALL 368
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039729385  976 LAAEEKARQEAEE--RRKQEEEAAKLALEEATKLAQEQIRQ-KAALDKHLHFHQELSKEASGLQ 1036
Cdd:COG4913    369 AALGLPLPASAEEfaALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
766-1022 3.15e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 3.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  766 HSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECE--EERSHEDPSKALQDKKQQEKasrDRIRIEKAEMRWLKVE 843
Cdd:TIGR00618  416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEklEKIHLQESAQSLKEREQQLQ---TKEQIHLQETRKKAVV 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  844 -QRRREQEELTWLHKEQLekaekMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 922
Cdd:TIGR00618  493 lARLLELQEEPCPLCGSC-----IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  923 KLQEIQRKKQQEAAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEA-AKLA 1000
Cdd:TIGR00618  568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlKLTA 647
                          250       260
                   ....*....|....*....|...
gi 1039729385 1001 LE-EATKLAQEQIRQKAALDKHL 1022
Cdd:TIGR00618  648 LHaLQLTLTQERVREHALSIRVL 670
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
907-1032 3.84e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRKLQEIQRKK--QQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQ 984
Cdd:pfam13868   19 KCNKERDAQIAEKKRIKAEEKEEERrlDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039729385  985 EAEERRK-------QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1032
Cdd:pfam13868   99 EREQMDEiveriqeEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE 153
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
900-1017 4.66e-04

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 43.87  E-value: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAE 979
Cdd:COG3064     44 LAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAE 123
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1039729385  980 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:COG3064    124 EAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
943-1017 5.18e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 41.70  E-value: 5.18e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039729385  943 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:COG0711     44 ERAKEEAEAALAEYEEKLAEAraeAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVA 121
PRK11637 PRK11637
AmiB activator; Provisional
894-998 5.24e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 43.91  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  894 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQ 972
Cdd:PRK11637   170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE-QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELrANESRLRDS 248
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1039729385  973 QQKLAAEEKARQEAEER-----RKQEEEAAK 998
Cdd:PRK11637   249 IARAEREAKARAEREAReaarvRDKQKQAKR 279
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
804-1036 7.79e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 7.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEdpsKALQ-DKKQQEKASRDRIRIEKAEMrwlkVEQRRREQEELTWLHK--EQLEKAEKMKEELELEQQRRTEE 880
Cdd:TIGR02168  220 AELRELE---LALLvLRLEELREELEELQEELKEA----EEELEELTAELQELEEklEELRLEVSELEEEIEELQKELYA 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  881 NRLRKQRLEEERqqqeEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKqqeaaeraeaeKQRQKELEmQLAEEQKRL 960
Cdd:TIGR02168  293 LANEISRLEQQK----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----------AELEEKLE-ELKEELESL 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  961 MEMAEEERLEYQQQklaaeEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL----DKHLHFHQELSKEASGLQ 1036
Cdd:TIGR02168  357 EAELEELEAELEEL-----ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerleDRRERLQQEIEELLKKLE 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
682-1016 7.92e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 7.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  682 HQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQG 761
Cdd:COG1196    419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  762 LLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEE----------RSHEDPSKALQDKKQQEKASRDRIR 831
Cdd:COG1196    499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLP 578
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  832 IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARE 911
Cdd:COG1196    579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  912 RARQQQEELRRKLQEIQRKKQQEAAE--RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEER 989
Cdd:COG1196    659 GGSLTGGSRRELLAALLEAEAELEELaeRLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
                          330       340
                   ....*....|....*....|....*..
gi 1039729385  990 RKQEEEAAKLALEEATKLAQEQIRQKA 1016
Cdd:COG1196    739 EELLEEEELLEEEALEELPEPPDLEEL 765
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
783-1045 9.18e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 42.91  E-value: 9.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  783 VAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKA-SRDRIRIEKAEMRwLKVEQRRREQEELTWLHKEQLE 861
Cdd:TIGR02794   41 VLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQrAAEQARQKELEQR-AAAEKAAKQAEQAAKQAEEKQK 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  862 KAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQqeaaeraea 941
Cdd:TIGR02794  120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK--------- 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  942 ekqrqkelemqlAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKqeeeAAKLALEEATKLAQEQIRQKAALDKH 1021
Cdd:TIGR02794  191 ------------AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK----ADEAELGDIFGLASGSNAEKQGGARG 254
                          250       260
                   ....*....|....*....|....*.
gi 1039729385 1022 LHFHQELSKEASGLQWT--QNISRPW 1045
Cdd:TIGR02794  255 AAAGSEVDKYAAIIQQAiqQNLYDDP 280
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
918-1020 1.01e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.15  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  918 EELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEaa 997
Cdd:COG0542    414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEAL--KARWEAEKELIEEIQELKEELEQRYGKIPE-- 489
                           90       100
                   ....*....|....*....|...
