NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|966984660|ref|XP_014969465|]
View 

inner centromere protein isoform X4 [Macaca mulatta]

Protein Classification

INCENP ARK-binding domain-containing protein( domain architecture ID 10573525)

inner centromere protein (INCENP) aurora-related kinase (ARK)-binding domain-containing protein, similar to Saccharomyces cerevisiae INCENP-related protein SLI15 that is required for high-fidelity chromosome segregation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
INCENP_N pfam12178
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ...
6-41 5.94e-17

Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.


:

Pssm-ID: 463484 [Multi-domain]  Cd Length: 36  Bit Score: 75.04  E-value: 5.94e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966984660    6 PGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEA 41
Cdd:pfam12178   1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
801-855 3.01e-15

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


:

Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 3.01e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966984660  801 NSDDSTDDEAHPRKPIPNWARGTPLSQAIIHQYyhPPNLLELFGAILPLDLEDIF 855
Cdd:pfam03941   1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
PTZ00121 super family cl31754
MAEBL; Provisional
529-756 2.80e-13

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEK 606
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKK 1648
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  607 AKEERlaeekakKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKA-AEAKRLAEQR 682
Cdd:PTZ00121 1649 AEELK-------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkaEELKKKeAEEKKKAEEL 1721
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966984660  683 EQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
Agg_substance super family cl41491
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
403-609 3.40e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


The actual alignment was detected with superfamily member NF033875:

Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 41.23  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  403 DTEIGNST-----PNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAvseldeeqhledeelqpprSKTP 477
Cdd:NF033875   47 DTQPGTTTvqpdnPDPQSGSETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGAEQS-------------------SATP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  478 SSpcpSSKVVRPLRTFLHTVQRNqmlmtPTSAPRSVMKSFikrNTPLRVDPKEKERQRLENLRRKEEAEQLRRqKVEEDK 557
Cdd:NF033875  108 ND---TTNAQQPTVGAEKSAQEQ-----PVVSPETTNEPL---GQPTEVAPAENEANKSTSIPKEFETPDVDK-AVDEAK 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  558 RRRLEEVKLKREERLRKV----LQARER-VEQMKEEKKKQIEQKFAQIDEKTEK-AKE 609
Cdd:NF033875  176 KDPNITVVEKPAEDLGNVsskdLAAKEKeVDQLQKEQAKKIAQQAAELKAKNEKiAKE 233
 
Name Accession Description Interval E-value
INCENP_N pfam12178
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ...
6-41 5.94e-17

Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.


Pssm-ID: 463484 [Multi-domain]  Cd Length: 36  Bit Score: 75.04  E-value: 5.94e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966984660    6 PGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEA 41
Cdd:pfam12178   1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
801-855 3.01e-15

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 3.01e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966984660  801 NSDDSTDDEAHPRKPIPNWARGTPLSQAIIHQYyhPPNLLELFGAILPLDLEDIF 855
Cdd:pfam03941   1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
PTZ00121 PTZ00121
MAEBL; Provisional
529-756 2.80e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEK 606
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKK 1648
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  607 AKEERlaeekakKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKA-AEAKRLAEQR 682
Cdd:PTZ00121 1649 AEELK-------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkaEELKKKeAEEKKKAEEL 1721
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966984660  683 EQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
530-758 5.38e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 530 EKERQRLENLRRKEEAEQLRRQKVEEDKrRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 609
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 610 ERlaeekaKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQ 689
Cdd:COG1196  349 AE------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966984660 690 ERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAA 758
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
529-756 8.53e-09

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: 59.37  E-value: 8.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQK--VEEDKRRRLEEVKLKRE---ERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEK 603
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEiaMEISRMRELERLQMERQqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  604 TEKAKEERlaeekakkkaaakkmeEVEARRKQEEEARRLRWLQQEEEERRHQelLQKKKEEEQERLRKAAEAKRLAEQRE 683
Cdd:pfam17380 426 RAEQEEAR----------------QREVRRLEEERAREMERVRLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRK 487
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  684 QERREQERQLAEQERRREQERLQAER-------ELQEREKALRLQKERLQREleekKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAMIEEERkrkllekEMEERQKAIYEEERRREAE----EERRKQQEMEERRRIQEQMRKATE 563
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
530-761 1.83e-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: 51.98  E-value: 1.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   530 EKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEqkfaQIDEKTEKAKE 609
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE----ALDELRAELTL 814
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   610 ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEL-LQKKKEEEQERLRKAAEAKRLAEQREQERRE 688
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRS 894
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966984660   689 QERQLAEQERRREQERLQAERELQEREKAL---RLQKERLQRELeekkkKEEQQRLAERQLQEEQEKKAKEAAGVS 761
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLaqlELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIED 965
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
427-638 2.13e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 42.01  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  427 QQEAKTDQADGPRepPQSarRKRSYKQAVSEldEEQHLEDEELQPPR-----------SKTPSSPCPSSKVVRPLRTFLH 495
Cdd:NF033875   49 QPGTTTVQPDNPD--PQS--GSETPKTAVSE--EATVQKDTTSQPTKveevasekngaEQSSATPNDTTNAQQPTVGAEK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  496 TVQRNqmlmtPTSAPRSVMKSFikrNTPLRVDPKEKERQRLENLRRKEEAEQLRRqKVEEDKRRRLEEVKLKREERLRKV 575
Cdd:NF033875  123 SAQEQ-----PVVSPETTNEPL---GQPTEVAPAENEANKSTSIPKEFETPDVDK-AVDEAKKDPNITVVEKPAEDLGNV 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  576 ----LQARER-VEQMKEEKKKQIEQKFAQIDEKTEKAKEERlaeekakkkaaakkmEEVEARRKQEEE 638
Cdd:NF033875  194 sskdLAAKEKeVDQLQKEQAKKIAQQAAELKAKNEKIAKEN---------------AEIAAKNKAEKE 246
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
403-609 3.40e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 41.23  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  403 DTEIGNST-----PNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAvseldeeqhledeelqpprSKTP 477
Cdd:NF033875   47 DTQPGTTTvqpdnPDPQSGSETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGAEQS-------------------SATP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  478 SSpcpSSKVVRPLRTFLHTVQRNqmlmtPTSAPRSVMKSFikrNTPLRVDPKEKERQRLENLRRKEEAEQLRRqKVEEDK 557
Cdd:NF033875  108 ND---TTNAQQPTVGAEKSAQEQ-----PVVSPETTNEPL---GQPTEVAPAENEANKSTSIPKEFETPDVDK-AVDEAK 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  558 RRRLEEVKLKREERLRKV----LQARER-VEQMKEEKKKQIEQKFAQIDEKTEK-AKE 609
Cdd:NF033875  176 KDPNITVVEKPAEDLGNVsskdLAAKEKeVDQLQKEQAKKIAQQAAELKAKNEKiAKE 233
MPSS6 cd23673
mitochondrial 3' processome (MPsome) subunit 6; MPSS6 is a subunit of the mitochondrial 3' ...
496-562 5.50e-03

mitochondrial 3' processome (MPsome) subunit 6; MPSS6 is a subunit of the mitochondrial 3' processome (MPsome) which is involved in 3'-5' trimming of messenger RNA (mRNA) precursors, in U-tailing of ribosomal RNA (rRNA) and some mRNAs, and in 3'-5' trimming and U-tailing of guide RNAs (gRNAs), during kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode gRNAs involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastids species. MPsome subunits include KDSS1 3'-5' exonuclease, RET1 terminal uridyltransferase (TUTase), and several subunits of as yet undefined functions (MPSS1-MPSS6). The maxicircle and minicircle RNAs are transcribed as 3' extended precursors and processed by MPsome-dependent 3'-5' degradation, and in the case of rRNAs and gRNAs also 3' uridylated. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. The MPsome catalyzes the primary uridylation of about 800 nt gRNA precursor transcripts, their processive degradation to a mature size of 40-60 nt, and secondary U-tail addition. MPSS6 is predicted (AlphaFold) to contain a C-terminal oligonucleotide/oligosaccharide binding (OB) fold-like domain.


Pssm-ID: 467890  Cd Length: 243  Bit Score: 39.69  E-value: 5.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966984660 496 TVQRNQMLMTPTSAPRSVMKSFIKRNTPLRVDPKEKERQRLE-----NLRR-----KEEAEQLRRQKVEEDKRRRLE 562
Cdd:cd23673   10 TSVHSKQSETPSKVSSKDPFATVSTSVPSNSPSSEDAKIRLEeskqkRLQRqlkdvEEELAALKNESERKTAAVRSA 86
 
Name Accession Description Interval E-value
INCENP_N pfam12178
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ...
6-41 5.94e-17

Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.


Pssm-ID: 463484 [Multi-domain]  Cd Length: 36  Bit Score: 75.04  E-value: 5.94e-17
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 966984660    6 PGPIHLLELCDQKLMEFLCNMDNKDLVWLEEIQEEA 41
Cdd:pfam12178   1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
801-855 3.01e-15

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 70.69  E-value: 3.01e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966984660  801 NSDDSTDDEAHPRKPIPNWARGTPLSQAIIHQYyhPPNLLELFGAILPLDLEDIF 855
Cdd:pfam03941   1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
PTZ00121 PTZ00121
MAEBL; Provisional
529-756 2.80e-13

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 74.41  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEK 606
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKK 1648
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  607 AKEERlaeekakKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKA-AEAKRLAEQR 682
Cdd:PTZ00121 1649 AEELK-------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkaEELKKKeAEEKKKAEEL 1721
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966984660  683 EQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
PTZ00121 PTZ00121
MAEBL; Provisional
529-755 5.08e-12

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 70.17  E-value: 5.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVK----LKREERLRKVLQARERVEQMKEEKKKQIEQKFAQ 599
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKKAEEAKkadeaKKAEEKKkadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  600 IDEKTEKAKEERLaeekaKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKAAEAK 676
Cdd:PTZ00121 1585 EAKKAEEARIEEV-----MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEEN 1659
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966984660  677 RLAEQREQERREQERQLAEQERrreqerlQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAK 755
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAK-------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
530-758 5.38e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 530 EKERQRLENLRRKEEAEQLRRQKVEEDKrRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 609
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 610 ERlaeekaKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQ 689
Cdd:COG1196  349 AE------EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966984660 690 ERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAA 758
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
PTZ00121 PTZ00121
MAEBL; Provisional
529-757 1.99e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 1.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK---------EEKKKQIEQKFAQ 599
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaeaakaeAEAAADEAEAAEE 1364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  600 IDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKAAEAK 676
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadEAKKKAEEAK 1444
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  677 RLAEQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQK--ERLQRELEEKKKKEEQQRLAERQLQEEQEKKA 754
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKkaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524

                  ...
gi 966984660  755 KEA 757
Cdd:PTZ00121 1525 DEA 1527
PTZ00121 PTZ00121
MAEBL; Provisional
519-724 4.41e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  519 KRNTPLRVDPKEKERQRLENLRRKEE----AEQLRRqkvEEDKRRRLEEVKLKREERLRKVLQARERVEQMK----EEKK 590
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKK---AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaEEAK 1668
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  591 KQIEQKfaQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQErlR 670
Cdd:PTZ00121 1669 KAEEDK--KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK--K 1744
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966984660  671 KAAEAKRLAEQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKER 724
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
529-764 7.24e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 7.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfAQIDEKTEKAK 608
Cdd:COG1196  244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 609 EERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERRE 688
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966984660 689 QERQLAEQERRREQERLQAER-ELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKAL 764
Cdd:COG1196  403 EELEEAEEALLERLERLEEELeELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
PTZ00121 PTZ00121
MAEBL; Provisional
529-764 8.61e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.32  E-value: 8.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKR----RRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIdEKT 604
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKnmalRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EEL 1625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  605 EKAKEERlaeekakkkaaakkMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQER----LRKAAEAKRLAE 680
Cdd:PTZ00121 1626 KKAEEEK--------------KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaeeAKKAEEDEKKAA 1691
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  681 QREQERREQERQLAEQERRREQERLQAErELQEREKALRLQKERLQRELEEKKKKEEQQRLAE------RQLQEEQEKKA 754
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAE-ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEKKA 1770
                         250
                  ....*....|
gi 966984660  755 KEAAGVSKAL 764
Cdd:PTZ00121 1771 EEIRKEKEAV 1780
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
529-766 1.20e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 529 KEKERQRLENLRRKEEAEQLRRQK-VEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKA 607
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIaRLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 608 KEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRwlqQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERR 687
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966984660 688 EQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKALNV 766
Cdd:COG1196  438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
530-764 8.85e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.65  E-value: 8.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 530 EKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfaQIDEKTEKAKE 609
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI--ARLEERRRELE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 610 ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQ 689
Cdd:COG1196  316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966984660 690 ERQLAeqerrREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKAL 764
Cdd:COG1196  396 AELAA-----QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
PTZ00121 PTZ00121
MAEBL; Provisional
529-757 1.11e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRK-EEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK--------EEKKKQIEQKFAQ 599
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadeakkaEEAKKADEAKKAE 1531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  600 IDEKTE---KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQ--------EEEERRHQELLQKKKEEEQER 668
Cdd:PTZ00121 1532 EAKKADeakKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeeakkaeEARIEEVMKLYEEEKKMKAEE 1611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  669 LRKAAEAKRLAEQreqerreqerqLAEQERRREQERLQAERELQEREKALRLQKE----RLQRELEEKKKKEEQQRLAER 744
Cdd:PTZ00121 1612 AKKAEEAKIKAEE-----------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenKIKAAEEAKKAEEDKKKAEEA 1680
                         250
                  ....*....|...
gi 966984660  745 QLQEEQEKKAKEA 757
Cdd:PTZ00121 1681 KKAEEDEKKAAEA 1693
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
529-756 8.53e-09

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: 59.37  E-value: 8.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQK--VEEDKRRRLEEVKLKRE---ERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEK 603
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEiaMEISRMRELERLQMERQqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  604 TEKAKEERlaeekakkkaaakkmeEVEARRKQEEEARRLRWLQQEEEERRHQelLQKKKEEEQERLRKAAEAKRLAEQRE 683
Cdd:pfam17380 426 RAEQEEAR----------------QREVRRLEEERAREMERVRLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRK 487
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  684 QERREQERQLAEQERRREQERLQAER-------ELQEREKALRLQKERLQREleekKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAMIEEERkrkllekEMEERQKAIYEEERRREAE----EERRKQQEMEERRRIQEQMRKATE 563
PTZ00121 PTZ00121
MAEBL; Provisional
529-757 1.19e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREER----------LRKVLQARERVEQMKEEKKKQIEQKFA 598
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERnneeirkfeeARMAHFARRQAAIKAEEARKADELKKA 1286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  599 QIDEKTEKAKE-ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKR 677
Cdd:PTZ00121 1287 EEKKKADEAKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA 1366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  678 LAEQREQERREQERQLAEQERRREQERLQAERELQE-REKALRLQKerlqRELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdKKKADELKK----AAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442