gi 1039729385  998 klaLEEATKLAQEQIRQKAALDK 1020
Cdd:COG0542    490 ---LEKELAELEEELAELAPLLR 509
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
801-1015 1.04e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  801 MECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRwLKVEQRRREQEELTWLHKEQLEKaekmkeelelEQQRRTEE 880
Cdd:pfam13868   82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAE-EKLEKQRQLREEIDEFNEEQAEW----------KELEKEEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  881 NRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQeELRRKLQEIQRKKQQE----AAERAEAEKQRQKELEMQLAEE 956
Cdd:pfam13868  151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIA-RLRAQQEKAQDEKAERdelrAKLYQEEQERKERQKEREEAEK 229
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039729385  957 QKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQK 1015
Cdd:pfam13868  230 KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
771-1020 1.12e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQ-VAIDGRLSSIQATDVasdmECEEERshEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVE----QR 845
Cdd:TIGR02168  751 QLSKELTELEAEiEELEERLEEAEEELA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRE 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  846 RREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQ 925
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  926 EIQRKKQQEAAERAeaeKQRQK---------ELEMQLAEEQKRLMEMAEEErLEYQQQKLAAEEKARQEAEERRKQEEEA 996
Cdd:TIGR02168  905 ELESKRSELRRELE---ELREKlaqlelrleGLEVRIDNLQERLSEEYSLT-LEEAEALENKIEDDEEEARRRLKRLENK 980
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1039729385  997 AK-------LALEEATKLAQEQI---RQKAALDK 1020
Cdd:TIGR02168  981 IKelgpvnlAAIEEYEELKERYDfltAQKEDLTE 1014
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
900-1036 1.13e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQrKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM---------------- 963
Cdd:COG4942     47 KKEEKALLKQLAALERRIAALARRIRALE-QELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplall 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  964 ---------------------AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1022
Cdd:COG4942    126 lspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
                          170
                   ....*....|....
gi 1039729385 1023 HFHQELSKEASGLQ 1036
Cdd:COG4942    206 KELAELAAELAELQ 219
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
900-1020 1.25e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 40.54  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeAEKQRQKELEMQLAEEQKRLMEMAEEErleyqqqklAAE 979
Cdd:COG0711     44 ERAKEEAEAALAEYEEKLAEARAEAAEIIAEARK-------EAEAIAEEAKAEAEAEAERIIAQAEAE---------IEQ 107
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039729385  980 EKARQEAEERrkqeEEAAKLALEEATKLAQEQI---RQKAALDK 1020
Cdd:COG0711    108 ERAKALAELR----AEVADLAVAIAEKILGKELdaaAQAALVDR 147
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
905-1033 1.26e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  905 QLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ------RQKELEMQLAEEQKRLMEmAEEERLEYQQQkLAA 978
Cdd:TIGR02168  695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarleaEVEQLEERIAQLSKELTE-LEAEIEELEER-LEE 772
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039729385  979 EEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL-DKHLHFHQELSKEAS 1033
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLES 828
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
900-1001 1.27e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAA 978
Cdd:COG4942    156 RADLAELAALRAELEAERAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
                           90       100
                   ....*....|....*....|...
gi 1039729385  979 EEKARQEAEERRKQEEEAAKLAL 1001
Cdd:COG4942    235 EAAAAAERTPAAGFAALKGKLPW 257
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
900-1015 1.47e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAE-EERLEYQQQKLAA 978
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIEN 755
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1039729385  979 EEKARQEAEER-RKQEEEAAKLALEEAT---KLAQEQIRQK 1015
Cdd:TIGR02169  756 VKSELKELEARiEELEEDLHKLEEALNDleaRLSHSRIPEI 796
PTZ00121 PTZ00121
MAEBL; Provisional
683-1033 1.59e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  683 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKE------RNMEMAAGLSKS---DITNSKE 753
Cdd:PTZ00121  1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalRKAEEAKKAEEArieEVMKLYE 1602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  754 AGGTSHQGLLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDV--ASDMECEEE----RSHEDPSKALQDKKQQEKASR 827
Cdd:PTZ00121  1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKK 1682
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  828 DRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAekmkeelelEQQRRTEENRLRKQRleeerqqqeeaekkrrlQLQ 907
Cdd:PTZ00121  1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA---------EELKKAEEENKIKAE-----------------EAK 1736
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  908 AARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKR---LMEMAEEERLEYQQQKLAAEEKARQ 984
Cdd:PTZ00121  1737 KEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEedeKRRMEVDKKIKDIFDNFANIIEGGK 1815
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1039729385  985 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEAS 1033
Cdd:PTZ00121  1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDG 1864
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