                  .
gi 966984660  757 A 757
Cdd:PTZ00121 1443 A 1443
PTZ00121 PTZ00121
MAEBL; Provisional
529-763 1.26e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK---EEKKKQIEQKFAqiDEKTE 605
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadEAKKKAEEKKKA--DEAKK 1438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  606 KAKEERlaeEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKAAEAKRLAEQR 682
Cdd:PTZ00121 1439 KAEEAK---KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKkkaDEAKKAAEAKKKADEA 1515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  683 EQERREQERQLAEQERRREQErlQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERqlQEEQEKKAKEAAGVSK 762
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKA--DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED--KNMALRKAEEAKKAEE 1591

                  .
gi 966984660  763 A 763
Cdd:PTZ00121 1592 A 1592
PTZ00121 PTZ00121
MAEBL; Provisional
529-763 1.29e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEE-----AEQLRR---QKVEEDKRRRLEEVklKREERLRKVLQARERVEQMK-EEKKKQIEQKFAq 599
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEeakkkADEAKKaaeAKKKADEAKKAEEA--KKADEAKKAEEAKKADEAKKaEEKKKADELKKA- 1554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  600 idEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKAAEAK 676
Cdd:PTZ00121 1555 --EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEK 1632
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  677 RLAEQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKaKE 756
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK-KE 1711

                  ....*..
gi 966984660  757 AAGVSKA 763
Cdd:PTZ00121 1712 AEEKKKA 1718
PTZ00121 PTZ00121
MAEBL; Provisional
529-757 2.80e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAeqlrrQKVEEDKR----RRLEEVKlKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKT 604
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEA-----RKAEDAKKaeavKKAEEAK-KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA 1274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  605 EKA-KEERLAEEKAKKKAAAKkmeevearrKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERL----RKAAEAKRLA 679
Cdd:PTZ00121 1275 EEArKADELKKAEEKKKADEA---------KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAdaakKKAEEAKKAA 1345
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  680 EQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEA 757
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA 1423
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
520-764 3.14e-08

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: 57.67  E-value: 3.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   520 RNTPLRVDPKEKERQRLENLRRKEEAEQLRR-----QKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIE 594
Cdd:pfam02463  196 KLQELKLKEQAKKALEYYQLKEKLELEEEYLlyldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   595 QKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAE 674
Cdd:pfam02463  276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEE 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   675 AKRLAEQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQREleekkkkeeQQRLAERQLQEEQEKKA 754
Cdd:pfam02463  356 EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQL---------LLELARQLEDLLKEEKK 426
                          250
                   ....*....|
gi 966984660   755 KEAAGVSKAL 764
Cdd:pfam02463  427 EELEILEEEE 436
PTZ00121 PTZ00121
MAEBL; Provisional
537-757 3.23e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  537 ENLRRKEEAEQLRRQKVEEDkrRRLEEVKlKREERLRKVLQARERVEQMK-EEKKKQIEQKFAQIDEKTEKAKEERLAEE 615
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEA--RKAEEAK-KKAEDARKAEEARKAEDARKaEEARKAEDAKRVEIARKAEDARKAEEARK 1171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  616 KAKKKAAAKKMEEVEARRKQE----EEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKR---LAEQREQERRE 688
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEElrkaEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKdaeEAKKAEEERNN 1251
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966984660  689 QERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEA 757
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
PTZ00121 PTZ00121
MAEBL; Provisional
526-757 3.37e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.84  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  526 VDPKEKERQRLENLRRKEE---------AEQLRRQ---KVEE----DKRRRLEEVK----LKREERLRKVLQARERVEQM 585
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEirkfeearmAHFARRQaaiKAEEarkaDELKKAEEKKkadeAKKAEEKKKADEAKKKAEEA 1314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  586 K---------EEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQE 656
Cdd:PTZ00121 1315 KkadeakkkaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  657 LLQKKKEEEQ---ERLRKAAEAKRLAEQ-REQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQ-RELEE 731
Cdd:PTZ00121 1395 EAKKKAEEDKkkaDELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEaKKADE 1474
                         250       260
                  ....*....|....*....|....*...
gi 966984660  732 KKKKEEQQRLAE--RQLQEEQEKKAKEA 757
Cdd:PTZ00121 1475 AKKKAEEAKKADeaKKKAEEAKKKADEA 1502
PTZ00121 PTZ00121
MAEBL; Provisional
529-756 4.13e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.46  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRlEEVKLKREERlRKVLQARERVEQMK----EEKKKQIEQKFAqiDEKT 604
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-DAAKKKAEEK-KKADEAKKKAEEDKkkadELKKAAAAKKKA--DEAK 1424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  605 EKAKEERlaeEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ---ERLRKAAEAKRLAEQ 681
Cdd:PTZ00121 1425 KKAEEKK---KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkadEAKKKAEEAKKKADE 1501
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966984660  682 REQERREQERQLAEQERRREQERLQAeRELQEREKALRLQKERLQRElEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEA-KKAEEAKKADEAKKAEEKKK-ADELKKAEELKKAEEKKKAEEAKKAEE 1574
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
530-765 5.78e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 5.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 530 EKERQrLENLRRkeEAEQLRR-QKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 608
Cdd:COG1196  197 ELERQ-LEPLER--QAEKAERyRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 609 EERLAEEKakkkaaakkmeevEARRKQEEEArrlrwlqqeeeerrhqeLLQKKKEEEQERLRKAAEAKRLAEQREQERRE 688
Cdd:COG1196  274 LELEELEL-------------ELEEAQAEEY-----------------ELLAELARLEQDIARLEERRRELEERLEELEE 323
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966984660 689 QERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKALN 765
Cdd:COG1196  324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
529-764 6.74e-08

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: 56.52  E-value: 6.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQRLENLRRKEE--AEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEK 606
Cdd:pfam02463  168 KRKKKEALKKLIEETEnlAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   607 AKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRlrwLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQER 686
Cdd:pfam02463  248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660   687 REQErqlAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKAL 764
Cdd:pfam02463  325 KAEK---ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
PTZ00121 PTZ00121
MAEBL; Provisional
529-758 7.47e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 7.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEE---AEQLRR----QKVEEDKR----RRLEEVK----LKREERLRKVLQARERVEQMKEEKKKQI 593
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEvrkAEELRKaedaRKAEAARKaeeeRKAEEARkaedAKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  594 EQKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEE-----EARRLRWLQQEEEERRHQELLQKKKEEEQER 668
Cdd:PTZ00121 1251 NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakkaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKK 1330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  669 L----RKAAEAKRLAEQREQERREQERQLAEQERRREQERLQAERElQEREKALRLQKERLQRELEEKKKKEEQQRLAER 744
Cdd:PTZ00121 1331 AdaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA-KKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
                         250
                  ....*....|....
gi 966984660  745 QLQEEQEKKAKEAA 758
Cdd:PTZ00121 1410 LKKAAAAKKKADEA 1423
PTZ00121 PTZ00121
MAEBL; Provisional
518-675 1.00e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  518 IKRNTPLRVDPKEKERQRLENLRRKEEAEQLRR----QKVEEDKR-----RRLEEVKLKREERLRKVLQARERVEQMKee 588
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAaeeaKKAEEDKKkaeeaKKAEEDEKKAAEALKKEAEEAKKAEELK-- 1708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  589 KKKQIEQKFAqidEKTEKAKEERLAEEKakkkaaakkmeevEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQER 668
Cdd:PTZ00121 1709 KKEAEEKKKA---EELKKAEEENKIKAE-------------EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772

                  ....*..
gi 966984660  669 LRKAAEA 675
Cdd:PTZ00121 1773 IRKEKEA 1779
PTZ00121 PTZ00121
MAEBL; Provisional
530-756 2.11e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  530 EKERQRLENLRRKEEAEQLRRQ-KVEEDKRRRLEEVKLKREERlRKVLQARERVEQMK--EEKKKQIEQKfAQIDEKTEK 606
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEEA-KKADEAKKKAEEAKkaEEAKKKAEEA-KKADEAKKK 1478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  607 AKEERlAEEKAKKKAAAKKMEEVEARRKQEE--EARRLRWLQQEEEERRHQELLQKKKEEE---QERLRKAAEAKRlAEQ 681
Cdd:PTZ00121 1479 AEEAK-KADEAKKKAEEAKKKADEAKKAAEAkkKADEAKKAEEAKKADEAKKAEEAKKADEakkAEEKKKADELKK-AEE 1556
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966984660  682 REQERREQERQLAEQERRREQERLQAERELQEREKAlRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
PTZ00121 PTZ00121
MAEBL; Provisional
530-763 5.55e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 5.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  530 EKERQRLENLRRKEEAEQLRRQKVEEDKrrrlEEVKLKREERLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEkTEKA 607
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADE-LKKA 1413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  608 KEERLAEEKAKKKaaAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQ--ERLRKAAEAKRLAEQREQE 685
Cdd:PTZ00121 1414 AAAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKK 1491
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  686 RREQERQlAEQERRREQERLQAE--RELQEREKALRLQKERLQRElEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKA 763
Cdd:PTZ00121 1492 AEEAKKK-ADEAKKAAEAKKKADeaKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
PTZ00121 PTZ00121
MAEBL; Provisional
529-762 9.54e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 9.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEE---AEQLRR----QKVEEDKR----RRLEEVK----LKREERLRKVLQARERVEQMKEEKKKQI 593
Cdd:PTZ00121 1117 AEEAKKKAEDARKAEEarkAEDARKaeeaRKAEDAKRveiaRKAEDARkaeeARKAEDAKKAEAARKAEEVRKAEELRKA 1196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  594 EQkfAQIDEKTEKAKEERLAEEKAKKKAAAKKME--EVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLrK 671
Cdd:PTZ00121 1197 ED--ARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI-K 1273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  672 AAEAKRLAEQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQE 751
Cdd:PTZ00121 1274 AEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE 1353
                         250
                  ....*....|.
gi 966984660  752 KKAKEAAGVSK 762
Cdd:PTZ00121 1354 AAADEAEAAEE 1364
PTZ00121 PTZ00121
MAEBL; Provisional
530-757 1.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  530 EKERQRLENLRRKEEAEQLRRQKVEEDKRRrLEEVKL----KREERLRKVLQARERVEQMKEEKKKQIEQkfAQIDEKTE 605
Cdd:PTZ00121 1112 EEARKAEEAKKKAEDARKAEEARKAEDARK-AEEARKaedaKRVEIARKAEDARKAEEARKAEDAKKAEA--ARKAEEVR 1188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  606 KAKEERlaeekakkkaAAKKMEEVEARRKQEEEAR--RLRWLQQEEEERRHQELLQKKKEEEQErlRKAAEAKRLAEQRE 683
Cdd:PTZ00121 1189 KAEELR----------KAEDARKAEAARKAEEERKaeEARKAEDAKKAEAVKKAEEAKKDAEEA--KKAEEERNNEEIRK 1256
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  684 QERREQERQLAEQERRREQERLQAE--RELQEREKALRLQKERLQRELEEKKKKEEQQRLAE--RQLQEEQEKKAKEA 757
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADelKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADeaKKKAEEAKKKADAA 1334
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
530-761 1.83e-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: 51.98  E-value: 1.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   530 EKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEqkfaQIDEKTEKAKE 609
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE----ALDELRAELTL 814
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   610 ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEL-LQKKKEEEQERLRKAAEAKRLAEQREQERRE 688
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEeLEELIEELESELEALLNERASLEEALALLRS 894
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966984660   689 QERQLAEQERRREQERLQAERELQEREKAL---RLQKERLQRELeekkkKEEQQRLAERQLQEEQEKKAKEAAGVS 761
Cdd:TIGR02168  895 ELEELSEELRELESKRSELRRELEELREKLaqlELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIED 965
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
529-755 4.94e-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: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQK-----FAQIDEK 603
Cdd:pfam13868  59 EEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRqlreeIDEFNEE 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  604 TEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKE--EEQERLRkaaeAKRLAEQ 681
Cdd:pfam13868 139 QAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDekAERDELR----AKLYQEE 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966984660  682 REQERREQERQLAeQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAK 755
Cdd:pfam13868 215 QERKERQKEREEA-EKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
PTZ00121 PTZ00121
MAEBL; Provisional
529-757 5.05e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAeqlrRQKVEEDKR----------RRLEEVKLKREERLRKVLQARE--RVEQMK--EEKKKQIE 594
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEA----KKDAEEAKKaeeernneeiRKFEEARMAHFARRQAAIKAEEarKADELKkaEEKKKADE 1294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  595 QKFAQIDEKTEKAKE--ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKA 672
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  673 AEAKRLAEQREQERREQErqlAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEK 752
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKK---ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451

                  ....*
gi 966984660  753 KAKEA 757
Cdd:PTZ00121 1452 KAEEA 1456
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
446-769 1.53e-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: 48.81  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   446 RRKRSYKQAVSELDEEQHLEDEELqpprsktpsspcpsskvVRPLRTFLHTVQRNQMLMTPTSAPRSVMKSFIKRNTPLR 525
Cdd:pfam02463  198 QELKLKEQAKKALEYYQLKEKLEL-----------------EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEI 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   526 VDPKEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTE 605
Cdd:pfam02463  261 EKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   606 KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQE 685
Cdd:pfam02463  341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDL 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   686 RREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEqqRLAERQLQEEQEKKAKEAAGVSKALN 765
Cdd:pfam02463  421 LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED--LLKETQLVKLQEQLELLLSRQKLEER 498

                   ....
gi 966984660   766 VTVD 769
Cdd:pfam02463  499 SQKE 502
PRK12704 PRK12704
phosphodiesterase; Provisional
529-609 1.79e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 529 KEKERQ-RLENLRRKEEAEQLRRQKveEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKA 607
Cdd:PRK12704  56 KEALLEaKEEIHKLRNEFEKELRER--RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL 133