805-1031 1.84e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  805 EERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRLR 884
Cdd:TIGR00618  275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS--RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  885 KQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMA 964
Cdd:TIGR00618  353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  965 EEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ-EQIRQKAALDK--HLHFHQELSKE 1031
Cdd:TIGR00618  433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETRKKavVLARLLELQEE 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
771-1036 1.88e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  771 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQ 849
Cdd:TIGR02169  748 SLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  850 EELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEK---KRRLQLQAARERARQQQEELRRKLQE 926
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEE 907
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  927 IQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEaeerrKQEEEAAKLALEEAT 1005
Cdd:TIGR02169  908 LEAQIEK--------KRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAE-----LQRVEEEIRALEPVN 974
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1039729385 1006 KLA-QEQIRQKAALDKHLHFHQELSKEASGLQ 1036
Cdd:TIGR02169  975 MLAiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
900-1006 2.05e-03

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 41.51  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQE--------ELRRKLQEiQRKKQqeaaeraeaekQRQKELEMQLAEEQKRLMEMAEEERLEY 971
Cdd:pfam07767  209 KKRLKEEEKLERVLEKIAEsaataearEEKRKTKA-QRNKE-----------KRRKEEEREAKEEKALKKKLAQLERLKE 276
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1039729385  972 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 1006
Cdd:pfam07767  277 IAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
900-1006 2.17e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-----QKELEMQ------LAEEQKRLMEMAE--- 965
Cdd:COG1579     44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealQKEIESLkrrisdLEDEILELMERIEele 123
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039729385  966 ------EERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 1006
Cdd:COG1579    124 eelaelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
819-1015 2.80e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  819 KKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEA 898
Cdd:PRK03918   227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  899 EKKRRLQLQAarERARQQQEELRRKLQEIQRKkqqeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLeYQQQKLAA 978
Cdd:PRK03918   307 DELREIEKRL--SRLEEEINGIEERIKELEEK------------EERLEELKKKLKELEKRLEELEERHEL-YEEAKAKK 371
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039729385  979 EEKARQEAEERRKQEEEAAKLaLEEATKlAQEQIRQK 1015
Cdd:PRK03918   372 EELERLKKRLTGLTPEKLEKE-LEELEK-AKEEIEEE 406
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
900-1011 2.85e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.74  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAAR-ERARQQQEELRRKLQEIQRK-KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKla 977
Cdd:PRK00409   528 LERELEQKAEEaEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-- 605
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1039729385  978 aeekaRQEAEERRKQEEEAAKLALEEATKLAQEQ 1011
Cdd:PRK00409   606 -----AHELIEARKRLNKANEKKEKKKKKQKEKQ 634
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
910-1017 3.35e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.36  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  910 RERARQQQEELRRKLQEIQRKKQQEAAERaeaekQRQKELEMQLAEEQKRLMEmaEEERLEYQQQKL-----AAEEKARQ 984
Cdd:pfam20492    1 REEAEREKQELEERLKQYEEETKKAQEEL-----EESEETAEELEEERRQAEE--EAERLEQKRQEAeeekeRLEESAEM 73
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039729385  985 EAEERRKQEEEAAklALEEATKLAQEQIRQKAA 1017
Cdd:pfam20492   74 EAEEKEQLEAELA--EAQEEIARLEEEVERKEE 104
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
804-1027 3.91e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  804 EEERSHEDPSKALQDKKQQEKAS-RDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQqrrTEENR 882
Cdd:pfam05557    3 ELIESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ---AELNR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  883 LRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRLME 962
Cdd:pfam05557   80 LKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELE------LQSTNSELEELQERLDLLKAKAS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729385  963 MAEE--ERLEYQQQKLAAEEKARQEAEERRKQEEEAAklaleEATKLAQEQIRQKAALDKHLHFHQE 1027
Cdd:pfam05557  150 EAEQlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS-----EIVKNSKSELARIPELEKELERLRE 211
fliH PRK06669
flagellar assembly protein H; Validated
916-1032 4.21e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 40.38  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  916 QQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEE 995
Cdd:PRK06669    31 SIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEE 110
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1039729385  996 AAKLALEEATKLAQEQIRQKaALDKHLHFHQELSKEA 1032
Cdd:PRK06669   111 ELERLIEEAKAEGYEEGYEK-GREEGLEEVRELIEQL 146
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
907-1017 4.30e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.79  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRKLQEIQRK-----KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEK 981
Cdd:COG3064     11 EAAAQERLEQAEAEKRAAAEAEQKakeeaEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAE 90