                 ..
gi 966984660 608 KE 609
Cdd:PRK12704 134 EE 135
PTZ00121 PTZ00121
MAEBL; Provisional
529-757 2.76e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVKlkREERLRKVLQARERVEQMKEEKKKQIEQkfAQIDEK 603
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEEARKAEDAKkaeaaRKAEEVR--KAEELRKAEDARKAEAARKAEEERKAEE--ARKAED 1222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  604 TEKAKEERLAEEKAKKKAAAKKMEEV---EARRKQE----------------EEARRLRWLQQEEEERRHQELLQKKKEE 664
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEErnnEEIRKFEearmahfarrqaaikaEEARKADELKKAEEKKKADEAKKAEEKK 1302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  665 EQERLRKAAEAKRLAEQREQERREQERQLAEQERRREQERLQAE-RELQEREKALRLQKERLQRELEEKKKKEEQQRLAE 743
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382
                         250
                  ....*....|....
gi 966984660  744 RQLQEEQEKKAKEA 757
Cdd:PTZ00121 1383 AKKKAEEKKKADEA 1396
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
427-711 2.78e-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: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  427 QQEAKTDQADGPREPPQSARRKRSYKQAVSELDEEQhLEDEELQPPRSKTPSSPCPSSKVVRPLRTFLHTVQRNQMLMTP 506
Cdd:pfam17380 319 EEAEKARQAEMDRQAAIYAEQERMAMERERELERIR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQE 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  507 TSAPRSVMKSFIKRNTPLRVDPKEKERQRLEnlrrKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVlqarERVEQMK 586
Cdd:pfam17380 398 LEAARKVKILEEERQRKIQQQKVEMEQIRAE----QEEARQREVRRLEEERAREMERVRLEEQERQQQV----ERLRQQE 469
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  587 EEKKKQieqkfaqideKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERrhqellQKKKEEEQ 666
Cdd:pfam17380 470 EERKRK----------KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER------QKAIYEEE 533
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 966984660  667 ERlRKAAEAKRLAEQREQERREQERQLAEQERRREQERLQAEREL 711
Cdd:pfam17380 534 RR-REAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
542-746 5.84e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 542 KEEAEQLRRQKveeDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIdEKTEKAKEERLAEEKAKKKA 621
Cdd:COG4717   52 EKEADELFKPQ---GRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-EAELEELREELEKLEKLLQL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 622 AAKKMEEVEARRKQEEEARRLRWLQQEEEERRHqeLLQKKKEEEQERLRKAAEAKRLAEQREQERREQERQLAEQERRRE 701
Cdd:COG4717  128 LPLYQELEALEAELAELPERLEELEERLEELRE--LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 966984660 702 QERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQL 746
Cdd:COG4717  206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
536-756 6.44e-05

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: 46.48  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  536 LENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEE 615
Cdd:pfam15709 325 LEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQE 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  616 KAKKKAAAKKMEEVEARRKQEEEARRlrwlqqeeeerrhqELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERQLAE 695
Cdd:pfam15709 405 EEERKQRLQLQAAQERARQQQEEFRR--------------KLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLME 470
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966984660  696 QERRREQERLQAERElqEREKALRLQKERLQREleekkkkEEQQRLAERQLQEEQEKKAKE 756
Cdd:pfam15709 471 MAEEERLEYQRQKQE--AEEKARLEAEERRQKE-------EEAARLALEEAMKQAQEQARQ 522
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
540-679 1.21e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.57  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 540 RRKEEaeqlRRQKVEEDKRRRLEEVKLKREERLRKVLQARErveQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEEKAKK 619
Cdd:PRK09510  75 KRAEE----QRKKKEQQQAEELQQKQAAEQERLKQLEKERL---AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 620 KAAAKKMEEVEARRKQEEEARRLrwlqQEEEERRHQELLQKKKEEEQERLRKAAEAKRLA 679
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKK----AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKA 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
524-771 1.58e-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: 45.82  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   524 LRVDPKEKERQRLEN----LRRKEEAEQLRRQKVEE------DKRRRLEEVKLKREERLRKVLQARERVEQMKE---EKK 590
Cdd:TIGR02168  232 LRLEELREELEELQEelkeAEEELEELTAELQELEEkleelrLEVSELEEEIEELQKELYALANEISRLEQQKQilrERL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   591 KQIEQKFAQID---EKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQE 667
Cdd:TIGR02168  312 ANLERQLEELEaqlEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   668 RLRKAAEAKRLAEQREQE---RREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAER 744
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLerlEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
                          250       260
                   ....*....|....*....|....*..
gi 966984660   745 QLQEEQEKKAKEAAGVSKALNVTVDVQ 771
Cdd:TIGR02168  472 EAEQALDAAERELAQLQARLDSLERLQ 498
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
524-642 1.73e-04

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: 45.33  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  524 LRVDPKEKERQRLENLRRKEeaeQLRRQKVEEDKRRRLEEVKLKREERLRKVLQ-ARERVEQMKEEKKKQIEQKFAQIDE 602
Cdd:pfam15709 391 LRKQRLEEERQRQEEEERKQ---RLQLQAAQERARQQQEEFRRKLQELQRKKQQeEAERAEAEKQRQKELEMQLAEEQKR 467
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 966984660  603 KTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRL 642
Cdd:pfam15709 468 LMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARL 507
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
529-755 2.11e-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: 45.35  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVK---LKREERLRKVLQARERVEQMKEEKKKQiEQKFAQIDEKTE 605
Cdd:pfam02463  691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVqeaQDKINEELKLLKQKIDEEEEEEEKSRL-KKEEKEEEKSEL 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   606 KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRwlqqeeeerrHQELLQKKKEEEQERLRKAAEAKRLAEQREQE 685
Cdd:pfam02463  770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALE----------EELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   686 RREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRlaERQLQEEQEKKAK 755
Cdd:pfam02463  840 LELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK--EKEEKKELEEESQ 907
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
529-760 2.66e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLeevklkrEERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 608
Cdd:COG1196  373 ELAEAEEELEELAEELLEALRAAAELAAQLEEL-------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 609 EERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERRE 688
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966984660 689 QERQLAEQERRREQERLQAERELQ----EREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGV 760
Cdd:COG1196  526 VAVLIGVEAAYEAALEAALAAALQnivvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAV 601
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
540-754 2.77e-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: 44.96  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   540 RRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKK-QIEQKFAQIDEKTEKAKEERLAEEKAK 618
Cdd:pfam02463  154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQaKKALEYYQLKEKLELEEEYLLYLDYLK 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   619 KKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERQLAEQER 698
Cdd:pfam02463  234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 966984660   699 RREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKA 754
Cdd:pfam02463  314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
519-676 3.97e-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: 43.68  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  519 KRNTPLRVDPKEKERQRLENLRRkeEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERveqmKEEKKKQIEQKFA 598
Cdd:TIGR02794  53 NRIQQQKKPAAKKEQERQKKLEQ--QAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQ----AEEKQKQAEEAKA 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  599 QiDEKTEKAKEErlaeekakkkAAAKKMEEVEARRKQEEEARrlrwlqqeeeerrHQELLQKKKEEEQERLRKAAEAK 676
Cdd:TIGR02794 127 K-QAAEAKAKAE----------AEAERKAKEEAAKQAEEEAK-------------AKAAAEAKKKAEEAKKKAEAEAK 180
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
541-763 4.03e-04

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 44.17  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 541 RKEEAEQLRRQKVE-EDKRRRLEEVKLKREERLRK------------VLQARERVEQMKEEKKKQIEQKFAQIDEKTEKA 607
Cdd:PRK05035 441 IEQEKKKAEEAKARfEARQARLEREKAAREARHKKaaearaakdkdaVAAALARVKAKKAAATQPIVIKAGARPDNSAVI 520
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 608 KEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRwlqqeEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERR 687
Cdd:PRK05035 521 AAREARKAQARARQAEKQAAAAADPKKAAVAAAIAR-----AKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 688 EQERQLAEQERRREQERLQAERELQ-EREKALRLQKERLQRELEEK---------------KKKEEQQRLAERQLQEEQE 751
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVdprkaavaaaiarakARKAAQQQANAEPEEAEDP 675
                        250
                 ....*....|..
gi 966984660 752 KKAKEAAGVSKA 763
Cdd:PRK05035 676 KKAAVAAAIARA 687
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
529-757 6.60e-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: 42.98  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFA---QIDEKTE 605
Cdd:pfam13868  29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQereQMDEIVE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  606 KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRK---AAEAKRLAEQR 682
Cdd:pfam13868 109 RIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEreeIEEEKEREIAR 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966984660  683 EQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEA 757
Cdd:pfam13868 189 LRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF 263
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
534-665 7.49e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 7.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 534 QRLENLRRkeEAEQlrrqkveedKRRRLEEvKLKREERLRKVLQAR-ERVEQMKEEKKKQIEQKFAQIdekTEKAKEERL 612
Cdd:PRK00409 523 ASLEELER--ELEQ---------KAEEAEA-LLKEAEKLKEELEEKkEKLQEEEDKLLEEAEKEAQQA---IKEAKKEAD 587
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966984660 613 AEEKAKKKAAAKKMEEVeaRRKQEEEARRLrwLQQEEEERRHQELLQKKKEEE 665
Cdd:PRK00409 588 EIIKELRQLQKGGYASV--KAHELIEARKR--LNKANEKKEKKKKKQKEKQEE 636
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
529-763 7.77e-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: 7.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK------EEKKKQIEQKFAQIDE 602
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSkeltelEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   603 KTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRwlQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQR 682
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   683 EQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQ------RELEEKKKKeeqqrlAERQLQEEQEKKAKE 756
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelseelRELESKRSE------LRRELEELREKLAQL 927

                   ....*..
gi 966984660   757 AAGVSKA 763
Cdd:TIGR02168  928 ELRLEGL 934
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
525-612 1.24e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 42.80  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  525 RVDPKEKERQRLE--NLRRKE-EAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQID 601
Cdd:PTZ00266  429 RVDKDHAERARIEkeNAHRKAlEMKILEKKRIERLEREERERLERERMERIERERLERERLERERLERDRLERDRLDRLE 508
                          90
                  ....*....|..
gi 966984660  602 -EKTEKAKEERL 612
Cdd:PTZ00266  509 rERVDRLERDRL 520
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
529-758 1.28e-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: 41.83  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVE-------EDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKK---QIEQKFA 598
Cdd:pfam13868  83 EEREQKRQEEYEEKLQEREQMDEIVEriqeedqAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREedeRILEYLK 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  599 QIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQK----KKEEEQERLRKAAE 674
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEReeaeKKARQRQELQQARE 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  675 AKrLAEQREQERREQERQLAEQERRREQERLQAERELQEREKAlRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKA 754
Cdd:pfam13868 243 EQ-IELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR-RMKRLEHRRELEKQIEEREEQRAAEREEELEEGERL 320

                  ....
gi 966984660  755 KEAA 758
Cdd:pfam13868 321 REEE 324
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
536-679 1.46e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.17  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 536 LENLRRKEEAEQLRRQKVEEDKRRRLEEVKLK---REERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEER- 611
Cdd:COG2268  186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAqanREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAe 265
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966984660 612 LAEEKAKKKAAAKKMEEVEARRKQEE----EARRLRWLQQEEEERRHQELLQKKKEEEQERLR-KAAEAKRLA 679
Cdd:COG2268  266 AAYEIAEANAEREVQRQLEIAEREREielqEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEaEAIRAKGLA 338
RNase_Y_N pfam12072
RNase Y N-terminal region;
542-609 1.48e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 40.64  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966984660  542 KEEAEQLRRQKVEEDKRRR-----LEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 609
Cdd:pfam12072  59 KEEIHKLRAEAERELKERRnelqrQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEE 131
PRK12704 PRK12704
phosphodiesterase; Provisional
543-676 1.49e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 543 EEAEQLRRQKVEEDKRrrleEVKLKREErlrKVLQARERVEQMKEEKKKQIEQKFAQID--EKTEKAKEERLAEEKAKKK 620
Cdd:PRK12704  34 KEAEEEAKRILEEAKK----EAEAIKKE---ALLEAKEEIHKLRNEFEKELRERRNELQklEKRLLQKEENLDRKLELLE 106
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966984660 621 aaakkmeeveaRRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAA-----EAK 676
Cdd:PRK12704 107 -----------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAK 156
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
518-765 1.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 518 IKRNTPLRVDPKEKERQRLENLRR------KEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKK 591
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEElikekeKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 592 qIEQKFAQIDEKTeKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLR-----WLQQEEEERRHQELLQKKKEEEQ 666
Cdd:PRK03918 250 -LEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSefyeeYLDELREIEKRLSRLEEEINGIE 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 667 ERLRKAAEAKRLAEQREQERREQERQLAEQERRREQerLQAERELQEREKALR-----LQKERLQRELEEKKKKEEQQRL 741
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAKEEIEE 405
                        250       260
                 ....*....|....*....|....
gi 966984660 742 AERQLQEEQEKKAKEAAGVSKALN 765
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIE 429
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
535-643 1.76e-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: 39.13  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  535 RLENLRRKEEAEQLRRQKVEEDKR-----RRLEEVKLKREERLRKVLQARERVEQmkeeKKKQIEQKFAQIDEKTEKAKE 609
Cdd:pfam20492   1 REEAEREKQELEERLKQYEEETKKaqeelEESEETAEELEEERRQAEEEAERLEQ----KRQEAEEEKERLEESAEMEAE 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 966984660  610 ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLR 643
Cdd:pfam20492  77 EKEQLEAELAEAQEEIARLEEEVERKEEEARRLQ 110
PRK12704 PRK12704
phosphodiesterase; Provisional
529-610 2.00e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 529 KEKERQ---RLENLRRKEEAEQLRRQKVE------EDKRRRLEEVKLKREERLRKVL-----QARERV-EQMKEEKKKQI 593
Cdd:PRK12704  92 LQKEENldrKLELLEKREEELEKKEKELEqkqqelEKKEEELEELIEEQLQELERISgltaeEAKEILlEKVEEEARHEA 171
                         90
                 ....*....|....*..
gi 966984660 594 eqkFAQIDEKTEKAKEE 610
Cdd:PRK12704 172 ---AVLIKEIEEEAKEE 185
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
427-638 2.13e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 42.01  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  427 QQEAKTDQADGPRepPQSarRKRSYKQAVSEldEEQHLEDEELQPPR-----------SKTPSSPCPSSKVVRPLRTFLH 495
Cdd:NF033875   49 QPGTTTVQPDNPD--PQS--GSETPKTAVSE--EATVQKDTTSQPTKveevasekngaEQSSATPNDTTNAQQPTVGAEK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  496 TVQRNqmlmtPTSAPRSVMKSFikrNTPLRVDPKEKERQRLENLRRKEEAEQLRRqKVEEDKRRRLEEVKLKREERLRKV 575
Cdd:NF033875  123 SAQEQ-----PVVSPETTNEPL---GQPTEVAPAENEANKSTSIPKEFETPDVDK-AVDEAKKDPNITVVEKPAEDLGNV 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  576 ----LQARER-VEQMKEEKKKQIEQKFAQIDEKTEKAKEERlaeekakkkaaakkmEEVEARRKQEEE 638
Cdd:NF033875  194 sskdLAAKEKeVDQLQKEQAKKIAQQAAELKAKNEKIAKEN---------------AEIAAKNKAEKE 246
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
529-755 2.25e-03