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039729385  982 ARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1017
Cdd:COG3064     91 KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK 126
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
904-1018 4.58e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 40.25  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  904 LQLQAARERA-RQQQEELRRKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLaaEEKA 982
Cdd:cd16269    176 LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAA-----EQERKLLEEQQRELEQKLEDQ--ERSYEEHLRQL--KEKM 246
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1039729385  983 RQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 1018
Cdd:cd16269    247 EEERENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
907-1014 4.60e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQ--KELEMQLAEEQKRLmemaeEERLEYQQQKlaAEEKARQ 984
Cdd:PRK11448   141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValEGLAAELEEKQQEL-----EAQLEQLQEK--AAETSQE 213
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039729385  985 EAEERRKQEEEAAK-LALEEAT--KLAQEQIRQ 1014
Cdd:PRK11448   214 RKQKRKEITDQAAKrLELSEEEtrILIDQQLRK 246
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
900-1022 5.15e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 5.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  900 KKRRLQLQAARERARQQQEELRRKLQEIQ--------RKKQQEAAERAEAEKQRQKELEMQ------LAEEQKRLMEMAE 965
Cdd:COG1579     41 AALEARLEAAKTELEDLEKEIKRLELEIEevearikkYEEQLGNVRNNKEYEALQKEIESLkrrisdLEDEILELMERIE 120
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039729385  966 EERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAALDKHL 1022
Cdd:COG1579    121 ELEEELAELEAELAELEAELEEKKAELDEELAELE-AELEELEAEREELAAKIPPEL 176
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
907-1002 5.23e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.96  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEqkrlMEMaEEERLEYQQQKLAAEEKARQEA 986
Cdd:pfam02841  210 RAKAEAAEAEQELLREKQKEEEQMMEAQ--------ERSYQEHVKQLIEK----MEA-EREQLLAEQERMLEHKLQEQEE 276
                           90
                   ....*....|....*.
gi 1039729385  987 EERRKQEEEAAKLALE 1002
Cdd:pfam02841  277 LLKEGFKTEAESLQKE 292
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
907-995 5.87e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.87  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  907 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM---QLAEEQKRLMEmaeeerLEYQQQKLAAEEKAR 983
Cdd:cd16269    204 RAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEereNLLKEQERALE------SKLKEQEALLEEGFK 277
                           90
                   ....*....|..
gi 1039729385  984 QEAEERRKQEEE 995
Cdd:cd16269    278 EQAELLQEEIRS 289
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
841-1016 7.54e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 7.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  841 KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEaekKRRLQLQAARER-------- 912
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAELEAELERldassddl 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  913 --ARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQkelemQLAEEQKRLMEMAEE-ERLEYQQQKLAAEEKARQEAEER 989
Cdd:COG4913    688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDA 762
                          170       180
                   ....*....|....*....|....*..
gi 1039729385  990 RkqeEEAAKLALEEATKLAQEQIRQKA 1016
Cdd:COG4913    763 V---ERELRENLEERIDALRARLNRAE 786
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
920-1017 7.77e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 37.68  E-value: 7.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  920 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQQQKLAAE--EKARQEAEERRKQEEEA 996
Cdd:pfam00430   20 AWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEaRAEAQEIIENAKKRAEKlkEEIVAAAEAEAERIIEQ 99
                           90       100
                   ....*....|....*....|.
gi 1039729385  997 AKLALEEATKLAQEQIRQKAA 1017
Cdd:pfam00430  100 AAAEIEQEKDRALAELRQQVV 120
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
943-1019 7.91e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 37.80  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  943 KQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAaeeKARQEAEERRKQEEEAAKLALEEATKLAQ---EQIRQKAALD 1019
Cdd:cd06503     29 DEREEKIAESLEEAEKAKEEA--EELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKeeaERILEQAKAE 103
RIB43A pfam05914
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ...
825-1022 9.50e-03

RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.


Pssm-ID: 461780 [Multi-domain]  Cd Length: 372  Bit Score: 39.49  E-value: 9.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  825 ASRDRIRIEKAEMR-WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEerqqqeeaekKRR 903
Cdd:pfam05914  141 NREERKKLQQEQMReWLEQQIEEKKQAEEEEKHAELLYDQKRLERDRRALELAKLEEECRRAVNAAT----------KNF 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039729385  904 LQLQAARERARQQQEELRR---KLQEIQ---------RKKQQEAAER--------------AEAEKQRQKELEMQLAEEQ 957
Cdd:pfam05914  211 NQALAAEQAERRRLEKRQEqedNLAEIYnhltsdlltENPEVAQSSLgphrvipdrwkgmsPEQLKEIRKEQEQQREEKE 290
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039729385  958 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAALDKHL 1022
Cdd:pfam05914  291 RRREEEKQRDAEWDRQRLELARAALLLEREQQRLRRELRRQLD-EENLQLAQEQKARQEYLNKEV 354
 
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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