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: 41.88  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfAQIDEKTEKAK 608
Cdd:pfam02463  774 KELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE-LKEEQKLEKLA 852
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   609 EERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRwlqqeeeERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERRE 688
Cdd:pfam02463  853 EEELERLEEEITKEELLQELLLKEEELEEQKLKDE-------LESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE 925
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   689 QERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKK--------------KKEEQQRLAERQLQEEQEKKA 754
Cdd:pfam02463  926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEelgkvnlmaieefeEKEERYNKDELEKERLEEEKK 1005

                   .
gi 966984660   755 K 755
Cdd:pfam02463 1006 K 1006
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
529-764 2.51e-03

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: 41.88  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQRLEnlrrkEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKqiEQKFAQIDEKTEKAK 608
Cdd:pfam02463  151 KPERRLEIE-----EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK--ALEYYQLKEKLELEE 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   609 EERLAEEKAKKKAAAKKMEEVEARRKQEEEArrlrwlqqeeeerRHQELLQKKKEEEQERLRKAAEAKRlaeqreqerre 688
Cdd:pfam02463  224 EYLLYLDYLKLNEERIDLLQELLRDEQEEIE-------------SSKQEIEKEEEKLAQVLKENKEEEK----------- 279
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966984660   689 qerqlaeqeRRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGVSKAL 764
Cdd:pfam02463  280 ---------EKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
514-728 3.39e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.79  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  514 MKSFIKRNTPLRVDPKEKERQRLENLRRKE-EAEQLRRQKveEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQ 592
Cdd:pfam15558  86 EKQVIEKESRWREQAEDQENQRQEKLERARqEAEQRKQCQ--EQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKER 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  593 IEQKFAQIDEKTEKAKEERLaeekakkkaaakkMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEE-QERLRK 671
Cdd:pfam15558 164 EEQKKVQENNLSELLNHQAR-------------KVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRElREKAQK 230
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966984660  672 AAE----AKRLAEQREQERREQERQLAEQERRREQERLQAERElQEREKALRLQKERLQRE 728
Cdd:pfam15558 231 EEEqfqrAKWRAEEKEEERQEHKEALAELADRKIQQARQVAHK-TVQDKAQRARELNLERE 290
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
403-609 3.40e-03

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 41.23  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  403 DTEIGNST-----PNPKPAASSPETPSAGQQEAKTDQADGPREPPQSARRKRSYKQAvseldeeqhledeelqpprSKTP 477
Cdd:NF033875   47 DTQPGTTTvqpdnPDPQSGSETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGAEQS-------------------SATP 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  478 SSpcpSSKVVRPLRTFLHTVQRNqmlmtPTSAPRSVMKSFikrNTPLRVDPKEKERQRLENLRRKEEAEQLRRqKVEEDK 557
Cdd:NF033875  108 ND---TTNAQQPTVGAEKSAQEQ-----PVVSPETTNEPL---GQPTEVAPAENEANKSTSIPKEFETPDVDK-AVDEAK 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  558 RRRLEEVKLKREERLRKV----LQARER-VEQMKEEKKKQIEQKFAQIDEKTEK-AKE 609
Cdd:NF033875  176 KDPNITVVEKPAEDLGNVsskdLAAKEKeVDQLQKEQAKKIAQQAAELKAKNEKiAKE 233
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
529-756 3.96e-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: 41.20  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQrLENLRRK-EEAEQLRRQKVE-------------EDKRRRLEEVK--LKREERLRKVLQARERVEQMK-EEKKK 591
Cdd:TIGR02168  196 NELERQ-LKSLERQaEKAERYKELKAElrelelallvlrlEELREELEELQeeLKEAEEELEELTAELQELEEKlEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   592 QIEQKFAQIDEKTEK---------AKEERLAEEKAKKKAAAKKMEEVEARRkQEEEARRLRWLQQEEEERRHQELLQKKK 662
Cdd:TIGR02168  275 EVSELEEEIEELQKElyalaneisRLEQQKQILRERLANLERQLEELEAQL-EELESKLDELAEELAELEEKLEELKEEL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   663 EEEQERLRKAAEAKRLAEQREQERREQERQLAEQ-ERRREQERLQAER--ELQEREKALRLQKERLQRELEEKKKKEEQQ 739
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQLETLRSKvAQLELQIASLNNEieRLEARLERLEDRRERLQQEIEELLKKLEEA 433
                          250
                   ....*....|....*..
gi 966984660   740 RLAERQLQEEQEKKAKE 756
Cdd:TIGR02168  434 ELKELQAELEELEEELE 450
Caldesmon pfam02029
Caldesmon;
534-756 4.33e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.62  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  534 QRLENLRRKEEAEQLRRQKVEEDKrrrLEEVKLKREERLRKVlqARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLA 613
Cdd:pfam02029  69 AKREERRQKRLQEALERQKEFDPT---IADEKESVAERKENN--EEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEN 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  614 EEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERQL 693
Cdd:pfam02029 144 KWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTT 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966984660  694 AEQERRREQERLQAERELQEREKALRLQKERLQR-ELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEAELELEELKKKRE 287
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
525-676 4.45e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 525 RVDPKEKERQRLENLRRKEEAEQLRRQKVEEdKRRRLEEVKLKREERLRKVLQARERVEQMKEekKKQIEQKFAQIDEKT 604
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERL 148
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966984660 605 EKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEL--LQKKKEEEQERLRKAAEAK 676
Cdd:COG4717  149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELeeLQQRLAELEEELEEAQEEL 222
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
530-756 4.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 530 EKERQRLENLrrKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfAQIDEKTEKAKE 609
Cdd:PRK03918 227 EKEVKELEEL--KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-AEEYIKLSEFYE 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 610 ERLAEEKAKKKAAAKKMEEVEARRKQ----EEEARRLRWLQQEEEErrhqelLQKKKEEEQERLRKAAEAKRLAEQREQE 685
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEERikelEEKEERLEELKKKLKE------LEKRLEELEERHELYEEAKAKKEELERL 377
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660 686 RREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQRELEEKKKKEEQQRLAE-------RQLQEEQEKKAKE 756
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLE 455
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
529-679 5.13e-03

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: 40.32  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKVEEDKRRRLEEVKLKREERLRK----VLQARERVEQMKEE----------KKKQIE 594
Cdd:pfam15709 364 QQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqrlqLQAAQERARQQQEEfrrklqelqrKKQQEE 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  595 QKFAQIDEKTEKAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEARRlrwlqqeeeerrhqellqkkKEEEQERLRKAAE 674
Cdd:pfam15709 444 AERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKA--------------------RLEAEERRQKEEE 503

                  ....*
gi 966984660  675 AKRLA 679
Cdd:pfam15709 504 AARLA 508
MPSS6 cd23673
mitochondrial 3' processome (MPsome) subunit 6; MPSS6 is a subunit of the mitochondrial 3' ...
496-562 5.50e-03

mitochondrial 3' processome (MPsome) subunit 6; MPSS6 is a subunit of the mitochondrial 3' processome (MPsome) which is involved in 3'-5' trimming of messenger RNA (mRNA) precursors, in U-tailing of ribosomal RNA (rRNA) and some mRNAs, and in 3'-5' trimming and U-tailing of guide RNAs (gRNAs), during kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode gRNAs involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastids species. MPsome subunits include KDSS1 3'-5' exonuclease, RET1 terminal uridyltransferase (TUTase), and several subunits of as yet undefined functions (MPSS1-MPSS6). The maxicircle and minicircle RNAs are transcribed as 3' extended precursors and processed by MPsome-dependent 3'-5' degradation, and in the case of rRNAs and gRNAs also 3' uridylated. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. The MPsome catalyzes the primary uridylation of about 800 nt gRNA precursor transcripts, their processive degradation to a mature size of 40-60 nt, and secondary U-tail addition. MPSS6 is predicted (AlphaFold) to contain a C-terminal oligonucleotide/oligosaccharide binding (OB) fold-like domain.


Pssm-ID: 467890  Cd Length: 243  Bit Score: 39.69  E-value: 5.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966984660 496 TVQRNQMLMTPTSAPRSVMKSFIKRNTPLRVDPKEKERQRLE-----NLRR-----KEEAEQLRRQKVEEDKRRRLE 562
Cdd:cd23673   10 TSVHSKQSETPSKVSSKDPFATVSTSVPSNSPSSEDAKIRLEeskqkRLQRqlkdvEEELAALKNESERKTAAVRSA 86
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
511-755 5.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 5.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 511 RSVMKSFIKRNTPLRVDPKEKERQRLENLRRKEEAEQLRRQKVEE--DKRRRLEEVKLKREE------RLRKVLQARERV 582
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEleKLEKEVKELEELKEEieelekELESLEGSKRKL 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 583 EQMKEEKKKQIEQKFAQIDEKTEKAKE--ERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQE-----EEERRHQ 655
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieeriKELEEKE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 656 ELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERQLAEQERRREQERLQAERELQEREKAlrlqKERLQRELEEKKKK 735
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA----KEEIEEEISKITAR 413
                        250       260
                 ....*....|....*....|..
gi 966984660 736 EEQ--QRLAERQLQEEQEKKAK 755
Cdd:PRK03918 414 IGElkKEIKELKKAIEELKKAK 435
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
525-609 5.92e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 525 RVDPKEKERQRLENLRRKEEAEQLRRQKVEEdKRRRLEEVKlKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKT 604
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543

                 ....*
gi 966984660 605 EKAKE 609
Cdd:PRK02224 544 ERAAE 548
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
560-676 6.14e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 6.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660 560 RLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEErlaeekakkkaaaKKMEEVEARRKQEEEA 639
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE-------------AQQAIKEAKKEADEII 590
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966984660 640 RRLRWLQQEEEERRHQELLQkkkeEEQERLRKAAEAK 676
Cdd:PRK00409 591 KELRQLQKGGYASVKAHELI----EARKRLNKANEKK 623
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
529-761 6.28e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.02  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  529 KEKERQRLENLRRKEEAEQLRRQKV---EEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTE 605
Cdd:pfam15558  50 RERRLLLQQSQEQWQAEKEQRKARLgreERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  606 KAKEERLAEEKAKKKAAAKKMEEVEARRKQEEEA-----RRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLae 680
Cdd:pfam15558 130 KEKEEELQALREQNSLQLQERLEEACHKRQLKEReeqkkVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQ-- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  681 qreqerreqerqlaeqERRREQERLQAERELQEREKALRlQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKEAAGV 760
Cdd:pfam15558 208 ----------------RSQENYEQLVEERHRELREKAQK-EEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQV 270

                  .
gi 966984660  761 S 761
Cdd:pfam15558 271 A 271
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
530-610 6.64e-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: 40.44  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   530 EKERQRLENLRRKEEAEQLRR----------QKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEK---------- 589
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRdklteeyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkreldrl 411
                           90       100
                   ....*....|....*....|....
gi 966984660   590 ---KKQIEQKFAQIDEKTEKAKEE 610
Cdd:TIGR02169  412 qeeLQRLSEELADLNAAIAGIEAK 435
PTZ00121 PTZ00121
MAEBL; Provisional
543-765 7.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 7.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  543 EEAEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQI-----DEKTEKAKEERLAEEKA 617
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKednraDEATEEAFGKAEEAKKT 1106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  618 KKKAAAKKMEEVEARrKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLAEQREQERREQERQLAEQE 697
Cdd:PTZ00121 1107 ETGKAEEARKAEEAK-KKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE 1185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  698 RRREQERLQAERELQEREKALRLQKERLQRELEEKKKkeeQQRLAERQLQEEQEKKAKEAAGVSKALN 765
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED---AKKAEAVKKAEEAKKDAEEAKKAEEERN 1250
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
530-756 8.15e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  530 EKERQRLENLRR-KEEAEQLRRQKVEEDKRRRLEEvKLKREERLRKVLQARERVEQMKEEKKkQIEQKFAQIDEKTEKAK 608
Cdd:COG4913   245 EDAREQIELLEPiRELAERYAAARERLAELEYLRA-ALRLWFAQRRLELLEAELEELRAELA-RLEAELERLEARLDALR 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  609 EERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRwlqqeeeerrhqellqkkkEEEQERLRKAAEAKRLAEQREqerre 688
Cdd:COG4913   323 EELDELEAQIRGNGGDRLEQLEREIERLERELEER-------------------ERRRARLEALLAALGLPLPAS----- 378
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966984660  689 qerqlaeqerrreqerlqaERELQEREKALRLQKERLQRELEEKKKKEEQQRLAERQLQEEQEKKAKE 756
Cdd:COG4913   379 -------------------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
532-668 8.33e-03

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: 37.71  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  532 ERQRLENLRRKEEaEQLRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEER 611
Cdd:pfam05672  18 EKRRQAREQRERE-EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQ 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 966984660  612 LAEEKAKKkaaakkmeevEARRKQEEEARRLRwlqqeeeeRRHQELLQKKKEEEQER 668
Cdd:pfam05672  97 ERLQKQKE----------EAEAKAREEAERQR--------QEREKIMQQEEQERLER 135
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
548-675 8.77e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 38.53  E-value: 8.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660  548 LRRQKVEEDKRRRLEE----VKLKREERLRKVL---QARERVEQMKEEKKKQIEQKFAQ-IDEKTEKAKEERLAEEKAKK 619
Cdd:pfam13904  41 ARKLEGLKLERQPLEAyenwLAAKQRQRQKELQaqkEEREKEEQEAELRKRLAKEKYQEwLQRKARQQTKKREESHKQKA 120
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966984660  620 KAAAKKMEEVEARRKQEEEARRL--RWLQQEEEERRHQEL-----LQKKKEEEQERLRKAAEA 675
Cdd:pfam13904 121 AESASKSLAKPERKVSQEEAKEVlqEWERKKLEQQQRKREeeqreQLKKEEEEQERKQLAEKA 183
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
529-758 9.97e-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: 39.67  E-value: 9.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   529 KEKERQRLENLRRKEEaeqlRRQKVEEDKRRRLEEVKLKREER-----LRKVLQARERVEQMKEEKK--KQIEQKFAQID 601
Cdd:TIGR02169  172 KEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAeryqaLLKEKREYEGYELLKEKEAleRQKEAIERQLA 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   602 EKT-EKAK-EERLAEEKAKKKAAAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQELLQKKKEEEQERLRKAAEAKRLA 679
Cdd:TIGR02169  248 SLEeELEKlTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966984660   680 EQREQERREQERQLAEQERRREQERLQAERELQEREKALRLQKERLQ-----------------RELEEKKKKEEQQRLA 742
Cdd:TIGR02169  328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkefaetrdelkdyrEKLEKLKREINELKRE 407
                          250
                   ....*....|....*.
gi 966984660   743 ERQLQEEQEKKAKEAA 758
Cdd:TIGR02169  408 LDRLQEELQRLSEELA 423
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH